J. Bergeron

发表

Specific inhibition by hGRB10ζ of insulin-induced glycogen synthase activation: evidence for a novel signaling pathway

David Y. Thomas, C. Mounier, B. Posner, 2001, Molecular and Cellular Endocrinology.

Standard guidelines for the chromosome-centric human proteome project.

S. Hanash, R. Aebersold, A. Bairoch, 2012, Journal of proteome research.

Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57*

David Y. Thomas, D. Tessier, M. Michalak, 1998, The Journal of Biological Chemistry.

Proteomic approaches in brain research and neuropharmacology.

L. Arckens, F. Vandesande, R. Quirion, 2004, European journal of pharmacology.

Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca(*)

David Y. Thomas, J. Bergeron, W. Ou, 1995, The Journal of Biological Chemistry.

Standard Guidelines for the Chromosome-Centric

S. Hanash, A. Bairoch, G. Omenn, 2012 .

Association of folding intermediates of glycoproteins with calnexin during protein maturation

P. H. Cameron, David Y. Thomas, J. Bergeron, 1993, Nature.

Calnexin, an ER Integral Membrane Chaperone in Health and Disease

David Y. Thomas, J. Bergeron, 2003 .

The Roles of Calnexin and Calreticulin as Endoplasmic Reticulum Molecular Chaperones

David Y. Thomas, F. Parlati, J. Bergeron, 1996 .

Proteomics Identifies Golgi phosphoprotein 3 (GOLPH3) with A Link Between Golgi Structure, Cancer, DNA Damage and Protection from Cell Death*

Catherine E. Au, David Y. Thomas, L. Hermo, 2017, Molecular & Cellular Proteomics.

The human proteome project: Current state and future direction.

R. Aebersold, D. Hochstrasser, A. Bairoch, 2011, Molecular & cellular proteomics : MCP.

Conformation-Independent Binding of Monoglucosylated Ribonuclease B to Calnexin

Pauline M Rudd, Raymond A Dwek, R. Dwek, 1997, Cell.

Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes

P. H. Cameron, E. Chevet, D. Y. Thomas, 1999, The EMBO journal.

Protein quality control in the ER: the recognition of misfolded proteins.

Kalle Gehring, David Y. Thomas, K. Gehring, 2010, Seminars in cell & developmental biology.

Dark side of the epididymis: tails of sperm maturation

L. Hermo, J. Bergeron, R. L. Oliveira, 2019, Andrology.

The Human Proteome Project: Current State and Future Direction

Cathy H. Wu, Sudhir Srivastava, Christoph H Borchers, 2011, Molecular & Cellular Proteomics.

Brain-specific Proteins Decline in the Cerebrospinal Fluid of Humans with Huntington Disease

Damon H. May, S. Hanash, B. Leavitt, 2009, Molecular & Cellular Proteomics.

Ca2+ Regulation of Interactions between Endoplasmic Reticulum Chaperones*

K. Krause, David Y. Thomas, D. Tessier, 1999, The Journal of Biological Chemistry.

Calnexin Phosphorylation Attenuates the Release of Partially Misfolded α1-Antitrypsin to the Secretory Pathway*

P. H. Cameron, David Y. Thomas, O. Pluquet, 2009, The Journal of Biological Chemistry.

The ER protein folding sensor UDP-glucose glycoprotein–glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation

David Y. Thomas, A. Ferguson, J. Bergeron, 2004, Nature Structural &Molecular Biology.

An organelle proteomic method to study neurotransmission‐related proteins, applied to a neurodevelopmental model of schizophrenia

L. Arckens, R. Quirion, J. Chabot, 2007, Proteomics.

Glycopeptide specificity of the secretory protein folding sensor UDP–glucose glycoprotein:glucosyltransferase

David Y. Thomas, D. Tessier, P. Thibault, 2003, EMBO reports.

The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

D. Y. Thomas, Y. Li, J. Schrag, 2001, Molecular cell.

The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation.

P. H. Cameron, E. Chevet, D. Y. Thomas, 2001, Current opinion in structural biology.

Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.

D. Y. Thomas, J. Bergeron, J. Bergeron, 1994, Trends in biochemical sciences.

Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complex.

M. Marzioch, D. Y. Thomas, J. Bergeron, 1999, Molecular biology of the cell.

N‐glycosylation mediated folding and quality control in serine proteases of the hepsin family

J. Bergeron, D. Thomas, 2023, The FEBS journal.

Protein folding in a specialized compartment: the endoplasmic reticulum.

D. Y. Thomas, J. Bergeron, J. Bergeron, 1999, Structure.

Association of calnexin with mutant peripheral myelin protein-22 ex vivo: A basis for “gain-of-function” ER diseases

Keith D. Dickson, D. Y. Thomas, J. Bergeron, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Lectins of the ER quality control machinery.

E. Chevet, D. Y. Thomas, J. Bergeron, 2001, Results and problems in cell differentiation.

Calnexin family members as modulators of genetic diseases.

E. Chevet, D. Y. Thomas, J. Bergeron, 1999, Seminars in cell & developmental biology.

SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane.

P. H. Cameron, D. Dignard, D. Y. Thomas, 1991, The Journal of biological chemistry.

The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.

R. Ménard, D. Tessier, E. Chevet, 2000, Glycobiology.