Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Adam A. Aboalroub"'
Autor:
Adam A. Aboalroub, Belal O. Al-Najjar
Publikováno v:
Results in Chemistry, Vol 11, Iss , Pp 101757- (2024)
The ATP-dependent molecular chaperone, Hsp90, is crucial for the activity of hundreds of client proteins. Several of Hsp90 clients are involved in cancer cell growth and proliferation. Thus, numerous Hsp90 inhibitors have been developed to target Hsp
Externí odkaz:
https://doaj.org/article/0816700e98f84beba89cff53eb8cb0c2
Autor:
Adam A Aboalroub, Ashleigh B Bachman, Ziming Zhang, Dimitra Keramisanou, David J Merkler, Ioannis Gelis
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0177270 (2017)
The transfer of an acetyl group from acetyl-CoA to an acceptor amine is a ubiquitous biochemical transformation catalyzed by Gcn5-related N-acetyltransferases (GNATs). Although it is established that the reaction proceeds through a sequential ordered
Externí odkaz:
https://doaj.org/article/ae15601347b4436b93c0145d219e22bc
Autor:
Dimitra Keramisanou, Ioannis Gelis, Adam A. Aboalroub, Devon Marshall, Wenjun Liu, Randy W. Larsen, Ralf Landgraf, Andrea Diviney, Ziming Zhang
Publikováno v:
Molecular Cell. 62:260-271
Despite the essential functions of Hsp90, little is known about the mechanism that controls substrate entry into its chaperone cycle. We show that the role of Cdc37 cochaperone reaches beyond that of an adaptor protein and find that it participates i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3545330d8b905e0cf70329633409c243
https://doi.org/10.1016/j.molcel.2016.04.005
https://doi.org/10.1016/j.molcel.2016.04.005
Autor:
Dimitra Keramisanou, Ziming Zhang, Ashleigh Bachman, Adam A. Aboalroub, Ioannis Gelis, David J. Merkler
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 5, p e0177270 (2017)
PLoS ONE, Vol 12, Iss 5, p e0177270 (2017)
The transfer of an acetyl group from acetyl-CoA to an acceptor amine is a ubiquitous biochemical transformation catalyzed by Gcn5-related N-acetyltransferases (GNATs). Although it is established that the reaction proceeds through a sequential ordered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77ffaad6445b80a09c790b5e018c659e
https://pubmed.ncbi.nlm.nih.gov/28486510
https://pubmed.ncbi.nlm.nih.gov/28486510
Publikováno v:
Biomolecular NMR assignments. 11(1)
Arylalkylamine N-acetyltransferases (AANATs) catalyze the transfer of an acetyl group from the acetyl-group donor, acetyl-CoA, to an arylalkylamine acceptor. Although a single AANAT has been identified in mammals, insects utilize multiple AANATs in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::106502953bcebfe936799d1b90d45f68
https://pubmed.ncbi.nlm.nih.gov/28236225
https://pubmed.ncbi.nlm.nih.gov/28236225
Publikováno v:
Biophysical Journal. 112:491a
The Hsp90 chaperone machinery is a ubiquitous mediator of protein homeostasis and activity. Despite its essential roles, little is known about the molecular mechanism that controls substrate entry into its chaperone cycle. Here we show that the funct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ab848e624f6a452a0548908291eefa6
https://doi.org/10.1016/j.bpj.2016.11.2658
https://doi.org/10.1016/j.bpj.2016.11.2658
Publikováno v:
Biophysical Journal. 112:347a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1fdaf188e68c852ea1419c8505165db1
https://doi.org/10.1016/j.bpj.2016.11.1881
https://doi.org/10.1016/j.bpj.2016.11.1881
Autor:
Keramisanou D; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Aboalroub A; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Zhang Z; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Liu W; Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA., Marshall D; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Diviney A; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Larsen RW; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA., Landgraf R; Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 33136, USA., Gelis I; Department of Chemistry, University of South Florida, Tampa, FL 33620, USA. Electronic address: igelis@usf.edu.
Publikováno v:
Molecular cell [Mol Cell] 2016 Apr 21; Vol. 62 (2), pp. 260-271.