O-GlcNAcylation is a key modulator of skeletal muscle sarcomeric morphometry associated to modulation of protein–protein interactions
The sarcomere structure of skeletal muscle is determined through multiple protein–protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylati...
Saved in:
| Published in | Biochimica et biophysica acta Vol. 1860; no. 9; pp. 2017 - 2030 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.09.2016
Elsevier |
| Series | Biochimica et biophysica acta. General subjects |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/j.bbagen.2016.06.011 |
Cover
Loading…
| Abstract | The sarcomere structure of skeletal muscle is determined through multiple protein–protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization.
C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level.
Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin.
For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure.
In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation.
•This paper supports the role of O-GlcNAcylation, a particular glycosylation, in the regulation of interactome, in particular the sarcomeric organization. For the first time, we demonstrated a key role of the O-GlcNAcylation in myofibrillar interactome by the modulation of protein-protein interactions between key structural proteins.•In this paper, e have shown that the interaction between desmin and its molecular chaperone, the αB-crystallin, seems to be modulated according to the global O-GlcNAc level of C2C12 myotubes.•This paper will have interest for glycobiologists (through O-GlcNAcylation), for physiologists and/or cell biologists (through the sarcomeric organization), as well as for proteomists (through interactome). |
|---|---|
| AbstractList | The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization.BACKGROUNDThe sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization.C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level.METHODSC2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level.Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin.RESULTSOur data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin.For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure.CONCLUSIONSFor the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure.In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation.GENERAL SIGNIFICANCEIn the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation. The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization.C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level.Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin.For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure.In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation. The sarcomere structure of skeletal muscle is determined through multiple protein–protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization. C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level. Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin. For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure. In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation. •This paper supports the role of O-GlcNAcylation, a particular glycosylation, in the regulation of interactome, in particular the sarcomeric organization. For the first time, we demonstrated a key role of the O-GlcNAcylation in myofibrillar interactome by the modulation of protein-protein interactions between key structural proteins.•In this paper, e have shown that the interaction between desmin and its molecular chaperone, the αB-crystallin, seems to be modulated according to the global O-GlcNAc level of C2C12 myotubes.•This paper will have interest for glycobiologists (through O-GlcNAcylation), for physiologists and/or cell biologists (through the sarcomeric organization), as well as for proteomists (through interactome). The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization. C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level. Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin. For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure. In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation. |
| Author | Bastide, Bruno Duban-Deweer, Sophie Deracinois, Barbara Lambert, Matthias Krzewinski, Frederic Cieniewski-Bernard, Caroline Richard, Elodie Dupont, Erwan |
| Author_xml | – sequence: 1 givenname: Matthias surname: Lambert fullname: Lambert, Matthias organization: Univ.Lille, EA7369-URePSSS, Unité de Recherche Pluridisciplinaire Sport, Santé, Société, Equipe « Activité Physique, Muscle, Santé », F-59000 Lille, France – sequence: 2 givenname: Elodie surname: Richard fullname: Richard, Elodie organization: BiCeL (BioImaging Center of Lille — Campus Lille 1), Univ.Lille, FR3688 CNRS FRABio, F-59000 Lille, France – sequence: 3 givenname: Sophie surname: Duban-Deweer fullname: Duban-Deweer, Sophie organization: Laboratoire de la Barrière Hémato-Encéphalique (LBHE), EA2465, Université d'Artois, Faculté Jean Perrin, 62307 Lens, France – sequence: 4 givenname: Frederic surname: Krzewinski fullname: Krzewinski, Frederic organization: PAGés (Plateforme d'Analyses des Glycoconjugués), Univ.Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France – sequence: 5 givenname: Barbara surname: Deracinois fullname: Deracinois, Barbara organization: Univ.Lille, EA7369-URePSSS, Unité de Recherche Pluridisciplinaire Sport, Santé, Société, Equipe « Activité Physique, Muscle, Santé », F-59000 Lille, France – sequence: 6 givenname: Erwan surname: Dupont fullname: Dupont, Erwan organization: Univ.Lille, EA7369-URePSSS, Unité de Recherche Pluridisciplinaire Sport, Santé, Société, Equipe « Activité Physique, Muscle, Santé », F-59000 Lille, France – sequence: 7 givenname: Bruno surname: Bastide fullname: Bastide, Bruno organization: Univ.Lille, EA7369-URePSSS, Unité de Recherche Pluridisciplinaire Sport, Santé, Société, Equipe « Activité Physique, Muscle, Santé », F-59000 Lille, France – sequence: 8 givenname: Caroline surname: Cieniewski-Bernard fullname: Cieniewski-Bernard, Caroline email: caroline.cieniewski-bernard@univ-lille1.fr organization: Univ.Lille, EA7369-URePSSS, Unité de Recherche Pluridisciplinaire Sport, Santé, Société, Equipe « Activité Physique, Muscle, Santé », F-59000 Lille, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27301331$$D View this record in MEDLINE/PubMed https://hal.univ-lille.fr/hal-02375890$$DView record in HAL |
| BookMark | eNqNkcFu1DAQhi1URLeFN0DIRzhksWN7k3BAWlXQIq3oBc7WxJlQb514sZ1Ke-PGA_CGPAkOu-2BA2CN5LH1_b9G85-Rk9GPSMhzzpac8dXr7bJt4QuOyzK_liwX54_IgtdVWdSMrU7IggkmC8lX6pScxbhl-ahGPSGnZSUYF4IvyPfr4tKZj2uzd5CsH6mNFOgt7unguyn_-UB9T-MtOkzg6DBF45BGCMYPGKzJXNjd5D6FPYUYvbGQsKPJ3zvMrtliF3xCO_789uPYUTsmDGBmID4lj3twEZ8d73Py-f27TxdXxeb68sPFelMYJXkq6gag7MoemEKEiremYqqTXatMW4LBkqvGIBPKNFj1EhojgDcghGB910spzsmrg-8NOL0LdoCw1x6svlpv9PzHSlGpumF3PLMvD2we-OuEMenBRoPOwYh-iprXpZKC1dXqP1CmZK1q0WT0xRGd2gG7hyHuM8mAPAAm-BgD9g8IZ3qOXm_1IXo9R69ZLj7L3vwhMzb93n4KYN2_xG8PYsy7v7MYdDQWR4OdDWiS7rz9u8EvLivPJg |
