Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains
At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspa...
Saved in:
Published in | Biochimica et biophysica acta Vol. 1780; no. 3; pp. 421 - 433 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.03.2008
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids,
N- or
O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed “glycosynapse”. In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head (
trans) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy. |
---|---|
AbstractList | At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed "glycosynapse". In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head (trans) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy. At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed "glycosynapse". In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head (trans) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy.At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed "glycosynapse". In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head (trans) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy. At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N - or O -linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed “glycosynapse”. In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head ( trans ) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy. At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed “glycosynapse”. In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts: (i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head ( trans) carbohydrate-to-carbohydrate interaction. (ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype. (iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain. Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy. |
Author | Hakomori, Sen-itiroh Regina Todeschini, Adriane |
Author_xml | – sequence: 1 givenname: Adriane surname: Regina Todeschini fullname: Regina Todeschini, Adriane email: adrianet@biof.ufrj.br – sequence: 2 givenname: Sen-itiroh surname: Hakomori fullname: Hakomori, Sen-itiroh |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17991443$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkcuOEzEQRS00iMkM_AFCXrFKQrnfYYGERgwgjcQG1pbbru6uyG2HtntG-Qc-GrcSngvwxlL5nluuulfswnmHjD0XsBUgqlf7bduqHt02A6hTaQvQPGIr0dTZpgGoLtgKcig2hajKS3YVwh7SKXflE3Yp6t1OFEW-Yt9uZ6cjeacsn7xF7jve26P24TCQ672lA5nAlTO8V6635AMZDJwc197FhCyERmu5MgOG5LTmo49kKR7XJ27yD3FY8zhMfu6Hs_3RqUMkzUfSkzd-VOTCU_a4Uzbgs_N9zb7cvvt882Fz9-n9x5u3dxtdZnXcFG2tKoB2V6IpStG0qBpQWZdVNRjQJtMKAbBrVZOrEptKd0Llmah0C6IUkF-zNyffw9yOaDSmQZSVh4lGNR2lVyT_fHE0yN7fyywXWVE2yeDl2WDyX2cMUY4UliUoh34OsoYCIBN1Er74vdPPFj8CSILiJEhbCGHC7pcE5JKz3MtTznLJeammnBP2-i9MU1RLjum_ZP8Hn8fHtON7wkkGTeg0GppQR2k8_dvgO6wAyu4 |
CitedBy_id | crossref_primary_10_3390_ijms22168844 crossref_primary_10_1038_s41598_019_57130_2 crossref_primary_10_3390_ijms21031063 crossref_primary_10_1016_j_febslet_2009_07_018 crossref_primary_10_1111_liv_16208 crossref_primary_10_3390_cells2030574 crossref_primary_10_3390_ijms252413353 crossref_primary_10_1007_s11010_011_1163_0 crossref_primary_10_1002_ange_201608827 crossref_primary_10_1080_07328303_2011_600490 crossref_primary_10_1194_jlr_D089797 crossref_primary_10_1016_j_ab_2017_01_010 crossref_primary_10_1002_rcm_7130 crossref_primary_10_1016_j_carres_2008_07_004 crossref_primary_10_1093_jee_tow040 crossref_primary_10_1016_j_bpj_2016_03_006 crossref_primary_10_1096_fj_202001872RRR crossref_primary_10_1016_j_pain_2010_10_036 crossref_primary_10_1038_s41598_018_20793_4 crossref_primary_10_1093_hmg_ddae153 crossref_primary_10_1002_jssc_202001248 crossref_primary_10_1038_s41467_024_53032_8 crossref_primary_10_2217_14622416_9_6_717 crossref_primary_10_1371_journal_pone_0019990 crossref_primary_10_1016_j_cbpa_2022_102210 crossref_primary_10_3390_molecules29163769 crossref_primary_10_1016_j_molonc_2009_12_001 crossref_primary_10_1002_pmic_200900077 crossref_primary_10_1007_s10456_013_9403_4 crossref_primary_10_1007_s41664_020_00140_1 crossref_primary_10_1016_j_carres_2016_05_006 crossref_primary_10_1246_bcsj_20150369 crossref_primary_10_1111_bju_12233 crossref_primary_10_1080_15421400802714106 crossref_primary_10_1039_D2AN00224H crossref_primary_10_1016_j_ejmech_2014_01_054 crossref_primary_10_1016_j_neulet_2012_04_049 crossref_primary_10_3390_ijms21155313 crossref_primary_10_1074_jbc_M110_127837 crossref_primary_10_1016_j_plipres_2023_101241 crossref_primary_10_1007_s10719_023_10136_5 crossref_primary_10_1002_cbic_201600705 crossref_primary_10_15252_embr_201439333 crossref_primary_10_1042_CS20220149 crossref_primary_10_1016_j_expneurol_2017_09_012 crossref_primary_10_18632_oncotarget_19433 crossref_primary_10_1021_acs_jpcb_6b07142 crossref_primary_10_1021_acs_chemrev_1c00380 crossref_primary_10_1016_j_carpta_2024_100452 crossref_primary_10_1016_j_joca_2018_11_003 crossref_primary_10_1111_febs_12559 crossref_primary_10_1038_srep43729 crossref_primary_10_1080_10428190902934928 crossref_primary_10_1007_s10719_021_10017_9 crossref_primary_10_1038_s41598_019_55867_4 crossref_primary_10_1016_j_bbagen_2014_06_006 crossref_primary_10_1016_j_jsb_2019_09_010 crossref_primary_10_1371_journal_pone_0108919 crossref_primary_10_3390_biom14101265 crossref_primary_10_3390_cancers13133330 crossref_primary_10_1089_wound_2013_0436 crossref_primary_10_3390_cancers16050942 crossref_primary_10_1016_j_plipres_2021_101115 crossref_primary_10_1016_j_bbalip_2011_05_011 crossref_primary_10_1021_acs_analchem_0c02313 crossref_primary_10_3390_ijms17101732 crossref_primary_10_1002_cbic_201100382 crossref_primary_10_1007_s10719_010_9313_2 crossref_primary_10_1016_j_febslet_2009_12_010 crossref_primary_10_1007_s10719_011_9350_5 crossref_primary_10_1021_jp511534u crossref_primary_10_1007_s11064_012_0733_1 crossref_primary_10_1093_glycob_cws103 crossref_primary_10_1016_j_bbalip_2013_10_016 crossref_primary_10_3390_ijms17060925 crossref_primary_10_1016_j_bbalip_2011_09_006 crossref_primary_10_3390_molecules181215153 crossref_primary_10_1016_j_bbrc_2019_08_161 crossref_primary_10_1021_acs_analchem_2c00981 crossref_primary_10_1038_gt_2015_71 crossref_primary_10_1016_j_gene_2019_144103 crossref_primary_10_1071_CH19353 crossref_primary_10_1002_1873_3468_12344 crossref_primary_10_1007_s13238_020_00741_7 crossref_primary_10_1007_s11064_010_0319_8 crossref_primary_10_1016_j_chroma_2015_07_110 crossref_primary_10_3892_mmr_2014_3087 crossref_primary_10_1093_glycob_cwae036 crossref_primary_10_1073_pnas_0909862107 crossref_primary_10_1093_glycob_cwae032 crossref_primary_10_4132_jptm_2016_10_02 crossref_primary_10_1093_hmg_ddt434 crossref_primary_10_1038_s41557_021_00655_9 crossref_primary_10_1016_j_bbamem_2013_10_019 crossref_primary_10_1016_j_cell_2012_08_037 crossref_primary_10_1021_acs_analchem_4c00077 crossref_primary_10_1128_JVI_01964_12 crossref_primary_10_1242_jcs_071233 crossref_primary_10_1093_carcin_bgw091 crossref_primary_10_1073_pnas_1800853116 crossref_primary_10_1093_glycob_cwp047 crossref_primary_10_3390_pathophysiology28010011 crossref_primary_10_1111_febs_13346 crossref_primary_10_1093_glycob_cwp049 crossref_primary_10_1016_j_bbapap_2019_02_003 crossref_primary_10_3233_CBM_170548 crossref_primary_10_1016_j_ejca_2008_08_021 crossref_primary_10_3892_ol_2019_11020 crossref_primary_10_1007_s10719_022_10052_0 crossref_primary_10_1016_j_biocel_2013_08_002 crossref_primary_10_1016_j_febslet_2009_05_032 crossref_primary_10_1080_14728222_2023_2255377 crossref_primary_10_1016_j_carbpol_2024_122471 crossref_primary_10_1586_14760584_2015_984691 crossref_primary_10_15264_cpho_2016_23_2_71 crossref_primary_10_3390_ijms21218295 crossref_primary_10_3390_metabo12121280 crossref_primary_10_1186_1742_2094_11_61 crossref_primary_10_1371_journal_pone_0196369 crossref_primary_10_1515_hsz_2014_0283 crossref_primary_10_1016_j_jchromb_2009_07_008 crossref_primary_10_1021_bi801090a crossref_primary_10_1038_nm_2969 crossref_primary_10_1111_cts_70176 crossref_primary_10_1016_j_bbalip_2011_06_008 crossref_primary_10_3389_fmed_2020_616578 crossref_primary_10_1016_j_ajpath_2011_05_025 crossref_primary_10_1074_jbc_M116_771253 crossref_primary_10_1002_mas_20253 crossref_primary_10_3390_ijms25179629 crossref_primary_10_1155_2018_3845027 crossref_primary_10_1073_pnas_0905912106 crossref_primary_10_1371_journal_pone_0093576 crossref_primary_10_1007_s10068_025_01863_6 crossref_primary_10_1039_C6RA05608C crossref_primary_10_3390_ijms21010056 crossref_primary_10_1021_jp303643u crossref_primary_10_1016_j_bbalip_2011_06_018 crossref_primary_10_15252_embj_2021110553 crossref_primary_10_1021_bi3003633 crossref_primary_10_1016_j_tet_2016_07_026 crossref_primary_10_1074_mcp_M113_030387 crossref_primary_10_1021_acscentsci_3c01170 crossref_primary_10_1016_j_jpeds_2009_08_022 crossref_primary_10_1016_j_cis_2013_10_016 crossref_primary_10_1016_j_plipres_2018_08_002 crossref_primary_10_1242_jcs_219204 crossref_primary_10_1021_jacs_4c03196 crossref_primary_10_1002_1873_3468_13114 crossref_primary_10_1039_C6CS00165C crossref_primary_10_3390_ijms252011261 crossref_primary_10_1016_j_biochi_2011_09_021 crossref_primary_10_1016_j_bbamem_2008_11_003 crossref_primary_10_3390_cells10030572 crossref_primary_10_1021_acs_analchem_0c04542 crossref_primary_10_1371_journal_pone_0106320 crossref_primary_10_1111_j_1600_0854_2009_01022_x crossref_primary_10_3390_cancers15225362 crossref_primary_10_1074_jbc_M805755200 crossref_primary_10_1182_blood_2008_04_149641 crossref_primary_10_1016_j_canlet_2013_10_005 crossref_primary_10_1111_j_1471_4159_2010_07099_x crossref_primary_10_1134_S0006297910050032 crossref_primary_10_1371_journal_pone_0280650 crossref_primary_10_18632_oncotarget_17665 crossref_primary_10_1111_jnc_14600 crossref_primary_10_3389_fonc_2015_00300 crossref_primary_10_1038_s41419_017_0025_4 crossref_primary_10_1002_rcm_4716 crossref_primary_10_1016_j_canlet_2009_01_013 crossref_primary_10_1016_j_jmb_2016_05_020 crossref_primary_10_1002_anie_201205972 crossref_primary_10_1074_jbc_M110_147272 crossref_primary_10_1189_jlb_3RI0116_021R crossref_primary_10_2183_pjab_87_179 crossref_primary_10_3389_fimmu_2014_00442 crossref_primary_10_1021_acs_analchem_9b01945 