Extracellular <scp>20S</scp> proteasome secreted via microvesicles can degrade poorly folded proteins and inhibit Galectin‐3 agglutination activity-Reference-Cited by-同舟云学术

Extracellular 20S proteasome secreted via microvesicles can degrade poorly folded proteins and inhibit Galectin‐3 agglutination activity

Published:2022-04-24 Issue:5 Volume:23 Page:287-304
ISSN:1398-9219
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Author:

Bonhoure Anne¹,Henry Laurent²,Bich Claudia²,Blanc Lionel³,Bergeret Blanche²,Bousquet Marie‐Pierre⁴,Coux Olivier⁵,Stoebner Pierre‐Emmanuel⁶⁷,Vidal Michel¹^ORCID

Affiliation:

1. Laboratory of Pathogen Host Interactions Université Montpellier, CNRS Montpellier France

2. Institut des Biomolécules Max Mousseron Université Montpellier, CNRS Montpellier France

3. The Feinstein Institutes for Medical Research Manhasset New York USA

4. Institut de Pharmacologie et de Biologie Structurale Université Toulouse, CNRS, UPS Toulouse France

5. Centre de Recherche en Biologie cellulaire de Montpellier Univ. Montpellier, CNRS Montpellier France

6. Service de Dermatologie, CHU Nîmes Nîmes France

7. Institut de Recherche en Cancérologie de Montpellier (IRCM) Université Montpellier Montpellier France

Funder

Cancéropôle Grand Ouest

Ligue Contre le Cancer

Université de Montpellier

Agence Nationale de la Recherche

Weizmann Institute of Science

Centre National de la Recherche Scientifique

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/tra.12840

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2. ATP Binding and ATP Hydrolysis Play Distinct Roles in the Function of 26S Proteasome

3. Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin.

4. Degradation of Oxidized Proteins in K562 Human Hematopoietic Cells by Proteasome

5. BIMEL, an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation