Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1

Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (P...

Full description

Saved in:

Bibliographic Details
Published in	Cancer cell Vol. 33; no. 2; pp. 187 - 201.e10
Main Authors	Li, Chia-Wei, Lim, Seung-Oe, Chung, Ezra M., Kim, Yong-Soo, Park, Andrew H., Yao, Jun, Cha, Jong-Ho, Xia, Weiya, Chan, Li-Chuan, Kim, Taewan, Chang, Shih-Shin, Lee, Heng-Huan, Chou, Chao-Kai, Liu, Yen-Liang, Yeh, Hsin-Chih, Perillo, Evan P., Dunn, Andrew K., Kuo, Chu-Wei, Khoo, Kay-Hooi, Hsu, Jennifer L., Wu, Yun, Hsu, Jung-Mao, Yamaguchi, Hirohito, Huang, Tzu-Hsuan, Sahin, Aysegul A., Hortobagyi, Gabriel N., Yoo, Stephen S., Hung, Mien-Chie
Format	Journal Article
Language	English
Published	United States Elsevier Inc 12.02.2018
Subjects	Animals Antibodies, Monoclonal - pharmacology antibody-drug conjugate B3GNT3 Cell Line, Tumor Female glycosylation Humans immune checkpoint blockade immunosuppression immunotherapy Lymphocytes, Tumor-Infiltrating - drug effects Lymphocytes, Tumor-Infiltrating - immunology Mice, Inbred BALB C N-Acetylglucosaminyltransferases - drug effects N-Acetylglucosaminyltransferases - metabolism PD-1 PD-L1 Programmed Cell Death 1 Receptor - immunology receptor internalization TNBC Triple Negative Breast Neoplasms - drug therapy Triple Negative Breast Neoplasms - immunology Triple Negative Breast Neoplasms - metabolism antibody-drug conjugate receptor internalization immunotherapy PD-L1 B3GNT3 glycosylation immunosuppression TNBC PD-1 immune checkpoint blockade
Online Access	Get full text

Cover

Loading…

Abstract	Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy. •N-linked glycosylation is required for physical contact between PD-L1 and PD-1•EGF/EGFR stimulates PD-L1 glycosylation via B3GNT3 glycosyltransferase•Glycosylated-PD-L1 antibody induces PD-L1 internalization•Glycosylated-PD-L1-ADC possesses potent toxicity as well as bystander effects Li et al. show that glycosylation of PD-L1 is essential for PD-L1/PD-1 interaction and immunosuppression in triple-negative breast cancer (TNBC). They generate a glycosylation-specific antibody that induces PD-L1 internalization and an antibody-drug conjugate with potent anti-tumor activities in TNBC models.
AbstractList	Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy. Protein glycosylation provides proteomic diversity in regulating protein localization, stability and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed EGF induces PD-L1 and receptor programmed cell death protein-1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces potent cell-killing effect as well as bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy. Li et al. show that glycosylation of PD-L1 is essential for PD-L1/PD-1 interaction and immunosuppression in triple-negative breast cancer (TNBC). They generate a glycosylation-specific antibody that induces PD-L1 internalization and an antibody-drug conjugate with potent anti-tumor activities in TNBC models. Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy.Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy. Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy. •N-linked glycosylation is required for physical contact between PD-L1 and PD-1•EGF/EGFR stimulates PD-L1 glycosylation via B3GNT3 glycosyltransferase•Glycosylated-PD-L1 antibody induces PD-L1 internalization•Glycosylated-PD-L1-ADC possesses potent toxicity as well as bystander effects Li et al. show that glycosylation of PD-L1 is essential for PD-L1/PD-1 interaction and immunosuppression in triple-negative breast cancer (TNBC). They generate a glycosylation-specific antibody that induces PD-L1 internalization and an antibody-drug conjugate with potent anti-tumor activities in TNBC models.
Author	Lim, Seung-Oe Perillo, Evan P. Khoo, Kay-Hooi Hung, Mien-Chie Chan, Li-Chuan Yeh, Hsin-Chih Hortobagyi, Gabriel N. Hsu, Jung-Mao Dunn, Andrew K. Sahin, Aysegul A. Li, Chia-Wei Park, Andrew H. Kim, Taewan Kuo, Chu-Wei Xia, Weiya Chou, Chao-Kai Liu, Yen-Liang Cha, Jong-Ho Chung, Ezra M. Wu, Yun Yamaguchi, Hirohito Yao, Jun Chang, Shih-Shin Kim, Yong-Soo Lee, Heng-Huan Hsu, Jennifer L. Huang, Tzu-Hsuan Yoo, Stephen S.
AuthorAffiliation	7 Core Facilities for Protein Structural Analysis, Academia Sinica, Taipei 115, Taiwan 6 Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA 3 Breast Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA 4 Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 151-742, Korea 11 STCube Pharmaceuticals, Inc., 401 Professional Dr. Suite 250, Gaithersburg, MD 20879, USA 1 Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA 2 Department of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA 10 Department of Biotechnology, Asia University, Taichung 413, Taiwan 12 Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA 9 Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical Univers
AuthorAffiliation_xml	– name: 2 Department of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA – name: 4 Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 151-742, Korea – name: 9 Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical University, Taichung 404, Taiwan – name: 12 Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA – name: 10 Department of Biotechnology, Asia University, Taichung 413, Taiwan – name: 5 Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA – name: 3 Breast Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA – name: 11 STCube Pharmaceuticals, Inc., 401 Professional Dr. Suite 250, Gaithersburg, MD 20879, USA – name: 7 Core Facilities for Protein Structural Analysis, Academia Sinica, Taipei 115, Taiwan – name: 6 Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA – name: 8 Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan – name: 1 Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA
Author_xml	– sequence: 1 givenname: Chia-Wei surname: Li fullname: Li, Chia-Wei organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 2 givenname: Seung-Oe surname: Lim fullname: Lim, Seung-Oe organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 3 givenname: Ezra M. surname: Chung fullname: Chung, Ezra M. organization: STCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA – sequence: 4 givenname: Yong-Soo surname: Kim fullname: Kim, Yong-Soo organization: STCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA – sequence: 5 givenname: Andrew H. surname: Park fullname: Park, Andrew H. organization: STCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA – sequence: 6 givenname: Jun surname: Yao fullname: Yao, Jun organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 7 givenname: Jong-Ho surname: Cha fullname: Cha, Jong-Ho organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 8 givenname: Weiya surname: Xia fullname: Xia, Weiya organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 9 givenname: Li-Chuan surname: Chan fullname: Chan, Li-Chuan organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 10 givenname: Taewan surname: Kim fullname: Kim, Taewan organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 11 givenname: Shih-Shin surname: Chang fullname: Chang, Shih-Shin organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 12 givenname: Heng-Huan surname: Lee fullname: Lee, Heng-Huan organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 13 givenname: Chao-Kai surname: Chou fullname: Chou, Chao-Kai organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 14 givenname: Yen-Liang surname: Liu fullname: Liu, Yen-Liang organization: Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 15 givenname: Hsin-Chih surname: Yeh fullname: Yeh, Hsin-Chih