| CitedBy_id | crossref_primary_10_1007_s10974_017_9478_4 crossref_primary_10_1093_glycob_cwac067 crossref_primary_10_1002_elps_202400043 crossref_primary_10_1016_j_biochi_2024_04_004 crossref_primary_10_1016_j_biochi_2023_10_002 crossref_primary_10_1038_s41598_022_14033_z crossref_primary_10_1113_JP274970 crossref_primary_10_3390_cells11111789 crossref_primary_10_1038_s41526_024_00434_z crossref_primary_10_1016_j_cbpb_2024_111009 crossref_primary_10_1007_s11033_022_07334_z crossref_primary_10_1152_ajprenal_00566_2018 crossref_primary_10_3389_fendo_2018_00578 crossref_primary_10_1111_apha_13301 crossref_primary_10_3390_metabo12100888 crossref_primary_10_1016_j_jprot_2018_07_005 crossref_primary_10_1016_j_jbc_2023_104963 crossref_primary_10_3390_biom14101252 |
| Cites_doi | 10.1152/ajpcell.00124.2010 10.1155/2011/569628 10.1002/0471143030.cb0610s38 10.1126/scisignal.132pe37 10.1093/glycob/cwq039 10.1016/j.bbagen.2009.07.018 10.1002/jssc.201000869 10.1016/j.bbagen.2009.07.017 10.1007/s00795-011-0542-7 10.1016/j.pharmthera.2013.11.005 10.1085/jgp.200709888 10.1074/jbc.M109.098996 10.1016/j.tcb.2005.11.007 10.1242/jcs.053678 10.1038/sj.emboj.7601242 10.1111/j.1748-1716.2006.01613.x 10.1161/CIRCRESAHA.110.224675 10.1152/ajpcell.00394.2010 10.1186/1559-0275-8-15 10.1177/153537020222701113 10.1016/j.abb.2013.10.016 10.1016/S0021-9258(19)39838-2 10.3389/fphys.2014.00421 10.1002/pmic.200800617 10.4172/2155-6156.S4-005 10.1074/mcp.M900275-MCP200 10.1152/japplphysiol.00783.2011 10.1016/j.abb.2010.09.024 10.1371/journal.pone.0025859 10.1098/rstb.2012.0375 10.1007/s00424-014-1453-y 10.2337/db14-1107 10.1007/s00418-013-1148-z 10.1016/j.nmd.2010.12.007 10.1016/j.febslet.2006.03.043 10.1002/dvdy.22263 10.1016/j.bbadis.2014.05.014 10.3389/fendo.2013.00099 10.1007/s11010-013-1627-5 10.1016/S0955-0674(99)00060-5 10.1074/jbc.M112.410316 10.1007/s00018-008-8080-8 10.1074/mcp.M400024-MCP200 10.1074/jbc.274.18.12803 10.1186/1478-811X-9-1 10.1038/nrm3753 10.1016/S0021-9258(17)32170-1 10.1146/annurev.cellbio.18.012502.105840 10.1007/s00109-005-0033-1 10.1016/j.yexcr.2004.08.004 10.1371/journal.pone.0048218 10.1016/j.yexcr.2007.03.033 10.1016/S0021-9258(17)43295-9 10.1016/j.cell.2014.10.056 10.1155/2010/858606 10.1091/mbc.e07-11-1146 10.1002/0471140864.ps1208s66 10.1007/s00018-004-4282-x 10.1007/s11068-008-9036-5 10.1093/emboj/16.2.211 10.1038/nchembio.96 10.1016/j.biocel.2009.03.008 10.1152/japplphysiol.00865.2005 10.1242/jcs.042234 10.1007/s00726-010-0698-9 10.1038/nature05815 10.1016/j.febslet.2005.01.071 10.1016/j.ceb.2010.12.001 10.1007/s10974-010-9201-1 10.1016/j.yexcr.2007.04.010 10.1074/jbc.M606787200 10.1073/pnas.1411493111 10.1161/CIRCRESAHA.108.184978 10.1146/annurev-biochem-060608-102511 |
| ContentType | Journal Article |
| Copyright | 2016 Elsevier B.V. Copyright © 2016 Elsevier B.V. All rights reserved. Distributed under a Creative Commons Attribution 4.0 International License |
| Copyright_xml | – notice: 2016 Elsevier B.V. – notice: Copyright © 2016 Elsevier B.V. All rights reserved. – notice: Distributed under a Creative Commons Attribution 4.0 International License |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 1XC VOOES |
| DOI | 10.1016/j.bbagen.2016.06.011 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic Hyper Article en Ligne (HAL) Hyper Article en Ligne (HAL) (Open Access) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | MEDLINE - Academic AGRICOLA MEDLINE |
| 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 | 2030 |
| ExternalDocumentID | oai_HAL_hal_02375890v1 27301331 10_1016_j_bbagen_2016_06_011 S0304416516302161 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| 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 PKN RIG TWZ UHS VH1 X7M Y6R YYP ZE2 ZGI ~KM 7X8 7S9 L.6 1XC VOOES |
| ID | FETCH-LOGICAL-c541t-89aa2d2fa05eea71bc705d4db5cb2ace2159ce035c9e7f4a9c3a19a3330fdf443 |
| IEDL.DBID | .~1 |
| ISSN | 0304-4165 0006-3002 |
| IngestDate | Fri May 09 12:24:48 EDT 2025 Fri Jul 11 07:45:50 EDT 2025 Fri Jul 11 11:09:46 EDT 2025 Wed Feb 19 02:00:06 EST 2025 Tue Jul 01 00:22:07 EDT 2025 Thu Apr 24 22:58:40 EDT 2025 Fri Feb 23 02:34:14 EST 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 9 |
| Keywords | Sarcomere structure O-GlcNAcylation Protein–protein interactions Skeletal muscle cells αB-crystallin Desmin Mesh:Protein Interaction Maps/physiology Mesh:Thiazoles/pharmacology Mesh:Crystallins/metabolism Mesh:Proteome/metabolism Mesh:Mice alpha B-crystallin Mesh:Microfilament Proteins/metabolism Mesh:Post-Translational/physiology Mesh:Desmin/metabolism Mesh:Protein Processing Mesh:Actinin/metabolism Mesh:Myofibrils/metabolism Mesh:Cell Line Mesh:Acylation/drug effects Mesh:Muscle Fibers Mesh:Muscle Contraction/physiology Mesh:Pyrans/pharmacology Mesh:Muscle Protein-protein interactions Mesh:Muscle Contraction/drug effects Mesh:Protein Interaction Maps/drug effects Mesh:Skeletal/metabolism Mesh:Skeletal/drug effects Mesh:Animals Mesh:Acylation/physiology Mesh:Post-Translational/drug effects Mesh:Sarcomeres/metabolism |
| Language | English |
| License | Copyright © 2016 Elsevier B.V. All rights reserved. Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c541t-89aa2d2fa05eea71bc705d4db5cb2ace2159ce035c9e7f4a9c3a19a3330fdf443 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0000-0003-0777-9734 0009-0007-3962-1305 0000-0002-0279-2449 0000-0003-1491-6899 |
| OpenAccessLink | https://hal.univ-lille.fr/hal-02375890 |
| PMID | 27301331 |
| PQID | 1805485839 |
| PQPubID | 23479 |
| PageCount | 14 |
| ParticipantIDs | hal_primary_oai_HAL_hal_02375890v1 proquest_miscellaneous_1825430876 proquest_miscellaneous_1805485839 pubmed_primary_27301331 crossref_primary_10_1016_j_bbagen_2016_06_011 crossref_citationtrail_10_1016_j_bbagen_2016_06_011 elsevier_sciencedirect_doi_10_1016_j_bbagen_2016_06_011 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | September 2016 2016-09-00 20160901 2016-09-01 |
| PublicationDateYYYYMMDD | 2016-09-01 |
| PublicationDate_xml | – month: 09 year: 2016 text: September 2016 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationSeriesTitle | Biochimica et biophysica acta. General subjects |
| PublicationTitle | Biochimica et biophysica acta |
| PublicationTitleAlternate | Biochim Biophys Acta |
| PublicationYear | 2016 |
| Publisher | Elsevier B.V Elsevier |
| Publisher_xml | – name: Elsevier B.V – name: Elsevier |
