Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Yue-Hao Wang"'
Publikováno v:
ChemMedChem. 2:1346-1360
3-Phenylpyrazolo[3,4-d]pyrimidine (PhPP) derivatives substituted with an alkyl or aryl carboxylic acid at the N1-endocyclic amine, such as PhPP-CH(2)COOH (IC(50)=250 microM), and peptides Ac-CIYKYY (IC(50)=400 microM) and Ac-YIYGSFK (IC(50)=570 micro
Publikováno v:
Journal of Biological Chemistry. 281:23776-23784
Src protein-tyrosine kinase contains a myristoylation motif, a unique region, an Src homology (SH) 3 domain, an SH2 domain, a catalytic domain, and a C-terminal tail. The C-terminal tail contains a Tyr residue, Tyr527. Phosphorylation of Tyr527 trigg
Publikováno v:
Journal of Molecular Biology. 357:1263-1273
The catalytic activity of protein tyrosine kinases is commonly regulated by domain-domain interactions. The C-terminal Src kinase (Csk) contains a catalytic domain and the regulatory SH3 and SH2 domains. Both the presence of the regulatory domains an
Autor:
Jiao-Nai Shi, Yue-Hao Wang
Publikováno v:
FEBS Letters. 459:448-452
Pyrophosphate-dependent 6-phosphofructo-1-phosphotransferase (PFP) consists of alpha (regulatory) and beta (catalytic) subunits. The alpha-subunit was previously reported to be much more susceptible to tryptic digestion than the beta-subunit. In this
Autor:
Yue-Hao Wang, Raymond Chollet
Publikováno v:
FEBS Letters. 328:215-218
C3-leaf phosphoenolpyruvate (PEP) carboxylase (PEPC) was purified about 1,000-fold from tobacco and displayed a final specific activity of 35 mumol/min/mg protein, an apparent Km (total PEP) of 95 muM [corrected] (both at pH 8.0, 30 degrees C), and a
Autor:
Yue-Hao Wang, Raymond Chollet
Publikováno v:
Archives of Biochemistry and Biophysics. 304:496-502
Following in situ renaturation and assay of protein kinase activity after denaturing electrophoresis of relatively impure samples of maize phosphoenolpyruvate carboxylase (PEPC) kinase, a approximately 30-kDa polypeptide was implicated as the best ca
Cytochrome P450c17 (P450c17) is the single microsomal enzyme that catalyzes steroid 17alpha-hydroxylase and 17,20 lyase activities. The ratio of lyase to hydroxylase activity of human P450c17 determines whether steroidogenesis leads to the synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ced3c885ebfb0ca03146d96dfac3c06d
https://europepmc.org/articles/PMC2850244/
https://europepmc.org/articles/PMC2850244/
Publikováno v:
Biochemistry. 46(35)
Csk and Src are two protein tyrosine kinases that share a similar overall multidomain structural organization and a high degree of sequence homology but have different substrate specificities and regulatory properties. In this study, we generated chi
Publikováno v:
Journal of medicinal chemistry. 49(25)
Protein tyrosine kinases use two Mg(2+) ions as cofactors in catalysis, one as the ATP-Mg complex (M1) and the other as an essential activator (M2). The M2-binding site has high affinity for transition metal cations such as cobalt and zinc. Taking ad
Publikováno v:
Biochemical and biophysical research communications. 346(2)
Enzymological studies of Src protein tyrosine kinase have been hindered by the lack of a suitable bacterial expression system. Poor expression of active Src appears to be due to toxicity associated with its kinase activity. To overcome this problem,