Zobrazeno 1 - 10
of 188
pro vyhledávání: '"Timothy A. Haystead"'
Autor:
Natela Dushukyan, Diana M. Dunn, Rebecca A. Sager, Mark R. Woodford, David R. Loiselle, Michael Daneshvar, Alexander J. Baker-Williams, John D. Chisholm, Andrew W. Truman, Cara K. Vaughan, Timothy A. Haystead, Gennady Bratslavsky, Dimitra Bourboulia, Mehdi Mollapour
Publikováno v:
Cell Reports, Vol 21, Iss 7, Pp 1883-1895 (2017)
Summary: The serine/threonine protein phosphatase 5 (PP5) regulates multiple cellular signaling networks. A number of cellular factors, including heat shock protein 90 (Hsp90), promote the activation of PP5. However, it is unclear whether post-transl
Externí odkaz:
https://doaj.org/article/1fd7653e1f7244c682e707f46ef9dd06
Autor:
Manjusha M. Kulkarni, Annette N. Ratcliff, Menakshi Bhat, Yazan Alwarawrah, Philip Hughes, Jesus Arcos, David Loiselle, Jordi B. Torrelles, Nicholas T. Funderburg, Timothy A. Haystead, Jesse J. Kwiek
Publikováno v:
Retrovirology, Vol 14, Iss 1, Pp 1-12 (2017)
Abstract Background Like all viruses, HIV-1 relies on host systems to replicate. The human purinome consists of approximately two thousand proteins that bind and use purines such as ATP, NADH, and NADPH. By virtue of their purine binding pockets, pur
Externí odkaz:
https://doaj.org/article/198c703fa7b643ab9fcf74aba658487f
Autor:
Rebecca A. Sager, Mark R. Woodford, Sarah J. Backe, Alan M. Makedon, Alexander J. Baker-Williams, Bryanna T. DiGregorio, David R. Loiselle, Timothy A. Haystead, Natasha E. Zachara, Chrisostomos Prodromou, Dimitra Bourboulia, Laura S. Schmidt, W. Marston Linehan, Gennady Bratslavsky, Mehdi Mollapour
Publikováno v:
Cell Reports, Vol 26, Iss 5, Pp 1344-1356.e5 (2019)
Summary: The molecular chaperone Hsp90 stabilizes and activates client proteins. Co-chaperones and post-translational modifications tightly regulate Hsp90 function and consequently lead to activation of clients. However, it is unclear whether this pr
Externí odkaz:
https://doaj.org/article/de66c6bb8ecb4bfabba4d27f34f19f26
Autor:
Mark R. Woodford, Diana M. Dunn, Adam R. Blanden, Dante Capriotti, David Loiselle, Chrisostomos Prodromou, Barry Panaretou, Philip F. Hughes, Aaron Smith, Wendi Ackerman, Timothy A. Haystead, Stewart N. Loh, Dimitra Bourboulia, Laura S. Schmidt, W. Marston Linehan, Gennady Bratslavsky, Mehdi Mollapour
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co
Externí odkaz:
https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd
Autor:
Diana M. Dunn, Mark R. Woodford, Andrew W. Truman, Sandra M. Jensen, Jacqualyn Schulman, Tiffany Caza, Taylor C. Remillard, David Loiselle, Donald Wolfgeher, Brian S.J. Blagg, Lucas Franco, Timothy A. Haystead, Soumya Daturpalli, Matthias P. Mayer, Jane B. Trepel, Rhodri M.L. Morgan, Chrisostomos Prodromou, Stephen J. Kron, Barry Panaretou, William G. Stetler-Stevenson, Steve K. Landas, Len Neckers, Gennady Bratslavsky, Dimitra Bourboulia, Mehdi Mollapour
Publikováno v:
Cell Reports, Vol 12, Iss 6, Pp 1006-1018 (2015)
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity, tailoring the chaperone function to specific “client” proteins. The intracellular signa
Externí odkaz:
https://doaj.org/article/513261747e0342e1bf436072b173cab8
Autor:
Swarna Bale, Priyanka Verma, Bharath Yalavarthi, Scott Arthur Scarneo, Philip Hughes, M. Asif Amin, Pei-Suen Tsou, Dinesh Khanna, Timothy A.J. Haystead, Swati Bhattacharyya, John Varga
Publikováno v:
JCI Insight, Vol 8, Iss 14 (2023)
Multiorgan fibrosis in systemic sclerosis (SSc) accounts for substantial mortality and lacks effective therapies. Lying at the crossroad of TGF-β and TLR signaling, TGF-β–activated kinase 1 (TAK1) might have a pathogenic role in SSc. We therefore
Externí odkaz:
https://doaj.org/article/b5bda06bbf254b1d930547a5f45e0f51
Autor:
Chaitanya R. Acharya, Xiao Yi Yang, H. Kim Lyerly, Joshua C. Snyder, Erika J. Crosby, Michael A. Morse, Rendon C. Nelson, Thomas J. Polascik, Ivan Spasojevic, Takuya Osada, Joshua D. Ginzel, Kensuke Kaneko, Timothy A.J. Haystead, Andre Rogatko, Jiaoti Huang, Amy Hobeika, Zachary C. Hartman, Philip F. Hughes, Leonard M. Neckers
Publikováno v:
Mol Cancer Ther
A noninvasive test to discriminate indolent prostate cancers from lethal ones would focus treatment where necessary while reducing overtreatment. We exploited the known activity of heat shock protein 90 (Hsp90) as a chaperone critical for the functio
Autor:
Scott A. Scarneo, Andrea G. Nackley, Yaomin Wang, Timothy A.J. Haystead, Kelly W. Yang, Xin Zhang, Shin Hyung Kim, Philip F. Hughes, Jiegen Chen
Publikováno v:
Pain
Heat shock protein 90 (Hsp90) is a ubiquitously expressed integral cellular protein essential for regulating proteomic stress. Previous research has shown that Hsp90 regulates critical signaling pathways underlying chronic pain and inflammation. Rece
Autor:
Sara R. Turner, David A. Carlson, Mona Chappellaz, Cindy Sutherland, Timothy A.J. Haystead, William C. Cole, Justin A. MacDonald
The vascular smooth muscle (VSM) of resistance blood vessels displays intrinsic autoregulatory responses to increased intraluminal pressure, the myogenic response. In the brain, the myogenic responses of cerebral arterioles are critical to homeostati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bff8b01e52ac963e63637ca0261ca8fd
https://doi.org/10.1101/2022.06.10.495652
https://doi.org/10.1101/2022.06.10.495652
Various signaling molecules affecting epithelial restitution and wound healing are dysregulated in ulcerative colitis. Recent evidence demonstrates the necessity of Hippo-YAP/TAZ signaling, interceded by cytoskeletal remodeling, for intestinal regene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23c6ba11bcc40c223a0ae719d2f8f6a4
https://doi.org/10.1101/2021.12.03.471118
https://doi.org/10.1101/2021.12.03.471118