Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Jill L Johnson"'
Publikováno v:
PLoS Genetics, Vol 19, Iss 5, p e1010772 (2023)
Molecular chaperones play a key role in maintaining proteostasis and cellular health. The abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and activation of hundreds of newly synthesized or misfolded client pr
Externí odkaz:
https://doaj.org/article/57c16cc9baa74c1ba21e578820b4d691
Autor:
Jannell V Bazurto, Dipti D Nayak, Tomislav Ticak, Milya Davlieva, Jessica A Lee, Chandler N Hellenbrand, Leah B Lambert, Olivia J Benski, Caleb J Quates, Jill L Johnson, Jagdish Suresh Patel, F Marty Ytreberg, Yousif Shamoo, Christopher J Marx
Publikováno v:
PLoS Biology, Vol 19, Iss 5, p e3001208 (2021)
Normal cellular processes give rise to toxic metabolites that cells must mitigate. Formaldehyde is a universal stressor and potent metabolic toxin that is generated in organisms from bacteria to humans. Methylotrophic bacteria such as Methylorubrum e
Externí odkaz:
https://doaj.org/article/ba4b2563d3db4235ade1603ec90ab87c
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e92569 (2014)
The molecular chaperone Hsp90 buffers the effects of genetic variation by assisting the stabilization and folding of multiple clients critical for cell signaling and growth. We identified an interaction of Hsp90 and associated proteins with the essen
Externí odkaz:
https://doaj.org/article/c0d2dd158ef941d38a3a920e8f172448
Hsp90 is an essential molecular chaperone responsible for the folding and activation of hundreds of ‘client’ proteins, including the glucocorticoid receptor (GR)1-3. Previously, we revealed that GR ligand binding activity is inhibited by Hsp70 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::00e1257fba501604a622e2b8752af2b0
https://doi.org/10.1101/2023.01.10.523504
https://doi.org/10.1101/2023.01.10.523504
Autor:
Ray Yu-Ruei Wang, Chari M. Noddings, Elaine Kirschke, Alexander G. Myasnikov, Jill L. Johnson, David A. Agard
Publikováno v:
Nature
Maintaining a healthy proteome is fundamental for the survival of all organisms(1). Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and maturation of the many’client proteins’ of Hsp90(
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
Autor:
Jill L. Johnson, Marissa E. Dean
Publikováno v:
Cell Stress Chaperones
The Hsp90 molecular chaperone is required for the function of hundreds of different cellular proteins. Hsp90 and a cohort of interacting proteins called cochaperones interact with clients in an ATP-dependent cycle. Cochaperone functions include targe
Autor:
Rebecca J. Mercier, Jonathan Schubert, Paul LaPointe, Annemarie Wolmarans, Hannes Neuweiler, Jill L. Johnson
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications
Nature Communications
Hsp90 is a dimeric molecular chaperone that is essential for the folding and activation of hundreds of client proteins. Co-chaperone proteins regulate the ATP-driven Hsp90 client activation cycle. Aha-type co-chaperones are the most potent stimulator
Publikováno v:
Genetics
The protein molecular chaperone Hsp90 (Heat shock protein, 90 kilodalton) plays multiple roles in the biogenesis and regulation of client proteins impacting myriad aspects of cellular physiology. Amino acid alterations located throughout Saccharomyce
Autor:
Chari Noddings, Jill L. Johnson, David A. Agard, Ray Yu-Ruei Wang, Elaine Kirschke, Alexander G. Myasnikov
Maintaining a healthy proteome is fundamental for organism survival1. Integral to this are Hsp90 and Hsp70 molecular chaperones that together facilitate the folding, remodeling and maturation of Hsp90’s many “client” proteins. The glucocorticoi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91974a9a4b3557b5bcb3dfc54dc6c22a
https://doi.org/10.21203/rs.3.rs-120723/v1
https://doi.org/10.21203/rs.3.rs-120723/v1