Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.

Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.

Item
http://www.wikidata.org/entity/Q35543592
Catalytically Active Guanylyl Cyclase B Requires Endoplasmic Reticulum-mediated Glycosylation, and Mutations That Inhibit This Process Cause DwarfismDephosphorylation 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.Cell surface protein disulfide isomerase regulates natriuretic peptide generation of cyclic guanosine monophosphate.Nucleotidyl cyclase activity of particulate guanylyl cyclase A: comparison with particulate guanylyl cyclases E and F, soluble guanylyl cyclase and bacterial adenylyl cyclases CyaA and edema factorA human skeletal overgrowth mutation increases maximal velocity and blocks desensitization of guanylyl cyclase-B.Allosteric regulation of nucleotidyl cyclases: an emerging pharmacological target.Structures of soluble guanylate cyclase: implications for regulatory mechanisms and drug development.cGMP: transition from bench to bedside: a report of the 6th International Conference on cGMP Generators, Effectors and Therapeutic Implications.Nucleotide-binding mechanisms in pseudokinases.A preliminary study on methylphenidate-regulated gene expression in lymphoblastoid cells of ADHD patients.The Influence of Nitric Oxide on Soluble Guanylate Cyclase Regulation by Nucleotides: ROLE OF THE PSEUDOSYMMETRIC SITE.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.
P2860

Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.

Item
http://www.wikidata.org/entity/Q35543592
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@ast
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@en
type
label
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@ast
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@en
prefLabel
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@ast
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P698
P932
P356
P1433
P1476
Guanylyl cyclases A and B are ...... nding to the catalytic domain.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P698
P932