organization: Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 16 givenname: Evan P. surname: Perillo fullname: Perillo, Evan P. organization: Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 17 givenname: Andrew K. surname: Dunn fullname: Dunn, Andrew K. organization: Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 18 givenname: Chu-Wei surname: Kuo fullname: Kuo, Chu-Wei organization: Core Facilities for Protein Structural Analysis, Academia Sinica, Taipei 115, Taiwan – sequence: 19 givenname: Kay-Hooi surname: Khoo fullname: Khoo, Kay-Hooi organization: Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan – sequence: 20 givenname: Jennifer L. surname: Hsu fullname: Hsu, Jennifer L. organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 21 givenname: Yun surname: Wu fullname: Wu, Yun organization: Department of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA – sequence: 22 givenname: Jung-Mao surname: Hsu fullname: Hsu, Jung-Mao organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 23 givenname: Hirohito surname: Yamaguchi fullname: Yamaguchi, Hirohito organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 24 givenname: Tzu-Hsuan surname: Huang fullname: Huang, Tzu-Hsuan organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA – sequence: 25 givenname: Aysegul A. surname: Sahin fullname: Sahin, Aysegul A. organization: Department of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA – sequence: 26 givenname: Gabriel N. surname: Hortobagyi fullname: Hortobagyi, Gabriel N. organization: Department of Breast Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA – sequence: 27 givenname: Stephen S. surname: Yoo fullname: Yoo, Stephen S. organization: STCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA – sequence: 28 givenname: Mien-Chie surname: Hung fullname: Hung, Mien-Chie email: mhung@mdanderson.org organization: Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/29438695$$D View this record in MEDLINE/PubMed
BookMark	eNp9kV-LEzEUxYOsuH_0EwiSR19mvEmazORBwa3rKhQVqc8hk7lTU6aTmqSFfnvT7a6oD_uUS-79nQPnXJKzKUxIyEsGNQOm3qxr53Acaw6srYHVAPoJuWBt01ZCteqszFLISjFoz8llSmsoFGv0M3LO9Uy0SssL8v0m2t47m32YaBjoMvrtiNUXXJWvPdLriDZlOreTw0jnxS_R7kCXNq4w-2lFb8eDC-kw2ow9_fahWrDn5Olgx4Qv7t8r8uPjzXL-qVp8vf08f7-onOQyV4j9ALpTHBonnFPCyg6sRo7A2zLLobeN7gc1413jlBxchzM2NNhYyaADcUXenXS3u26DvcMpRzuabfQbGw8mWG_-3Uz-p1mFvZEtnzXiKPD6XiCGXztM2Wx8OkZqJwy7ZDgA50yAVuX01d9ef0wegiwH-nTgYkgp4mCcz3epFms_GgbmWJpZm7vSzLE0A8yU0gor_mMf5B-n3p4oLBnvPUaTnMdSU-8jumz64B_lfwOt37K4
CitedBy_id	crossref_primary_10_1002_mc_23176 crossref_primary_10_3389_fimmu_2022_1088560 crossref_primary_10_1007_s13402_022_00736_y crossref_primary_10_3389_fmolb_2025_1529507 crossref_primary_10_3390_curroncol30010016 crossref_primary_10_1038_s41571_022_00601_9 crossref_primary_10_1158_0008_5472_CAN_18_1892 crossref_primary_10_1002_mc_23170 crossref_primary_10_1186_s13578_022_00756_z crossref_primary_10_1016_j_imlet_2020_11_003 crossref_primary_10_1039_D2RA02903K crossref_primary_10_1016_j_immuni_2018_03_014 crossref_primary_10_3389_fonc_2021_703681 crossref_primary_10_1186_s13578_023_01137_w crossref_primary_10_1002_path_5280 crossref_primary_10_1080_07391102_2023_2263569 crossref_primary_10_1007_s10238_023_01274_z crossref_primary_10_1016_j_apsb_2024_01_009 crossref_primary_10_1038_s41388_019_0700_2 crossref_primary_10_1016_j_bios_2022_114179 crossref_primary_10_1038_s41423_023_01019_8 crossref_primary_10_1136_jitc_2020_002258 crossref_primary_10_3390_cancers14092128 crossref_primary_10_1038_s42003_022_03845_4 crossref_primary_10_1016_j_it_2021_09_002 crossref_primary_10_3390_cancers17061001 crossref_primary_10_1016_j_biopha_2020_110621 crossref_primary_10_1073_pnas_2114851119 crossref_primary_10_3389_fimmu_2024_1434078 crossref_primary_10_1038_s41388_020_01592_6 crossref_primary_10_1186_s13046_020_01767_9 crossref_primary_10_3389_fonc_2021_747012 crossref_primary_10_3389_fonc_2022_815437 crossref_primary_10_1021_acs_analchem_1c03287 crossref_primary_10_3389_fimmu_2019_02928 crossref_primary_10_1101_cshperspect_a036863 crossref_primary_10_1038_s41421_022_00507_x crossref_primary_10_1186_s12929_020_00670_x crossref_primary_10_1016_j_ymthe_2022_07_006 crossref_primary_10_1172_JCI160456 crossref_primary_10_2147_BCTT_S444077 crossref_primary_10_1038_s41368_024_00289_w crossref_primary_10_1158_2767_9764_CRC_22_0468 crossref_primary_10_1002_ange_202414327 crossref_primary_10_3390_cancers13133330 crossref_primary_10_3390_cells10040872 crossref_primary_10_1038_s41589_020_0622_x crossref_primary_10_1021_acs_analchem_1c04148 crossref_primary_10_1126_sciadv_adp4917 crossref_primary_10_3390_cancers14235936 crossref_primary_10_3390_biomedicines10081805 crossref_primary_10_1016_j_pan_2021_01_023 crossref_primary_10_1016_j_compbiolchem_2020_107362 crossref_primary_10_1039_D3MD00636K crossref_primary_10_1016_j_ejcb_2021_151186 crossref_primary_10_1126_sciadv_abj9513 crossref_primary_10_1038_s41467_021_24703_7 crossref_primary_10_1002_1878_0261_12664 crossref_primary_10_1016_j_bbcan_2025_189274 crossref_primary_10_1177_15330338211019442 crossref_primary_10_1186_s12964_020_00612_y crossref_primary_10_3389_fphar_2019_00373 crossref_primary_10_1007_s12094_021_02613_w crossref_primary_10_1016_j_molcel_2018_10_034 crossref_primary_10_1038_s41551_019_0375_6 crossref_primary_10_1136_jitc_2020_001377 crossref_primary_10_3390_jpm13030529 crossref_primary_10_1186_s13045_024_01532_x crossref_primary_10_3390_cancers13184509 crossref_primary_10_1021_acs_biochem_4c00418 crossref_primary_10_1016_j_advnut_2024_100240 crossref_primary_10_3389_fonc_2021_650853 crossref_primary_10_1007_s12032_023_02183_7 crossref_primary_10_3389_fonc_2024_1415820 crossref_primary_10_1016_j_modpat_2023_100159 crossref_primary_10_3390_cells10051100 crossref_primary_10_1016_j_semcancer_2021_04_002 crossref_primary_10_1124_pharmrev_121_000499 crossref_primary_10_31857_S0132342324060136 crossref_primary_10_1111_sji_13205 crossref_primary_10_3390_ph15121451 crossref_primary_10_1007_s11684_019_0679_7 crossref_primary_10_1136_jitc_2023_007529 crossref_primary_10_1515_cclm_2018_0379 crossref_primary_10_3389_fonc_2023_1214413 crossref_primary_10_1126_scitranslmed_aav4810 crossref_primary_10_1007_s13258_023_01428_z crossref_primary_10_1016_j_mattod_2021_08_002 crossref_primary_10_1038_s41467_024_48597_3 crossref_primary_10_1158_0008_5472_CAN_19_3133 crossref_primary_10_1007_s11684_022_0964_8 crossref_primary_10_3390_jcm8122168 crossref_primary_10_1126_sciadv_ade4186 crossref_primary_10_1186_s12943_025_02277_y crossref_primary_10_1002_smll_202302834 crossref_primary_10_1038_s41392_023_01365_z crossref_primary_10_1186_s40364_024_00633_6 crossref_primary_10_1016_j_hbpd_2022_08_002 crossref_primary_10_1186_s13046_022_02375_5 crossref_primary_10_1007_s10549_025_07659_w crossref_primary_10_1038_s41418_024_01432_0 crossref_primary_10_1016_j_phrs_2019_104258 crossref_primary_10_3389_fimmu_2022_752065 crossref_primary_10_1097_COC_0000000000000950 crossref_primary_10_1186_s12964_021_00816_w crossref_primary_10_1158_1078_0432_CCR_20_0778 crossref_primary_10_1016_j_biomaterials_2023_122392 crossref_primary_10_1016_j_ijpharm_2024_124685 crossref_primary_10_1111_1440_1681_13056 crossref_primary_10_2147_CMAR_S236565 crossref_primary_10_1016_j_copbio_2021_12_008 crossref_primary_10_1016_j_jid_2021_03_030 crossref_primary_10_1016_j_jconrel_2025_113614 crossref_primary_10_1136_jitc_2020_001222 crossref_primary_10_3724_abbs_2024107 crossref_primary_10_1002_advs_202409764 crossref_primary_10_1016_j_heliyon_2024_e25895 crossref_primary_10_1021_acs_jmedchem_0c01957 crossref_primary_10_1038_s41571_023_00850_2 