| References | Witt, Burkart, Labeit, McNabb, Wu, Granzier, Labeit (bb0265) 2006; 25 Burattini, Ferri, Battistelli, Curci, Luchetti, Falcieri (bb0240) 2004; 48 Capetanaki, Bloch, Kouloumenta, Mavroidis, Psarras (bb0325) 2007; 313 Hart, Slawson, Ramirez-Correa, Lagerlof (bb0070) 2011; 80 Huang, Li, Foster, Lemanski, Dube, Zhang, Lemanski (bb0050) 2002; 227 Huang (bb0315) 2012; 01 Sadikot, Hammond, Ferrari (bb0045) 2010; 239 Dráb, Kračmerová, Tichá, Hanzlíková, Tichá, Liberda (bb0235) 2011; 34 Snider, Omary (bb0340) 2014; 15 Ramirez-Correa, Jin, Wang, Zhong, Gao, Dias, Vecoli, Hart, Murphy (bb0385) 2008; 103 Akimoto, Miura, Toda, Wolfert, Wells, Boons, Hart, Endo, Kawakami (bb0105) 2011; 8 Hnia, Ramspacher, Vermot, Laporte (bb0360) 2014; 49 Frank, Kuhn, Katus, Frey (bb0035) 2006; 84 Kim, Kim, Lee, Yang, Park, Kim, Cho (bb0245) 2006; 580 Huang, Wong, Lin, Furthmayr (bb0310) 1999; 274 Förster, Welleford, Triplett, Sultana, Schmitz, Butterfield (bb0125) 2014; 1842 Herrmann, Aebi (bb0330) 2000; 12 Houck, Landsbury, Clark, Quinlan (bb0370) 2011; 6 Schamel (bb0230) 2008 Haltiwanger, Holt, Hart (bb0090) 1990; 265 Cieniewski-Bernard, Montel, Stevens, Bastide (bb0185) 2009; 30 Cieniewski-Bernard, Dupont, Richard, Bastide (bb0165) 2014; 466 Tonino, Pappas, Hudson, Labeit, Gregorio, Granzier (bb0270) 2010; 123 Knöll, Buyandelger, Lab (bb0380) 2011; 2011 Au (bb0025) 2004; 61 Lange, Ehler, Gautel (bb0030) 2006; 16 Elliott, Der Perng, Prescott, Jansen, Koenderink, Quinlan (bb0250) 2013; 368 Ji, Kang, Park, Lee, Oh, Cho (bb0350) 2011; 40 Hart, Housley, Slawson (bb0080) 2007; 446 Huang, Ho, Wang, Roessler, Zhang, Hu, Bowe, Kudlow, Paterson (bb0145) 2011; 300 Sanger, Wang, Fan, White, Sanger (bb0010) 2010; 2010 Granzier, Hutchinson, Tonino, Methawasin, Li, Slater, Bull, Saripalli, Pappas, Gregorio, Smith (bb0275) 2014; 111 Sanger, Sanger (bb0295) 2008; 1 Mishra, Ande, Salter (bb0065) 2011; 9 Hedou, Cieniewski-Bernard, Leroy, Michalski, Mounier, Bastide (bb0170) 2007; 282 Slawson, Lakshmanan, Knapp, Hart (bb0205) 2008; 19 Obermann, Gautel, Weber, Fürst (bb0040) 1997; 16 Cieniewski-Bernard, Lambert, Dupont, Montel, Stevens, Bastide (bb0160) 2014; 5 Cieniewski-Bernard, Montel, Berthoin, Bastide (bb0175) 2012; 7 de A. Ribeiro, Pinotsis, Ghisleni, Salmazo, Konarev, Kostan, Sjöblom, Schreiner, Polyansky, Gkougkoulia, Holt, Aachmann, Žagrović, Bordignon, Pirker, Svergun, Gautel, Djinović-Carugo (bb0305) 2014; 159 Cieniewski-Bernard, Mounier, Michalski, Bastide (bb0140) 2006; 100 Ise, Kobayashi, Goto, Sato, Kawakubo, Takahashi, Ikeda, Akaike (bb0210) 2010; 20 Paulin, Li (bb0320) 2004; 301 Mamczur, Rakus, Gizak, Dus, Dzugaj (bb0290) 2005; 579 Dassanayaka, Jones (bb0135) 2014; 142 Hanover, Krause, Love (bb0095) 2010; 1800 Dong, Hart (bb0100) 1994; 269 Yuzwa, Macauley, Heinonen, Shan, Dennis, He, Whitworth, Stubbs, McEachern, Davies, Vocadlo (bb0220) 2008; 4 Hédou, Bastide, Page, Michalski, Morelle (bb0195) 2009; 9 Selcen (bb0375) 2011; 21 Winter, Paulin, Mericskay, Li (bb0335) 2014; 141 Sjöblom, Salmazo, Djinović-Carugo (bb0300) 2008; 65 Farach, Galileo (bb0200) 2008; 36 Slawson, Hart (bb0110) 2012; 11 Srikanth, Vaidya, Kalraiya (bb0345) 2010; 285 Gu, Ande, Mishra (bb0085) 2011; 505 Butkinaree, Park, Hart (bb0285) 2010; 1800 Krishnamoorthy, Donofrio, Martin (bb0365) 2013; 379 Cieniewski-Bernard, Bastide, Lefebvre, Lemoine, Mounier, Michalski (bb0180) 2004; 3 Leung, Hitchen, Ward, Messer, Marston (bb0190) 2013; 288 Gautel (bb0005) 2011; 23 Sihag, Inagaki, Yamaguchi, Shea, Pant (bb0055) 2007; 313 Stevens, Bastide, Hedou, Cieniewski-Bernard, Montel, Cochon, Dupont, Mounier (bb0155) 2013; 540 Zachara, Vosseller, Hart (bb0215) 2011 Zeidan, Hart (bb0060) 2010; 123 Ngoh, Facundo, Zafir, Jones (bb0130) 2010; 107 Yin, Cuello, Mayr, Hao, Hornshaw, Ehler, Avkiran, Mayr (bb0225) 2010; 9 Clark, McElhinny, Beckerle, Gregorio (bb0020) 2002; 18 Kawano, Fujita, Nakai, Terada, Ohira, Ohira (bb0355) 2012; 112 Fardini, Dehennaut, Lefebvre, Issad (bb0115) 2013; 4 Boonyarom, Inui (bb0015) 2006; 188 Lazarus, Love, Hanover (bb0120) 2009; 41 Lovering, O'Neill, Muriel, Prosser, Strong, Bloch (bb0260) 2011; 300 Ramirez-Correa, MA, Slawson, Zeidan, Lugo-Fagundo, Xu, Shen, Gao, Caceres, Chakir, Murphy (bb0255) 2015; 64 Torres, Hart (bb0075) 1984; 259 Nakamura, Nakano, Nishii, Kaneko, Kusaka (bb0150) 2012; 45 Udaka, Ohmori, Terui, Ohtsuki, Ishiwata, Kurihara, Fukuda (bb0280) 2008; 131 Kim (10.1016/j.bbagen.2016.06.011_bb0245) 2006; 580 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0185) 2009; 30 Capetanaki (10.1016/j.bbagen.2016.06.011_bb0325) 2007; 313 Ramirez-Correa (10.1016/j.bbagen.2016.06.011_bb0385) 2008; 103 Förster (10.1016/j.bbagen.2016.06.011_bb0125) 2014; 1842 Hedou (10.1016/j.bbagen.2016.06.011_bb0170) 2007; 282 Au (10.1016/j.bbagen.2016.06.011_bb0025) 2004; 61 Hanover (10.1016/j.bbagen.2016.06.011_bb0095) 2010; 1800 Hédou (10.1016/j.bbagen.2016.06.011_bb0195) 2009; 9 Boonyarom (10.1016/j.bbagen.2016.06.011_bb0015) 2006; 188 Zachara (10.1016/j.bbagen.2016.06.011_bb0215) 2011 Huang (10.1016/j.bbagen.2016.06.011_bb0310) 1999; 274 Stevens (10.1016/j.bbagen.2016.06.011_bb0155) 2013; 540 Elliott (10.1016/j.bbagen.2016.06.011_bb0250) 2013; 368 Herrmann (10.1016/j.bbagen.2016.06.011_bb0330) 2000; 12 Krishnamoorthy (10.1016/j.bbagen.2016.06.011_bb0365) 2013; 379 Snider (10.1016/j.bbagen.2016.06.011_bb0340) 2014; 15 Ngoh (10.1016/j.bbagen.2016.06.011_bb0130) 2010; 107 Ramirez-Correa (10.1016/j.bbagen.2016.06.011_bb0255) 2015; 64 Udaka (10.1016/j.bbagen.2016.06.011_bb0280) 2008; 131 Lovering (10.1016/j.bbagen.2016.06.011_bb0260) 2011; 300 Zeidan (10.1016/j.bbagen.2016.06.011_bb0060) 2010; 123 Mishra (10.1016/j.bbagen.2016.06.011_bb0065) 2011; 9 Sihag (10.1016/j.bbagen.2016.06.011_bb0055) 2007; 313 Hart (10.1016/j.bbagen.2016.06.011_bb0080) 2007; 446 Fardini (10.1016/j.bbagen.2016.06.011_bb0115) 2013; 4 Sanger (10.1016/j.bbagen.2016.06.011_bb0295) 2008; 1 Huang (10.1016/j.bbagen.2016.06.011_bb0050) 2002; 227 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0175) 2012; 7 Clark (10.1016/j.bbagen.2016.06.011_bb0020) 2002; 18 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0160) 2014; 5 Frank (10.1016/j.bbagen.2016.06.011_bb0035) 2006; 84 Hnia (10.1016/j.bbagen.2016.06.011_bb0360) 2014; 49 Farach (10.1016/j.bbagen.2016.06.011_bb0200) 2008; 36 Granzier (10.1016/j.bbagen.2016.06.011_bb0275) 2014; 111 Schamel (10.1016/j.bbagen.2016.06.011_bb0230) 2008 Sanger (10.1016/j.bbagen.2016.06.011_bb0010) 2010; 2010 Dong (10.1016/j.bbagen.2016.06.011_bb0100) 1994; 269 Burattini (10.1016/j.bbagen.2016.06.011_bb0240) 2004; 48 Hart (10.1016/j.bbagen.2016.06.011_bb0070) 2011; 80 Ise (10.1016/j.bbagen.2016.06.011_bb0210) 2010; 20 Ji (10.1016/j.bbagen.2016.06.011_bb0350) 2011; 40 Dassanayaka (10.1016/j.bbagen.2016.06.011_bb0135) 2014; 142 Yin (10.1016/j.bbagen.2016.06.011_bb0225) 2010; 9 Witt (10.1016/j.bbagen.2016.06.011_bb0265) 2006; 25 de A. Ribeiro (10.1016/j.bbagen.2016.06.011_bb0305) 2014; 159 Winter (10.1016/j.bbagen.2016.06.011_bb0335) 2014; 141 Mamczur (10.1016/j.bbagen.2016.06.011_bb0290) 2005; 579 Akimoto (10.1016/j.bbagen.2016.06.011_bb0105) 2011; 8 Lazarus (10.1016/j.bbagen.2016.06.011_bb0120) 2009; 41 Srikanth (10.1016/j.bbagen.2016.06.011_bb0345) 2010; 285 Slawson (10.1016/j.bbagen.2016.06.011_bb0205) 2008; 19 Butkinaree (10.1016/j.bbagen.2016.06.011_bb0285) 2010; 1800 Houck (10.1016/j.bbagen.2016.06.011_bb0370) 2011; 6 Slawson (10.1016/j.bbagen.2016.06.011_bb0110) 2012; 11 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0140) 2006; 100 Huang (10.1016/j.bbagen.2016.06.011_bb0145) 2011; 300 Nakamura (10.1016/j.bbagen.2016.06.011_bb0150) 2012; 45 Paulin (10.1016/j.bbagen.2016.06.011_bb0320) 2004; 301 Gu (10.1016/j.bbagen.2016.06.011_bb0085) 2011; 505 Yuzwa (10.1016/j.bbagen.2016.06.011_bb0220) 2008; 4 Dráb (10.1016/j.bbagen.2016.06.011_bb0235) 2011; 34 Lange (10.1016/j.bbagen.2016.06.011_bb0030) 2006; 16 Obermann (10.1016/j.bbagen.2016.06.011_bb0040) 1997; 16 Kawano (10.1016/j.bbagen.2016.06.011_bb0355) 2012; 112 Selcen (10.1016/j.bbagen.2016.06.011_bb0375) 2011; 21 Huang (10.1016/j.bbagen.2016.06.011_bb0315) 2012; 01 Gautel (10.1016/j.bbagen.2016.06.011_bb0005) 2011; 23 Knöll (10.1016/j.bbagen.2016.06.011_bb0380) 2011; 2011 Leung (10.1016/j.bbagen.2016.06.011_bb0190) 2013; 288 Sadikot (10.1016/j.bbagen.2016.06.011_bb0045) 2010; 239 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0165) 2014; 466 Torres (10.1016/j.bbagen.2016.06.011_bb0075) 1984; 259 Cieniewski-Bernard (10.1016/j.bbagen.2016.06.011_bb0180) 2004; 3 Sjöblom (10.1016/j.bbagen.2016.06.011_bb0300) 2008; 65 Haltiwanger (10.1016/j.bbagen.2016.06.011_bb0090) 1990; 265 Tonino (10.1016/j.bbagen.2016.06.011_bb0270) 2010; 123 |
