Extensive lipidation of a Torpedo cysteine string protein.
about
Quercetin targets cysteine string protein (CSPalpha) and impairs synaptic transmissionThe cysteine-string domain of the secretory vesicle cysteine-string protein is required for membrane targetingGAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunitsPlasma membrane localization is required for RGS4 function in Saccharomyces cerevisiaeHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation.Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases.Cysteine string protein (CSP) is an insulin secretory granule-associated protein regulating beta-cell exocytosis.Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein.Increased Expression of the Large Conductance, Calcium-Activated K+ (BK) Channel in Adult-Onset Neuronal Ceroid LipofuscinosisThe core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.Palmitoylation supports assembly and function of integrin-tetraspanin complexesNeuronal ceroid lipofuscinosis with DNAJC5/CSPα mutation has PPT1 pathology and exhibit aberrant protein palmitoylation.Cysteine string protein promotes proteasomal degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) by increasing its interaction with the C terminus of Hsp70-interacting protein and promoting CFTR ubiquitylation.Interaction between constitutively expressed heat shock protein, Hsc 70, and cysteine string protein is important for cortical granule exocytosis in Xenopus oocytesMolecular chaperones, α-synuclein, and neurodegeneration.Cysteine string protein (CSP) and its role in preventing neurodegeneration.Cysteine string protein functions directly in regulated exocytosis.Dual role of the cysteine-string domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein.Phosphorylation of Cysteine String Protein Triggers a Major Conformational SwitchA cluster of palmitoylated cysteines are essential for aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis.Autopalmitoylation of tubulin.Molecular basis for the RIN4 negative regulation of RPS2 disease resistance.
P2860
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P2860
Extensive lipidation of a Torpedo cysteine string protein.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Extensive lipidation of a Torpedo cysteine string protein.
@ast
Extensive lipidation of a Torpedo cysteine string protein.
@en
Extensive lipidation of a Torpedo cysteine string protein.
@nl
type
label
Extensive lipidation of a Torpedo cysteine string protein.
@ast
Extensive lipidation of a Torpedo cysteine string protein.
@en
Extensive lipidation of a Torpedo cysteine string protein.
@nl
prefLabel
Extensive lipidation of a Torpedo cysteine string protein.
@ast
Extensive lipidation of a Torpedo cysteine string protein.
@en
Extensive lipidation of a Torpedo cysteine string protein.
@nl
P2093
P1476
Extensive lipidation of a Torpedo cysteine string protein
@en
P2093
Gundersen CB
Mastrogiacomo A
P304
19197-19199
P407
P577
1994-07-01T00:00:00Z