Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
about
Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complexNuclear localization of protein kinase U-alpha is regulated by 14-3-3Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteinsModulation of human DNA topoisomerase IIalpha function by interaction with 14-3-3epsilonMRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrestImpaired binding of 14-3-3 to C-RAF in Noonan syndrome suggests new approaches in diseases with increased Ras signalingDynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sitesMADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3 binding site of myeloid leukemia factor 1Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motifParkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3Regulation of Raf-1 kinase activity by the 14-3-3 family of proteinsYSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zetaProtein binding and signaling properties of RIN1 suggest a unique effector function14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent mannerActivation-modulated association of 14-3-3 proteins with Cbl in T cells14-3-3 proteins associate with cdc25 phosphatasesPhosphorylation-dependent regulation of SCF(Fbx4) dimerization and activity involves a novel component, 14-3-3ɛ14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylationMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsPhosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteinsIsoform-specific localization of A-RAF in mitochondriaInhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cellsBcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding sitePhosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signalingRheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals.Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and functionIncreased expression of the Ras suppressor Rsu-1 enhances Erk-2 activation and inhibits Jun kinase activationRegulation of poly(A) polymerase by 14-3-3epsilonRaf-interactome in tuning the complexity and diversity of Raf function.The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307.Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Uncoupling proteins 2 and 3 interact with members of the 14.3.3 familyIdentification of a novel interaction between integrin beta1 and 14-3-3betaTrihydrophobin 1 is a new negative regulator of A-Raf kinase14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent mannerProtection against beta-amyloid-induced apoptosis by peptides interacting with beta-amyloid14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain14-3-3 protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain14-3-3 proteins interact with specific MEK kinases
P2860
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P2860
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
description
1994 nî lūn-bûn
@nan
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին 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
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@ast
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en-gb
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@nl
type
label
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@ast
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en-gb
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@nl
prefLabel
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@ast
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en-gb
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@nl
P2093
P3181
P356
P1433
P1476
Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
@en
P2093
F McCormick
R Ruggieri
S G Macdonald
P304
P3181
P356
10.1126/SCIENCE.8085158
P407
P577
1994-09-16T00:00:00Z