crossref_primary_10_1016_j_bpj_2016_05_003 crossref_primary_10_1002_cbic_201900269 crossref_primary_10_1073_pnas_0903279106 crossref_primary_10_1016_j_bbalip_2011_04_006 crossref_primary_10_1038_srep01452 crossref_primary_10_3390_ijms20061363 crossref_primary_10_1074_jbc_M111_257196 crossref_primary_10_1111_j_1471_4159_2010_06627_x crossref_primary_10_1371_journal_pone_0058979 crossref_primary_10_1371_journal_pone_0062559 crossref_primary_10_1016_j_febslet_2009_01_007 crossref_primary_10_5010_JPB_2019_46_3_217 crossref_primary_10_1007_s00418_008_0509_5 crossref_primary_10_1038_s41598_018_20230_6 crossref_primary_10_1016_j_febslet_2009_10_011 crossref_primary_10_3390_membranes11010052 crossref_primary_10_21931_RB_CS_2019_02_01_28 crossref_primary_10_1194_jlr_M055319 crossref_primary_10_3892_mmr_2015_3466 crossref_primary_10_3389_fmolb_2022_813637 crossref_primary_10_3389_fonc_2014_00114 crossref_primary_10_1002_jms_3116 crossref_primary_10_1039_C8OB01817K crossref_primary_10_1016_j_crci_2011_05_004 crossref_primary_10_1007_s00018_012_1060_z crossref_primary_10_1021_acscatal_3c01563 crossref_primary_10_1074_jbc_M114_635268 crossref_primary_10_1517_14712598_2011_542140 crossref_primary_10_1016_j_bbamem_2014_01_003 crossref_primary_10_1002_ejoc_200900424 crossref_primary_10_1021_acscatal_8b01993 crossref_primary_10_1038_onc_2010_85 crossref_primary_10_1016_j_febslet_2009_10_020 crossref_primary_10_1248_cpb_c17_00455 crossref_primary_10_1016_j_bbamem_2018_12_018 crossref_primary_10_18632_oncotarget_13878 crossref_primary_10_1194_jlr_D061176 crossref_primary_10_1021_cr300419p crossref_primary_10_1016_j_bmcl_2016_08_053 crossref_primary_10_1007_s10969_013_9167_5 crossref_primary_10_1007_s00018_023_04889_3 crossref_primary_10_1093_nutrit_nuaa091 crossref_primary_10_1007_s10495_015_1103_7 crossref_primary_10_1371_journal_pone_0064728 crossref_primary_10_3390_ijms25063323 crossref_primary_10_1038_s41598_020_68516_y crossref_primary_10_3390_biom11010062 crossref_primary_10_1016_j_jff_2018_04_035 crossref_primary_10_1002_ange_201205972 crossref_primary_10_1007_s10719_023_10108_9 crossref_primary_10_1186_s12974_018_1367_2 crossref_primary_10_1002_cbf_3467 crossref_primary_10_1039_C4SM00147H crossref_primary_10_1007_s10719_022_10061_z crossref_primary_10_1093_glycob_cww086 crossref_primary_10_1351_PAC_CON_08_09_14 crossref_primary_10_1039_D1OB01150B crossref_primary_10_3389_fonc_2022_837930 crossref_primary_10_1093_glycob_cwq098 crossref_primary_10_1134_S0006297913070067 crossref_primary_10_1016_j_tet_2011_12_019 crossref_primary_10_3390_cimb46090608 crossref_primary_10_3390_ijms21061906 crossref_primary_10_1152_ajplung_00322_2013 crossref_primary_10_3389_fonc_2023_1261090 crossref_primary_10_1007_s10719_013_9516_4 crossref_primary_10_1002_jcb_24503 crossref_primary_10_1158_0008_5472_CAN_10_4108 crossref_primary_10_1021_acs_biochem_6b00267 crossref_primary_10_1134_S0006297915070020 crossref_primary_10_1016_j_ab_2008_03_039 crossref_primary_10_1016_j_carres_2014_06_029 crossref_primary_10_1016_j_jlr_2024_100609 crossref_primary_10_1007_s10529_010_0352_3 crossref_primary_10_3389_fimmu_2020_01928 crossref_primary_10_3390_biom3010198 crossref_primary_10_3390_cells10061545 crossref_primary_10_5402_2012_506160 crossref_primary_10_1194_jlr_M000984 crossref_primary_10_3390_cancers14030645 crossref_primary_10_1016_j_bbapap_2018_07_004 crossref_primary_10_3390_nu7053891 crossref_primary_10_1074_jbc_RA118_007083 crossref_primary_10_1021_jacsau_0c00058 crossref_primary_10_1586_ern_09_77 crossref_primary_10_1093_glycob_cww098 crossref_primary_10_1021_acs_joc_0c02490 crossref_primary_10_1016_j_bbalip_2009_01_008 crossref_primary_10_1007_s10157_014_1003_0 crossref_primary_10_1093_glycob_cws049 crossref_primary_10_1517_14728222_2014_986459 crossref_primary_10_1016_j_joca_2013_11_015 crossref_primary_10_1002_anie_201608827 crossref_primary_10_1007_s12035_021_02346_5 crossref_primary_10_1007_s00418_016_1518_4 crossref_primary_10_1111_jnc_15743 crossref_primary_10_3390_ijms21010106 crossref_primary_10_1152_physrev_00033_2013 crossref_primary_10_1002_anie_200804583 crossref_primary_10_1002_iub_477 crossref_primary_10_1016_j_ejmech_2019_01_016 crossref_primary_10_1515_cclm_2019_1161 crossref_primary_10_1007_s11426_010_0021_3 crossref_primary_10_1007_s10719_011_9325_6 crossref_primary_10_3390_genes11121436 crossref_primary_10_1194_jlr_M031781 crossref_primary_10_1016_j_bbrc_2012_08_090 crossref_primary_10_1371_journal_pone_0168794 crossref_primary_10_1371_journal_pone_0062919 crossref_primary_10_1152_ajpcell_00168_2013 crossref_primary_10_1093_carcin_bgp061 crossref_primary_10_1007_s10719_015_9587_5 crossref_primary_10_1016_j_biochi_2017_03_001 crossref_primary_10_3390_cells5040043 crossref_primary_10_1194_jlr_D800038_JLR200 crossref_primary_10_1007_s11064_022_03576_2 crossref_primary_10_1016_j_bbagen_2010_11_001 crossref_primary_10_1016_j_cellsig_2015_07_004 crossref_primary_10_3390_cancers13235871 crossref_primary_10_1016_j_bbagen_2012_04_008 crossref_primary_10_1002_ange_200804583 crossref_primary_10_1021_acs_jmedchem_1c01301 crossref_primary_10_1021_acs_orglett_0c02847 crossref_primary_10_3892_mmr_2020_11467 crossref_primary_10_1586_17446651_2013_846213 crossref_primary_10_1021_acs_chemrev_8b00070 crossref_primary_10_1371_journal_pone_0206881 crossref_primary_10_3390_cells2040751 crossref_primary_10_1089_omi_2009_0148 crossref_primary_10_1080_14760584_2021_1945449 crossref_primary_10_1155_2015_640540 crossref_primary_10_3390_cells9030674 crossref_primary_10_1155_2022_7819235 crossref_primary_10_1016_j_bbamem_2017_07_006 crossref_primary_10_1038_s41598_020_78926_7 crossref_primary_10_1093_glycob_cwn137 crossref_primary_10_1177_19476035241311542 crossref_primary_10_1002_elps_201100067 crossref_primary_10_3390_ijms21176213 |
Cites_doi | 10.1016/S0021-9258(18)55985-8 10.1023/B:GLYC.0000043741.47559.30 10.1146/annurev.bi.50.070181.003505 10.1074/jbc.M403857200 10.1074/jbc.M611407200 10.1016/0005-2736(83)90086-X 10.1016/S0091-679X(08)61167-X 10.1007/s11373-004-8169-5 10.1002/anie.200461224 10.1016/0014-4827(84)90205-2 10.1042/bj1090051 10.1016/0005-2760(73)90183-5 10.1074/jbc.M200383200 10.1016/S0022-2275(20)37221-7 10.1006/bbrc.2000.4030 10.1073/pnas.72.9.3585 10.1007/BF00731214 10.1126/science.175.4023.720 10.1007/BF00220302 10.1083/jcb.97.3.627 10.1002/1521-3773(20010817)40:16<3052::AID-ANIE3052>3.0.CO;2-Q 10.1021/bi00215a003 10.1126/science.7754374 10.1038/nrm1261 10.1016/S0021-9258(17)30541-0 10.1007/BF00731224 10.1084/jem.174.6.1347 10.1073/pnas.172380699 10.1016/0092-8674(86)90841-X 10.1083/jcb.99.6.2131 10.1021/bi00488a040 10.1093/oxfordjournals.glycob.a018822 10.1016/j.carres.2005.02.026 10.1126/science.2006419 10.1023/B:GLYC.0000044842.34958.f8 10.1084/jem.160.5.1591 10.1074/jbc.M507878200 10.1016/S0021-9258(18)60556-3 10.1016/0092-8674(92)90143-Z 10.1016/0012-1606(84)90101-5 10.1073/pnas.052707599 10.1006/bbrc.1997.6933 10.1073/pnas.73.2.549 10.1016/S0021-9258(17)35954-9 10.1074/jbc.M505630200 10.1074/jbc.R200020200 10.1021/ja0431354 10.1073/pnas.012540899 10.1590/S0001-37652004000300010 10.1159/000046451 10.1074/jbc.M200771200 10.1073/pnas.0407297101 10.1021/bi00467a009 10.1023/B:GLYC.0000044843.72595.7d 10.1016/0168-9525(93)90250-L 10.1016/S0021-9258(19)38662-4 10.1038/nrm1736 10.1083/jcb.200309005 10.1002/1521-3773(20010618)40:12<2257::AID-ANIE2257>3.0.CO;2-S 10.1007/s10719-006-9001-4 10.1002/ijc.11491 10.1002/chem.200500505 10.1073/pnas.0609281103 10.1093/jnci/94.19.1494 10.1007/s10719-007-9051-2 10.1016/S0021-9258(17)39801-0 10.1016/j.bbrc.2007.04.101 10.1038/sj.onc.1209269 10.1002/ana.20222 10.1023/B:GLYC.0000044846.80014.cb 10.1006/bbrc.1997.7575 10.2183/pjab.81.189 10.1039/B313934D 10.1016/0005-2736(76)90316-3 10.1016/S0014-5793(02)03479-8 10.1126/science.1719635 10.1074/jbc.270.10.5089 10.1021/bi0101998 10.1002/1521-3773(20000915)39:18<3245::AID-ANIE3245>3.0.CO;2-9 10.1016/S0952-7915(01)00299-0 10.1074/jbc.275.20.15174 10.1146/annurev.biochem.67.1.199 10.1074/jbc.M005599200 10.1016/B978-0-12-024915-2.50007-4 10.1016/S0076-6879(06)17016-0 10.1002/j.1460-2075.1986.tb04237.x 10.1016/0168-9525(87)90238-1 10.1016/j.abb.2004.02.032 10.1073/pnas.80.20.6274 10.1016/j.jneuroim.2006.09.013 10.1038/42408 |
ContentType | Journal Article |
Copyright | 2007 Elsevier B.V. |
Copyright_xml | – notice: 2007 Elsevier B.V. |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM |
DOI | 10.1016/j.bbagen.2007.10.008 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
DatabaseTitleList | MEDLINE MEDLINE - Academic |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Biology |
EISSN | 1872-8006 |
EndPage | 433 |
ExternalDocumentID | PMC2312458 17991443 10_1016_j_bbagen_2007_10_008 S0304416507002401 |
Genre | Review Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NCI NIH HHS grantid: R01 CA080054 – fundername: NCI NIH HHS grantid: CA080054 |
GroupedDBID | --- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 23N 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABGSF ABMAC ABUDA ABXDB ABYKQ ACDAQ ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEHWI AEKER AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ IHE J1W KOM LX3 M41 MO0 N9A O-L O9- OAUVE OHT OZT P-8 P-9 PC. Q38 R2- ROL RPZ SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K UQL WH7 WUQ XJT XPP ~G- AAHBH AATTM AAXKI AAYWO AAYXX ABWVN ACRPL ACVFH ADCNI ADNMO AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH -~X .55 .GJ AAYJJ ABJNI AFFNX AI. CGR CUY CVF ECM EIF F5P H~9 K-O MVM NPM RIG TWZ UHS VH1 X7M Y6R YYP ZE2 ZGI ~KM 7X8 5PM |
ID | FETCH-LOGICAL-c527t-4b7a600b95ed4518bea80a2f2670d0cd2cae00efba83a5e86cf1a3216cb015103 |
IEDL.DBID | .~1 |
ISSN | 0304-4165 0006-3002 |
IngestDate | Thu Aug 21 18:20:23 EDT 2025 Fri Jul 11 12:12:54 EDT 2025 Fri May 30 10:48:57 EDT 2025 Thu Apr 24 23:08:20 EDT 2025 Tue Jul 01 00:21:54 EDT 2025 Fri Feb 23 02:32:38 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Keywords | GPI GSL Ecad LN nOe TSPs HGF CCI Glycosphingolipids microdomain Glycosylation FGFR EGFR ECM GEM TD Neu3 GFR NMR Integrin Ganglioside Le Glycosynapse Tetraspanin |
Language | English |