crossref_primary_10_3389_fimmu_2018_02485 crossref_primary_10_18632_aging_102646 crossref_primary_10_1186_s40164_025_00627_6 crossref_primary_10_1016_j_gendis_2022_07_024 crossref_primary_10_1186_s12951_025_03171_x crossref_primary_10_1038_s41467_021_25473_y crossref_primary_10_1002_anie_202414327 crossref_primary_10_1016_j_isci_2024_109946 crossref_primary_10_1093_glycob_cwy069 crossref_primary_10_14789_jmj_JMJ22_0039_OA crossref_primary_10_3389_fimmu_2023_1230135 crossref_primary_10_1080_21691401_2019_1703731 crossref_primary_10_3389_fchem_2019_00833 crossref_primary_10_3389_fphar_2018_00536 crossref_primary_10_1039_D4CB00247D crossref_primary_10_3724_abbs_2024085 crossref_primary_10_1007_s00432_023_05345_2 crossref_primary_10_1016_j_canlet_2023_216498 crossref_primary_10_1038_s41467_023_42883_2 crossref_primary_10_1007_s11033_023_08868_6 crossref_primary_10_3389_fimmu_2023_1255667 crossref_primary_10_3390_cancers11121910 crossref_primary_10_1038_s41467_021_24769_3 crossref_primary_10_1002_jmv_28478 crossref_primary_10_1186_s40164_024_00515_5 crossref_primary_10_1016_j_ccell_2019_06_008 crossref_primary_10_1016_j_intimp_2022_108897 crossref_primary_10_1096_fj_201800664RR crossref_primary_10_1016_j_ccell_2019_06_006 crossref_primary_10_1007_s12072_023_10572_3 crossref_primary_10_1016_j_ijbiomac_2023_127911 crossref_primary_10_1186_s13045_022_01242_2 crossref_primary_10_1002_ijc_32410 crossref_primary_10_1021_acs_analchem_4c00330 crossref_primary_10_2217_fon_2021_1110 crossref_primary_10_1016_j_apsb_2020_11_005 crossref_primary_10_1172_jci_insight_146945 crossref_primary_10_1177_1535370218820287 crossref_primary_10_1158_2326_6066_CIR_20_0203 crossref_primary_10_1007_s11427_020_1714_8 crossref_primary_10_1016_j_jphotobiol_2021_112355 crossref_primary_10_18632_aging_202255 crossref_primary_10_3389_fimmu_2023_1229397 crossref_primary_10_1080_14789450_2019_1645604 crossref_primary_10_1186_s12943_024_02176_8 crossref_primary_10_3390_nu13051718 crossref_primary_10_1002_cam4_6776 crossref_primary_10_1038_s41392_022_01046_3 crossref_primary_10_1016_j_chembiol_2023_07_004 crossref_primary_10_1016_j_oraloncology_2023_106562 crossref_primary_10_3389_fimmu_2019_01337 crossref_primary_10_1038_s41467_021_25331_x crossref_primary_10_1002_ctm2_872 crossref_primary_10_1021_acscatal_1c03919 crossref_primary_10_1021_acs_jmedchem_4c00102 crossref_primary_10_1146_annurev_anchem_091922_073057 crossref_primary_10_1016_j_apsb_2024_12_036 crossref_primary_10_1002_mas_21790 crossref_primary_10_1016_j_ymthe_2023_07_021 crossref_primary_10_1002_ange_201916039 crossref_primary_10_3390_cancers14081854 crossref_primary_10_3390_cancers13174426 crossref_primary_10_1016_j_mam_2022_101097 crossref_primary_10_1016_j_molstruc_2022_132455 crossref_primary_10_1016_j_ccell_2024_11_008 crossref_primary_10_1093_glycob_cwy023 crossref_primary_10_1186_s12967_023_04135_1 crossref_primary_10_1016_j_phrs_2020_104738 crossref_primary_10_3389_fimmu_2018_02754 crossref_primary_10_1016_j_isci_2019_03_017 crossref_primary_10_1002_ctm2_803 crossref_primary_10_1038_s41422_020_0343_4 crossref_primary_10_1016_j_biopha_2023_116078 crossref_primary_10_1007_s00262_024_03774_7 crossref_primary_10_1111_cas_14549 crossref_primary_10_1186_s12967_020_02522_6 crossref_primary_10_1007_s10555_024_10213_7 crossref_primary_10_1016_j_aca_2020_06_060 crossref_primary_10_1038_s41467_024_49156_6 crossref_primary_10_1097_BS9_0000000000000149 crossref_primary_10_1158_0008_5472_CAN_23_2664 crossref_primary_10_1016_j_celrep_2024_113937 crossref_primary_10_1136_jitc_2021_002443 crossref_primary_10_1007_s12094_024_03396_6 crossref_primary_10_1155_2022_3665617 crossref_primary_10_1186_s13046_022_02273_w crossref_primary_10_3390_ijms222413571 crossref_primary_10_1172_JCI181314 crossref_primary_10_1016_j_yexcr_2019_03_025 crossref_primary_10_3390_cells13050395 crossref_primary_10_1007_s00216_021_03659_z crossref_primary_10_1021_acsomega_3c01547 crossref_primary_10_1007_s11684_018_0657_5 crossref_primary_10_1093_glycob_cwad005 crossref_primary_10_1111_1759_7714_13450 crossref_primary_10_1158_2326_6066_CIR_22_0953 crossref_primary_10_1126_scitranslmed_ade5855 crossref_primary_10_1016_j_lfs_2020_118297 crossref_primary_10_1016_j_tibs_2018_09_004 crossref_primary_10_1088_1748_605X_ab9f57 crossref_primary_10_1111_bph_16054 crossref_primary_10_1136_jitc_2021_002699 crossref_primary_10_3389_fimmu_2022_1021452 crossref_primary_10_1038_s41392_024_01886_1 crossref_primary_10_1051_medsci_2020099 crossref_primary_10_1021_jacs_0c10008 crossref_primary_10_1016_j_microc_2023_109005 crossref_primary_10_1186_s12943_024_02023_w crossref_primary_10_1016_j_modpat_2023_100220 crossref_primary_10_1126_scitranslmed_abg3072 crossref_primary_10_3390_ijms21197139 crossref_primary_10_2147_CCID_S404381 crossref_primary_10_1080_2162402X_2019_1624128 crossref_primary_10_1111_imm_13494 crossref_primary_10_1166_jbn_2022_3296 crossref_primary_10_3390_cancers14246258 crossref_primary_10_1158_2326_6066_CIR_18_0910 crossref_primary_10_1007_s11904_019_00433_w crossref_primary_10_3389_fimmu_2022_880769 crossref_primary_10_1186_s12964_021_00769_0 crossref_primary_10_1186_s12929_022_00855_6 crossref_primary_10_3390_ijms25052939 crossref_primary_10_1016_j_jhydrol_2024_132358 crossref_primary_10_1177_15353702211049220 crossref_primary_10_1186_s13046_021_02055_w crossref_primary_10_1016_j_bcp_2023_115984 crossref_primary_10_1039_D1LC00443C crossref_primary_10_3390_cells12192338 crossref_primary_10_1016_j_phrs_2021_105576 crossref_primary_10_1016_j_ejmech_2024_116267 crossref_primary_10_3389_fendo_2023_1216193 crossref_primary_10_1021_acs_analchem_1c00693 crossref_primary_10_5812_ijpr_123909 crossref_primary_10_1016_j_cca_2019_12_015 crossref_primary_10_1631_jzus_B2200195 crossref_primary_10_1016_j_biopha_2022_113906 crossref_primary_10_1089_dna_2019_5089 crossref_primary_10_1016_j_canlet_2023_216318 crossref_primary_10_1038_s41467_020_18828_4 crossref_primary_10_3390_biomedicines10123265 crossref_primary_10_1080_26895293_2022_2049901 crossref_primary_10_1038_s42003_019_0642_9 crossref_primary_10_1186_s12964_022_00981_6 crossref_primary_10_3390_ijms24098193 crossref_primary_10_1186_s12967_024_05502_2 crossref_primary_10_1080_17568919_2024_2366146 crossref_primary_10_1016_j_lfs_2020_117923 crossref_primary_10_3390_ijms20236074 crossref_primary_10_1111_imm_13573 crossref_primary_10_1016_j_csbj_2021_12_020 crossref_primary_10_1007_s00018_022_04431_x crossref_primary_10_1073_pnas_2007297117 crossref_primary_10_1007_s13402_023_00770_4 crossref_primary_10_3390_cancers17030498 crossref_primary_10_1186_s13046_022_02523_x crossref_primary_10_1002_med_21774 crossref_primary_10_1021_acsami_9b18730 crossref_primary_10_1021_acs_jmedchem_0c01262 crossref_primary_10_1038_s41401_020_0366_x crossref_primary_10_1073_pnas_2310866121 crossref_primary_10_1158_1078_0432_CCR_20_3364 crossref_primary_10_1186_s12885_024_12712_w crossref_primary_10_3389_fonc_2022_856712 crossref_primary_10_1039_D1SC05894K crossref_primary_10_1007_s11033_024_09405_9 crossref_primary_10_1172_JCI126022 crossref_primary_10_12677_acm_2024_1441312 crossref_primary_10_1080_08916934_2023_2289362 crossref_primary_10_1016_j_bcp_2022_115113 crossref_primary_10_1038_s41587_024_02494_8 crossref_primary_10_1016_j_phrs_2021_106019 crossref_primary_10_3389_fonc_2021_716246 crossref_primary_10_1186_s13018_024_05223_8 crossref_primary_10_1038_s41565_021_00972_7 crossref_primary_10_1155_2021_6668573 crossref_primary_10_1158_1535_7163_MCT_23_0449 crossref_primary_10_3389_fimmu_2022_830158 crossref_primary_10_1016_j_jnutbio_2022_109186 crossref_primary_10_1039_D2CS00446A crossref_primary_10_1038_s41467_024_46557_5 