Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Mark R, Woodford"'
Autor:
Sarah J. Backe, Rebecca A. Sager, Jennifer A. Heritz, Laura A. Wengert, Katherine A. Meluni, Xavier Aran-Guiu, Barry Panaretou, Mark R. Woodford, Chrisostomos Prodromou, Dimitra Bourboulia, Mehdi Mollapour
Publikováno v:
Cell Reports, Vol 43, Iss 1, Pp 113672- (2024)
Externí odkaz:
https://doaj.org/article/9fda5e1eb2a7419281fc9e680ef89a78
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-3 (2023)
Molecular chaperones establish essential protein-protein interaction networks. Modified versions of these assemblies are generally enriched in certain maladies. A study published in Nature Communications used epichaperomics to identify unique changes
Externí odkaz:
https://doaj.org/article/a241236799494cd1a0e80b7c486f47bf
Autor:
Sarah J. Backe, Rebecca A. Sager, Jennifer A. Heritz, Laura A. Wengert, Katherine A. Meluni, Xavier Aran-Guiu, Barry Panaretou, Mark R. Woodford, Chrisostomos Prodromou, Dimitra Bourboulia, Mehdi Mollapour
Publikováno v:
Cell Reports, Vol 42, Iss 7, Pp 112807- (2023)
Summary: Cellular homeostasis relies on both the chaperoning of proteins and the intracellular degradation system that delivers cytoplasmic constituents to the lysosome, a process known as autophagy. The crosstalk between these processes and their un
Externí odkaz:
https://doaj.org/article/4372f2b85d70407f912e42e25ea43467
Autor:
Sarah J. Backe, SarahBeth D. Votra, Matthew P. Stokes, Endre Sebestyén, Matteo Castelli, Luca Torielli, Giorgio Colombo, Mark R. Woodford, Mehdi Mollapour, Dimitra Bourboulia
Publikováno v:
Cell Reports, Vol 42, Iss 6, Pp 112539- (2023)
Summary: c-Src tyrosine kinase is a renowned key intracellular signaling molecule and a potential target for cancer therapy. Secreted c-Src is a recent observation, but how it contributes to extracellular phosphorylation remains elusive. Using a seri
Externí odkaz:
https://doaj.org/article/cd824932e9ec4ba28ad2022efbf0249e
Autor:
Rebecca A. Sager, Farzana Khan, Lorenzo Toneatto, SarahBeth D. Votra, Sarah J. Backe, Mark R. Woodford, Mehdi Mollapour, Dimitra Bourboulia
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The molecular chaperone Heat Shock Protein-90 (Hsp90) is known to interact with over 300 client proteins as well as regulatory factors (eg. nucleotide and proteins) that facilitate execution of its role as a chaperone and, ultimately, client protein
Externí odkaz:
https://doaj.org/article/6e665a91972e47c9bdf7bdf90d269459
Autor:
Sarah J. Backe, Rebecca A. Sager, Katherine A. Meluni, Mark R. Woodford, Dimitra Bourboulia, Mehdi Mollapour
Publikováno v:
Biomolecules, Vol 12, Iss 7, p 928 (2022)
Heat shock protein-90 (Hsp90) is an ATP-dependent molecular chaperone that is tightly regulated by a group of proteins termed co-chaperones. This chaperone system is essential for the stabilization and activation of many key signaling proteins. Recen
Externí odkaz:
https://doaj.org/article/318844d88a05455f8a84a8a3e70f9abe
Publikováno v:
Biomolecules, Vol 12, Iss 6, p 786 (2022)
Mitochondrial function is dependent on molecular chaperones, primarily due to their necessity in the formation of respiratory complexes and clearance of misfolded proteins. Heat shock proteins (Hsps) are a subset of molecular chaperones that function
Externí odkaz:
https://doaj.org/article/5d47277248ea418dae3ad6a40be19fdb
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