| References_xml | – volume: 16 start-page: 211 year: 1997 end-page: 220 ident: bb0040 article-title: Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin publication-title: EMBO J. – volume: 274 start-page: 12803 year: 1999 end-page: 12810 ident: bb0310 article-title: Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin: regulation by conformational change publication-title: J. Biol. Chem. – volume: 01 year: 2012 ident: bb0315 article-title: Ezrin/radixin/moesin proteins in the development of diabetes and its cardiovascular complications publication-title: J. Diabetes Metab. – volume: 41 start-page: 2134 year: 2009 end-page: 2146 ident: bb0120 article-title: -GlcNAc cycling: implications for neurodegenerative disorders publication-title: J. Biochem. Cell Biol. – volume: 1800 start-page: 80 year: 2010 end-page: 95 ident: bb0095 article-title: The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine publication-title: Biochim. Biophys. Acta – volume: 580 start-page: 2311 year: 2006 end-page: 2316 ident: bb0245 article-title: Heat shock protein 60 modified with publication-title: FEBS Lett. – volume: 300 start-page: C456 year: 2011 end-page: C465 ident: bb0145 article-title: Muscle-specific overexpression of NCOATGK, splice variant of publication-title: Am. J. Physiol. Cell Physiol. – volume: 111 start-page: 14589 year: 2014 end-page: 14594 ident: bb0275 article-title: Deleting titin's I-band/A-band junction reveals critical roles for titin in biomechanical sensing and cardiac function publication-title: Proc. Natl. Acad. Sci. – volume: 8 start-page: 15 year: 2011 ident: bb0105 article-title: Morphological changes in diabetic kidney are associated with increased publication-title: Clin. Proteomics – volume: 49 year: 2014 ident: bb0360 article-title: Desmin in muscle and associated diseases: beyond the structural function publication-title: Cell Tissue Res. – volume: 466 start-page: 2139 year: 2014 end-page: 2151 ident: bb0165 article-title: Phospho-GlcNAc modulation of slow MLC2 during soleus atrophy through a multienzymatic and sarcomeric complex publication-title: Pflugers Arch. - Eur. J. Physiol. – volume: 131 start-page: 33 year: 2008 end-page: 41 ident: bb0280 article-title: Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization publication-title: J. Gen. Physiol. – volume: 159 start-page: 1447 year: 2014 end-page: 1460 ident: bb0305 article-title: The structure and regulation of human muscle α-actinin publication-title: Cell – year: 2011 ident: bb0215 article-title: Detection and analysis of proteins modified by publication-title: Curr. Protoc. Protein Sci. – volume: 21 start-page: 161 year: 2011 end-page: 171 ident: bb0375 article-title: Myofibrillar myopathies publication-title: Neuromuscul. Disord. – volume: 2010 year: 2010 ident: bb0010 article-title: Assembly and dynamics of myofibrils publication-title: J. Biomed. Biotechnol. – volume: 4 start-page: 1 year: 2013 end-page: 14 ident: bb0115 article-title: -GlcNAcylation: a new cancer hallmark? publication-title: Front. Endocrinol. (Lausanne) – volume: 282 start-page: 10360 year: 2007 end-page: 10369 ident: bb0170 article-title: -linked publication-title: J. Biol. Chem. – volume: 313 start-page: 2098 year: 2007 end-page: 2109 ident: bb0055 article-title: Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments publication-title: Exp. Cell Res. – volume: 227 start-page: 1039 year: 2002 end-page: 1046 ident: bb0050 article-title: Protein kinase C-mediated desmin phosphorylation is related to myofibril disarray in cardiomyopathic hamster heart publication-title: Exp. Biol. Med. (Maywood) – volume: 103 start-page: 1354 year: 2008 end-page: 1358 ident: bb0385 article-title: -linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function publication-title: Circ. Res. – volume: 300 start-page: C803 year: 2011 end-page: C813 ident: bb0260 article-title: Physiology, structure, and susceptibility to injury of skeletal muscle in mice lacking keratin 19-based and desmin-based intermediate filaments publication-title: Am. J. Physiol. Cell Physiol. – volume: 313 start-page: 2063 year: 2007 end-page: 2076 ident: bb0325 article-title: Muscle intermediate filaments and their links to membranes and membranous organelles publication-title: Exp. Cell Res. – volume: 5 start-page: 1 year: 2014 end-page: 7 ident: bb0160 article-title: -GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle publication-title: Front. Physiol. – volume: 65 start-page: 2688 year: 2008 end-page: 2701 ident: bb0300 article-title: α-Actinin structure and regulation publication-title: Cell. Mol. Life Sci. – volume: 259 start-page: 3308 year: 1984 end-page: 3317 ident: bb0075 article-title: Topography and polypeptide distribution of terminal publication-title: J. Biol. Chem. – volume: 36 start-page: 191 year: 2008 end-page: 202 ident: bb0200 article-title: -GlcNAc modification of radial glial vimentin filaments in the developing chick brain publication-title: Brain Cell Biol. – volume: 540 start-page: 125 year: 2013 end-page: 132 ident: bb0155 article-title: Potential regulation of human muscle plasticity by MLC2 post-translational modifications during bed rest and countermeasures publication-title: Arch. Biochem. Biophys. – volume: 40 start-page: 809 year: 2011 end-page: 818 ident: bb0350 article-title: -GlcNAcylation of tubulin inhibits its polymerization publication-title: Amino Acids – volume: 48 start-page: 223 year: 2004 end-page: 233 ident: bb0240 article-title: C2C12 murine myoblasts as a model of skeletal muscle development: morpho-functional characterization publication-title: Eur. J. Histochem. – volume: 12 start-page: 79 year: 2000 end-page: 90 ident: bb0330 article-title: Intermediate filaments and their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics publication-title: Curr. Opin. Cell Biol. – volume: 288 start-page: 4891 year: 2013 end-page: 4898 ident: bb0190 article-title: Z-band alternatively spliced PDZ motif protein (ZASP) is the major publication-title: J. Biol. Chem. – volume: 1800 start-page: 96 year: 2010 end-page: 106 ident: bb0285 article-title: -linked β- publication-title: Biochim. Biophys. Acta, Gen. Subj. – volume: 18 start-page: 637 year: 2002 end-page: 706 ident: bb0020 article-title: Striated muscle cytoarchitecture: an intricate web of form and function publication-title: Annu. Rev. Cell Dev. Biol. – volume: 64 start-page: 3573 year: 2015 end-page: 3587 ident: bb0255 article-title: Removal of abnormal myofilament