Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity.
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Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking grooveStructure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2Growth arrest signaling of the Raf/MEK/ERK pathway in cancer.Quantitative in vivo fluorescence cross-correlation analyses highlight the importance of competitive effects in the regulation of protein-protein interactionsDual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.Enzyme kinetics and interaction studies for human JNK1β1 and substrates activating transcription factor 2 (ATF2) and c-Jun N-terminal kinase (c-Jun).Examining docking interactions on ERK2 with modular peptide substrates.Small-molecule inhibitors of ERK-mediated immediate early gene expression and proliferation of melanoma cells expressing mutated BRafStructure of extracellular signal-regulated kinase 2 in complex with ATP and ADP.Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomicsA derivative of chrysin suppresses two-stage skin carcinogenesis by inhibiting mitogen- and stress-activated kinase 1.ERK mutations confer resistance to mitogen-activated protein kinase pathway inhibitors.Autophagy proteins regulate ERK phosphorylation.Stepwise evolution of Elk-1 in early deuterostomes.Constitutive K-RasG12D activation of ERK2 specifically regulates 3D invasion of human pancreatic cancer cells via MMP-1.Feedback regulation by Atf3 in the endothelin-1-responsive transcriptome of cardiomyocytes: Egr1 is a principal Atf3 targetStathmin regulates microtubule dynamics and microtubule organizing center polarization in activated T cells.A cellular threshold for active ERK1/2 levels determines Raf/MEK/ERK-mediated growth arrest versus death responses.Extracellular-Regulated Kinases: Signaling From Ras to ERK Substrates to Control Biological Outcomes.
P2860
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P2860
Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
Quantitative analysis of ERK2 ...... determining binding affinity.
@ast
Quantitative analysis of ERK2 ...... determining binding affinity.
@en
Quantitative analysis of ERK2 ...... determining binding affinity.
@nl
type
label
Quantitative analysis of ERK2 ...... determining binding affinity.
@ast
Quantitative analysis of ERK2 ...... determining binding affinity.
@en
Quantitative analysis of ERK2 ...... determining binding affinity.
@nl
prefLabel
Quantitative analysis of ERK2 ...... determining binding affinity.
@ast
Quantitative analysis of ERK2 ...... determining binding affinity.
@en
Quantitative analysis of ERK2 ...... determining binding affinity.
@nl
P2093
P2860
P356
P1476
Quantitative analysis of ERK2 ...... determining binding affinity.
@en
P2093
Fengming Chen
Kimberly A Burkhard
Paul Shapiro
P2860
P304
P356
10.1074/JBC.M110.177899
P407
P577
2010-11-22T00:00:00Z