Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
about
Catalytically Active Guanylyl Cyclase B Requires Endoplasmic Reticulum-mediated Glycosylation, and Mutations That Inhibit This Process Cause DwarfismHigh density and ligand affinity confer ultrasensitive signal detection by a guanylyl cyclase chemoreceptor.A functional screen provides evidence for a conserved, regulatory, juxtamembrane phosphorylation site in guanylyl cyclase a and B.Dephosphorylation and inactivation of NPR2 guanylyl cyclase in granulosa cells contributes to the LH-induced decrease in cGMP that causes resumption of meiosis in rat oocytes.Allosteric modification, the primary ATP activation mechanism of atrial natriuretic factor receptor guanylate cyclaseThe indolocarbazole, Gö6976, inhibits guanylyl cyclase-A and -B.ATP potentiates competitive inhibition of guanylyl cyclase A and B by the staurosporine analog, Gö6976: reciprocal regulation of ATP and GTP bindingGuanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.ANP-induced signaling cascade and its implications in renal pathophysiologyRegulation and therapeutic targeting of peptide-activated receptor guanylyl cyclases.Dephosphorylation of juxtamembrane serines and threonines of the NPR2 guanylyl cyclase is required for rapid resumption of oocyte meiosis in response to luteinizing hormone.Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation.Skeletal overgrowth-causing mutations mimic an allosterically activated conformation of guanylyl cyclase-B that is inhibited by 2,4,6,-trinitrophenyl ATP.A Glutamate-Substituted Mutant Mimics the Phosphorylated and Active Form of Guanylyl Cyclase-A.Mutation of a conserved lysine in the kinase homology domain reduces the natriuretic peptide-dependent activity and phosphorylation of guanylyl cyclase-A.Dephosphorylation of juxtamembrane serines and threonines of the NPR2 guanylyl cyclase regulates oocyte meiotic resumption.
P2860
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P2860
Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
@en
type
label
Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
@en
prefLabel
Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
@en
P2093
P2860
P356
P1433
P1476
Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.
@en
P2093
Andrea R Yoder
Lincoln R Potter
Matthew D Stone
Timothy J Griffin
P2860
P304
10137-10145
P356
10.1021/BI101700E
P407
P577
2010-11-08T00:00:00Z