publication-title: Diabetes – volume: 9 start-page: 2139 year: 2009 end-page: 2148 ident: bb0195 article-title: Mapping of publication-title: Proteomics – volume: 2011 start-page: 569628 year: 2011 ident: bb0380 article-title: The sarcomeric Z-disc and Z-discopathies publication-title: J. Biomed. Biotechnol. – volume: 1842 start-page: 1333 year: 2014 end-page: 1339 ident: bb0125 article-title: Increased publication-title: Biochim. Biophys. Acta Mol. basis Dis. – volume: 505 start-page: 98 year: 2011 end-page: 104 ident: bb0085 article-title: Altered publication-title: Arch. Biochem. Biophys. – volume: 9 start-page: 1 year: 2011 ident: bb0065 article-title: -GlcNAc modification: why so intimately associated with phosphorylation? publication-title: Cell Commun. Signal – volume: 265 start-page: 2563 year: 1990 end-page: 2568 ident: bb0090 article-title: Enzymatic addition of publication-title: J. Biol. Chem. – volume: 15 start-page: 163 year: 2014 end-page: 177 ident: bb0340 article-title: Postranslational modifications of intermediate filament proteins: mechanisms and functions publication-title: Nat. Rev. Mol. Cell Biol. – volume: 4 start-page: 483 year: 2008 end-page: 490 ident: bb0220 article-title: A potent mechanism-inspired publication-title: Nat. Chem. Biol. – volume: 368 start-page: 20120375 year: 2013 ident: bb0250 article-title: The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability publication-title: Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. – volume: 379 start-page: 59 year: 2013 end-page: 68 ident: bb0365 article-title: -GlcNAcylation of publication-title: Mol. Cell. Biochem. – volume: 188 start-page: 77 year: 2006 end-page: 89 ident: bb0015 article-title: Atrophy and hypertrophy of skeletal muscles: structural and functional aspects publication-title: Acta Physiol. – volume: 3 start-page: 577 year: 2004 end-page: 585 ident: bb0180 article-title: Identification of publication-title: Mol. Cell. Proteomics – volume: 25 start-page: 3843 year: 2006 end-page: 3855 ident: bb0265 article-title: Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo publication-title: EMBO J. – volume: 61 start-page: 3016 year: 2004 end-page: 3033 ident: bb0025 article-title: The muscle ultrastructure: a structural perspective of the sarcomere publication-title: Cell. Mol. Life Sci. – volume: 123 start-page: 13 year: 2010 end-page: 22 ident: bb0060 article-title: The intersections between publication-title: J. Cell Sci. – volume: 301 start-page: 1 year: 2004 end-page: 7 ident: bb0320 article-title: Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle publication-title: Exp. Cell Res. – volume: 100 start-page: 1499 year: 2006 end-page: 1505 ident: bb0140 article-title: -GlcNAc level variations are associated with the development of skeletal muscle atrophy publication-title: J. Appl. Physiol. – volume: 80 start-page: 825 year: 2011 end-page: 858 ident: bb0070 article-title: Cross talk between publication-title: Annu. Rev. Biochem. – volume: 142 start-page: 62 year: 2014 end-page: 71 ident: bb0135 article-title: -GlcNAc and the cardiovascular system publication-title: Pharmacol. Ther. – volume: 446 start-page: 1017 year: 2007 end-page: 1022 ident: bb0080 article-title: Cycling of publication-title: Nature – volume: 84 start-page: 446 year: 2006 end-page: 468 ident: bb0035 article-title: The sarcomeric Z-disc: a nodal point in signalling and disease publication-title: J. Mol. Med. – volume: 45 start-page: 86 year: 2012 end-page: 90 ident: bb0150 article-title: Localization of publication-title: Med. Mol. Morphol. – volume: 1 start-page: pe37 year: 2008 ident: bb0295 article-title: The dynamic Z bands of striated muscle cells publication-title: Sci. Signal. – volume: 7 year: 2012 ident: bb0175 article-title: Increasing publication-title: PLoS One – volume: 19 start-page: 4130 year: 2008 end-page: 4140 ident: bb0205 article-title: A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin publication-title: Mol. Biol. Cell – volume: 34 start-page: 1692 year: 2011 end-page: 1695 ident: bb0235 article-title: Native polyacrylamide electrophoresis in the presence of Ponceau Red to study oligomeric states of protein complexes publication-title: J. Sep. Sci. – volume: 269 start-page: 19321 year: 1994 end-page: 19330 ident: bb0100 article-title: Purification and characterization of an publication-title: J. Biol. Chem. – volume: 6 year: 2011 ident: bb0370 article-title: Multiple sites in publication-title: PLoS One – volume: 579 start-page: 1607 year: 2005 end-page: 1612 ident: bb0290 article-title: The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle publication-title: FEBS Lett. – volume: 285 start-page: 34062 year: 2010 end-page: 34071 ident: bb0345 article-title: -GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18 publication-title: J. Biol. Chem. – volume: 112 start-page: 176 year: 2012 end-page: 186 ident: bb0355 article-title: HSP25 can modulate myofibrillar desmin cytoskeleton following the phosphorylation at Ser15 in rat soleus muscle publication-title: J. Appl. Physiol. – volume: 9 start-page: 497 year: 2010 end-page: 509 ident: bb0225 article-title: Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution publication-title: Mol. Cell. Proteomics – volume: 16 start-page: 11 year: 2006 end-page: 18 ident: bb0030 article-title: From a to Z and back? Multicompartment proteins in the sarcomere publication-title: Trends Cell Biol. – volume: 11 start-page: 678 year: 2012 end-page: 684 ident: bb0110 article-title: -GlcNAc signalling – volume: 123 start-page: 384 year: 2010 end-page: 391 ident: bb0270 article-title: Reduced myofibrillar connectivity and increased Z-disk width in nebulin-deficient skeletal muscle publication-title: J. Cell Sci. – volume: 23 start-page: 39 year: 2011 end-page: 46 ident: bb0005 article-title: The sarcomeric cytoskeleton: who picks up the strain? publication-title: Curr. Opin. Cell Biol. – volume: 141 start-page: 1 year: 2014 end-page: 16 ident: bb0335 article-title: Posttranslational modifications of desmin and their implication in biological processes and pathologies publication-title: Histochem. Cell Biol. – year: 2008 ident: bb0230 article-title: Two-dimensional blue native polyacrylamide gel electrophoresis publication-title: Curr. Protoc. Cell Biol. – volume: 30 start-page: 281 year: 2009 end-page: 287 ident: bb0185 article-title: -GlcNAcylation, an original modulator of contractile activity in striated muscle publication-title: J. Muscle Res. Cell Motil. – volume: 107 start-page: 171 year: 2010 end-page: 185 ident: bb0130 article-title: -GlcNAc signaling in the cardiovascular system publication-title: Circ. Res. – volume: 20 start-page: 843 year: 2010 end-page: 864 ident: bb0210 article-title: Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces publication-title: Glycobiology – volume: 239 start-page: 1124 year: 2010 end-page: 1135 ident: bb0045 article-title: Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance publication-title: Dev. Dyn. – volume: 300 start-page: C456 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0145 article-title: Muscle-specific overexpression