crossref_primary_10_1159_000518664 crossref_primary_10_1097_JBR_0000000000000025 crossref_primary_10_2174_1389203719666180928105632 crossref_primary_10_1038_s41467_024_45215_0 crossref_primary_10_1016_j_bbrc_2021_05_034 crossref_primary_10_1016_j_molcel_2019_09_030 crossref_primary_10_1186_s13046_023_02711_3 crossref_primary_10_3389_fphar_2022_972046 crossref_primary_10_1186_s12935_022_02805_6 crossref_primary_10_1172_JCI139434 crossref_primary_10_1016_j_pharmthera_2019_02_006 crossref_primary_10_2147_JHC_S417407 crossref_primary_10_1016_j_tranon_2023_101851 crossref_primary_10_1158_2159_8290_CD_20_0402 crossref_primary_10_1016_j_heliyon_2024_e27624 crossref_primary_10_1080_07853890_2021_1937694 crossref_primary_10_3390_ijms26031238 crossref_primary_10_1002_rcm_9838 crossref_primary_10_1038_s41420_024_02027_x crossref_primary_10_3389_fonc_2020_568059 crossref_primary_10_1016_j_compbiomed_2025_109980 crossref_primary_10_1016_j_intimp_2023_111321 crossref_primary_10_1002_mco2_70062 crossref_primary_10_1016_j_ccell_2018_01_015 crossref_primary_10_1016_j_fsi_2019_01_016 crossref_primary_10_1186_s12929_021_00746_2 crossref_primary_10_1038_s41368_024_00311_1 crossref_primary_10_18632_aging_103753 crossref_primary_10_1155_2020_5497015 crossref_primary_10_1016_j_athoracsur_2018_08_056 crossref_primary_10_3390_biomedicines12071446 crossref_primary_10_3389_fmolb_2022_816102 crossref_primary_10_1002_adhm_202401649 crossref_primary_10_1021_acsnano_0c05392 crossref_primary_10_1016_j_jbc_2022_101817 crossref_primary_10_1038_s41568_020_00322_0 crossref_primary_10_1097_MD_0000000000031307 crossref_primary_10_1039_D2SC01672A crossref_primary_10_1002_anie_201916039 crossref_primary_10_1016_j_tranon_2020_101003 crossref_primary_10_1186_s12943_018_0928_4 crossref_primary_10_1016_j_celrep_2019_12_036 crossref_primary_10_1016_j_heliyon_2024_e28600 crossref_primary_10_1016_j_canlet_2025_217453 crossref_primary_10_3389_fimmu_2024_1405485 crossref_primary_10_3389_fonc_2021_731535 crossref_primary_10_1016_j_ijbiomac_2023_123855 crossref_primary_10_3390_biomedicines9111702 crossref_primary_10_1080_2162402X_2020_1831153 crossref_primary_10_1016_j_intimp_2019_106012 crossref_primary_10_1002_pmic_201800278 crossref_primary_10_3389_fonc_2019_01459 crossref_primary_10_1016_j_ymthe_2023_04_011 crossref_primary_10_1038_s41467_018_04313_6 crossref_primary_10_1038_s41467_021_22618_x crossref_primary_10_1158_0008_5472_CAN_19_2314 crossref_primary_10_1158_0008_5472_CAN_19_1108 crossref_primary_10_1016_j_canlet_2018_10_042 crossref_primary_10_1016_j_semcancer_2019_11_011 crossref_primary_10_1016_j_gendis_2022_11_003 crossref_primary_10_1038_s41467_024_51242_8 crossref_primary_10_1080_21645515_2020_1730658 crossref_primary_10_1016_j_jconrel_2022_01_004 crossref_primary_10_1016_j_jid_2021_05_004 crossref_primary_10_3390_medicines10020015 crossref_primary_10_1084_jem_20211505 crossref_primary_10_1371_journal_ppat_1011219 crossref_primary_10_1002_1878_0261_13699 crossref_primary_10_1021_acs_jproteome_0c00521 crossref_primary_10_1038_s41417_023_00693_0 crossref_primary_10_1016_j_archoralbio_2021_105085 crossref_primary_10_1134_S1068162024060311 crossref_primary_10_3389_fimmu_2023_1145682 crossref_primary_10_1186_s40364_022_00396_y crossref_primary_10_1042_BST20200763 crossref_primary_10_1073_pnas_2303400120 crossref_primary_10_1007_s00299_025_03475_0 crossref_primary_10_3389_fgene_2021_755245 crossref_primary_10_3390_pharmaceutics13020287 crossref_primary_10_1038_s41389_024_00532_3 crossref_primary_10_3390_cancers16061237 crossref_primary_10_1002_advs_202303175 crossref_primary_10_1097_MD_0000000000038146 crossref_primary_10_1007_s00262_021_03097_x crossref_primary_10_3390_cancers11101598 crossref_primary_10_1186_s12943_021_01447_y crossref_primary_10_1038_s41589_018_0161_x crossref_primary_10_1016_j_ejso_2018_04_001 crossref_primary_10_1016_j_ymthe_2024_12_044 crossref_primary_10_1016_j_lfs_2023_121781 crossref_primary_10_1038_s41388_018_0303_3 crossref_primary_10_2174_1389201023666211230113658 crossref_primary_10_3389_fimmu_2023_1154146 crossref_primary_10_3390_cancers14051343 crossref_primary_10_1002_ctm2_70161 crossref_primary_10_1002_cpz1_944 crossref_primary_10_1126_sciadv_abd2712 crossref_primary_10_1039_D1CC00168J crossref_primary_10_1016_j_canlet_2025_217498 crossref_primary_10_1038_s41392_021_00825_8 crossref_primary_10_3389_fimmu_2023_1029438 crossref_primary_10_1038_s41419_020_03140_2
Cites_doi	10.1038/nm730 10.1016/S0092-8674(01)00394-4 10.1158/1078-0432.CCR-09-2069 10.1038/nrc3239 10.1093/glycob/cwg090 10.1073/pnas.1608069113 10.1038/nbt.1480 10.1200/JCO.2015.64.8931 10.1001/jamaoncol.2015.3638 10.1200/JCO.2009.26.7609 10.1158/1538-7445.AM2017-2986 10.1200/JCO.2017.35.15_suppl.1008 10.1042/BST0361472 10.1111/cas.12294 10.1158/0008-5472.CAN-11-3123 10.1016/j.ccell.2015.12.008 10.1016/j.cell.2014.01.043 10.1038/70932 10.1016/j.sbi.2011.08.005 10.1016/j.ymeth.2006.10.002 10.1016/j.ccell.2016.10.010 10.1073/pnas.0703394104 10.1091/mbc.11.3.819 10.1038/srep00680 10.1084/jem.182.2.459 10.1038/nm863 10.1093/annonc/mdw424 10.1158/1538-7445.SABCS15-S1-04 10.1038/ncomms12632 10.1158/1078-0432.CCR-12-2063 10.1074/jbc.M004800200 10.1016/j.cell.2016.08.069 10.1056/NEJMoa1604958 10.1016/j.bbrc.2009.11.098 10.1016/S0140-6736(16)00561-4 10.1038/nri2326 10.1182/blood-2006-10-051482 10.1172/JCI80011 10.1074/jbc.273.1.58 10.1038/ncomms8874 10.1073/pnas.1402041111
ContentType	Journal Article
Copyright	2018 Published by Elsevier Inc.
Copyright_xml	– notice: 2018 – notice: Published by Elsevier Inc.
DBID	6I. AAFTH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM
DOI	10.1016/j.ccell.2018.01.009
DatabaseName	ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access 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	Medicine
EISSN	1878-3686
EndPage	201.e10
ExternalDocumentID	PMC5824730 29438695 10_1016_j_ccell_2018_01_009 S1535610818300096
Genre	Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural
GrantInformation_xml	– fundername: NIBIB NIH HHS grantid: T32 EB007507 – fundername: NCI NIH HHS grantid: P30 CA016672 – fundername: NIEHS NIH HHS grantid: 27303C0140 – fundername: NCI NIH HHS grantid: R21 CA193038
GroupedDBID	--- --K 0R~ 1~5 29B 2WC 4.4 457 4G. 53G 5GY 62- 6I. 6J9 7-5 AACTN AAEDT AAEDW AAFTH AAIAV AAKRW AAKUH AALRI AAUCE AAVLU AAXJY AAXUO ABJNI ABMAC ABMWF ABVKL ACGFO ACGFS ADBBV ADEZE ADJPV AEFWE AENEX AEXQZ AFTJW AGKMS AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL CS3 DIK DU5 E3Z EBS EJD F5P FCP FDB FEDTE FIRID HVGLF IH2 IHE IXB J1W JIG M3Z M41 NCXOZ O-L O9- OK1 P2P RCE RIG ROL RPZ SES SSZ TR2 UDS WQ6 ZA5 5VS AAFWJ AAIKJ AAMRU AAQFI AAYWO AAYXX ABDGV ACVFH ADCNI ADVLN AEUPX AFPUW AGCQF AGHFR AIGII AKAPO AKBMS AKRWK AKYEP APXCP CITATION HZ~ OZT UHS CGR CUY CVF ECM EIF NPM 7X8 EFKBS 5PM
ID	FETCH-LOGICAL-c525t-eedf09b6207c3cc63a5b0a9e2e028a5b5fda79df642b7c65fcbe41f7e7a510b03
IEDL.DBID	IXB
ISSN	1535-6108 1878-3686
IngestDate	Thu Aug 21 14:31:58 EDT 2025 Mon Jul 21 10:19:10 EDT 2025 Thu Apr 03 07:03:52 EDT 2025 Tue Jul 01 01:26:21 EDT 2025 Thu Apr 24 23:13:28 EDT 2025 Fri Feb 23 02:27:45 EST 2024
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	2
Keywords	antibody-drug conjugate receptor internalization immunotherapy PD-L1 B3GNT3 glycosylation immunosuppression TNBC PD-1 immune checkpoint blockade
Language	English
License	This article is made available under the Elsevier license. Published by Elsevier Inc.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c525t-eedf09b6207c3cc63a5b0a9e2e028a5b5fda79df642b7c65fcbe41f7e7a510b03
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Lead Contact These authors contributed equally to this work.
