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Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle

PLoS genetics, 2023-05, Vol.19 (5), p.e1010772-e1010772

2023

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The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Nature communications, 2019-03, Vol.10 (1), p.1273-1273, Article 1273

2019

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Structural Basis for Cargo Regulation of COPII Coat Assembly

Cell, 2008-08, Vol.134 (3), p.474-484

2008

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Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

Cell, 2006-11, Vol.127 (4), p.803-815

2006

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Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies

Molecular biology of the cell, 2009-07, Vol.20 (14), p.3273-3284

2009

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The role of cellular proteostasis in antitumor immunity

The Journal of biological chemistry, 2022-05, Vol.298 (5), p.101930-101930, Article 101930

2022

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An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

Nature communications, 2017-05, Vol.8 (1), p.15328-15328, Article 15328

2017

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Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis

Molecular biology of the cell, 2010-03, Vol.21 (6), p.871-884

2010

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Hsp90 inhibition leads to an increase in surface expression of multiple immunological receptors in cancer cells

Frontiers in molecular biosciences, 2024, Vol.11, p.1334876-1334876

2024

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The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922

PloS one, 2012-11, Vol.7 (11), p.e49322

2012

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Macrophages and Epithelial Cells Mutually Interact through NLRP3 to Clear Infection and Enhance the Gastrointestinal Barrier

Immuno, 2022-03, Vol.2 (1), p.13-25

2022

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A Small Molecule Inhibitor of Pex3–Pex19 Interaction Disrupts Glycosome Biogenesis and Causes Lethality in Trypanosoma brucei

Frontiers in cell and developmental biology, 2021-07, Vol.9, p.703603-703603

2021

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Éditorial / Editorial

Relations industrielles (Québec, Québec), 2014-03, Vol.69 (2), p.417-422

Lapointe, Paul-André

2014

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A Role for the Protease-sensitive Loop Region of Shiga-like Toxin 1 in the Retrotranslocation of Its A1 Domain from the Endoplasmic Reticulum Lumen

The Journal of biological chemistry, 2005-06, Vol.280 (24), p.23310-23318

2005

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A novel method for site-specific chemical SUMOylation: SUMOylation of Hsp90 modulates co-chaperone binding in vitro

Biological chemistry, 2019-03, Vol.400 (4), p.487

2019

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The Mechanism of Hsp90 ATPase Stimulation by Aha1

Scientific reports, 2016-09, Vol.6 (1), p.33179-33179, Article 33179

2016

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Petits poèmes animaux

Études françaises (Montreal), 2012, Vol.48 (1), p.21-45

Lapointe, Paul-Marie

2012

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Analysis of co‐chaperone interactions with Hsp90 (567.7)

The FASEB journal, 2014-04, Vol.28 (S1), p.n/a

2014

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Abstract LB-187: Hsp90 inhibitor SNX-2112 enhances neoantigen presentation on the surface of tumor cells

Cancer research (Chicago, Ill.), 2019-07, Vol.79 (13_Supplement), p.LB-187-LB-187

2019

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The Hsp90 Chaperone: 1H and 19F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme

Biochemistry (Easton), 2019-04, Vol.58 (14), p.1869-1877

2019

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The Hsp90 Chaperone: 1 H and 19 F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme

Biochemistry (Easton), 2019-04, Vol.58 (14), p.1869-1877

2019

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The COPII cage: unifying principles of vesicle coat assembly

Nature reviews. Molecular cell biology, 2006-10, Vol.7 (10), p.727-738

2006

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Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells

Molecular biology of the cell, 2013-08, Vol.24 (15), p.2303-2310

2013

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Structure of the Sec13/31 COPII coat cage

Nature, 2006-01, Vol.439 (7073), p.234-238

2006

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The diverse roles of Hsp90 and where to find them

Nature structural & molecular biology, 2017-01, Vol.24 (1), p.1

2017

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Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle

The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Structural Basis for Cargo Regulation of COPII Coat Assembly

Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies

The role of cellular proteostasis in antitumor immunity

An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis

Hsp90 inhibition leads to an increase in surface expression of multiple immunological receptors in cancer cells

The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922

Macrophages and Epithelial Cells Mutually Interact through NLRP3 to Clear Infection and Enhance the Gastrointestinal Barrier

A Small Molecule Inhibitor of Pex3–Pex19 Interaction Disrupts Glycosome Biogenesis and Causes Lethality in Trypanosoma brucei

Éditorial / Editorial

A Role for the Protease-sensitive Loop Region of Shiga-like Toxin 1 in the Retrotranslocation of Its A1 Domain from the Endoplasmic Reticulum Lumen

A novel method for site-specific chemical SUMOylation: SUMOylation of Hsp90 modulates co-chaperone binding in vitro

The Mechanism of Hsp90 ATPase Stimulation by Aha1

Petits poèmes animaux

Analysis of co‐chaperone interactions with Hsp90 (567.7)

Abstract LB-187: Hsp90 inhibitor SNX-2112 enhances neoantigen presentation on the surface of tumor cells

The Hsp90 Chaperone: 1H and 19F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme

The Hsp90 Chaperone: 1 H and 19 F Dynamic Nuclear Magnetic Resonance Spectroscopy Reveals a Perfect Enzyme

The COPII cage: unifying principles of vesicle coat assembly

Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells

Structure of the Sec13/31 COPII coat cage

The diverse roles of Hsp90 and where to find them

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