of NCOATGK, splice variant of O-GlcNAcase, induces skeletal muscle atrophy publication-title: Am. J. Physiol. Cell Physiol. doi: 10.1152/ajpcell.00124.2010 – volume: 2011 start-page: 569628 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0380 article-title: The sarcomeric Z-disc and Z-discopathies publication-title: J. Biomed. Biotechnol. doi: 10.1155/2011/569628 – year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0230 article-title: Two-dimensional blue native polyacrylamide gel electrophoresis publication-title: Curr. Protoc. Cell Biol. doi: 10.1002/0471143030.cb0610s38 – volume: 1 start-page: pe37 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0295 article-title: The dynamic Z bands of striated muscle cells publication-title: Sci. Signal. doi: 10.1126/scisignal.132pe37 – volume: 20 start-page: 843 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0210 article-title: Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces publication-title: Glycobiology doi: 10.1093/glycob/cwq039 – volume: 48 start-page: 223 year: 2004 ident: 10.1016/j.bbagen.2016.06.011_bb0240 article-title: C2C12 murine myoblasts as a model of skeletal muscle development: morpho-functional characterization publication-title: Eur. J. Histochem. – volume: 1800 start-page: 96 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0285 article-title: O-linked β-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress publication-title: Biochim. Biophys. Acta, Gen. Subj. doi: 10.1016/j.bbagen.2009.07.018 – volume: 34 start-page: 1692 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0235 article-title: Native polyacrylamide electrophoresis in the presence of Ponceau Red to study oligomeric states of protein complexes publication-title: J. Sep. Sci. doi: 10.1002/jssc.201000869 – volume: 1800 start-page: 80 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0095 article-title: The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagen.2009.07.017 – volume: 45 start-page: 86 year: 2012 ident: 10.1016/j.bbagen.2016.06.011_bb0150 article-title: Localization of O-GlcNAc-modified proteins in neuromuscular diseases publication-title: Med. Mol. Morphol. doi: 10.1007/s00795-011-0542-7 – volume: 142 start-page: 62 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0135 article-title: O-GlcNAc and the cardiovascular system publication-title: Pharmacol. Ther. doi: 10.1016/j.pharmthera.2013.11.005 – volume: 131 start-page: 33 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0280 article-title: Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization publication-title: J. Gen. Physiol. doi: 10.1085/jgp.200709888 – volume: 285 start-page: 34062 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0345 article-title: O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.098996 – volume: 16 start-page: 11 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0030 article-title: From a to Z and back? Multicompartment proteins in the sarcomere publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2005.11.007 – volume: 123 start-page: 13 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0060 article-title: The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways publication-title: J. Cell Sci. doi: 10.1242/jcs.053678 – volume: 25 start-page: 3843 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0265 article-title: Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo publication-title: EMBO J. doi: 10.1038/sj.emboj.7601242 – volume: 188 start-page: 77 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0015 article-title: Atrophy and hypertrophy of skeletal muscles: structural and functional aspects publication-title: Acta Physiol. doi: 10.1111/j.1748-1716.2006.01613.x – volume: 107 start-page: 171 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0130 article-title: O-GlcNAc signaling in the cardiovascular system publication-title: Circ. Res. doi: 10.1161/CIRCRESAHA.110.224675 – volume: 300 start-page: C803 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0260 article-title: Physiology, structure, and susceptibility to injury of skeletal muscle in mice lacking keratin 19-based and desmin-based intermediate filaments publication-title: Am. J. Physiol. Cell Physiol. doi: 10.1152/ajpcell.00394.2010 – volume: 8 start-page: 15 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0105 article-title: Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4 publication-title: Clin. Proteomics doi: 10.1186/1559-0275-8-15 – volume: 227 start-page: 1039 year: 2002 ident: 10.1016/j.bbagen.2016.06.011_bb0050 article-title: Protein kinase C-mediated desmin phosphorylation is related to myofibril disarray in cardiomyopathic hamster heart publication-title: Exp. Biol. Med. (Maywood) doi: 10.1177/153537020222701113 – volume: 540 start-page: 125 year: 2013 ident: 10.1016/j.bbagen.2016.06.011_bb0155 article-title: Potential regulation of human muscle plasticity by MLC2 post-translational modifications during bed rest and countermeasures publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2013.10.016 – volume: 265 start-page: 2563 year: 1990 ident: 10.1016/j.bbagen.2016.06.011_bb0090 article-title: Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)39838-2 – volume: 5 start-page: 1 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0160 article-title: O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle publication-title: Front. Physiol. doi: 10.3389/fphys.2014.00421 – volume: 9 start-page: 2139 year: 2009 ident: 10.1016/j.bbagen.2016.06.011_bb0195 article-title: Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle publication-title: Proteomics doi: 10.1002/pmic.200800617 – volume: 01 year: 2012 ident: 10.1016/j.bbagen.2016.06.011_bb0315 article-title: Ezrin/radixin/moesin proteins in the development of diabetes and its cardiovascular complications publication-title: J. Diabetes Metab. doi: 10.4172/2155-6156.S4-005 – volume: 9 start-page: 497 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0225 article-title: Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M900275-MCP200 – volume: 112 start-page: 176 year: 2012 ident: 10.1016/j.bbagen.2016.06.011_bb0355 article-title: HSP25 can modulate myofibrillar desmin cytoskeleton following the phosphorylation at Ser15 in rat soleus muscle publication-title: J. Appl. Physiol. doi: 10.1152/japplphysiol.00783.2011 – volume: 49 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0360 article-title: Desmin in muscle and associated diseases: beyond the structural function publication-title: Cell Tissue Res. – volume: 505 start-page: 98 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0085 article-title: Altered O-GlcNAc modification and phosphorylation of mitochondrial proteins in myoblast cells exposed to high glucose publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2010.09.024 – volume: 6 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0370 article-title: Multiple sites inalphaB-crystallin modulate its interactions with desmin filaments assembled in vitro publication-title: PLoS One doi: 10.1371/journal.pone.0025859 – volume: 368 start-page: 20120375 year: 