License | https://www.elsevier.com/tdm/userlicense/1.0 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c527t-4b7a600b95ed4518bea80a2f2670d0cd2cae00efba83a5e86cf1a3216cb015103 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
OpenAccessLink | http://doi.org/10.1016/j.bbagen.2007.10.008 |
PMID | 17991443 |
PQID | 70400217 |
PQPubID | 23479 |
PageCount | 13 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_2312458 proquest_miscellaneous_70400217 pubmed_primary_17991443 crossref_primary_10_1016_j_bbagen_2007_10_008 crossref_citationtrail_10_1016_j_bbagen_2007_10_008 elsevier_sciencedirect_doi_10_1016_j_bbagen_2007_10_008 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2008-03-01 |
PublicationDateYYYYMMDD | 2008-03-01 |
PublicationDate_xml | – month: 03 year: 2008 text: 2008-03-01 day: 01 |
PublicationDecade | 2000 |
PublicationPlace | Netherlands |
PublicationPlace_xml | – name: Netherlands |
PublicationTitle | Biochimica et biophysica acta |
PublicationTitleAlternate | Biochim Biophys Acta |
PublicationYear | 2008 |
Publisher | Elsevier B.V |
Publisher_xml | – name: Elsevier B.V |
References | A.R. Todeschini, J.N. Dos Santos, K. Handa, S. Hakomori, Ganglioside GM2/GM3 complex affixed on silica nanospheres inhibits cell motility strongly through CD82/Met/integrin-mediated processes. Proc. Natl. Acad. Sci. U. S. A. (submited for publication). Tosin, Muller-Bunz, Murphy (bib48) 2004 Peyrieras, Hyafil, Louvard, Ploegh, Jacob (bib36) 1983; 80 Forstner, Tanaka, Isselbacher (bib12) 1968; 109 Wang, Hansen, Radisky, Yoneda, Barcellos-Hoff, Petersen, Turley, Bissell (bib92) 2002; 94 Forstner, Wherrett (bib13) 1973; 306 Kojima, Fenderson, Stroud, Goldberg, Habermann, Toyokuni, Hakomori (bib35) 1994; 11 Murphy, Muller-Bunz, Velasco-Torrijos (bib49) 2005; 340 Illmensee, Mintz (bib91) 1976; 73 Liu, Rudick, Anderson (bib25) 2002; 277 Ono, Handa, Withers, Hakomori (bib65) 1999; 59 Hemler (bib70) 2005; 6 Folch, Lees (bib75) 1951; 191 Carvalho de Souza, Kamerling (bib45) 2006; 417 Fernandes, Cohen, Bishayee (bib62) 2001; 276 Krieger, Reddy, Kozarsky, Kingsley, Hobbie, Penman (bib74) 1989; 32 Ono, Handa, Sonnino, Withers, Nagai, Hakomori (bib66) 2001; 40 Garcia-Manyes, Bucior, Ros, Anselmetti, Sanz, Burger, Fernàndez-Busquets (bib98) 2006; 281 Hakomori (bib2) 1998; 161 Bucior, Scheuring, Engel, Burger (bib54) 2004; 165 Hansson, Simons, van Meer (bib14) 1986; 5 Bremer, Hakomori, Bowen-Pope, Raines, Ross (bib28) 1984; 259 Fenderson, Zehavi, Hakomori (bib33) 1984; 160 Sorice, Parolini, Sansolini, Garofalo, Dolo, Sargiacomo, Tai, Peschle, Torrisi, Pavan (bib21) 1997; 38 Dong, Suzuki, Pin, Bova, Schalken, Isaacs, Barrett, Isaacs (bib82) 1996; 56 Murozuka, Watanabe, Hatanaka, Hakomori (bib95) 2007; 24 Matlin, Simons (bib16) 1984; 99 Ono, Handa, Withers, Hakomori (bib88) 2000; 279 Rothberg, Heuser, Donzell, Ying, Glenney, Anderson (bib24) 1992; 68 Hakomori (bib1) 1981; 50 Kingsley, Kozarsky, Hobbie, Krieger (bib73) 1986; 44 Boggs, Wang, Gao, Arvanitis, Gong, Min (bib100) 2004; 21 Cajot, Sordat, Silvestre, Sordat (bib72) 1997; 57 Matlin, Bainton, Pesonen, Louvard, Genty, Simons (bib15) 1983; 97 Hakomori, Handa, Iwabuchi, Yamamura, Prinetti (bib3) 1998; 8 Hakomori (bib8) 2004; 76 Bird, Kimber (bib50) 1984; 104 Simons, Ikonen (bib27) 1997; 387 Kaida, Morita, Kanzaki, Kamakura, Motoyoshi, Hirakawa, Kusunoki (bib63) 2004; 56 Kenny, Bissell (bib93) 2003; 107 Okada, Mugnai, Bremer, Hakomori (bib5) 1984; 155 Krummel, Davis (bib31) 2002; 14 de la Fuente, Eaton, Barrientos, Menendez, Penades (bib42) 2005; 127 Kawakami, Kawakami, Steelant, Ono, Baek, Handa, Withers, Hakomori (bib67) 2002; 277 Satoh, Ito, Nojiri, Handa, Numahata, Ohyama, Saito, Hoshi, Hakomori (bib80) 2001; 19 Miyake, Koyama, Seno, Ikeyama (bib71) 1991; 174 Miura, Kainuma, Jiang, Velasco, Vogt, Hakomori (bib77) 2004; 101 Mitsuzuka, Handa, Satoh, Arai, Hakomori (bib79) 2005; 280 Adachi, Taki, Ieki, Huang, Higashiyama, Miyake (bib83) 1996; 56 Iwabuchi, Zhang, Handa, Withers, Sinaÿ, Hakomori (bib94) 2000; 275 Sridhar, Miranti (bib84) 2006; 25 Siebert, Born, Andre, Frank, Kaltner, von der Lieth, Heck, Jimenez-Barbero, Kopitz, Gabius (bib38) 2005; 12 Yamamura, Handa, Hakomori (bib22) 1997; 236 Spillmann, Thomas-Oates, van Kuik, Vliegenthart, Misevic, Burger, Finne (bib53) 1995; 270 Singer, Nicolson (bib10) 1972; 185 Toledo, Suzuki, Handa, Hakomori (bib78) 2004; 279 Gu, Fujibayashi, Yamada, Sekiguchi (bib96) 2002; 277 Anderson (bib23) 1998; 67 Brown, London (bib6) 1997; 240 de la Fuente, Penades (bib41) 2004; 21 Hehlgans, Haase, Cordes (bib68) 2007; 1775 Eggens, Fenderson, Toyokuni, Dean, Stroud, Hakomori (bib34) 1989; 264 Tillack, Allietta, Moran, Young (bib18) 1983; 733 Stefanova, Horejsi, Ansotegui, Knapp, Stockinger (bib30) 1991; 254 Todeschini, Dos Santos, Handa, Hakomori (bib86) 2007; 282 Yu, Kojima, Hakomori, Kudo, Inoue, Inoue (bib101) 2002; 99 Handa, Takatani-Nakase, Larue, Stemmler, Kemler, Hakomori (bib43) 2007; 358 Gu, Taniguchi (bib69) 2004; 21 Lee, Pope (bib76) 2004 Hakomori, Ishizuka (bib97) 2001 Gourier, Pincet, Perez, Zhang, Zhu, Mallet, Sinay (bib46) 2005; 44 Rahmann, Rösner, Körtje, Beitinger, Veybold (bib26) 1994; vol. 101 Takeichi (bib57) 1991; 251 Hakomori (bib44) 2004; 426 Nagai, Iwamori (bib17) 1980; 29 Yoon, Nakayama, Takahashi, Yagi, Utkina, Wang, Kato, Sadilek, Hakomori (bib60) 2006; 23 Kaida, Morita, Kanzaki, Kamakura, Motoyoshi, Hirakawa, Kusunoki (bib64) 2007; 182 Yoon, Nakayama, Hikita, Handa, Hakomori (bib61) 2006; 103 Hakomori (bib9) 2005; 81 Geyer, Gege, Schmidt (bib40) 2000; 39 Hakomori, Handa (bib7) 2002; 531 Hakomori (bib89) 2002; 99 Rock, Allietta, Young, Thompson, Tillack (bib19) 1990; 29 Pascher (bib4) 1976; 455 Dong, Lamb, Rinker-Schaeffer, Vukanovic, Ichikawa, Isaacs, Barrett (bib81) 1995; 268 de la Fuente, Barrientos, Rojas, Rojo, Canada, Fernandez, Penades (bib59) 2001; 40 Bremer, Schlessinger, Hakomori (bib29) 1986; 261 Bucior, Burger (bib55) 2004; 21 Mintz, Illmensee (bib90) 1975; 72 Elola, Chiesa, Alberti, Mordoh, Fink (bib39) 2005; 12 Spillmann, Hard, Thomas-Oates, Vliegenthart, Misevic, Burger, Finne (bib52) 1993; 268 Tromas, Rojo, de la Fuente, Barrientos, Garcia, Penades (bib58) 2001; 40 Spillmann (bib47) 1994; 11 Misevic, Burger (bib51) 1990; 265 Jain, White (bib11) 1977; 15 Hakomori (bib32) 2002; 99 Rock, Allietta, Young, Thompson, Tillack (bib20) 1991; 30 Takeichi (bib37) 1987; 3 Stewart, Boggs (bib99) 1990; 29 Kemler (bib56) 1993; 9 Birchmeier, Birchmeier, Gherardi, Vande Woude (bib85) 2003; 4 Rock (10.1016/j.bbagen.2007.10.008_bib19) 1990; 29 Liu (10.1016/j.bbagen.2007.10.008_bib25) 2002; 277 Spillmann (10.1016/j.bbagen.2007.10.008_bib52) 1993; 268 Stewart (10.1016/j.bbagen.2007.10.008_bib99) 1990; 29 Miyake (10.1016/j.bbagen.2007.10.008_bib71) 1991; 174 Boggs (10.1016/j.bbagen.2007.10.008_bib100) 2004; 21 Okada (10.1016/j.bbagen.2007.10.008_bib5) 1984; 155 Carvalho de Souza (10.1016/j.bbagen.2007.10.008_bib45) 2006; 417 Mintz (10.1016/j.bbagen.2007.10.008_bib90) 1975; 72 Brown (10.1016/j.bbagen.2007.10.008_bib6) 1997; 240 Eggens (10.1016/j.bbagen.2007.10.008_bib34) 1989; 264 Rothberg (10.1016/j.bbagen.2007.10.008_bib24) 1992; 68 Hakomori (10.1016/j.bbagen.2007.10.008_bib8) 2004; 76 Gu (10.1016/j.bbagen.2007.10.008_bib69) 2004; 21 Matlin (10.1016/j.bbagen.2007.10.008_bib16) 1984; 99 Cajot (10.1016/j.bbagen.2007.10.008_bib72) 1997; 57 Kaida (10.1016/j.bbagen.2007.10.008_bib63) 2004; 56 Hansson (10.1016/j.bbagen.2007.10.008_bib14) 1986; 5 Geyer (10.1016/j.bbagen.2007.10.008_bib40) 2000; 39 Dong (10.1016/j.bbagen.2007.10.008_bib81) 1995; 268 Jain (10.1016/j.bbagen.2007.10.008_bib11) 1977; 15 Ono (10.1016/j.bbagen.2007.10.008_bib65) 1999; 59 de la Fuente (10.1016/j.bbagen.2007.10.008_bib41) 2004; 21 Adachi (10.1016/j.bbagen.2007.10.008_bib83) 1996; 56 Nagai (10.1016/j.bbagen.2007.10.008_bib17) 1980; 29 Bremer (10.1016/j.bbagen.2007.10.008_bib28) 1984; 259 Gu (10.1016/j.bbagen.2007.10.008_bib96) 2002; 277 Peyrieras (10.1016/j.bbagen.2007.10.008_bib36) 1983; 80 Krummel (10.1016/j.bbagen.2007.10.008_bib31) 2002; 14 Lee (10.1016/j.bbagen.2007.10.008_bib76) 2004 de la Fuente (10.1016/j.bbagen.2007.10.008_bib59) 2001; 40 Stefanova (10.1016/j.bbagen.2007.10.008_bib30) 1991; 254 Takeichi (10.1016/j.bbagen.2007.10.008_bib37) 1987; 3 Kenny (10.1016/j.bbagen.2007.10.008_bib93) 2003; 107 Siebert (10.1016/j.bbagen.2007.10.008_bib38) 2005; 12 Tillack (10.1016/j.bbagen.2007.10.008_bib18) 1983; 733 Wang (10.1016/j.bbagen.2007.10.008_bib92) 2002; 94 Fernandes (10.1016/j.bbagen.2007.10.008_bib62) 2001; 276 Illmensee (10.1016/j.bbagen.2007.10.008_bib91) 1976; 73 Yoon (10.1016/j.bbagen.2007.10.008_bib60) 2006; 23 Pascher (10.1016/j.bbagen.2007.10.008_bib4) 1976; 455 Hakomori (10.1016/j.bbagen.2007.10.008_bib9) 2005; 81 Kaida (10.1016/j.bbagen.2007.10.008_bib64) 2007; 182 de la Fuente (10.1016/j.bbagen.2007.10.008_bib42) 2005; 127 Hehlgans (10.1016/j.bbagen.2007.10.008_bib68) 2007; 1775 Hakomori (10.1016/j.bbagen.2007.10.008_bib3) 1998; 8 Gourier (10.1016/j.bbagen.2007.10.008_bib46) 2005; 44 Krieger (10.1016/j.bbagen.2007.10.008_bib74) 1989; 32 Dong (10.1016/j.bbagen.2007.10.008_bib82) 1996; 56 Folch (10.1016/j.bbagen.2007.10.008_bib75) 1951; 191 Yoon (10.1016/j.bbagen.2007.10.008_bib61) 2006; 103 Miura (10.1016/j.bbagen.2007.10.008_bib77) 2004; 101 Sridhar (10.1016/j.bbagen.2007.10.008_bib84) 2006; 25 Misevic (10.1016/j.bbagen.2007.10.008_bib51) 1990; 265 Singer (10.1016/j.bbagen.2007.10.008_bib10) 1972; 185 Yu (10.1016/j.bbagen.2007.10.008_bib101) 2002; 99 Ono (10.1016/j.bbagen.2007.10.008_bib66) 2001; 40 Bremer (10.1016/j.bbagen.2007.10.008_bib29) 1986; 261 Kemler (10.1016/j.bbagen.2007.10.008_bib56) 1993; 9 Bucior (10.1016/j.bbagen.2007.10.008_bib54) 2004; 165 Forstner (10.1016/j.bbagen.2007.10.008_bib12) 1968; 109 Kojima (10.1016/j.bbagen.2007.10.008_bib35) 1994; 11 Rock (10.1016/j.bbagen.2007.10.008_bib20) 1991; 30 Hakomori (10.1016/j.bbagen.2007.10.008_bib7) 2002; 531 Toledo (10.1016/j.bbagen.2007.10.008_bib78) 2004; 279 Rahmann (10.1016/j.bbagen.2007.10.008_bib26) 1994; vol. 101 Forstner (10.1016/j.bbagen.2007.10.008_bib13) 1973; 306 Tromas (10.1016/j.bbagen.2007.10.008_bib58) 2001; 40 Spillmann (10.1016/j.bbagen.2007.10.008_bib47) 1994; 11 Spillmann (10.1016/j.bbagen.2007.10.008_bib53) 1995; 270 Ono (10.1016/j.bbagen.2007.10.008_bib88) 2000; 279 Takeichi (10.1016/j.bbagen.2007.10.008_bib57) 1991; 251 Hemler (10.1016/j.bbagen.2007.10.008_bib70) 2005; 6 Todeschini (10.1016/j.bbagen.2007.10.008_bib86) 2007; 282 Birchmeier (10.1016/j.bbagen.2007.10.008_bib85) 2003; 4 Elola (10.1016/j.bbagen.2007.10.008_bib39) 2005; 12 Hakomori (10.1016/j.bbagen.2007.10.008_bib97) 2001 Hakomori (10.1016/j.bbagen.2007.10.008_bib2) 1998; 161 Garcia-Manyes (10.1016/j.bbagen.2007.10.008_bib98) 2006; 281 Handa (10.1016/j.bbagen.2007.10.008_bib43) 2007; 358 Murphy (10.1016/j.bbagen.2007.10.008_bib49) 2005; 340 Kingsley (10.1016/j.bbagen.2007.10.008_bib73) 1986; 44 Simons (10.1016/j.bbagen.2007.10.008_bib27) 1997; 387 Yamamura (10.1016/j.bbagen.2007.10.008_bib22) 1997; 236 Hakomori (10.1016/j.bbagen.2007.10.008_bib89) 2002; 99 Mitsuzuka (10.1016/j.bbagen.2007.10.008_bib79) 2005; 280 Sorice (10.1016/j.bbagen.2007.10.008_bib21) 1997; 38 Anderson (10.1016/j.bbagen.2007.10.008_bib23) 1998; 67 Satoh (10.1016/j.bbagen.2007.10.008_bib80) 2001; 19 Fenderson (10.1016/j.bbagen.2007.10.008_bib33) 1984; 160 Matlin (10.1016/j.bbagen.2007.10.008_bib15) 1983; 97 Tosin (10.1016/j.bbagen.2007.10.008_bib48) 2004 Hakomori (10.1016/j.bbagen.2007.10.008_bib1) 1981; 50 Bucior (10.1016/j.bbagen.2007.10.008_bib55) 2004; 21 10.1016/j.bbagen.2007.10.008_bib87 Iwabuchi (10.1016/j.bbagen.2007.10.008_bib94) 2000; 275 Bird (10.1016/j.bbagen.2007.10.008_bib50) 1984; 104 Kawakami (10.1016/j.bbagen.2007.10.008_bib67) 2002; 277 Hakomori (10.1016/j.bbagen.2007.10.008_bib44) 2004; 426 Murozuka (10.1016/j.bbagen.2007.10.008_bib95) 2007; 24 Hakomori (10.1016/j.bbagen.2007.10.008_bib32) 2002; 99 |
References_xml | – volume: 109 start-page: 51 year: 1968 end-page: 59 ident: bib12 article-title: Lipid composition of the isolated rat intestinal microvillus membrane publication-title: Biochem. J. – volume: 19 start-page: 723 year: 2001 end-page: 731 ident: bib80 article-title: Enhanced GM3 expression, associated with decreased invasiveness, is induced by brefeldin A in bladder cancer cells publication-title: Int. J. Oncol. – volume: 279 start-page: 34655 year: 2004 end-page: 34664 ident: bib78 article-title: Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13 publication-title: J. Biol. Chem. – volume: 25 start-page: 2367 year: 2006 end-page: 2378 ident: bib84 article-title: Tetraspanin KAI1/CD82 suppresses invasion by inhibiting integrin-dependent crosstalk with c-Met receptor and Src kinases publication-title: Oncogene – volume: 531 start-page: 88 year: 2002 end-page: 92 ident: bib7 article-title: Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy publication-title: FEBS Lett. – volume: 56 start-page: 1751 year: 1996 end-page: 1755 ident: bib83 article-title: Correlation of KAII/CD82 gene expression with good prognosis in patients with non-small cell lung cancer publication-title: Cancer Res. – volume: 387 start-page: 569 year: 1997 end-page: 572 ident: bib27 article-title: Functional rafts in cell membranes publication-title: Nature – volume: 1775 start-page: 163 year: 2007 end-page: 180 ident: bib68 article-title: Signalling via integrins: implications for cell survival and anticancer strategies publication-title: Biochim. Biophys. Acta – volume: 94 start-page: 1494 year: 2002 end-page: 1503 ident: bib92 article-title: Phenotypic reversion or death of cancer cells by altering signaling pathways in three-dimensional contexts publication-title: J. Natl. Cancer Inst. – volume: 56 start-page: 567 year: 2004 end-page: 571 ident: bib63 article-title: Ganglioside complexes as new target antigens in Guillain–Barre syndrome publication-title: Ann. Neurol. – volume: 268 start-page: 884 year: 1995 end-page: 886 ident: bib81 article-title: KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2 publication-title: Science – volume: 306 start-page: 446 year: 1973 end-page: 459 ident: bib13 article-title: Plasma membrane and mucosal glycosphingolipids in the rat intestine publication-title: Biochim. Biophys. Acta – volume: 32 start-page: 57 year: 1989 end-page: 84 ident: bib74 article-title: Analysis of the synthesis, intracellular sorting, and function of glycoproteins using a mammalian cell mutant with reversible glycosylation defects publication-title: Methods Cell Biol. – volume: 426 start-page: 173 year: 2004 end-page: 181 ident: bib44 article-title: Carbohydrate-to-carbohydrate interaction in basic cell biology: a brief overview publication-title: Arch. Biochem. Biophys. – volume: 59 start-page: 2335 year: 1999 end-page: 2339 ident: bib65 article-title: Motility inhibition and apoptosis are induced by metastasis-suppressing gene product CD82 and its analogue CD9, with concurrent glycosylation publication-title: Cancer Res. – volume: 80 start-page: 6274 year: 1983 end-page: 6277 ident: bib36 article-title: Uvomorulin: a nonintegral membrane protein of early mouse embryo publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 21 start-page: 97 year: 2004 end-page: 110 ident: bib100 article-title: A glycosynapse in myelin? publication-title: Glycoconj. J. – volume: 6 start-page: 801 year: 2005 end-page: 811 ident: bib70 article-title: Tetraspanin functions and associated microdomains publication-title: Nat. Rev., Mol. Cell Biol. – volume: 56 start-page: 4387 year: 1996 end-page: 4390 ident: bib82 article-title: Down-regulation of the KAI1 metastasis suppressor gene during the progression of human prostatic cancer infrequently involves gene mutation or allelic loss publication-title: Cancer Res. – volume: 160 start-page: 1591 year: 1984 end-page: 1596 ident: bib33 article-title: A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective publication-title: J. Exp. Med. – start-page: 494 year: 2004 end-page: 495 ident: bib48 article-title: Synthesis and X-ray single crystal structure of a bivalent glycocluster publication-title: Chem. Commun. (Camb.) – volume: 127 start-page: 6192 year: 2005 end-page: 6197 ident: bib42 article-title: Thermodynamic evidence for Ca2+-mediated self-aggregation of Lewis X gold glyconanoparticles. A model for cell adhesion via carbohydrate–carbohydrate interaction publication-title: J. Am. Chem. Soc. – volume: 236 start-page: 218 year: 1997 end-page: 222 ident: bib22 article-title: A close association of GM3 with c-Src and Rho in GM3-enriched microdomains at the B16 melanoma cell surface membrane: a preliminary note publication-title: Biochem. Biophys. Res. Commun. – volume: 358 start-page: 247 year: 2007 end-page: 252 ident: bib43 article-title: Le publication-title: Biochem. Biophys. Res. Commun. – volume: 9 start-page: 317 year: 1993 end-page: 321 ident: bib56 article-title: From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion publication-title: Trends Genet. – volume: 254 start-page: 1016 year: 1991 end-page: 1019 ident: bib30 article-title: GPI-anchored cell-surface molecules complexed to protein tyrosine kinases publication-title: Science – volume: 279 start-page: 744 year: 2000 end-page: 750 ident: bib88 article-title: Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional α3, α5-CD82 glycosylation complex in ldlD 14 cells publication-title: Biochem. Biophys. Res. Commun. – volume: 161 start-page: 79 year: 1998 end-page: 90 ident: bib2 article-title: Cancer-associated glycosphingolipid antigens: their structure, organization, and function publication-title: Acta Anat. – volume: 261 start-page: 2434 year: 1986 end-page: 2440 ident: bib29 article-title: Ganglioside-mediated modulation of cell growth: specific effects of GM publication-title: J. Biol. Chem. – volume: 240 start-page: 1 year: 1997 end-page: 7 ident: bib6 article-title: Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? publication-title: Biochem. Biophys. Res. Commun. – volume: 264 start-page: 9476 year: 1989 end-page: 9484 ident: bib34 article-title: Specific interaction between Le publication-title: J. Biol. Chem. – volume: 259 start-page: 6818 year: 1984 end-page: 6825 ident: bib28 article-title: Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation publication-title: J. Biol. Chem. – volume: 275 start-page: 15174 year: 2000 end-page: 15181 ident: bib94 article-title: Reconstitution of membranes simulating “glycosignaling domain” and their susceptibility to lyso-GM3 publication-title: J. Biol. Chem. – volume: 40 start-page: 6414 year: 2001 end-page: 6421 ident: bib66 article-title: GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: co-expression of GM3 and CD9 is essential in down-regulation of tumor cell motility and malignancy publication-title: Biochemistry – volume: 733 start-page: 15 year: 1983 end-page: 24 ident: bib18 article-title: Localization of globoside and Forssman glycolipids on erythrocyte membranes publication-title: Biochim. Biophys. Acta – volume: 3 start-page: 213 year: 1987 end-page: 217 ident: bib37 article-title: Cadherins: a molecular family essential for selective cell–cell adhesion and animal morphogenesis publication-title: Trends Genet. – volume: 14 start-page: 66 year: 2002 end-page: 74 ident: bib31 article-title: Dynamics of the immunological synapse: finding, establishing and solidifying a connection publication-title: Curr. Opin. Immunol. – volume: 276 start-page: 5375 year: 2001 end-page: 5383 ident: bib62 article-title: Glycosylation-induced conformational modification positively regulates receptor–receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DEGFR) expressed in cancer cells publication-title: J. Biol. Chem. – volume: 174 start-page: 1347 year: 1991 end-page: 1354 ident: bib71 article-title: Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility publication-title: J. Exp. Med. – volume: 103 start-page: 18987 year: 2006 end-page: 18991 ident: bib61 article-title: Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 73 start-page: 549 year: 1976 end-page: 553 ident: bib91 article-title: Totipotency and normal differentiation of single teratocarcinoma cells cloned by injection into blastocysts publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 265 start-page: 20577 year: 1990 end-page: 20584 ident: bib51 article-title: The species-specific