Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Alexander J. Baker-Williams"'
Autor:
Javier Sánchez-Pozo, Alexander J. Baker-Williams, Mark R. Woodford, Renee Bullard, Beiyang Wei, Mehdi Mollapour, William G. Stetler-Stevenson, Gennady Bratslavsky, Dimitra Bourboulia
Publikováno v:
iScience, Vol 1, Iss , Pp 87-96 (2018)
Summary: The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-
Externí odkaz:
https://doaj.org/article/162e0a659f004ddc931c533bf3fe8b79
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:
Alexander J. Baker-Williams, Fiza Hashmi, Marek A. Budzyński, Mark R. Woodford, Stephanie Gleicher, Samu V. Himanen, Alan M. Makedon, Derek Friedman, Stephanie Cortes, Sara Namek, William G. Stetler-Stevenson, Gennady Bratslavsky, Alaji Bah, Mehdi Mollapour, Lea Sistonen, Dimitra Bourboulia
Publikováno v:
Cell Reports, Vol 28, Iss 7, Pp 1894-1906.e6 (2019)
Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion. Although co-chaperones are critical modulators of intracellular HSP90:clie
Externí odkaz:
https://doaj.org/article/5c2fb5f7bb824f3faae72044a1736056
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:
Mehdi Mollapour, Dimitra Bourboulia, Michael Hughes, Joseph M. Jacob, Alexander J. Baker-Williams, Oleg Shapiro, Gennady Bratslavsky, Mark R. Woodford, Michael Wong, Rebecca A. Sager, Michael S. Bratslavsky, Sarah J. Backe
Publikováno v:
Oncotarget
The molecular chaperone Heat shock protein 90 (Hsp90) is essential for the folding, stability, and activity of several drivers of oncogenesis. Hsp90 inhibitors are currently under clinical evaluation for cancer treatment, however their efficacy is li
Autor:
Fiza Hashmi, Samu V. Himanen, Sara Namek, Alexander J. Baker-Williams, Gennady Bratslavsky, Dimitra Bourboulia, Lea Sistonen, Stephanie Gleicher, Derek Friedman, William G. Stetler-Stevenson, Marek A. Budzynski, Alaji Bah, Alan M. Makedon, Stephanie Cortes, Mehdi Mollapour, Mark R. Woodford
Publikováno v:
Cell Reports, Vol 28, Iss 7, Pp 1894-1906.e6 (2019)
Cell Rep
Cell Rep
Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion. Although co-chaperones are critical modulators of intracellular HSP90:clie
Autor:
Timothy A.J. Haystead, Adam R. Blanden, Mehdi Mollapour, Sarah J. Backe, Matteo Castelli, Laura S. Schmidt, Sandra M. Jensen, Alexander J. Baker-Williams, Rebecca A. Sager, William G. Stetler-Stevenson, Fiza Hashmi, W. Marston Linehan, David R. Loiselle, Stefano A. Serapian, Mark R. Woodford, Dimitra Bourboulia, Gennady Bratslavsky, Alessandro Gori, Stewart N. Loh, Alaji Bah, Priyanka Kancherla, Giorgio Colombo
Publikováno v:
Nature structural & molecular biology 28 (2021): 662–670. doi:10.1038/s41594-021-00633-2
info:cnr-pdr/source/autori:Woodford M.R.; Baker-Williams A.J.; Sager R.A.; Backe S.J.; Blanden A.R.; Hashmi F.; Kancherla P.; Gori A.; Loiselle D.R.; Castelli M.; Serapian S.A.; Colombo G.; Haystead T.A.; Jensen S.M.; Stetler-Stevenson W.G.; Loh S.N.; Schmidt L.S.; Linehan W.M.; Bah A.; Bourboulia D.; Bratslavsky G.; Mollapour M./titolo:The tumor suppressor folliculin inhibits lactate dehydrogenase A and regulates the Warburg effect/doi:10.1038%2Fs41594-021-00633-2/rivista:Nature structural & molecular biology/anno:2021/pagina_da:662/pagina_a:670/intervallo_pagine:662–670/volume:28
Nat Struct Mol Biol
info:cnr-pdr/source/autori:Woodford M.R.; Baker-Williams A.J.; Sager R.A.; Backe S.J.; Blanden A.R.; Hashmi F.; Kancherla P.; Gori A.; Loiselle D.R.; Castelli M.; Serapian S.A.; Colombo G.; Haystead T.A.; Jensen S.M.; Stetler-Stevenson W.G.; Loh S.N.; Schmidt L.S.; Linehan W.M.; Bah A.; Bourboulia D.; Bratslavsky G.; Mollapour M./titolo:The tumor suppressor folliculin inhibits lactate dehydrogenase A and regulates the Warburg effect/doi:10.1038%2Fs41594-021-00633-2/rivista:Nature structural & molecular biology/anno:2021/pagina_da:662/pagina_a:670/intervallo_pagine:662–670/volume:28
Nat Struct Mol Biol
Aerobic glycolysis in cancer cells, also known as the ‘Warburg effect’, is driven by hyperactivity of lactate dehydrogenase A (LDHA). LDHA is thought to be a substrate-regulated enzyme, but it is unclear whether a dedicated intracellular protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fe3b954dbdf0a623040e491e111ed86
http://www.cnr.it/prodotto/i/456866
http://www.cnr.it/prodotto/i/456866
Autor:
Mehdi Mollapour, Alexander J. Baker-Williams, William G. Stetler-Stevenson, Gennady Bratslavsky, Renee Bullard, Beiyang Wei, Mark R. Woodford, Javier Sánchez-Pozo, Dimitra Bourboulia
Publikováno v:
iScience, Vol 1, Iss, Pp 87-96 (2018)
Summary: The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-
Autor:
John D. Chisholm, Dimitra Bourboulia, Gennady Bratslavsky, David R. Loiselle, Andrew W. Truman, Cara K. Vaughan, Natela Dushukyan, Rebecca A. Sager, Diana M. Dunn, Alexander J. Baker-Williams, Mark R. Woodford, Michael Daneshvar, Mehdi Mollapour, Timothy A.J. Haystead
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
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1709
Heat Shock Protein 90 (Hsp90) is a ubiquitous molecular chaperone that comprises about 1-3% of the total cellular protein. Over the last decade, Hsp90 has been detected and studied in the extracellular space (extracellular or eHsp90) of normal and ne