OpenAccessLink	https://www.sciencedirect.com/science/article/pii/S1535610818300096
PMID	29438695
PQID	2002213096
PQPubID	23479
ParticipantIDs	pubmedcentral_primary_oai_pubmedcentral_nih_gov_5824730 proquest_miscellaneous_2002213096 pubmed_primary_29438695 crossref_citationtrail_10_1016_j_ccell_2018_01_009 crossref_primary_10_1016_j_ccell_2018_01_009 elsevier_sciencedirect_doi_10_1016_j_ccell_2018_01_009
ProviderPackageCode	CITATION AAYXX
PublicationCentury	2000
PublicationDate	2018-02-12
PublicationDateYYYYMMDD	2018-02-12
PublicationDate_xml	– month: 02 year: 2018 text: 2018-02-12 day: 12
PublicationDecade	2010
PublicationPlace	United States
PublicationPlace_xml	– name: United States
PublicationTitle	Cancer cell
PublicationTitleAlternate	Cancer Cell
PublicationYear	2018
Publisher	Elsevier Inc
Publisher_xml	– name: Elsevier Inc
References	Perillo, Liu, Huynh, Liu, Chou, Hung, Yeh, Dunn (bib28) 2015; 6 Torreno-Pina, Castro, Manzo, Buschow, Cambi, Garcia-Parajo (bib38) 2014; 111 Shiraishi, Natsume, Togayachi, Endo, Akashima, Yamada, Imai, Nakagawa, Koizumi, Sekine (bib32) 2001; 276 Altschuler, Kinlough, Poland, Bruns, Apodaca, Weisz, Hughey (bib2) 2000; 11 Li, Lim, Xia, Lee, Chan, Kuo, Khoo, Chang, Cha, Kim (bib19) 2016; 7 Sugahara, Kaji, Sugihara, Asano, Narimatsu (bib33) 2012; 2 Dong, Strome, Salomao, Tamura, Hirano, Flies, Roche, Lu, Zhu, Tamada (bib10) 2002; 8 Chen, Han (bib5) 2015; 125 Gao, Shi, Zhao, Chen, Xiong, He, Chen, Roszik, Bernatchez, Woodman (bib12) 2016; 167 Hennet, Dinter, Kuhnert, Mattu, Rudd, Berger (bib14) 1998; 273 Li, Xia, Huo, Lim, Wu, Hsu, Chao, Yamaguchi, Yang, Ding (bib20) 2012; 72 Li, Perry, Muniz-Medina, Wang, Wetzel, Rebelatto, Hinrichs, Bezabeh, Fleming, Dimasi (bib21) 2016; 29 Liu, Hamrouni, Wolowiec, Coiteux, Kuliczkowski, Hetuin, Saudemont, Quesnel (bib23) 2007; 110 Nanda, Chow, Dees, Berger, Gupta, Geva, Pusztai, Pathiraja, Aktan, Cheng (bib25) 2016; 34 Zou, Chen (bib42) 2008; 8 Garner, Baum (bib13) 2008; 36 Schmid, Cruz, Braiteh, Eder, Tolaney, Kuter, Nanda, Chung, Cassier, Delord (bib30) 2017; 77 Asano (bib3) 2003; 13 Croci, Cerliani, Dalotto-Moreno, Mendez-Huergo, Mascanfroni, Dergan-Dylon, Toscano, Caramelo, Garcia-Vallejo, Ouyang (bib7) 2014; 156 Junutula, Raab, Clark, Bhakta, Leipold, Weir, Chen, Simpson, Tsai, Dennis (bib16) 2008; 26 Lim, Li, Xia, Cha, Chan, Wu, Chang, Lin, Hsu, Hsu (bib22) 2016; 30 McLaughlin, Han, Schalper, Carvajal-Hausdorf, Pelekanou, Rehman, Velcheti, Herbst, LoRusso, Rimm (bib24) 2016; 2 Pardoll (bib27) 2012; 12 Schwarz, Aebi (bib31) 2011; 21 Tolcher (bib37) 2016; 27 Adams, Schmid, Rugo, Winer, Loirat, Awada, Cescon, Iwata, Campone, Nanda (bib1) 2017; 35 Ho, Che, Chou, Chang, Jeng, Hsu, Lin, Huang (bib15) 2013; 104 Okeley, Miyamoto, Zhang, Sanderson, Benjamin, Sievers, Senter, Alley (bib26) 2010; 16 Xiao, Woods, Vukojicic, Bertozzi (bib39) 2016; 113 Rosenberg, Hoffman-Censits, Powles, van der Heijden, Balar, Necchi, Dawson, O'Donnell, Balmanoukian, Loriot (bib29) 2016; 387 Tansky, Pothoulakis, Leeman (bib35) 2007; 104 Cheung, Reithmeier (bib6) 2007; 41 Dong, Zhu, Tamada, Chen (bib11) 1999; 5 . Dirix, Takacs, Nikolinakos, Jerusalem, Arkenau, Hamilton, von Heydebreck, Grote, Chin, Lippman (bib9) 2016; 76 The Human Protein Atlas. (2017). Expression of B3GNT3 in cancer. In: The Human Protein Atlas. Yeh, Hiraoka, Petryniak, Nakayama, Ellies, Rabuka, Hindsgaul, Marth, Lowe, Fukuda (bib40) 2001; 105 Kamei, Fukui, Suzuki, Kajihara, Kinoshita, Kakehi, Hojo, Tezuka, Tsuji (bib17) 2010; 391 Zaretsky, Garcia-Diaz, Shin, Escuin-Ordinas, Hugo, Hu-Lieskovan, Torrejon, Abril-Rodriguez, Sandoval, Barthly (bib41) 2016; 375 Brahmer, Drake, Wollner, Powderly, Picus, Sharfman, Stankevich, Pons, Salay, McMiller (bib4) 2010; 28 Sznol, Chen (bib34) 2013; 19 Krummel, Allison (bib18) 1995; 182 Curiel, Wei, Dong, Alvarez, Cheng, Mottram, Krzysiek, Knutson, Daniel, Zimmermann (bib8) 2003; 9 Nanda (10.1016/j.ccell.2018.01.009_bib25) 2016; 34 Junutula (10.1016/j.ccell.2018.01.009_bib16) 2008; 26 Li (10.1016/j.ccell.2018.01.009_bib20) 2012; 72 Okeley (10.1016/j.ccell.2018.01.009_bib26) 2010; 16 Altschuler (10.1016/j.ccell.2018.01.009_bib2) 2000; 11 Dong (10.1016/j.ccell.2018.01.009_bib11) 1999; 5 Pardoll (10.1016/j.ccell.2018.01.009_bib27) 2012; 12 Adams (10.1016/j.ccell.2018.01.009_bib1) 2017; 35 Sznol (10.1016/j.ccell.2018.01.009_bib34) 2013; 19 Krummel (10.1016/j.ccell.2018.01.009_bib18) 1995; 182 Sugahara (10.1016/j.ccell.2018.01.009_bib33) 2012; 2 Schmid (10.1016/j.ccell.2018.01.009_bib30) 2017; 77 Zaretsky (10.1016/j.ccell.2018.01.009_bib41) 2016; 375 Lim (10.1016/j.ccell.2018.01.009_bib22) 2016; 30 Shiraishi (10.1016/j.ccell.2018.01.009_bib32) 2001; 276 Tansky (10.1016/j.ccell.2018.01.009_bib35) 2007; 104 Xiao (10.1016/j.ccell.2018.01.009_bib39) 2016; 113 Dong (10.1016/j.ccell.2018.01.009_bib10) 2002; 8 Li (10.1016/j.ccell.2018.01.009_bib19) 2016; 7 Gao (10.1016/j.ccell.2018.01.009_bib12) 2016; 167 Chen (10.1016/j.ccell.2018.01.009_bib5) 2015; 125 Zou (10.1016/j.ccell.2018.01.009_bib42) 2008; 8 Cheung (10.1016/j.ccell.2018.01.009_bib6) 2007; 41 Curiel (10.1016/j.ccell.2018.01.009_bib8) 2003; 9 Ho (10.1016/j.ccell.2018.01.009_bib15) 2013; 104 McLaughlin (10.1016/j.ccell.2018.01.009_bib24) 2016; 2 Liu (10.1016/j.ccell.2018.01.009_bib23) 2007; 110 Yeh (10.1016/j.ccell.2018.01.009_bib40) 2001; 105 Schwarz (10.1016/j.ccell.2018.01.009_bib31) 2011; 21 Asano (10.1016/j.ccell.2018.01.009_bib3) 2003; 13 Hennet (10.1016/j.ccell.2018.01.009_bib14) 1998; 273 Perillo (10.1016/j.ccell.2018.01.009_bib28) 2015; 6 Tolcher (10.1016/j.ccell.2018.01.009_bib37) 2016; 27 Torreno-Pina (10.1016/j.ccell.2018.01.009_bib38) 2014; 111 Li (10.1016/j.ccell.2018.01.009_bib21) 2016; 29 10.1016/j.ccell.2018.01.009_bib36 Garner (10.1016/j.ccell.2018.01.009_bib13) 2008; 36 Dirix (10.1016/j.ccell.2018.01.009_bib9) 2016; 76 Rosenberg (10.1016/j.ccell.2018.01.009_bib29) 2016; 387 Kamei (10.1016/j.ccell.2018.01.009_bib17) 2010; 391 Brahmer (10.1016/j.ccell.2018.01.009_bib4) 2010; 28 Croci (10.1016/j.ccell.2018.01.009_bib7) 2014; 156 29438689 - Cancer Cell. 2018 Feb 12;33(2):155-157. doi: 10.1016/j.ccell.2018.01.015
References_xml	– volume: 5 start-page: 1365 year: 1999 end-page: 1369 ident: bib11 article-title: B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation and interleukin-10 secretion publication-title: Nat. Med. – volume: 7 start-page: 12632 year: 2016 ident: bib19 article-title: Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity publication-title: Nat. Commun. – volume: 110 start-page: 296 year: 2007 end-page: 304 ident: bib23 article-title: Plasma cells from multiple myeloma patients express B7-H1 (PD-L1) and increase expression after stimulation with IFN-{gamma} and TLR ligands via a MyD88-, TRAF6-, and MEK-dependent pathway publication-title: Blood – volume: 6 start-page: 7874 year: 2015 ident: bib28 article-title: Deep and high-resolution 3D tracking of single particles using nonlinear and multiplexed illumination publication-title: Nat. Commun. – volume: 8 start-page: 467 year: 2008 end-page: 477 ident: bib42 article-title: Inhibitory B7-family molecules in the tumour microenvironment publication-title: Nat. Rev. Immunol. – volume: 125 start-page: 3384 year: 2015 end-page: 3391 ident: bib5 article-title: Anti-PD-1/PD-L1 therapy of human cancer: past, present, and future publication-title: J. Clin. Invest. – volume: 12 start-page: 252 year: 2012 end-page: 264 ident: bib27 article-title: The blockade of immune checkpoints in cancer immunotherapy publication-title: Nat. Rev. Cancer – volume: 276 start-page: 3498 year: 2001 end-page: 3507 ident: bib32 article-title: Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family publication-title: J. Biol. Chem. – volume: 375 start-page: 819 year: 2016 end-page: 829 ident: bib41 article-title: Mutations associated with acquired resistance to PD-1 blockade in melanoma publication-title: N. Engl. J. Med. – volume: 273 start-page: 58 year: 1998 end-page: 65 ident: bib14 article-title: Genomic cloning and expression of three murine UDP-galactose: beta-N-acetylglucosamine beta1,3-galactosyltransferase genes publication-title: J. Biol. Chem. – volume: 2 start-page: 46 year: 2016 end-page: 54 ident: bib24 article-title: Quantitative assessment of the heterogeneity of PD-L1 expression in non-small-cell lung cancer publication-title: JAMA Oncol. – volume: 113 start-page: 10304 year: 2016 end-page: 10309 ident: bib39 article-title: Precision glycocalyx editing as a strategy for cancer immunotherapy publication-title: Proc. Natl. Acad. Sci. USA – volume: 11 start-page: 819 year: 2000 end-page: 831 ident: bib2 article-title: Clathrin-mediated endocytosis of MUC1 is modulated by its glycosylation state publication-title: Mol. Biol. Cell – volume: 182 start-page: 459 year: 1995 end-page: 465 ident: bib18 article-title: CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation publication-title: J. Exp. Med. – volume: 2 start-page: 680 year: 2012 ident: bib33 article-title: Large-scale identification of target proteins of a glycosyltransferase isozyme by Lectin-IGOT-LC/MS, an LC/MS-based glycoproteomic approach publication-title: Sci. Rep. – volume: 41 start-page: 451 year: 2007 end-page: 459 ident: bib6 article-title: Scanning N-glycosylation mutagenesis of membrane proteins publication-title: Methods – volume: 16 start-page: 888 year: 2010 end-page: 897 ident: bib26 article-title: Intracellular activation of SGN-35, a potent anti-CD30 antibody-drug conjugate publication-title: Clin. Cancer Res. – volume: 9 start-page: 562 year: 2003 end-page: 567 ident: bib8 article-title: Blockade of B7-H1 improves myeloid dendritic cell-mediated antitumor immunity publication-title: Nat. Med. – volume: 26 start-page: 925 year: 2008 end-page: 932 ident: bib16 article-title: Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index publication-title: Nat. Biotechnol. – volume: 30 start-page: 925 year: 2016 end-page: 939 ident: bib22 article-title: Deubiquitination and stabilization of PD-L1 by CSN5 publication-title: Cancer Cell – volume: 76 year: 2016 ident: bib9 article-title: Abstract S1-04: Avelumab (MSB0010718C), an anti-PD-L1 antibody, in patients with locally advanced or metastatic breast cancer: a phase Ib JAVELIN solid tumor trial publication-title: Cancer Res. – volume: 387 start-page: 1909 year: 2016 end-page: 1920 ident: bib29 article-title: Atezolizumab in patients with locally advanced and metastatic urothelial carcinoma who have progressed following treatment with platinum-based chemotherapy: a single-arm, multicentre, phase 2 trial publication-title: Lancet – volume: 77 start-page: 2986 year: 2017 ident: bib30 article-title: Abstract 2986: atezolizumab in metastatic TNBC (mTNBC): Long-term clinical outcomes and biomarker analyses publication-title: Cancer Res. – volume: 36 start-page: 1472 year: 2008 end-page: 1477 ident: bib13 article-title: Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling publication-title: Biochem. Soc. Trans. – volume: 19 start-page: 1021 year: 2013 end-page: 1034 ident: bib34 article-title: Antagonist antibodies to PD-1 and B7-H1 (PD-L1) in the treatment of advanced human cancer publication-title: Clin. Cancer Res. – volume: 111 start-page: 11037 year: 2014 end-page: 11042 ident: bib38 article-title: Enhanced receptor-clathrin interactions induced by N-glycan-mediated membrane micropatterning publication-title: Proc. Natl. Acad. Sci. USA – volume: 8 start-page: 793 year: 2002 end-page: 800 ident: bib10 article-title: Tumor-associated B7-H1 promotes T-cell apoptosis: a potential mechanism of immune evasion publication-title: Nat. Med. – volume: 104 start-page: 1600 year: 2013 end-page: 1608 ident: bib15 article-title: B3GNT3 expression suppresses cell migration and invasion and predicts favorable outcomes in neuroblastoma publication-title: Cancer Sci. – reference: . – volume: 156 start-page: 744 year: 2014 end-page: 758 ident: bib7 article-title: Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors publication-title: Cell – volume: 105 start-page: 957 year: 2001 end-page: 969 ident: bib40 article-title: Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase publication-title: Cell – volume: 35 start-page: 1008 year: 2017 ident: bib1 article-title: Phase 2 study of pembrolizumab (pembro) monotherapy for previously treated metastatic triple-negative breast cancer (mTNBC): KEYNOTE-086 cohort A publication-title: J. Clin. Oncol. – volume: 104 start-page: 10691 year: 2007 end-page: 10696 ident: bib35 article-title: Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor publication-title: Proc. Natl. Acad. Sci. USA – volume: 13 start-page: 93R year: 2003 end-page: 104R ident: bib3 article-title: Glycosidase inhibitors: update and perspectives on practical use publication-title: Glycobiology – volume: 28 start-page: 3167 year: 2010 end-page: 3175 ident: bib4 article-title: Phase I study of single-agent anti-programmed death-1 (MDX-1106) in refractory solid tumors: safety, clinical activity, pharmacodynamics, and immunologic correlates publication-title: J. Clin. Oncol. – volume: 391 start-page: 557 year: 2010 end-page: 563 ident: bib17 article-title: Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding publication-title: Biochem. Biophys. Res. Commun. – volume: 29 start-page: 117 year: 2016 end-page: 129 ident: bib21 article-title: A biparatopic HER2-targeting antibody-drug conjugate induces tumor regression in primary models refractory to or ineligible for HER2-targeted therapy publication-title: Cancer Cell – volume: 27 start-page: 2168 year: 2016 end-page: 2172 ident: bib37 article-title: Antibody drug conjugates: lessons from 20 years of clinical experience publication-title: Ann. Oncol. – reference: The Human Protein Atlas. (2017). Expression of B3GNT3 in cancer. In: The Human Protein Atlas. – volume: 21 start-page: 576 year: 2011 end-page: 582 ident: bib31 article-title: Mechanisms and principles of N-linked protein glycosylation publication-title: Curr. Opin. Struct. Biol. – volume: 167 start-page: 397 year: 2016 end-page: 404.e9 ident: bib12 article-title: Loss of IFN-gamma pathway genes in tumor cells