cell-binding site of the aggregation factor from the sponge Microciona prolifera is a highly repetitive novel glycan containing glucuronic acid, fucose, and mannose publication-title: J. Biol. Chem. – reference: A.R. Todeschini, J.N. Dos Santos, K. Handa, S. Hakomori, Ganglioside GM2/GM3 complex affixed on silica nanospheres inhibits cell motility strongly through CD82/Met/integrin-mediated processes. Proc. Natl. Acad. Sci. U. S. A. (submited for publication). – volume: 23 start-page: 639 year: 2006 end-page: 649 ident: bib60 article-title: Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside publication-title: Glycoconj. J. – volume: 155 start-page: 448 year: 1984 end-page: 456 ident: bib5 article-title: Glycosphingolipids in detergent-insoluble substrate attachment matrix (DISAM) prepared from substrate attachment material (SAM): their possible role in regulating cell adhesion publication-title: Exp. Cell Res. – volume: 185 start-page: 720 year: 1972 end-page: 731 ident: bib10 article-title: The fluid mosaic model of the structure of cell membrane publication-title: Science – volume: 99 start-page: 2131 year: 1984 end-page: 2139 ident: bib16 article-title: Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells publication-title: J. Cell Biol. – volume: 29 start-page: 81 year: 1980 end-page: 90 ident: bib17 article-title: Brain and thymus gangliosides: their molecular diversity and its biological implications and a dynamic annular model for their function in cell surface membranes publication-title: Mol. Cell. Biochem. – volume: 50 start-page: 733 year: 1981 end-page: 764 ident: bib1 article-title: Glycosphingolipids in cellular interaction, differentiation, and oncogenesis publication-title: Ann. Rev. Biochem. – volume: 44 start-page: 749 year: 1986 end-page: 759 ident: bib73 article-title: Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant publication-title: Cell – volume: 8 start-page: xi year: 1998 end-page: xviii ident: bib3 article-title: New insights in glycosphingolipid function: “Glycosignaling domain,” a cell surface assembly of glycosphingolipids with signal transducer molecules, involved in cell adhesion coupled with signaling publication-title: Glycobiology – volume: vol. 101 start-page: 127 year: 1994 end-page: 145 ident: bib26 article-title: Ca publication-title: Biological function of gangliosides – year: 2001 ident: bib97 article-title: Glycolipids: Animal. Encyclopedia of Life Sciences – volume: 68 start-page: 673 year: 1992 end-page: 682 ident: bib24 article-title: Caveolin, a protein component of caveolae membrane coats publication-title: Cell – volume: 15 start-page: 1 year: 1977 end-page: 60 ident: bib11 article-title: Long-range order in biomembranes publication-title: Adv. Lipid Res. – volume: 11 start-page: 169 year: 1994 end-page: 171 ident: bib47 article-title: Carbohydrates in cellular recognition: from leucine-zipper to sugar-zipper? publication-title: Glycoconj. J. – volume: 99 start-page: 10231 year: 2002 end-page: 10233 ident: bib89 article-title: Glycosylation defining cancer malignancy: new wine in an old bottle publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 107 start-page: 688 year: 2003 end-page: 695 ident: bib93 article-title: Tumor reversion: correction of malignant behavior by microenvironmental cues publication-title: Int. J. Cancer – volume: 40 start-page: 3052 year: 2001 end-page: 3055 ident: bib58 article-title: Adhesion forces between Lewis publication-title: Angew. Chem., Int. Ed. Engl. – volume: 99 start-page: 2854 year: 2002 end-page: 2859 ident: bib101 article-title: Binding of rainbow trout sperm to egg is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 21 start-page: 149 year: 2004 end-page: 163 ident: bib41 article-title: Understanding carbohydrate–carbohydrate interactions by means of glyconanotechnology publication-title: Glycoconj. J. – volume: 39 start-page: 3245 year: 2000 end-page: 3249 ident: bib40 article-title: Calcium-dependent carbohydrate–carbohydrate recognition between Lewis(X) blood group antigens publication-title: Angew. Chem., Int. Ed. Engl. – volume: 277 start-page: 41295 year: 2002 end-page: 41298 ident: bib25 article-title: Multiple functions of caveolin-1 publication-title: J. Biol. Chem. – volume: 99 start-page: 225 year: 2002 end-page: 232 ident: bib32 article-title: The glycosynapse publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 165 start-page: 529 year: 2004 end-page: 537 ident: bib54 article-title: Carbohydrate–carbohydrate interaction provides adhesion force and specificity for cellular recognition publication-title: J. Cell Biol. – volume: 30 start-page: 19 year: 1991 end-page: 25 ident: bib20 article-title: Ganglioside G publication-title: Biochemistry – volume: 101 start-page: 16204 year: 2004 end-page: 16209 ident: bib77 article-title: Reversion of the Jun-induced oncogenic phenotype by enhanced synthesis of sialosyllactosylceramide (GM3 ganglioside) publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 277 start-page: 19922 year: 2002 end-page: 19928 ident: bib96 article-title: Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways publication-title: J. Biol. Chem. – volume: 44 start-page: 1683 year: 2005 end-page: 1687 ident: bib46 article-title: The natural LewisX-bearing lipids promote membrane adhesion: influence of ceramide on carbohydrate–carbohydrate recognition publication-title: Angew. Chem., Int. Ed. Engl. – volume: 268 start-page: 13378 year: 1993 end-page: 13387 ident: bib52 article-title: Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera publication-title: J. Biol. Chem. – volume: 29 start-page: 8484 year: 1990 end-page: 8490 ident: bib19 article-title: Organization of glycosphingolipids in phosphatidylcholine bilayers: use of antibody molecules and Fab fragments as morphologic markers publication-title: Biochemistry – volume: 12 start-page: 13 year: 2005 end-page: 29 ident: bib39 article-title: Galectin-1 receptors in different cell types publication-title: J. Biomed. Sci. – volume: 182 start-page: 212 year: 2007 end-page: 218 ident: bib64 article-title: Anti-ganglioside complex antibodies associated with severe disability in GBS publication-title: J. Neuroimmunol. – volume: 5 start-page: 483 year: 1986 end-page: 489 ident: bib14 article-title: Two strains of the Madin–Darby canine kidney (MDCK) cell line have distinct glycosphingolipid compositions publication-title: EMBO J. – volume: 67 start-page: 199 year: 1998 end-page: 225 ident: bib23 article-title: The caveolae membrane system publication-title: Ann. Rev. Biochem. – volume: 81 start-page: 189 year: 2005 end-page: 203 ident: bib9 article-title: Organization and function of glycosphingolipids in membrane publication-title: Proc. Jpn. Acad., Ser. B Phys. Biol. Sci. – volume: 340 start-page: 1437 year: 2005 end-page: 1440 ident: bib49 article-title: The crystal structure of a cyclic glycolipid reveals a carbohydrate–carbohydrate interaction interface publication-title: Carbohydr. Res. – volume: 282 start-page: 8123 year: 2007 end-page: 8133 ident: bib86 article-title: Ganglioside GM2-tetraspanin CD82 complex inhibits Met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse publication-title: J. Biol. Chem. – volume: 270 start-page: 5089 year: 1995 end-page: 5097 ident: bib53 article-title: Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate–carbohydrate-mediated cell aggregation of the marine sponge Microciona prolifera publication-title: J. Biol. Chem. – volume: 76 start-page: 553 year: 2004 end-page: 572 ident: bib8 article-title: Glycosynapses: microdomains controlling carbohydrate-dependent cell adhesion and signaling publication-title: Ann. Braz Acad. Sci. – volume: 251 start-page: 1451 year: 1991 end-page: 1455 ident: bib57 article-title: Cadherin cell adhesion receptors as a morphogenetic regulator publication-title: Science – volume: 417 start-page: 221 year: 2006 end-page: 243 ident: bib45 article-title: Analysis of carbohydrate–carbohydrate interactions using gold glyconanoparticles and oligosaccharide self-assembling monolayers publication-title: Methods Enzymol. – volume: 280 start-page: 35545 year: 2005 end-page: 35553 ident: bib79 article-title: A specific microdomain (“glycosynapse 3”) controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9 publication-title: J. Biol. Chem. – volume: 29 start-page: 3644 year: 1990 end-page: 3653 ident: bib99 article-title: Dependence of the surface expression of the glycolipid cerebroside sulfate on its lipid environment: comparison of sphingomyelin and phosphatidylcholine publication-title: Biochemistry – volume: 455 start-page: 433 year: 1976 end-page: 451 ident: bib4 article-title: Molecular arrangements in sphingolipids: conformation and hydrogen bonding of ceramide and their implication on membrane stability and permeability publication-title: Biochim. Biophys. Acta – volume: 4 start-page: 915 year: 2003 end-page: 925 ident: bib85 article-title: Met, metastasis, motility and more publication-title: Nat. Rev., Mol. Cell Biol. – volume: 21 start-page: 111 year: 2004 end-page: 123 ident: bib55 article-title: Carbohydrate–carbohydrate interaction as a major force initiating cell–cell recognition publication-title: Glycoconj. J. – volume: 277 start-page: 34349 year: 2002 end-page: 34358 ident: bib67 article-title: Tetraspanin CD9 is a “proteolipid”, and its interaction with a3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility publication-title: J. Biol. Chem. – volume: 38 start-page: 969 year: 1997 end-page: 980 ident: bib21 article-title: Evidence for the existence of ganglioside-enriched plasma membrane domains in human peripheral lymphocytes publication-title: J. Lipid Res. – volume: 11 start-page: 238 year: 1994 end-page: 248 ident: bib35 article-title: Further studies on cell adhesion based on Le publication-title: Glycoconj. J. – volume: 24 start-page: 551 year: 2007 end-page: 563 ident: bib95 article-title: Lyso-GM3, its dimer, and multimer: Their synthesis, and their effect on epidermal growth factor-induced receptor tyrosine kinase publication-title: Glycoconj. J. – volume: 97 start-page: 627 year: 1983 end-page: 637 