The pleckstrin homology (PH) domain of the Arf exchange factor Brag2 is an allosteric binding site.
about
Integrated Conformational and Lipid-Sensing Regulation of Endosomal ArfGEF BRAG2The BRAG/IQSec family of Arf GEFs.EFA6 controls Arf1 and Arf6 activation through a negative feedback loop.Quantitative Analysis of Guanine Nucleotide Exchange Factors (GEFs) as Enzymes.Polyphosphoinositide binding domains: Key to inositol lipid biology.Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease.Nucleotide exchange factors: Kinetic analyses and the rationale for studying kinetics of GEFs.Allosteric properties of PH domains in Arf regulatory proteins.Allosteric regulation of Arf GTPases and their GEFs at the membrane interface.Quantifying lipid changes in various membrane compartments using lipid binding protein domains.Using HHsearch to tackle proteins of unknown function: A pilot study with PH domainsKinetics of interaction between ADP-ribosylation factor-1 (Arf1) and the Sec7 domain of Arno guanine nucleotide exchange factor, modulation by allosteric factors, and the uncompetitive inhibitor brefeldin A.Multiple interactions between an Arf/GEF complex and charged lipids determine activation kinetics on the membrane.Brag2 differentially regulates β1- and β3-integrin-dependent adhesion in endothelial cells and is involved in developmental and pathological angiogenesis.
P2860
Q27680018-77F858A4-7B21-429D-831D-E26515C7CBCEQ30275740-F1C91BA3-2906-4FE2-9734-3CEA08B9619EQ34120075-DF1B3F91-228D-49A3-A1A5-7E5E21C53AA1Q34295121-274C9F1C-B089-4961-AF8B-B1A842F6B277Q35236004-71360571-C44D-48F0-B626-C9749C3D2835Q35749188-9EE90B87-3104-48DC-973D-729F675094AFQ36398898-2C0C62DC-AED0-4314-B2BE-B23E818E22D4Q36931366-7EA627AD-65D9-4679-9072-46AEDE2B24B6Q37457340-CBB78151-A95A-4DF1-B544-5808B65A4DC1Q39088749-A64D1EAA-F654-4C5E-9A44-4BCFD812A145Q39416569-612E9360-4C84-4D5B-BD41-3DDFA50527F7Q41915041-AD892B8C-E788-4779-A3E0-E794B11BFEE4Q46328382-095B793E-EB87-4EBA-93CE-055894FE916FQ47073755-95B765BB-400A-4035-BBEA-67DB38B550B0
P2860
The pleckstrin homology (PH) domain of the Arf exchange factor Brag2 is an allosteric binding site.
description
2012 nî lūn-bûn
@nan
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
2012年论文
@zh
2012年论文
@zh-cn
name
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@ast
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@en
type
label
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@ast
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@en
prefLabel
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@ast
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@en
P2093
P2860
P356
P1476
The pleckstrin homology (PH) d ...... is an allosteric binding site.
@en
P2093
Elizabeth Sztul
James M Gruschus
Paul A Randazzo
Xiaoying Jian
P2860
P304
24273-24283
P356
10.1074/JBC.M112.368084
P407
P577
2012-05-21T00:00:00Z