Výsledky vyhledávání - "HSP70 Heat-Shock Proteins/genetics"

First Virtual International Congress on Cellular and Organismal Stress Responses, November 5-6, 2020

Publikováno v: Cell stress & chaperones. 26(2):289-295

Members of the Cell Stress Society International (CSSI), Patricija van Oosten-Hawle (University of Leeds, UK), Mehdi Mollapour (SUNY Upstate Medical University, USA), Andrew Truman (University of North Carolina at Charlotte, USA) organized a new virt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___01423::aeefd7121c0d9cd868d01058b66e6816
https://research.rug.nl/en/publications/7037eec0-2788-424e-a500-f9cdb68673f3

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First Virtual International Congress on Cellular and Organismal Stress Responses, November 5-6, 2020

Publikováno v: Cell Stress & Chaperones
Cell Stress and Chaperones
Cell Stress and Chaperones, 2021, 26 (2), pp.289-295. ⟨10.1007/s12192-021-01192-7⟩
Cell Stress and Chaperones, Springer Verlag, 2021, 26 (2), pp.289-295. ⟨10.1007/s12192-021-01192-7⟩

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2157c71bd2f03481bb806d4b6d32f004
https://hdl.handle.net/11370/7037eec0-2788-424e-a500-f9cdb68673f3

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HSPA9/Mortalin mediates axo-protection and modulates mitochondrial dynamics in neurons

Autor: Ferré, Cécile, Thouard, Anne, Bétourné, Alexandre, Le Dorze, Anne-Louise, Belenguer, Pascale, Miquel, Marie-Christine, Peyrin, Jean-Michel, Gonzalez-Dunia, Daniel, Szelechowski, Marion

Publikováno v: Scientific Reports
Scientific Reports, Nature Publishing Group, 2021, 11 (1), ⟨10.1038/s41598-021-97162-1⟩
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Scientific Reports, 2021, 11 (1), pp.17705. ⟨10.1038/s41598-021-97162-1⟩
Scientific Reports, Nature Publishing Group, 2021, 11 (1), pp.17705. ⟨10.1038/s41598-021-97162-1⟩

International audience; Abstract Mortalin is a mitochondrial chaperone protein involved in quality control of proteins imported into the mitochondrial matrix, which was recently described as a sensor of neuronal stress. Mortalin is down-regulated in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::5bdfacbb75cb9f9458677eb3bc34d63f
https://hal.archives-ouvertes.fr/hal-03424565

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On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life

Autor: Pierre Goloubinoff, Dan S. Tawfik, Mathieu E. Rebeaud, Saurav Mallik

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 21, pp. e2020885118

Significance Across the Tree of Life, life’s phenotypic diversity has been accompanied by a massive expansion of the protein universe. Compared with simple prokaryotes that harbor thousands of proteins, plants and animals harbor hundreds of thousan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17e4166f68468716db9dec5da3410cfc
http://europepmc.org/articles/PMC8166112

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The Balance between Mono- and NEDD8-Chains Controlled by NEDP1 upon DNA Damage Is a Regulatory Module of the HSP70 ATPase Activity

Autor: Aurélien Perrin, Helene Trauchessec, Orsolya Leidecker, Aymeric P. Bailly, Chantal Maghames, Anton Gartner, Marina Serrano-Macia, Dimitris P. Xirodimas, María L. Martínez-Chantar

Publikováno v: Cell Reports
Cell Reports, 2019, 29 (1), pp.212-224.e8. ⟨10.1016/j.celrep.2019.08.070⟩
Cell Reports, Elsevier Inc, 2019, 29 (1), pp.212-224.e8. ⟨10.1016/j.celrep.2019.08.070⟩
Cell Reports, Vol 29, Iss 1, Pp 212-224.e8 (2019)

Summary Ubiquitin and ubiquitin-like chains are finely balanced by conjugating and de-conjugating enzymes. Alterations in this balance trigger the response to stress conditions and are often observed in pathologies. How such changes are detected is n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5d39ecc1dfd219f6cb99ac162e2d477
https://hal.umontpellier.fr/hal-02339558

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Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Autor: Rayees U.H. Mattoo, Andrija Finka, Pierre Goloubinoff

Publikováno v: Annual Review of Biochemistry, vol. 85, pp. 715-742

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54a6cf180c4f25cc28bdaff5e6fef370
https://doi.org/10.1146/annurev-biochem-060815-014124

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Drosophila Spag Is the Homolog of RNA Polymerase II-associated Protein 3 (RPAP3) and Recruits the Heat Shock Proteins 70 and 90 (Hsp70 and Hsp90) during the Assembly of Cellular Machineries

Autor: Ioannis Iliopoulos, Nour El Houda Benbahouche, Tore Kempf, Istvan Török, Philippe Meyer, Robert Farkaš, Edouard Bertrand, István Kiss, Julien Henri, Bernard M. Mechler, Bérengère Pradet-Balade, Andrey V. Kajava, Joachim Marhold, Martina Schnölzer

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 2014, 289 (9), pp.6236--47. ⟨10.1074/jbc.M113.499608⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (9), pp.6236--47. ⟨10.1074/jbc.M113.499608⟩

The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2. In mammals, the R2TP is involved in the biogenesis of cellular machineries such as RNA polymerases, s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96e0637b89bada28a508ab1d8fe16075
https://doi.org/10.1074/jbc.m113.499608

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Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins

Autor: Satoru Watanabe, Hitoshi Nakamoto, Takahiro Maruyama, Emi Suenaga, Kensaku Fujita, Tomoko Misono, Hirofumi Yoshikawa, Pierre Goloubinoff, Shoichi Narumi, Aguru Ohtaki, Penmetcha K. R. Kumar

Publikováno v: The Journal of biological chemistry
Journal of Biological Chemistry, vol. 289, no. 9, pp. 6110-6119

In eukaryotes, heat shock protein 90 (Hsp90) is an essential ATP-dependent molecular chaperone that associates with numerous client proteins. HtpG, a prokaryotic homolog of Hsp90, is essential for thermotolerance in cyanobacteria, and in vitro it sup

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Species- and Strain-Specific Adaptation of the HSP70 Super Family in Pathogenic Trypanosomatids

Autor: Gerald F. Späth, Pierre Lechat, Jean-Claude Dujardin, Najma Rachidi, Tomáš Skalický, Julius Lukeš, Hideo Imamura, Alexis Criscuolo, Sima Drini

Publikováno v: Genome Biology and Evolution
Genome Biology and Evolution, Society for Molecular Biology and Evolution, 2016, 8 (6), pp.1980-1995. ⟨10.1093/gbe/evw140⟩
Genome Biology and Evolution, 2016, 8 (6), pp.1980-1995. ⟨10.1093/gbe/evw140⟩

International audience; All eukaryotic genomes encode multiple members of the heat shock protein 70 (HSP70) family, which evolved distinctive structural and functional features in response to specific environmental constraints. Phylogenetic analysis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f214e270c84ce7da06096068653a3379
https://hal-pasteur.archives-ouvertes.fr/pasteur-02635182/document

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