ident: bib15 article-title: Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin–Darby canine kidney cells. I. Morphological evidence publication-title: J. Cell Biol. – volume: 21 start-page: 9 year: 2004 end-page: 15 ident: bib69 article-title: Regulation of integrin functions by N-glycans publication-title: Glycoconj. J. – volume: 191 start-page: 807 year: 1951 end-page: 817 ident: bib75 article-title: Proteolipides, a new type of tissue lipoproteins: their isolation from brain publication-title: J. Biol. Chem. – volume: 40 start-page: 2259 year: 2001 end-page: 2261 ident: bib59 article-title: Gold glyconanoparticles as water-soluble polyvalent models to study carbohydrate interactions publication-title: Angew. Chem., Int. Ed. Engl. – volume: 12 start-page: 388 year: 2005 end-page: 402 ident: bib38 article-title: Carbohydrate chain of ganglioside GM1 as a ligand: identification of the binding strategies of three 15 mer peptides and their divergence from the binding modes of growth-regulatory galectin-1 and cholera toxin publication-title: Chemistry – volume: 281 start-page: 5992 year: 2006 end-page: 5999 ident: bib98 article-title: Proteoglycan mechanics studied by single-molecule force spectroscopy of allotypic cell adhesion glycans publication-title: J. Biol. Chem. – volume: 104 year: 1984 ident: bib50 article-title: Oligosaccharides containing fucose linked α(1,3) and α(1,4) to N-acetylglucosamine cause decompaction of mouse morulae publication-title: Dev. Biol. – start-page: 1 year: 2004 end-page: 12 ident: bib76 article-title: Jordi Folch-Pi. publication-title: National Academy of Sciences Online Memoirs – volume: 57 start-page: 2593 year: 1997 end-page: 2597 ident: bib72 article-title: Differential display cloning identifies motility-related protein (MRP1/CD9) as highly expressed in primary compared to metastatic human colon carcinoma cells publication-title: Cancer Res. – volume: 72 start-page: 3585 year: 1975 end-page: 3589 ident: bib90 article-title: Normal genetically mosaic mice produced from malignant teratocarcinoma cells publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 191 start-page: 807 year: 1951 ident: 10.1016/j.bbagen.2007.10.008_bib75 article-title: Proteolipides, a new type of tissue lipoproteins: their isolation from brain publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)55985-8 – volume: 59 start-page: 2335 year: 1999 ident: 10.1016/j.bbagen.2007.10.008_bib65 article-title: Motility inhibition and apoptosis are induced by metastasis-suppressing gene product CD82 and its analogue CD9, with concurrent glycosylation publication-title: Cancer Res. – volume: 56 start-page: 1751 year: 1996 ident: 10.1016/j.bbagen.2007.10.008_bib83 article-title: Correlation of KAII/CD82 gene expression with good prognosis in patients with non-small cell lung cancer publication-title: Cancer Res. – volume: 21 start-page: 9 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib69 article-title: Regulation of integrin functions by N-glycans publication-title: Glycoconj. J. doi: 10.1023/B:GLYC.0000043741.47559.30 – volume: 50 start-page: 733 year: 1981 ident: 10.1016/j.bbagen.2007.10.008_bib1 article-title: Glycosphingolipids in cellular interaction, differentiation, and oncogenesis publication-title: Ann. Rev. Biochem. doi: 10.1146/annurev.bi.50.070181.003505 – volume: 279 start-page: 34655 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib78 article-title: Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M403857200 – volume: 282 start-page: 8123 year: 2007 ident: 10.1016/j.bbagen.2007.10.008_bib86 article-title: Ganglioside GM2-tetraspanin CD82 complex inhibits Met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse publication-title: J. Biol. Chem. doi: 10.1074/jbc.M611407200 – volume: 733 start-page: 15 year: 1983 ident: 10.1016/j.bbagen.2007.10.008_bib18 article-title: Localization of globoside and Forssman glycolipids on erythrocyte membranes publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2736(83)90086-X – volume: 56 start-page: 4387 year: 1996 ident: 10.1016/j.bbagen.2007.10.008_bib82 article-title: Down-regulation of the KAI1 metastasis suppressor gene during the progression of human prostatic cancer infrequently involves gene mutation or allelic loss publication-title: Cancer Res. – volume: 32 start-page: 57 year: 1989 ident: 10.1016/j.bbagen.2007.10.008_bib74 article-title: Analysis of the synthesis, intracellular sorting, and function of glycoproteins using a mammalian cell mutant with reversible glycosylation defects publication-title: Methods Cell Biol. doi: 10.1016/S0091-679X(08)61167-X – volume: 12 start-page: 13 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib39 article-title: Galectin-1 receptors in different cell types publication-title: J. Biomed. Sci. doi: 10.1007/s11373-004-8169-5 – volume: 44 start-page: 1683 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib46 article-title: The natural LewisX-bearing lipids promote membrane adhesion: influence of ceramide on carbohydrate–carbohydrate recognition publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/anie.200461224 – volume: 155 start-page: 448 year: 1984 ident: 10.1016/j.bbagen.2007.10.008_bib5 article-title: Glycosphingolipids in detergent-insoluble substrate attachment matrix (DISAM) prepared from substrate attachment material (SAM): their possible role in regulating cell adhesion publication-title: Exp. Cell Res. doi: 10.1016/0014-4827(84)90205-2 – volume: 109 start-page: 51 year: 1968 ident: 10.1016/j.bbagen.2007.10.008_bib12 article-title: Lipid composition of the isolated rat intestinal microvillus membrane publication-title: Biochem. J. doi: 10.1042/bj1090051 – volume: 306 start-page: 446 year: 1973 ident: 10.1016/j.bbagen.2007.10.008_bib13 article-title: Plasma membrane and mucosal glycosphingolipids in the rat intestine publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2760(73)90183-5 – volume: 277 start-page: 19922 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib96 article-title: Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways publication-title: J. Biol. Chem. doi: 10.1074/jbc.M200383200 – volume: 38 start-page: 969 year: 1997 ident: 10.1016/j.bbagen.2007.10.008_bib21 article-title: Evidence for the existence of ganglioside-enriched plasma membrane domains in human peripheral lymphocytes publication-title: J. Lipid Res. doi: 10.1016/S0022-2275(20)37221-7 – volume: 279 start-page: 744 year: 2000 ident: 10.1016/j.bbagen.2007.10.008_bib88 article-title: Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional α3, α5-CD82 glycosylation complex in ldlD 14 cells publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.2000.4030 – volume: 72 start-page: 3585 year: 1975 ident: 10.1016/j.bbagen.2007.10.008_bib90 article-title: Normal genetically mosaic mice produced from malignant teratocarcinoma cells publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.72.9.3585 – volume: 11 start-page: 169 year: 1994 ident: 10.1016/j.bbagen.2007.10.008_bib47 article-title: Carbohydrates in cellular recognition: from leucine-zipper to sugar-zipper? publication-title: Glycoconj. J. doi: 10.1007/BF00731214 – volume: 185 start-page: 720 year: 1972 ident: 10.1016/j.bbagen.2007.10.008_bib10 article-title: The fluid mosaic model of the structure of cell membrane publication-title: Science doi: 10.1126/science.175.4023.720 – volume: 29 start-page: 81 year: 1980 ident: 10.1016/j.bbagen.2007.10.008_bib17 article-title: Brain and thymus gangliosides: their molecular diversity and its biological implications and a dynamic annular model for their function in cell surface membranes publication-title: Mol. Cell. Biochem. doi: 10.1007/BF00220302 – volume: 97 start-page: 627 year: 1983 ident: 10.1016/j.bbagen.2007.10.008_bib15 article-title: Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin–Darby canine kidney cells. I. Morphological evidence publication-title: J. Cell Biol. doi: 10.1083/jcb.97.3.627 – volume: 40 start-page: 3052 year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib58 article-title: Adhesion forces between Lewisx determinant antigens as measured by atomic force microscopy publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/1521-3773(20010817)40:16<3052::AID-ANIE3052>3.0.CO;2-Q – volume: 30 start-page: 19 year: 1991 ident: 10.1016/j.bbagen.2007.10.008_bib20 article-title: Ganglioside GM1 and asialo-GM1 at low concentration are preferentially incorporated into the gel phase in two-component, two-phase phosphatidylcholine bilayers publication-title: Biochemistry doi: 10.1021/bi00215a003 – volume: 268 start-page: 884 year: 1995 ident: 10.1016/j.bbagen.2007.10.008_bib81 article-title: KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2 publication-title: Science doi: 10.1126/science.7754374 – volume: 4 start-page: 915 year: 2003 ident: 10.1016/j.bbagen.2007.10.008_bib85 article-title: Met, metastasis, motility and more publication-title: Nat. Rev., Mol. Cell Biol. doi: 10.1038/nrm1261 – volume: 265 start-page: 20577 year: 1990 ident: 10.1016/j.bbagen.2007.10.008_bib51 article-title: The species-specific cell-binding site of the aggregation factor from the sponge Microciona prolifera is a highly repetitive novel glycan containing glucuronic acid, fucose, and mannose publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)30541-0 – volume: 11 start-page: 238 year: 1994 ident: 10.1016/j.bbagen.2007.10.008_bib35 article-title: Further studies on cell adhesion based on Lex–Lex interaction, with new approaches: embryoglycan aggregation of F9 teratocarcinoma cells, and adhesion of various tumour cells based on Lex expression publication-title: Glycoconj. J. doi: 10.1007/BF00731224 – volume: 174 start-page: 1347 year: 1991 ident: 10.1016/j.bbagen.2007.10.008_bib71 article-title: Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility publication-title: J. Exp. Med. doi: 10.1084/jem.174.6.1347 – volume: 19 start-page: 723 year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib80 article-title: Enhanced GM3 expression, associated with decreased invasiveness, is induced by brefeldin A in bladder cancer cells publication-title: Int. J. Oncol. – volume: 99 start-page: 10231 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib89 article-title: Glycosylation defining cancer malignancy: new wine in an old bottle publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.172380699 – volume: 44 start-page: 749 year: 1986 ident: 10.1016/j.bbagen.2007.10.008_bib73 article-title: Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant publication-title: Cell doi: 10.1016/0092-8674(86)90841-X – volume: 99 start-page: 2131 year: 1984 ident: 10.1016/j.bbagen.2007.10.008_bib16 article-title: Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells publication-title: J. Cell Biol. doi: 10.1083/jcb.99.6.2131 – volume: 29 start-page: 8484 year: 1990 ident: 10.1016/j.bbagen.2007.10.008_bib19 article-title: Organization of glycosphingolipids in phosphatidylcholine bilayers: use of antibody molecules and Fab fragments as morphologic markers publication-title: Biochemistry doi: 10.1021/bi00488a040 – volume: vol. 101 start-page: 127 year: 1994 ident: 10.1016/j.bbagen.2007.10.008_bib26 article-title: Ca2+-ganglioside interaction in neuronal differentiation and development – volume: 8 start-page: xi year: 1998 ident: 10.1016/j.bbagen.2007.10.008_bib3 article-title: New insights in glycosphingolipid function: “Glycosignaling domain,” a cell surface assembly of glycosphingolipids with signal transducer molecules, involved in cell adhesion coupled with signaling publication-title: Glycobiology doi: 10.1093/oxfordjournals.glycob.a018822 – volume: 340 start-page: 1437 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib49 article-title: The crystal structure of a cyclic glycolipid reveals a carbohydrate–carbohydrate interaction interface publication-title: Carbohydr. Res. doi: 10.1016/j.carres.2005.02.026 – volume: 251 start-page: 1451 year: 1991 ident: 10.1016/j.bbagen.2007.10.008_bib57 article-title: Cadherin cell adhesion receptors as a morphogenetic regulator publication-title: Science doi: 10.1126/science.2006419 – volume: 21 start-page: 97 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib100 article-title: A glycosynapse in myelin? publication-title: Glycoconj. J. doi: 10.1023/B:GLYC.0000044842.34958.f8 – volume: 160 start-page: 1591 year: 1984 ident: 10.1016/j.bbagen.2007.10.008_bib33 article-title: A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective publication-title: J. Exp. Med. doi: 10.1084/jem.160.5.1591 – volume: 281 start-page: 5992 year: 2006 ident: 10.1016/j.bbagen.2007.10.008_bib98 article-title: Proteoglycan mechanics studied by single-molecule force spectroscopy of allotypic cell adhesion glycans publication-title: J. Biol. Chem. doi: 10.1074/jbc.M507878200 – volume: 264 start-page: 9476 year: 1989 ident: 10.1016/j.bbagen.2007.10.008_bib34 article-title: Specific interaction between Lex and Lex determinants: a possible basis for cell recognition in preimplantation embryos and in embryonal carcinoma cells publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)60556-3 – volume: 68 start-page: 673 year: 1992 ident: 10.1016/j.bbagen.2007.10.008_bib24 article-title: Caveolin, a protein component of caveolae membrane coats publication-title: Cell doi: 10.1016/0092-8674(92)90143-Z – volume: 104 year: 1984 ident: 10.1016/j.bbagen.2007.10.008_bib50 article-title: Oligosaccharides containing fucose linked α(1,3) and α(1,4) to N-acetylglucosamine cause decompaction of mouse morulae publication-title: Dev. Biol. doi: 10.1016/0012-1606(84)90101-5 – volume: 99 start-page: 2854 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib101 article-title: Binding of rainbow trout sperm to egg is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.052707599 – volume: 236 start-page: 218 year: 1997 ident: 10.1016/j.bbagen.2007.10.008_bib22 article-title: A close association of GM3 with c-Src and Rho in GM3-enriched microdomains at the B16 melanoma cell surface membrane: a preliminary note publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.6933 – volume: 73 start-page: 549 year: 1976 ident: 10.1016/j.bbagen.2007.10.008_bib91 article-title: Totipotency and normal differentiation of single teratocarcinoma cells cloned by injection into blastocysts publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.73.2.549 – volume: 261 start-page: 2434 year: 1986 ident: 10.1016/j.bbagen.2007.10.008_bib29 article-title: Ganglioside-mediated modulation of cell growth: specific effects of GM3 on tyrosine phosphorylation of the epidermal growth factor receptor publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35954-9 – volume: 280 start-page: 35545 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib79 article-title: A specific microdomain (“glycosynapse 3”) controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M505630200 – volume: 277 start-page: 41295 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib25 article-title: Multiple functions of caveolin-1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.R200020200 – year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib97 – volume: 57 start-page: 2593 year: 1997 ident: 10.1016/j.bbagen.2007.10.008_bib72 article-title: Differential display cloning identifies motility-related protein (MRP1/CD9) as highly expressed in primary compared to metastatic human colon carcinoma cells publication-title: Cancer Res. – volume: 127 start-page: 6192 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib42 article-title: Thermodynamic evidence for Ca2+-mediated self-aggregation of Lewis X gold glyconanoparticles. A model for cell adhesion via carbohydrate–carbohydrate interaction publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0431354 – volume: 99 start-page: 225 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib32 article-title: The glycosynapse publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.012540899 – ident: 10.1016/j.bbagen.2007.10.008_bib87 – volume: 76 start-page: 553 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib8 article-title: Glycosynapses: microdomains controlling carbohydrate-dependent cell adhesion and signaling publication-title: Ann. Braz Acad. Sci. doi: 10.1590/S0001-37652004000300010 – volume: 161 start-page: 79 year: 1998 ident: 10.1016/j.bbagen.2007.10.008_bib2 article-title: Cancer-associated glycosphingolipid antigens: their structure, organization, and function publication-title: Acta Anat. doi: 10.1159/000046451 – volume: 277 start-page: 34349 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib67 article-title: Tetraspanin CD9 is a “proteolipid”, and its interaction with a3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility publication-title: J. Biol. Chem. doi: 10.1074/jbc.M200771200 – volume: 101 start-page: 16204 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib77 article-title: Reversion of the Jun-induced oncogenic phenotype by enhanced synthesis of sialosyllactosylceramide (GM3 ganglioside) publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0407297101 – volume: 29 start-page: 3644 year: 1990 ident: 10.1016/j.bbagen.2007.10.008_bib99 article-title: Dependence of the surface expression of the glycolipid cerebroside sulfate on its lipid environment: comparison of sphingomyelin and phosphatidylcholine publication-title: Biochemistry doi: 10.1021/bi00467a009 – volume: 21 start-page: 111 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib55 article-title: Carbohydrate–carbohydrate interaction as a major force initiating cell–cell recognition publication-title: Glycoconj. J. doi: 10.1023/B:GLYC.0000044843.72595.7d – volume: 9 start-page: 317 year: 1993 ident: 10.1016/j.bbagen.2007.10.008_bib56 article-title: From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion publication-title: Trends Genet. doi: 10.1016/0168-9525(93)90250-L – volume: 268 start-page: 13378 year: 1993 ident: 10.1016/j.bbagen.2007.10.008_bib52 article-title: Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)38662-4 – volume: 6 start-page: 801 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib70 article-title: Tetraspanin functions and associated microdomains publication-title: Nat. Rev., Mol. Cell Biol. doi: 10.1038/nrm1736 – volume: 165 start-page: 529 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib54 article-title: Carbohydrate–carbohydrate interaction provides adhesion force and specificity for cellular recognition publication-title: J. Cell Biol. doi: 10.1083/jcb.200309005 – volume: 40 start-page: 2259 year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib59 article-title: Gold glyconanoparticles as water-soluble polyvalent models to study carbohydrate interactions publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/1521-3773(20010618)40:12<2257::AID-ANIE2257>3.0.CO;2-S – volume: 23 start-page: 639 year: 2006 ident: 10.1016/j.bbagen.2007.10.008_bib60 article-title: Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside publication-title: Glycoconj. J. doi: 10.1007/s10719-006-9001-4 – volume: 107 start-page: 688 year: 2003 ident: 10.1016/j.bbagen.2007.10.008_bib93 article-title: Tumor reversion: correction of malignant behavior by microenvironmental cues publication-title: Int. J. Cancer doi: 10.1002/ijc.11491 – volume: 12 start-page: 388 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib38 article-title: Carbohydrate chain of ganglioside GM1 as a ligand: identification of the binding strategies of three 15 mer peptides and their divergence from the binding modes of growth-regulatory galectin-1 and cholera toxin publication-title: Chemistry doi: 10.1002/chem.200500505 – volume: 103 start-page: 18987 year: 2006 ident: 10.1016/j.bbagen.2007.10.008_bib61 article-title: Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0609281103 – volume: 94 start-page: 1494 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib92 article-title: Phenotypic reversion or death of cancer cells by altering signaling pathways in three-dimensional contexts publication-title: J. Natl. Cancer Inst. doi: 10.1093/jnci/94.19.1494 – volume: 24 start-page: 551 year: 2007 ident: 10.1016/j.bbagen.2007.10.008_bib95 article-title: Lyso-GM3, its dimer, and multimer: Their synthesis, and their effect on epidermal