Zobrazeno 1 - 7
of 7
pro vyhledávání: '"HSP90 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
https://research.rug.nl/en/publications/7037eec0-2788-424e-a500-f9cdb68673f3
First Virtual International Congress on Cellular and Organismal Stress Responses, November 5-6, 2020
Autor:
Adrienne L. Edkins, Harm H. Kampinga, Linda M. Hendershot, Ruth Scherz-Shouval, Andrew W. Truman, Steven Bergink, Veena Prahlad, Chris Prodromou, Olivier Genest, Antonio De Maio, Gabriele Multhoff, Jill L. Johnson, Brian C. Freeman, Mehdi Mollapour, Jeff Brodsky, Patricija van Oosten-Hawle, Brian S. J. Blagg, Dan Masison, Anastasia Zhuravleva, Kevin A. Morano
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⟩
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⟩
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=doi_dedup___::2157c71bd2f03481bb806d4b6d32f004
https://hdl.handle.net/11370/7037eec0-2788-424e-a500-f9cdb68673f3
https://hdl.handle.net/11370/7037eec0-2788-424e-a500-f9cdb68673f3
Autor:
Tilman Grune, Henrique Almeida, Raquel Fernando, José Pedro Castro, Sandra Reeg, Walter Meinl
Publikováno v:
Redox Biology, Vol 21, Iss, Pp-(2019)
Redox Biology
Redox Biology
Aging is accompanied by the accumulation of oxidized proteins. To remove them, cells employ the proteasomal and autophagy-lysosomal systems; however, if the clearance rate is inferior to its formation, protein aggregates form as a hallmark of proteos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b699b02bf2aeb0a16d74f0d4b19b2ba
http://www.sciencedirect.com/science/article/pii/S2213231718312369
http://www.sciencedirect.com/science/article/pii/S2213231718312369
Autor:
Loana Musso, Raquel T. Lima, Raffaella Cincinelli, Ana Bizarro, Michelandrea De Cesare, Sabrina Dallavalle, M. Helena Vasconcelos, Valentina Zuco, Diana Sousa
Publikováno v:
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules, Vol 23, Iss 2, p 407 (2018)
Molecules; Volume 23; Issue 2; Pages: 407
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Molecules, Vol 23, Iss 2, p 407 (2018)
Molecules; Volume 23; Issue 2; Pages: 407
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Background: Heat shock protein 90 (HSP90) is a well-known target for cancer therapy. In a previous work, some of us have reported a series of 3-aryl-naphtho[2,3-d]isoxazole-4,9-diones as inhibitors of HSP90. Methods: In the present work, various comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::638850e929e3ec4d77bf8fdf3caa98da
http://europepmc.org/articles/PMC6017909
http://europepmc.org/articles/PMC6017909
Autor:
Girish R Mali, Patricia L Yeyati, Seiya Mizuno, Daniel O Dodd, Peter A Tennant, Margaret A Keighren, Petra zur Lage, Amelia Shoemark, Amaya Garcia-Munoz, Atsuko Shimada, Hiroyuki Takeda, Frank Edlich, Satoru Takahashi, Alex von Kreigsheim, Andrew P Jarman, Pleasantine Mill
Publikováno v:
eLife
Mali, G R, Yeyati, P L, Mizuno, S, Dodd, D O, Tennant, P A, Keighren, M A, Zur Lage, P, Shoemark, A, Garcia-Munoz, A, Shimada, A, Takeda, H, Edlich, F, Takahashi, S, von Kreigsheim, A, Jarman, A P & Mill, P 2018, ' ZMYND10 functions in a chaperone relay during axonemal dynein assembly ', eLife, vol. 7, e34389 . https://doi.org/10.7554/eLife.34389
eLife, Vol 7 (2018)
Mali, G R, Yeyati, P L, Mizuno, S, Dodd, D O, Tennant, P A, Keighren, M A, zur Lage, P, Shoemark, A, Garcia-Munoz, A, Shimada, A, Takeda, H, Edlich, F, Takahashi, S, von Kreigsheim, A, Jarman, A P & Mill, P 2018, ' ZMYND10 functions in a chaperone relay during axonemal dynein assembly ', eLIFE, vol. 7, e34389 . https://doi.org/10.7554/eLife.34389
Mali, G R, Yeyati, P L, Mizuno, S, Dodd, D O, Tennant, P A, Keighren, M A, Zur Lage, P, Shoemark, A, Garcia-Munoz, A, Shimada, A, Takeda, H, Edlich, F, Takahashi, S, von Kreigsheim, A, Jarman, A P & Mill, P 2018, ' ZMYND10 functions in a chaperone relay during axonemal dynein assembly ', eLife, vol. 7, e34389 . https://doi.org/10.7554/eLife.34389
eLife, Vol 7 (2018)
Mali, G R, Yeyati, P L, Mizuno, S, Dodd, D O, Tennant, P A, Keighren, M A, zur Lage, P, Shoemark, A, Garcia-Munoz, A, Shimada, A, Takeda, H, Edlich, F, Takahashi, S, von Kreigsheim, A, Jarman, A P & Mill, P 2018, ' ZMYND10 functions in a chaperone relay during axonemal dynein assembly ', eLIFE, vol. 7, e34389 . https://doi.org/10.7554/eLife.34389
Molecular chaperones promote the folding and macromolecular assembly of a diverse set of ‘client’ proteins. How ubiquitous chaperone machineries direct their activities towards specific sets of substrates is unclear. Through the use of mouse gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::fe9afdf204c3777902853e0c311205d4
https://pubmed.ncbi.nlm.nih.gov/29916806
https://pubmed.ncbi.nlm.nih.gov/29916806
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc267e0d60c616546cae5ddadd849f93
Autor:
Fukushima, Toshiaki, Okajima, H., Yamanaka, D., Ariga, M., Nagata, S., Ito, A., Yoshida, M., Asano, T., Chida, K., Hakuno, F., Takahashi, S.
Publikováno v:
Molecular and Cellular Endocrinology. 344:81-89
Prolonged stimulation of FRTL-5 thyroid cells with cAMP-generating agents including thyroid-stimulating hormone (TSH) or cAMP analogues potentiates tyrosine phosphorylation of insulin receptor substrate (IRS)-2 triggered by insulin-like growth factor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::086e2ad4839097a88f9972d30496b59d
https://doi.org/10.1016/j.mce.2011.06.029
https://doi.org/10.1016/j.mce.2011.06.029