as a mechanism of resistance to anti-CTLA-4 therapy publication-title: Cell – volume: 72 start-page: 1290 year: 2012 end-page: 1300 ident: bib20 article-title: Epithelial-mesenchymal transition induced by TNF-alpha requires NF-kappaB-mediated transcriptional upregulation of Twist1 publication-title: Cancer Res. – volume: 34 start-page: 2460 year: 2016 end-page: 2467 ident: bib25 article-title: Pembrolizumab in patients with advanced triple-negative breast cancer: phase Ib KEYNOTE-012 study publication-title: J. Clin. Oncol. – volume: 8 start-page: 793 year: 2002 ident: 10.1016/j.ccell.2018.01.009_bib10 article-title: Tumor-associated B7-H1 promotes T-cell apoptosis: a potential mechanism of immune evasion publication-title: Nat. Med. doi: 10.1038/nm730 – volume: 105 start-page: 957 year: 2001 ident: 10.1016/j.ccell.2018.01.009_bib40 article-title: Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase publication-title: Cell doi: 10.1016/S0092-8674(01)00394-4 – volume: 16 start-page: 888 year: 2010 ident: 10.1016/j.ccell.2018.01.009_bib26 article-title: Intracellular activation of SGN-35, a potent anti-CD30 antibody-drug conjugate publication-title: Clin. Cancer Res. doi: 10.1158/1078-0432.CCR-09-2069 – volume: 12 start-page: 252 year: 2012 ident: 10.1016/j.ccell.2018.01.009_bib27 article-title: The blockade of immune checkpoints in cancer immunotherapy publication-title: Nat. Rev. Cancer doi: 10.1038/nrc3239 – ident: 10.1016/j.ccell.2018.01.009_bib36 – volume: 13 start-page: 93R year: 2003 ident: 10.1016/j.ccell.2018.01.009_bib3 article-title: Glycosidase inhibitors: update and perspectives on practical use publication-title: Glycobiology doi: 10.1093/glycob/cwg090 – volume: 113 start-page: 10304 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib39 article-title: Precision glycocalyx editing as a strategy for cancer immunotherapy publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1608069113 – volume: 26 start-page: 925 year: 2008 ident: 10.1016/j.ccell.2018.01.009_bib16 article-title: Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index publication-title: Nat. Biotechnol. doi: 10.1038/nbt.1480 – volume: 34 start-page: 2460 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib25 article-title: Pembrolizumab in patients with advanced triple-negative breast cancer: phase Ib KEYNOTE-012 study publication-title: J. Clin. Oncol. doi: 10.1200/JCO.2015.64.8931 – volume: 2 start-page: 46 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib24 article-title: Quantitative assessment of the heterogeneity of PD-L1 expression in non-small-cell lung cancer publication-title: JAMA Oncol. doi: 10.1001/jamaoncol.2015.3638 – volume: 28 start-page: 3167 year: 2010 ident: 10.1016/j.ccell.2018.01.009_bib4 article-title: Phase I study of single-agent anti-programmed death-1 (MDX-1106) in refractory solid tumors: safety, clinical activity, pharmacodynamics, and immunologic correlates publication-title: J. Clin. Oncol. doi: 10.1200/JCO.2009.26.7609 – volume: 77 start-page: 2986 year: 2017 ident: 10.1016/j.ccell.2018.01.009_bib30 article-title: Abstract 2986: atezolizumab in metastatic TNBC (mTNBC): Long-term clinical outcomes and biomarker analyses publication-title: Cancer Res. doi: 10.1158/1538-7445.AM2017-2986 – volume: 35 start-page: 1008 year: 2017 ident: 10.1016/j.ccell.2018.01.009_bib1 article-title: Phase 2 study of pembrolizumab (pembro) monotherapy for previously treated metastatic triple-negative breast cancer (mTNBC): KEYNOTE-086 cohort A publication-title: J. Clin. Oncol. doi: 10.1200/JCO.2017.35.15_suppl.1008 – volume: 36 start-page: 1472 year: 2008 ident: 10.1016/j.ccell.2018.01.009_bib13 article-title: Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0361472 – volume: 104 start-page: 1600 year: 2013 ident: 10.1016/j.ccell.2018.01.009_bib15 article-title: B3GNT3 expression suppresses cell migration and invasion and predicts favorable outcomes in neuroblastoma publication-title: Cancer Sci. doi: 10.1111/cas.12294 – volume: 72 start-page: 1290 year: 2012 ident: 10.1016/j.ccell.2018.01.009_bib20 article-title: Epithelial-mesenchymal transition induced by TNF-alpha requires NF-kappaB-mediated transcriptional upregulation of Twist1 publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-11-3123 – volume: 29 start-page: 117 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib21 article-title: A biparatopic HER2-targeting antibody-drug conjugate induces tumor regression in primary models refractory to or ineligible for HER2-targeted therapy publication-title: Cancer Cell doi: 10.1016/j.ccell.2015.12.008 – volume: 156 start-page: 744 year: 2014 ident: 10.1016/j.ccell.2018.01.009_bib7 article-title: Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors publication-title: Cell doi: 10.1016/j.cell.2014.01.043 – volume: 5 start-page: 1365 year: 1999 ident: 10.1016/j.ccell.2018.01.009_bib11 article-title: B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation and interleukin-10 secretion publication-title: Nat. Med. doi: 10.1038/70932 – volume: 21 start-page: 576 year: 2011 ident: 10.1016/j.ccell.2018.01.009_bib31 article-title: Mechanisms and principles of N-linked protein glycosylation publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2011.08.005 – volume: 41 start-page: 451 year: 2007 ident: 10.1016/j.ccell.2018.01.009_bib6 article-title: Scanning N-glycosylation mutagenesis of membrane proteins publication-title: Methods doi: 10.1016/j.ymeth.2006.10.002 – volume: 30 start-page: 925 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib22 article-title: Deubiquitination and stabilization of PD-L1 by CSN5 publication-title: Cancer Cell doi: 10.1016/j.ccell.2016.10.010 – volume: 104 start-page: 10691 year: 2007 ident: 10.1016/j.ccell.2018.01.009_bib35 article-title: Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0703394104 – volume: 11 start-page: 819 year: 2000 ident: 10.1016/j.ccell.2018.01.009_bib2 article-title: Clathrin-mediated endocytosis of MUC1 is modulated by its glycosylation state publication-title: Mol. Biol. Cell doi: 10.1091/mbc.11.3.819 – volume: 2 start-page: 680 year: 2012 ident: 10.1016/j.ccell.2018.01.009_bib33 article-title: Large-scale identification of target proteins of a glycosyltransferase isozyme by Lectin-IGOT-LC/MS, an LC/MS-based glycoproteomic approach publication-title: Sci. Rep. doi: 10.1038/srep00680 – volume: 182 start-page: 459 year: 1995 ident: 10.1016/j.ccell.2018.01.009_bib18 article-title: CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation publication-title: J. Exp. Med. doi: 10.1084/jem.182.2.459 – volume: 9 start-page: 562 year: 2003 ident: 10.1016/j.ccell.2018.01.009_bib8 article-title: Blockade of B7-H1 improves myeloid dendritic cell-mediated antitumor immunity publication-title: Nat. Med. doi: 10.1038/nm863 – volume: 27 start-page: 2168 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib37 article-title: Antibody drug conjugates: lessons from 20 years of clinical experience publication-title: Ann. Oncol. doi: 10.1093/annonc/mdw424 – volume: 76 