growth factor-induced receptor tyrosine kinase publication-title: Glycoconj. J. doi: 10.1007/s10719-007-9051-2 – volume: 259 start-page: 6818 year: 1984 ident: 10.1016/j.bbagen.2007.10.008_bib28 article-title: Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)39801-0 – volume: 358 start-page: 247 year: 2007 ident: 10.1016/j.bbagen.2007.10.008_bib43 article-title: Lex glycan mediates homotypic adhesion of embryonal cells independently from E cadherin: a preliminary note publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2007.04.101 – volume: 25 start-page: 2367 year: 2006 ident: 10.1016/j.bbagen.2007.10.008_bib84 article-title: Tetraspanin KAI1/CD82 suppresses invasion by inhibiting integrin-dependent crosstalk with c-Met receptor and Src kinases publication-title: Oncogene doi: 10.1038/sj.onc.1209269 – volume: 56 start-page: 567 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib63 article-title: Ganglioside complexes as new target antigens in Guillain–Barre syndrome publication-title: Ann. Neurol. doi: 10.1002/ana.20222 – volume: 21 start-page: 149 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib41 article-title: Understanding carbohydrate–carbohydrate interactions by means of glyconanotechnology publication-title: Glycoconj. J. doi: 10.1023/B:GLYC.0000044846.80014.cb – volume: 240 start-page: 1 year: 1997 ident: 10.1016/j.bbagen.2007.10.008_bib6 article-title: Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.7575 – volume: 81 start-page: 189 year: 2005 ident: 10.1016/j.bbagen.2007.10.008_bib9 article-title: Organization and function of glycosphingolipids in membrane publication-title: Proc. Jpn. Acad., Ser. B Phys. Biol. Sci. doi: 10.2183/pjab.81.189 – start-page: 494 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib48 article-title: Synthesis and X-ray single crystal structure of a bivalent glycocluster publication-title: Chem. Commun. (Camb.) doi: 10.1039/B313934D – volume: 1775 start-page: 163 year: 2007 ident: 10.1016/j.bbagen.2007.10.008_bib68 article-title: Signalling via integrins: implications for cell survival and anticancer strategies publication-title: Biochim. Biophys. Acta – volume: 455 start-page: 433 year: 1976 ident: 10.1016/j.bbagen.2007.10.008_bib4 article-title: Molecular arrangements in sphingolipids: conformation and hydrogen bonding of ceramide and their implication on membrane stability and permeability publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2736(76)90316-3 – volume: 531 start-page: 88 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib7 article-title: Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy publication-title: FEBS Lett. doi: 10.1016/S0014-5793(02)03479-8 – volume: 254 start-page: 1016 year: 1991 ident: 10.1016/j.bbagen.2007.10.008_bib30 article-title: GPI-anchored cell-surface molecules complexed to protein tyrosine kinases publication-title: Science doi: 10.1126/science.1719635 – volume: 270 start-page: 5089 year: 1995 ident: 10.1016/j.bbagen.2007.10.008_bib53 article-title: Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate–carbohydrate-mediated cell aggregation of the marine sponge Microciona prolifera publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.10.5089 – volume: 40 start-page: 6414 year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib66 article-title: GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: co-expression of GM3 and CD9 is essential in down-regulation of tumor cell motility and malignancy publication-title: Biochemistry doi: 10.1021/bi0101998 – volume: 39 start-page: 3245 year: 2000 ident: 10.1016/j.bbagen.2007.10.008_bib40 article-title: Calcium-dependent carbohydrate–carbohydrate recognition between Lewis(X) blood group antigens publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/1521-3773(20000915)39:18<3245::AID-ANIE3245>3.0.CO;2-9 – volume: 14 start-page: 66 year: 2002 ident: 10.1016/j.bbagen.2007.10.008_bib31 article-title: Dynamics of the immunological synapse: finding, establishing and solidifying a connection publication-title: Curr. Opin. Immunol. doi: 10.1016/S0952-7915(01)00299-0 – start-page: 1 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib76 article-title: Jordi Folch-Pi. – volume: 275 start-page: 15174 year: 2000 ident: 10.1016/j.bbagen.2007.10.008_bib94 article-title: Reconstitution of membranes simulating “glycosignaling domain” and their susceptibility to lyso-GM3 publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.20.15174 – volume: 67 start-page: 199 year: 1998 ident: 10.1016/j.bbagen.2007.10.008_bib23 article-title: The caveolae membrane system publication-title: Ann. Rev. Biochem. doi: 10.1146/annurev.biochem.67.1.199 – volume: 276 start-page: 5375 year: 2001 ident: 10.1016/j.bbagen.2007.10.008_bib62 article-title: Glycosylation-induced conformational modification positively regulates receptor–receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DEGFR) expressed in cancer cells publication-title: J. Biol. Chem. doi: 10.1074/jbc.M005599200 – volume: 15 start-page: 1 year: 1977 ident: 10.1016/j.bbagen.2007.10.008_bib11 article-title: Long-range order in biomembranes publication-title: Adv. Lipid Res. doi: 10.1016/B978-0-12-024915-2.50007-4 – volume: 417 start-page: 221 year: 2006 ident: 10.1016/j.bbagen.2007.10.008_bib45 article-title: Analysis of carbohydrate–carbohydrate interactions using gold glyconanoparticles and oligosaccharide self-assembling monolayers publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(06)17016-0 – volume: 5 start-page: 483 year: 1986 ident: 10.1016/j.bbagen.2007.10.008_bib14 article-title: Two strains of the Madin–Darby canine kidney (MDCK) cell line have distinct glycosphingolipid compositions publication-title: EMBO J. doi: 10.1002/j.1460-2075.1986.tb04237.x – volume: 3 start-page: 213 year: 1987 ident: 10.1016/j.bbagen.2007.10.008_bib37 article-title: Cadherins: a molecular family essential for selective cell–cell adhesion and animal morphogenesis publication-title: Trends Genet. doi: 10.1016/0168-9525(87)90238-1 – volume: 426 start-page: 173 year: 2004 ident: 10.1016/j.bbagen.2007.10.008_bib44 article-title: Carbohydrate-to-carbohydrate interaction in basic cell biology: a brief overview publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2004.02.032 – volume: 80 start-page: 6274 year: 1983 ident: 10.1016/j.bbagen.2007.10.008_bib36 article-title: Uvomorulin: a nonintegral membrane protein of early mouse embryo publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.80.20.6274 – volume: 182 start-page: 212 year: 2007 ident: 10.1016/j.bbagen.2007.10.008_bib64 article-title: Anti-ganglioside complex antibodies associated with severe disability in GBS publication-title: J. Neuroimmunol. doi: 10.1016/j.jneuroim.2006.09.013 – volume: 387 start-page: 569 year: 1997 ident: 10.1016/j.bbagen.2007.10.008_bib27 article-title: Functional rafts in cell membranes publication-title: Nature doi: 10.1038/42408 |
SSID | ssj0000595 ssj0025309 |
Score | 2.4308765 |
SecondaryResourceType | review_article |
Snippet | At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids,
N- or
O-linked oligosaccharides, are recognized by carbohydrate-binding... At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N- or O-linked oligosaccharides, are recognized by carbohydrate-binding... At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N - or O -linked oligosaccharides, are recognized by... |
SourceID | pubmedcentral proquest pubmed crossref elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 421 |
SubjectTerms | Animals Caveolae - metabolism Cell Adhesion Cell Movement Cell Proliferation Ganglioside Gangliosides - chemistry Gangliosides - metabolism Glycosphingolipids microdomain Glycosylation Glycosynapse Humans Integrin Membrane Microdomains - metabolism Tetraspanin |
Title | Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains |
URI | https://dx.doi.org/10.1016/j.bbagen.2007.10.008 https://www.ncbi.nlm.nih.gov/pubmed/17991443 https://www.proquest.com/docview/70400217 https://pubmed.ncbi.nlm.nih.gov/PMC2312458 |
Volume | 1780 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaqIgQXBOW1PIoPHDds4thxcqxWrBZW9ABU9BY5ttNNtXVWZHvYS39BfzQzsdOyIFSJUyTHTqzMeObz5PMMIe_rHPy2TnRUMNibcB2nURHbIoqtsUZkleAVxju-HGfzE_75VJzukelwFgZplcH2e5veW-vQMglfc7Jumsk3_KkHcAIATZ-oqz_BziVq-YerW5oHwAfh_yTwCHsPx-d6jldVwaJ1PpFhz_HK_-We_oaff7Iof3NLs8fkUcCT9MhP-QnZs-6A3PcVJrcH5MF0KOj2lFzPwIf50B9FUiFta3q22uq2W2MYql0168Z0VDlDzxSe7m2xlGdHG0cDoR1HYKSfKrO0GGYbU-TyIZIf-3Gwqd8sxzRU_wmP3zoFhknTCyT_mfZCNa57Rk5mH79P51EoxhBpweQmApkpAEdVIazhIskrq_JYsZplMjaxNkwrG8e2rlSeKmHzTNeJSlmS6QoQRxKnz8m-a519SWjBapHJhKskY1zpJK9FUYPllcza1Fg9Iukgg1KHTOVYMGNVDpS089JLDotoSmwFyY1IdDNq7TN13NFfDuItdzSuBGdyx8h3gzaUIEL87srZ9rIrJZpE2OSNyAuvG7czkQDEOU_hrTtac9MB03zv3nHNsk_3DQiccZG_-u_5viYPPcsFmXNvyP7m56V9C1BqUx32a-WQ3Dv6tJgf43Xx9cfiF-nqI_k |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaqIlQuFZTXQqE-cNywjmPncUSrrhZoe6GVeosc2-kGbZ1Vsz3shV_Aj2YmdloWhCpxTTyJ5bFnPo8_zxDyoc7Bb-tYRwWHvYnQLIkKZouIWWONTCspKox3nJ6l8wvx5VJe7pDpcBcGaZXB9nub3lvr8GQSRnOyaprJNzzUAzgBgKZP1AVboEcCli-WMfj4457nAfhB-qMEEWHz4f5cT_KqKli1zmcy7Ele-b_809_4808a5W9-afaU7AdAST_5Pj8jO9YdkMe-xOTmgOxNh4puz8nPGTgxH_ujyCqkbU2vlhvddiuMQ7XLZtWYjipn6JXC670t1vLsaONoYLSjBIb6qTILi3G2MUUyH0L5sZeDXf16Maah_E_4_MYpsEyaXiP7z7TXqnHdC3IxOz6fzqNQjSHSkmfrCJSmAB1VhbRGyDivrMqZ4jVPM2aYNlwry5itK5UnSto81XWsEh6nugLIEbPkJdl1rbOvCS14LdMsFipOuVA6zmtZ1GB6M25tYqwekWTQQalDqnKsmLEsB07a99JrDqtoZvgUNDci0Z3UyqfqeKB9Nqi33JpyJXiTBySPhtlQggpx3JWz7W1XZmgTYZc3Iq_83LjvSQZIXIgE_ro1a-4aYJ7v7TeuWfT5vgGCcyHzN__d3yOyNz8_PSlPPp99fUueeMoL0ugOye765ta-A1y1rt736-YXNq8j5A |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Functional+role+of+glycosphingolipids+and+gangliosides+in+control+of+cell+adhesion%2C+motility%2C+and+growth%2C+through+glycosynaptic+microdomains&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Regina+Todeschini%2C+Adriane&rft.au=Hakomori%2C+Sen-itiroh&rft.date=2008-03-01&rft.issn=0304-4165&rft.volume=1780&rft.issue=3&rft.spage=421&rft.epage=433&rft_id=info:doi/10.1016%2Fj.bbagen.2007.10.008&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_bbagen_2007_10_008 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon |