Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Shui-Zhong Yan"'
Autor:
Sergei V. Bykov, Adrian C. Murza, Wei-Jen Tang, Jeff A. Beeler, Sanford A. Asher, Shui-Zhong Yan
Publikováno v:
Biochemistry. 43:15463-15471
Adenylyl cyclase (AC) is a prototypical cell-signaling molecule expressed in virtually all organisms from bacteria to man. While C1b, a poorly conserved region within mammalian AC, has been implicated in numerous isoform-specific regulatory propertie
Publikováno v:
Journal of Biological Chemistry. 276:8500-8506
Mammalian membrane-bound adenylyl cyclase consists of two highly conserved cytoplasmic domains (C1a and C2a) separated by a less conserved connecting region, C1b, and one of two transmembrane domains, M2. The C1a and C2a domains form a catalytic core
Autor:
Radmila Sarac, Kathy Beckingham, Shui-Zhong Yan, Wei-Jen Tang, A. Bohm, Zenon Grabarek, Chester L. Drum, Yasuko Mabuchi
Publikováno v:
Journal of Biological Chemistry. 275:36334-36340
The edema factor exotoxin produced by Bacillus anthracis is an adenylyl cyclase that is activated by calmodulin (CaM) at resting state calcium concentrations in infected cells. A C-terminal 60-kDa fragment corresponding to the catalytic domain of ede
Publikováno v:
Molecular Pharmacology. 53:182-187
Forskolin potently activates all cloned mammalian adenylyl cyclases except type IX by interacting with two homologous cytoplasmic domains (C1 and C2) that form the catalytic core. A mutational analysis of the IIC2 protein (C2 domain from type II aden
Publikováno v:
Journal of Biological Chemistry. 272:12342-12349
Mammalian adenylyl cyclases have two homologous cytoplasmic domains (C1 and C2), and both domains are required for the high enzymatic activity. Mutational and genetic analyses of type I and soluble adenylyl cyclases suggest that the C2 domain is cata
Publikováno v:
Journal of Biological Chemistry. 271:10941-10945
Mammalian adenylyl cyclases have two homologous cytoplasmic domains (C1 and C2). The first cytoplasmic domain of type I enzyme (IC1) and the second cytoplasmic domain of type II enzyme (IIC2-delta 3, a construct in which 36 N-terminal amino acids of
Publikováno v:
Biochemistry. 43(49)
Adenylyl cyclase (AC) is a prototypical cell-signaling molecule expressed in virtually all organisms from bacteria to man. While C1b, a poorly conserved region within mammalian AC, has been implicated in numerous isoform-specific regulatory propertie
Autor:
Zenon Grabarek, Shui-Zhong Yan, Dan Lu, Joel Bard, Wei-Jen Tang, Yuequan Shen, Chester L. Drum, Sandriyana Soelaiman, Andrew Bohm
Publikováno v:
Nature. 415(6870)
Oedema factor, a calmodulin-activated adenylyl cyclase, is important in the pathogenesis of anthrax. Here we report the X-ray structures of oedema factor with and without bound calmodulin. Oedema factor shares no significant structural homology with
Autor:
Shui-Zhong, Yan, Wei-Jen, Tang
Publikováno v:
Methods in enzymology. 344
Autor:
Wei-Jen Tang, Shui-Zhong Yan
Adenylyl cyclase is the sole enzyme to synthesize cyclic AMP (cAMP), a key, second messenger that regulates diverse physiological responses including sugar and lipid metabolism, olfaction, and cell growth and differentiation. Most adenylyl cyclase ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfca524e2ef6ecfa06674f4d42782e6f
https://doi.org/10.1016/s0076-6879(02)45019-7
https://doi.org/10.1016/s0076-6879(02)45019-7