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib9 article-title: Abstract S1-04: Avelumab (MSB0010718C), an anti-PD-L1 antibody, in patients with locally advanced or metastatic breast cancer: a phase Ib JAVELIN solid tumor trial publication-title: Cancer Res. doi: 10.1158/1538-7445.SABCS15-S1-04 – volume: 7 start-page: 12632 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib19 article-title: Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity publication-title: Nat. Commun. doi: 10.1038/ncomms12632 – volume: 19 start-page: 1021 year: 2013 ident: 10.1016/j.ccell.2018.01.009_bib34 article-title: Antagonist antibodies to PD-1 and B7-H1 (PD-L1) in the treatment of advanced human cancer publication-title: Clin. Cancer Res. doi: 10.1158/1078-0432.CCR-12-2063 – volume: 276 start-page: 3498 year: 2001 ident: 10.1016/j.ccell.2018.01.009_bib32 article-title: Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family publication-title: J. Biol. Chem. doi: 10.1074/jbc.M004800200 – volume: 167 start-page: 397 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib12 article-title: Loss of IFN-gamma pathway genes in tumor cells as a mechanism of resistance to anti-CTLA-4 therapy publication-title: Cell doi: 10.1016/j.cell.2016.08.069 – volume: 375 start-page: 819 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib41 article-title: Mutations associated with acquired resistance to PD-1 blockade in melanoma publication-title: N. Engl. J. Med. doi: 10.1056/NEJMoa1604958 – volume: 391 start-page: 557 year: 2010 ident: 10.1016/j.ccell.2018.01.009_bib17 article-title: Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2009.11.098 – volume: 387 start-page: 1909 year: 2016 ident: 10.1016/j.ccell.2018.01.009_bib29 article-title: Atezolizumab in patients with locally advanced and metastatic urothelial carcinoma who have progressed following treatment with platinum-based chemotherapy: a single-arm, multicentre, phase 2 trial publication-title: Lancet doi: 10.1016/S0140-6736(16)00561-4 – volume: 8 start-page: 467 year: 2008 ident: 10.1016/j.ccell.2018.01.009_bib42 article-title: Inhibitory B7-family molecules in the tumour microenvironment publication-title: Nat. Rev. Immunol. doi: 10.1038/nri2326 – volume: 110 start-page: 296 year: 2007 ident: 10.1016/j.ccell.2018.01.009_bib23 article-title: Plasma cells from multiple myeloma patients express B7-H1 (PD-L1) and increase expression after stimulation with IFN-{gamma} and TLR ligands via a MyD88-, TRAF6-, and MEK-dependent pathway publication-title: Blood doi: 10.1182/blood-2006-10-051482 – volume: 125 start-page: 3384 year: 2015 ident: 10.1016/j.ccell.2018.01.009_bib5 article-title: Anti-PD-1/PD-L1 therapy of human cancer: past, present, and future publication-title: J. Clin. Invest. doi: 10.1172/JCI80011 – volume: 273 start-page: 58 year: 1998 ident: 10.1016/j.ccell.2018.01.009_bib14 article-title: Genomic cloning and expression of three murine UDP-galactose: beta-N-acetylglucosamine beta1,3-galactosyltransferase genes publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.1.58 – volume: 6 start-page: 7874 year: 2015 ident: 10.1016/j.ccell.2018.01.009_bib28 article-title: Deep and high-resolution 3D tracking of single particles using nonlinear and multiplexed illumination publication-title: Nat. Commun. doi: 10.1038/ncomms8874 – volume: 111 start-page: 11037 year: 2014 ident: 10.1016/j.ccell.2018.01.009_bib38 article-title: Enhanced receptor-clathrin interactions induced by N-glycan-mediated membrane micropatterning publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1402041111 – reference: 29438689 - Cancer Cell. 2018 Feb 12;33(2):155-157. doi: 10.1016/j.ccell.2018.01.015
SSID	ssj0016179
Score	2.6708648
Snippet	Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar... Protein glycosylation provides proteomic diversity in regulating protein localization, stability and activity; it remains largely unknown whether the sugar...
SourceID	pubmedcentral proquest pubmed crossref elsevier
SourceType	Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	187
SubjectTerms	Animals Antibodies, Monoclonal - pharmacology antibody-drug conjugate B3GNT3 Cell Line, Tumor Female glycosylation Humans immune checkpoint blockade immunosuppression immunotherapy Lymphocytes, Tumor-Infiltrating - drug effects Lymphocytes, Tumor-Infiltrating - immunology Mice, Inbred BALB C N-Acetylglucosaminyltransferases - drug effects N-Acetylglucosaminyltransferases - metabolism PD-1 PD-L1 Programmed Cell Death 1 Receptor - immunology receptor internalization TNBC Triple Negative Breast Neoplasms - drug therapy Triple Negative Breast Neoplasms - immunology Triple Negative Breast Neoplasms - metabolism
Title	Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1
URI	https://dx.doi.org/10.1016/j.ccell.2018.01.009 https://www.ncbi.nlm.nih.gov/pubmed/29438695 https://www.proquest.com/docview/2002213096 https://pubmed.ncbi.nlm.nih.gov/PMC5824730
Volume	33
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
link	http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT-MwELYQB8RltTx26fKQkThiNXFsJz5CeQkBQlCk3izbsdmuqhS15dB_z9hJKsoiDtyS2JZGM575vtjjMUJH0jHGwW8IY6UgTDpLCl1KwnNqnWApM0k4jXx7J66e2PWAD1ZQrz0LE9Iqm9hfx_QYrZsv3Uab3ZfhsPsIvhrAHxAni0wc4nDGiniIb3C62EkAhJZ1zVROQu-28lDM8bJhdTzkdxWxdmfISvwcnf5nnx-TKN-h0sVP9KOhk_iklngDrbhqE63dNhvmW-jhfKLLZlkOjz3uT8LCOrlzz7HgNz4NOekz3Au2n-AeyDnFZo77MT8cUA1fjuZ2PJ2PgJKW-P6M3KTb6OnivN-7Is01CsRyymcEUNAn0gia5DazVmSam0RLRx1wC3jmvtS5LD38iZjcCu6tcSz1ucs1OKxJsl9otRpXbgfhxAO9szTh3hfAPFJZWO6M0MDipC6LrINoqz5lmxrj4aqLkWqTyf6pqHMVdK6SVIHOO-h4MeilLrHxdXfR2kUtzRQFIPD1wMPWigp8KDTryo1fp-EqTkoBzKXooN-1VReSUMmyQkjeQfmSvRcdQn3u5ZZq-DfW6eYFZRBA_3xX4F20Ht5IvH5mD63OJq9uHyjQzBzEOf4GW5wE6A
linkProvider	Elsevier
linkToHtml	http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwED6NIQEvaPwuMDASj1hNHNuJH1m30UFbIeikvlmOY0NRlU5t99D_nrOTVHSgPfAWxY50uvPd98U-3wG8V45zgX5DOa8k5cpZWphKUZEz6yRPeZmE28jjiRxe8s8zMTuAQXcXJqRVtrG_iekxWrdv-q02-1fzef87-moAf0ScLDLxO3AX2UAe-jdczE52RwkI0aopmipomN6VHopJXjZsj4cEryIW7wxpif-Gp7_p580syj9g6fwIHrZ8knxsRH4EB65-DPfG7Yn5E_h2tjJVuy9Hlp5MV2FnnU7cj1jxm5yEpPQNGQTjr8gA5VyTckumMUEcYY18Wmztcr1dICetyNdTOkqfwuX52XQwpG0fBWoFExuKMOgTVUqW5DazVmZGlIlRjjkkF_gsfGVyVXn8FSlzK4W3peOpz11u0GPLJHsGh_Wydi-AJB75nWWJ8L5A6pGqwgpXSoM0TpmqyHrAOvVp2xYZD70uFrrLJvulo8510LlOUo0678GH3UdXTY2N26fLzi56b6loRIHbP3zXWVGjE4VhU7vl9Tr04mQM0VzJHjxvrLqThCmeFVKJHuR79t5NCAW690fq-c9YqFsUjGMEffm_Ar-F-8PpeKRHF5Mvr-BBGKGxF81rONysrt0x8qFN-Sau9994bAgH
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=Eradication+of+Triple-Negative+Breast+Cancer+Cells+by+Targeting+Glycosylated+PD-L1&rft.jtitle=Cancer+cell&rft.au=Li%2C+Chia-Wei&rft.au=Lim%2C+Seung-Oe&rft.au=Chung%2C+Ezra+M&rft.au=Kim%2C+Yong-Soo&rft.date=2018-02-12&rft.eissn=1878-3686&rft.volume=33&rft.issue=2&rft.spage=187&rft_id=info:doi/10.1016%2Fj.ccell.2018.01.009&rft_id=info%3Apmid%2F29438695&rft.externalDocID=29438695
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1535-6108&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1535-6108&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1535-6108&client=summon