2013 ident: 10.1016/j.bbagen.2016.06.011_bb0250 article-title: The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability publication-title: Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. doi: 10.1098/rstb.2012.0375 – volume: 466 start-page: 2139 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0165 article-title: Phospho-GlcNAc modulation of slow MLC2 during soleus atrophy through a multienzymatic and sarcomeric complex publication-title: Pflugers Arch. - Eur. J. Physiol. doi: 10.1007/s00424-014-1453-y – volume: 64 start-page: 3573 year: 2015 ident: 10.1016/j.bbagen.2016.06.011_bb0255 article-title: Removal of abnormal myofilament O-GlcNAcylation restores Ca2+ sensitivity in diabetic cardiac muscle publication-title: Diabetes doi: 10.2337/db14-1107 – volume: 141 start-page: 1 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0335 article-title: Posttranslational modifications of desmin and their implication in biological processes and pathologies publication-title: Histochem. Cell Biol. doi: 10.1007/s00418-013-1148-z – volume: 21 start-page: 161 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0375 article-title: Myofibrillar myopathies publication-title: Neuromuscul. Disord. doi: 10.1016/j.nmd.2010.12.007 – volume: 580 start-page: 2311 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0245 article-title: Heat shock protein 60 modified with O-linked N-acetylglucosamine is involved in pancreatic β-cell death under hyperglycemic conditions publication-title: FEBS Lett. doi: 10.1016/j.febslet.2006.03.043 – volume: 239 start-page: 1124 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0045 article-title: Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance publication-title: Dev. Dyn. doi: 10.1002/dvdy.22263 – volume: 1842 start-page: 1333 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0125 article-title: Increased O-GlcNAc levels correlate with decreased O-GlcNAcase levels in Alzheimer disease brain publication-title: Biochim. Biophys. Acta Mol. basis Dis. doi: 10.1016/j.bbadis.2014.05.014 – volume: 4 start-page: 1 year: 2013 ident: 10.1016/j.bbagen.2016.06.011_bb0115 article-title: O-GlcNAcylation: a new cancer hallmark? publication-title: Front. Endocrinol. (Lausanne) doi: 10.3389/fendo.2013.00099 – volume: 379 start-page: 59 year: 2013 ident: 10.1016/j.bbagen.2016.06.011_bb0365 article-title: O-GlcNAcylation ofalphab-crystallin regulates its stress-induced translocation and cytoprotection publication-title: Mol. Cell. Biochem. doi: 10.1007/s11010-013-1627-5 – volume: 12 start-page: 79 year: 2000 ident: 10.1016/j.bbagen.2016.06.011_bb0330 article-title: Intermediate filaments and their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics publication-title: Curr. Opin. Cell Biol. doi: 10.1016/S0955-0674(99)00060-5 – volume: 288 start-page: 4891 year: 2013 ident: 10.1016/j.bbagen.2016.06.011_bb0190 article-title: Z-band alternatively spliced PDZ motif protein (ZASP) is the major o-linkedbeta-N-acetylglucosamine-substituted protein in human heart myofibrils publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.410316 – volume: 65 start-page: 2688 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0300 article-title: α-Actinin structure and regulation publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-008-8080-8 – volume: 3 start-page: 577 year: 2004 ident: 10.1016/j.bbagen.2016.06.011_bb0180 article-title: Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M400024-MCP200 – volume: 274 start-page: 12803 year: 1999 ident: 10.1016/j.bbagen.2016.06.011_bb0310 article-title: Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin: regulation by conformational change publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.18.12803 – volume: 9 start-page: 1 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0065 article-title: O-GlcNAc modification: why so intimately associated with phosphorylation? publication-title: Cell Commun. Signal doi: 10.1186/1478-811X-9-1 – volume: 15 start-page: 163 issue: 3 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0340 article-title: Postranslational modifications of intermediate filament proteins: mechanisms and functions publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3753 – volume: 269 start-page: 19321 year: 1994 ident: 10.1016/j.bbagen.2016.06.011_bb0100 article-title: Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)32170-1 – volume: 18 start-page: 637 year: 2002 ident: 10.1016/j.bbagen.2016.06.011_bb0020 article-title: Striated muscle cytoarchitecture: an intricate web of form and function publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev.cellbio.18.012502.105840 – volume: 84 start-page: 446 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0035 article-title: The sarcomeric Z-disc: a nodal point in signalling and disease publication-title: J. Mol. Med. doi: 10.1007/s00109-005-0033-1 – volume: 301 start-page: 1 year: 2004 ident: 10.1016/j.bbagen.2016.06.011_bb0320 article-title: Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2004.08.004 – volume: 7 year: 2012 ident: 10.1016/j.bbagen.2016.06.011_bb0175 article-title: Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers publication-title: PLoS One doi: 10.1371/journal.pone.0048218 – volume: 313 start-page: 2063 year: 2007 ident: 10.1016/j.bbagen.2016.06.011_bb0325 article-title: Muscle intermediate filaments and their links to membranes and membranous organelles publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2007.03.033 – volume: 259 start-page: 3308 year: 1984 ident: 10.1016/j.bbagen.2016.06.011_bb0075 article-title: Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)43295-9 – volume: 159 start-page: 1447 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0305 article-title: The structure and regulation of human muscle α-actinin publication-title: Cell doi: 10.1016/j.cell.2014.10.056 – volume: 2010 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0010 article-title: Assembly and dynamics of myofibrils publication-title: J. Biomed. Biotechnol. doi: 10.1155/2010/858606 – volume: 19 start-page: 4130 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0205 article-title: A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e07-11-1146 – year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0215 article-title: Detection and analysis of proteins modified by O-linked N-acetylglucosamine publication-title: Curr. Protoc. Protein Sci. doi: 10.1002/0471140864.ps1208s66 – volume: 61 start-page: 3016 year: 2004 ident: 10.1016/j.bbagen.2016.06.011_bb0025 article-title: The muscle ultrastructure: a structural perspective of the sarcomere publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-004-4282-x – volume: 36 start-page: 191 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0200 article-title: O-GlcNAc modification of radial glial vimentin filaments in the developing chick brain publication-title: Brain Cell Biol. doi: 10.1007/s11068-008-9036-5 – volume: 16 start-page: 211 year: 1997 ident: 10.1016/j.bbagen.2016.06.011_bb0040 article-title: Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin publication-title: EMBO J. doi: 