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Extracellular chaperones and proteostasis

Annual review of biochemistry, 2013-01, Vol.82 (1), p.295-322

2013

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PZP and PAI-2: Structurally-diverse, functionally similar pregnancy proteins?

The international journal of biochemistry & cell biology, 2016-10, Vol.79, p.113-117

2016

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Hypochlorite-induced structural modifications enhance the chaperone activity of human α₂-macroglobulin

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (20), p.E2081-E2090

2014

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Clusterin facilitates in vivo clearance of extracellular misfolded proteins

Cellular and molecular life sciences : CMLS, 2011-12, Vol.68 (23), p.3919-3931

2011

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Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies

PloS one, 2015-06, Vol.10 (6), p.e0130036-e0130036

2015

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Structural Characterization of Clusterin-Chaperone Client Protein Complexes

The Journal of biological chemistry, 2009-08, Vol.284 (33), p.21920-21927

2009

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Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42

Redox biology, 2023-07, Vol.63, p.102736-102736, Article 102736

2023

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Hypochlorite-induced aggregation of fibrinogen underlies a novel antioxidant role in blood plasma

Redox biology, 2021-04, Vol.40, p.101847-101847, Article 101847

2021

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Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

The Journal of biological chemistry, 2010-02, Vol.285 (6), p.3532-3539

2010

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A Novel Role for Plasminogen Activator Inhibitor Type-2 as a Hypochlorite-Resistant Serine Protease Inhibitor and Holdase Chaperone

Cells (Basel, Switzerland), 2022-03, Vol.11 (7), p.1152

2022

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Quality control of protein folding in extracellular space

EMBO reports, 2005-12, Vol.6 (12), p.1131-1136

2005

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Alpha-2-Macroglobulin, a Hypochlorite-Regulated Chaperone and Immune System Modulator

Oxidative medicine and cellular longevity, 2019, Vol.2019, p.5410657-9

2019

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Amorphous protein aggregates stimulate plasminogen activation, leading to release of cytotoxic fragments that are clients for extracellular chaperones

The Journal of biological chemistry, 2017-09, Vol.292 (35), p.14425-14437

2017

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Roles of Extracellular Chaperones in Amyloidosis

Journal of molecular biology, 2012-08, Vol.421 (4-5), p.499-516

2012

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Acute phase proteins are major clients for the chaperone action of α2-macroglobulin in human plasma

Cell stress & chaperones, 2013-03, Vol.18 (2), p.161-170

2013

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Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms

FEBS letters, 2013-03, Vol.587 (5), p.398-403

2013

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Extracellular chaperones

Topics in current chemistry, 2013, Vol.328, p.241

2013

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WITHDRAWN: Corrigendum to ‘Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1–42’ [Redox Biol. 63 (2023) 102736]

Redox biology, 2023-06, p.102768, Article 102768

2023

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Corrigendum to 'Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42' [Redox Biol. 63 (2023) 102736]

Redox biology, 2023-06, p.102768-102768

2023

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Acute phase proteins are major clients for the chaperone action of [alpha]^sub 2^-macroglobulin in human plasma

Cell stress & chaperones, 2013-03, Vol.18 (2), p.161

2013

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Erratum to: Acute phase proteins are major clients for the chaperone action of [alpha]^sub 2^-macroglobulin in human plasma

Cell stress & chaperones, 2013-09, Vol.18 (5), p.683

2013

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Erratum to: Acute phase proteins are major clients for the chaperone action of α2-macroglobulin in human plasma

Cell stress & chaperones, 2013-09, Vol.18 (5), p.683-683

2013

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Hypochlorite-induced structural modifications enhance the chaperone activity of human [Alpha]^sub 2^-macroglobulin

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (20), p.E2081

2014

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Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (20), p.7174-7174

2014

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Hypochlorite-induced structural modifications enhance the chaperone activity of human α 2 -macroglobulin

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (20)

2014

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Extracellular chaperones and proteostasis

PZP and PAI-2: Structurally-diverse, functionally similar pregnancy proteins?

Hypochlorite-induced structural modifications enhance the chaperone activity of human α₂-macroglobulin

Clusterin facilitates in vivo clearance of extracellular misfolded proteins

Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies

Structural Characterization of Clusterin-Chaperone Client Protein Complexes

Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42

Hypochlorite-induced aggregation of fibrinogen underlies a novel antioxidant role in blood plasma

Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

A Novel Role for Plasminogen Activator Inhibitor Type-2 as a Hypochlorite-Resistant Serine Protease Inhibitor and Holdase Chaperone

Quality control of protein folding in extracellular space

Alpha-2-Macroglobulin, a Hypochlorite-Regulated Chaperone and Immune System Modulator

Amorphous protein aggregates stimulate plasminogen activation, leading to release of cytotoxic fragments that are clients for extracellular chaperones

Roles of Extracellular Chaperones in Amyloidosis

Acute phase proteins are major clients for the chaperone action of α2-macroglobulin in human plasma

Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms

Extracellular chaperones

WITHDRAWN: Corrigendum to ‘Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1–42’ [Redox Biol. 63 (2023) 102736]

Corrigendum to 'Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42' [Redox Biol. 63 (2023) 102736]

Acute phase proteins are major clients for the chaperone action of [alpha]^sub 2^-macroglobulin in human plasma

Erratum to: Acute phase proteins are major clients for the chaperone action of [alpha]^sub 2^-macroglobulin in human plasma

Erratum to: Acute phase proteins are major clients for the chaperone action of α2-macroglobulin in human plasma

Hypochlorite-induced structural modifications enhance the chaperone activity of human [Alpha]^sub 2^-macroglobulin

Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin

Hypochlorite-induced structural modifications enhance the chaperone activity of human α 2 -macroglobulin

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