O-GlcNAcylation is a key modulator of skeletal muscle sarcomeric morphometry associated to modulation of protein–protein interactions-Reference-Cited by-同舟云学术

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O-GlcNAcylation is a key modulator of skeletal muscle sarcomeric morphometry associated to modulation of protein–protein interactions

Published:2016-09 Issue:9 Volume:1860 Page:2017-2030
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Lambert Matthias,Richard Elodie,Duban-Deweer Sophie,Krzewinski Frederic,Deracinois Barbara,Dupont Erwan,Bastide Bruno,Cieniewski-Bernard Caroline

Funder

Région Nord-Pas-de-Calais 2011

Centre National d'Etudes Spatiales

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference77 articles.

1. The sarcomeric cytoskeleton: who picks up the strain?;Gautel;Curr. Opin. Cell Biol.,2011

2. Assembly and dynamics of myofibrils;Sanger;J. Biomed. Biotechnol.,2010

3. Atrophy and hypertrophy of skeletal muscles: structural and functional aspects;Boonyarom;Acta Physiol.,2006

4. Striated muscle cytoarchitecture: an intricate web of form and function;Clark;Annu. Rev. Cell Dev. Biol.,2002

5. The muscle ultrastructure: a structural perspective of the sarcomere;Au;Cell. Mol. Life Sci.,2004

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1. O-GlcNAcylation of SERCA protects skeletal muscle in hibernating Spermophilus dauricus from disuse atrophy;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2025-01

2. A novel 2D‐electrophoresis method for the simultaneous visualization of phosphorylated and O‐GlcNAcylated proteoforms of a protein;ELECTROPHORESIS;2024-05-03

3. Impact of MG132 induced-proteotoxic stress on αB-crystallin and desmin phosphorylation and O-GlcNAcylation and their partition towards cytoskeleton;Biochimie;2024-04

4. Desmin and its molecular chaperone, the αB-crystallin: How post-translational modifications modulate their functions in heart and skeletal muscles?;Biochimie;2024-01

5. Extracellular vimentin is sufficient to promote cell attachment, spreading, and motility by a mechanism involving N-acetyl glucosamine-containing structures;Journal of Biological Chemistry;2023-08

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