10.1093/emboj/16.2.211 – volume: 4 start-page: 483 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0220 article-title: A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.96 – volume: 41 start-page: 2134 year: 2009 ident: 10.1016/j.bbagen.2016.06.011_bb0120 article-title: O-GlcNAc cycling: implications for neurodegenerative disorders publication-title: J. Biochem. Cell Biol. doi: 10.1016/j.biocel.2009.03.008 – volume: 100 start-page: 1499 year: 2006 ident: 10.1016/j.bbagen.2016.06.011_bb0140 article-title: O-GlcNAc level variations are associated with the development of skeletal muscle atrophy publication-title: J. Appl. Physiol. doi: 10.1152/japplphysiol.00865.2005 – volume: 123 start-page: 384 year: 2010 ident: 10.1016/j.bbagen.2016.06.011_bb0270 article-title: Reduced myofibrillar connectivity and increased Z-disk width in nebulin-deficient skeletal muscle publication-title: J. Cell Sci. doi: 10.1242/jcs.042234 – volume: 40 start-page: 809 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0350 article-title: O-GlcNAcylation of tubulin inhibits its polymerization publication-title: Amino Acids doi: 10.1007/s00726-010-0698-9 – volume: 446 start-page: 1017 year: 2007 ident: 10.1016/j.bbagen.2016.06.011_bb0080 article-title: Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins publication-title: Nature doi: 10.1038/nature05815 – volume: 579 start-page: 1607 year: 2005 ident: 10.1016/j.bbagen.2016.06.011_bb0290 article-title: The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle publication-title: FEBS Lett. doi: 10.1016/j.febslet.2005.01.071 – volume: 23 start-page: 39 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0005 article-title: The sarcomeric cytoskeleton: who picks up the strain? publication-title: Curr. Opin. Cell Biol. doi: 10.1016/j.ceb.2010.12.001 – volume: 30 start-page: 281 year: 2009 ident: 10.1016/j.bbagen.2016.06.011_bb0185 article-title: O-GlcNAcylation, an original modulator of contractile activity in striated muscle publication-title: J. Muscle Res. Cell Motil. doi: 10.1007/s10974-010-9201-1 – volume: 313 start-page: 2098 year: 2007 ident: 10.1016/j.bbagen.2016.06.011_bb0055 article-title: Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2007.04.010 – volume: 282 start-page: 10360 year: 2007 ident: 10.1016/j.bbagen.2016.06.011_bb0170 article-title: O-linked N-acetylglucosaminylation is involved in the Ca2+ activation properties of rat skeletal muscle publication-title: J. Biol. Chem. doi: 10.1074/jbc.M606787200 – volume: 11 start-page: 678 year: 2012 ident: 10.1016/j.bbagen.2016.06.011_bb0110 article-title: O-GlcNAc signalling: implications for cancer cell biology – volume: 111 start-page: 14589 year: 2014 ident: 10.1016/j.bbagen.2016.06.011_bb0275 article-title: Deleting titin's I-band/A-band junction reveals critical roles for titin in biomechanical sensing and cardiac function publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1411493111 – volume: 103 start-page: 1354 year: 2008 ident: 10.1016/j.bbagen.2016.06.011_bb0385 article-title: O-linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function publication-title: Circ. Res. doi: 10.1161/CIRCRESAHA.108.184978 – volume: 80 start-page: 825 year: 2011 ident: 10.1016/j.bbagen.2016.06.011_bb0070 article-title: Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-060608-102511 |
| SSID | ssj0000595 ssj0025309 |
| Score | 2.291448 |
| Snippet | The sarcomere structure of skeletal muscle is determined through multiple protein–protein interactions within an intricate sarcomeric cytoskeleton network. The... The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The... |
| SourceID | hal proquest pubmed crossref elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 2017 |
| SubjectTerms | Actinin - metabolism Acylation - drug effects Acylation - physiology Animals Cell Line Crystallins - metabolism cytoskeleton Desmin Desmin - metabolism Life Sciences Mice Microfilament Proteins - metabolism morphometry Muscle Contraction - drug effects Muscle Contraction - physiology Muscle Fibers, Skeletal - metabolism Muscle, Skeletal - drug effects Muscle, Skeletal - metabolism Myofibrils - metabolism neuromuscular disorders O-GlcNAcylation post-translational modification Protein Interaction Maps - drug effects Protein Interaction Maps - physiology Protein Processing, Post-Translational - drug effects Protein Processing, Post-Translational - physiology Protein–protein interactions proteome Proteome - metabolism Pyrans - pharmacology Sarcomere structure sarcomeres Sarcomeres - metabolism skeletal muscle Skeletal muscle cells structural proteins Thiazoles - pharmacology αB-crystallin |
| Title | O-GlcNAcylation is a key modulator of skeletal muscle sarcomeric morphometry associated to modulation of protein–protein interactions |
| URI | https://dx.doi.org/10.1016/j.bbagen.2016.06.011 https://www.ncbi.nlm.nih.gov/pubmed/27301331 https://www.proquest.com/docview/1805485839 https://www.proquest.com/docview/1825430876 https://hal.univ-lille.fr/hal-02375890 |
| Volume | 1860 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELZKEYILgvJaHpVBXM3Gr018XK0oCwuLBFT0ZjmOIxbapNrsIvWCuPUH9B_2l3QmThZxKJU4xYnG4yRjez7L428IeRmUSUMwkinuBFNeKGYSP2LCOV3I4LRsDwp_mI-m--rdgT7YIpP-LAyGVXZzf5zT29m6ezLs_ubweLEYfsZNPYATGhAFOKp2CaRUir381a8_YR4AH3TcSVAMpfvjc22MV57DoEUWVD5qWTw5v8w9XfuGcZKXgdDWGe3dIbc7FEnH8UXvkq1Q7ZAbMa_kyQ65OenTuN0jpx_Zm0M_H_uTGPVGFw11FIYuPaoLzN1VL2ld0uYH-B8A4vRo3YBK2sAAqNvdHJADW0AZ1FHXWTMUdFX3GlArqGgpHxbV-e-zrkSRi2IZT04098n-3usvkynrsi8wrxVfscw4JwpRukSH4FKe-zTRhSpy7XPhfACsYDDZmPYmpKVyxkvHjZNSJmVRKiUfkO2qrsIjQnEZ5JVyqcy1EsJleRY0LjX5KC-9KgdE9j_d-o6aHDNkHNo-Bu27jaayaCqLoXicDwjb1DqO1BxXyKe9Pe1fXcyC97ii5gsw_6YRZOSejt9bfAaQB1ZcJvkJQs_73mHBxLjv4qpQrxvLM8DFmQYo-i8ZZCVAfsABeRi71qY9gbOwlPzxf3_AE3IL72Js3FOyvVquwzMAU6t8tx0tu-T6-O1sOsfr7NPX2QWNRyIu |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELbKVqhcEJTX8jSIq7Xxa5McV6uWlG6XA63Um-U4jlhok2qzi9Qbt_6A_kN-SWfiZBGHUolb5Iwnj7FnPsvjbwj56FUae59KprgVTDmhWBq5MRPW6kJ6q2V7UPhoPs5O1OdTfbpFpv1ZGEyr7Hx_8Omtt-5aRt3fHF0sFqOvuKkHcEIDooBAhUugbWSn0gOyPTk4zOZ_HLJui6-gPMMO_Qm6Ns0rz2HeIhEqH7dEnpzfFqHufcNUydtwaBuP9h-Rhx2QpJPwro_Jlq92yf1QWvJyl-xM-0puT8jVF_bpzM0n7jIkvtFFQy2F2UvP6wLLd9VLWpe0-QEhCLA4PV83oJI2MAfqdkMH5MAccA3qqO0M6gu6qnsNqBVUtKwPi-r3r-vuiiIdxTIcnmiekpP9veNpxroCDMxpxVcsSa0VhShtpL23Mc9dHOlCFbl2ubDOA1xIsd6YdqmPS2VTJy1PrZQyKotSKfmMDKq68i8IxZWQU8rGMtdKCJvkide42uTjvHSqHBLZ_3TjOnZyLJJxZvo0tO8mmMqgqQxm43E-JGzT6yKwc9whH_f2NH-NMgMB5I6eH8D8m4cgKXc2mRlsA9QDi640-glC7_vRYcDEuPViK1-vG8MTgMaJBjT6LxkkJkCKwCF5HobW5nkCHbGU_OV_f8A7spMdH83M7GB--Io8wDshVe41GayWa_8GsNUqf9vNnRtM9yM8 |
| 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=O-GlcNAcylation+is+a+key+modulator+of+skeletal+muscle+sarcomeric+morphometry+associated+to+modulation+of+protein-protein+interactions&rft.jtitle=Biochimica+et+biophysica+acta&rft.au=Lambert%2C+Matthias&rft.au=Richard%2C+Elodie&rft.au=Duban-Deweer%2C+Sophie&rft.au=Krzewinski%2C+Frederic&rft.date=2016-09-01&rft.issn=0006-3002&rft.volume=1860&rft.issue=9&rft.spage=2017&rft_id=info:doi/10.1016%2Fj.bbagen.2016.06.011&rft.externalDBID=NO_FULL_TEXT |
| 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 |