Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Q Khai, Huynh"'
Autor:
Erinn E. Pagratis, Benjamin A. Turner, Xiaohong Liu, Kelly R. Pitts, Q. Khai Huynh, Nikos Pagratis, Laurie A. Castonguay, Sarah Wise, David Koditek, Christopher B. Glascock, Keith A. Koch, Brian Reid, Magdeleine Hung, Bin Han
Publikováno v:
SLAS Discovery. 16:724-733
Transforming growth factor β (TGF-β) type I receptor (activin receptor-like kinase 5, ALK5) has been identified as a promising target for fibrotic diseases. To find a novel inhibitor of ALK5, the authors performed a high-throughput screen of a libr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51895707278fcc75e88009c53f1325d5
https://doi.org/10.1177/1087057111405846
https://doi.org/10.1177/1087057111405846
Autor:
Nikos Pagratis, Q. Khai Huynh
Publikováno v:
Archives of Biochemistry and Biophysics. 506:130-136
Many of the cellular responses to Ca++ signaling are modulated by a family of multifunctional Ca++/calmodulin dependent protein kinases (CaMKs): CaMK I, CaMK II and CaMK IV. In order to further understand the role of CaMKs, we investigated the kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1af4f14c3f50c1a9c829dce6b05b805a
https://doi.org/10.1016/j.abb.2010.11.008
https://doi.org/10.1016/j.abb.2010.11.008
Autor:
Q. Khai Huynh
Publikováno v:
Archives of Biochemistry and Biophysics. 506:173-180
Signaling via pro-growth G protein coupled receptors triggers phosphorylation of HDAC5 on two serine residues (Ser₂₅₉ and Ser₄₉₈), resulting in nuclear export of HDAC5 and de-repression of downstream target genes. In the previous paper we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8496653ef3b78b2cd8932a8223b57beb
https://doi.org/10.1016/j.abb.2010.12.005
https://doi.org/10.1016/j.abb.2010.12.005
Autor:
Q. Khai Huynh, Timothy A. McKinsey
Publikováno v:
Archives of Biochemistry and Biophysics. 450:141-148
Class II histone deacetylases (HDACs) are signal-responsive repressors of gene transcription. In the heart, class II HDAC5 suppresses expression of genes that govern stress-induced cardiomyocyte growth. Signaling via pro-growth G protein coupled rece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cba664cbdc3429d33084518eb63742ce
https://doi.org/10.1016/j.abb.2006.02.014
https://doi.org/10.1016/j.abb.2006.02.014
Autor:
Sumathy Mathialagan, Hymavathi Boddupalli, Q. Khai Huynh, Sharon Rouw, Gary Lange, Troii Hall, David Creely, Rodney G. Combs, Catherine S. Tripp, Ann M. Donnelly, Kuniko Kretzmer, Beverley Reitz, James Caroll, Nandini Kishore
Publikováno v:
Journal of Biological Chemistry. 277:13840-13847
NF-kappaB is sequestered in the cytoplasm by the inhibitory IkappaB proteins. Stimulation of cells by agonists leads to the rapid phosphorylation of IkappaBs leading to their degradation that results in NF-kappaB activation. IKK-1 and IKK-2 are two d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b8e2af8226f4a10b1f6807157139c867
https://doi.org/10.1074/jbc.m110474200
https://doi.org/10.1074/jbc.m110474200
Publikováno v:
Journal of Biological Chemistry. 277:12550-12558
Nuclear factor-kappaB activation depends on phosphorylation and degradation of its inhibitor protein, IkappaB. The phosphorylation of IkappaBalpha on Ser(32) and Ser(36) is initiated by an IkappaB kinase (IKK) complex that includes a catalytic hetero
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1156e5228b5b2cb19e3d221838fb4879
https://doi.org/10.1074/jbc.m111526200
https://doi.org/10.1074/jbc.m111526200
Autor:
Troii Hall, Catherine S. Tripp, Bryan F. Kilpatrick, Beverly A. Reitz, Carol M. Koboldt, Cindy Sommers, Rodney G. Combs, Hymavathi Boddupalli, Jennifer L. Pierce, Q. Khai Huynh, Sharon A. Rouw, Robin A. Weinberg, Scott D. Hauser, Becky L. Hood, Judy A. Diaz-Collier
Publikováno v:
Journal of Biological Chemistry. 275:25883-25891
Nuclear factor kappa B (NF-kappaB) is a ubiquitous, inducible transcription factor that regulates the initiation and progression of immune and inflammatory stress responses. NF-kappaB activation depends on phosphorylation and degradation of its inhib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b22aa869e2c4f4a40e73ba43cbda7da2
https://doi.org/10.1074/jbc.m000296200
https://doi.org/10.1074/jbc.m000296200
Publikováno v:
Biochemical and biophysical research communications. 411(2)
Protein kinase D (PKD) regulates cardiac myocyte growth and contractility through phosphorylation of proteins such as class IIa histone deacetylases (HDACs) and troponin I (TnI). In response to agonists that activate G-protein-coupled receptors (GPCR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1516b6d0e6018c50081e3b26c7313ab
https://pubmed.ncbi.nlm.nih.gov/21726532
https://pubmed.ncbi.nlm.nih.gov/21726532
Autor:
Nandini, Kishore, Q Khai, Huynh, Sumathy, Mathialagan, Troii, Hall, Sharon, Rouw, David, Creely, Gary, Lange, James, Caroll, Beverley, Reitz, Ann, Donnelly, Hymavathi, Boddupalli, Rodney G, Combs, Kuniko, Kretzmer, Catherine S, Tripp
Publikováno v:
The Journal of biological chemistry. 277(16)
NF-kappaB is sequestered in the cytoplasm by the inhibitory IkappaB proteins. Stimulation of cells by agonists leads to the rapid phosphorylation of IkappaBs leading to their degradation that results in NF-kappaB activation. IKK-1 and IKK-2 are two d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fa6a95c23e5f054e1f97bbcd2ed5b370
https://pubmed.ncbi.nlm.nih.gov/11839743
https://pubmed.ncbi.nlm.nih.gov/11839743
Publikováno v:
Archives of biochemistry and biophysics. 379(2)
The enzyme glutamine:fructose 6-phosphate amidotransferase ( l -glutamine: d -fructose-6-phosphate amidotransferase; EC 2.6.1.16, GFAT) catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine. In view of the importa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::059398e2eda3f01c20974d745e9167dd
https://pubmed.ncbi.nlm.nih.gov/10898949
https://pubmed.ncbi.nlm.nih.gov/10898949