Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove
about
Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) moduleJNK Signaling: Regulation and Functions Based on Complex Protein-Protein PartnershipsMAPK-Activated Protein Kinases (MKs): Novel Insights and ChallengesProtein–peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinaseStructure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPKCrystal structure of the p38α MAP kinase in complex with a docking peptide from TAB1The structural pathway of interleukin 1 (IL-1) initiated signaling reveals mechanisms of oncogenic mutations and SNPs in inflammation and cancerCo-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tailStructure-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 2Selective mitogen activated protein kinase activity sensors through the application of directionally programmable D domain motifsStructure and dynamics of the MKK7-JNK signaling complexERK1/2/MAPK pathway-dependent regulation of the telomeric factor TRF2.Structural and functional characterization of the recombinant death domain from death-associated protein kinase.Structural and functional basis for p38-MK2-activated Rsk signaling in toll-like receptor-stimulated dendritic cells.Structural basis and biological consequences for JNK2/3 isoform selective aminopyrazoles.Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex.The Structure of an NDR/LATS Kinase-Mob Complex Reveals a Novel Kinase-Coactivator System and Substrate Docking Mechanism.The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteinsMapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.Effects of MEK inhibitors GSK1120212 and PD0325901 in vivo using 10-plex quantitative proteomics and phosphoproteomics.The human Na(+)/H(+) exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions.Failure to Target RANKL Signaling Through p38-MAPK Results in Defective Osteoclastogenesis in the Microphthalmia Cloudy-Eyed Mutant.Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY.Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated KinaseThe differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular studyA Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation.Structural basis for the regulation of the mitogen-activated protein (MAP) kinase p38α by the dual specificity phosphatase 16 MAP kinase binding domain in solutionPhosphorylation of DGCR8 increases its intracellular stability and induces a progrowth miRNA profile.Small G proteins Rac1 and Ras regulate serine/threonine protein phosphatase 5 (PP5)·extracellular signal-regulated kinase (ERK) complexes involved in the feedback regulation of Raf1.PPARγ recruitment to active ERK during memory consolidation is required for Alzheimer's disease-related cognitive enhancementMolecular basis of MAP kinase regulation.Revisiting protein kinase-substrate interactions: Toward therapeutic development.Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist.Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases.Structure-Guided Strategy for the Development of Potent Bivalent ERK Inhibitors.The eukaryotic linear motif resource - 2018 update.Engineering and cytosolic delivery of a native regulatory protein and its variants for modulation of ERK2 signaling pathway.Specificity of phosphorylation responses to MAP kinase pathway inhibitors in melanoma cells.
P2860
Q24600375-970BCB36-311C-40F3-9724-7C3BDB99506DQ26741279-3C6EF84A-F27E-40CB-94B2-89F435935B83Q26771339-904F3E53-C8B3-48DB-B34D-23658E0AF5F4Q27676946-7A427737-39D7-4DDE-BA18-E84B9C35AA22Q27677302-82D5AED7-55C7-447A-8273-263E0C83D53FQ27684727-EEF93A94-53AB-4152-9518-570274CE9285Q28539757-183AAD6A-A14A-4A1A-8AC4-4A4138E3D9AEQ28544906-A88EAE0F-2E70-4A60-9C4D-52F8C19C92D9Q30376203-8CF3E673-2083-4D37-8398-72995A2F2F42Q34193885-29CED376-5AC0-4EE1-8396-05B9DAF2C0E5Q34465579-8B5065D8-6161-46B1-9A2C-F254E6B198B6Q34532595-20839A3E-C56F-445E-862B-3D9E7106EBDFQ34905825-E9372C3E-36F1-407F-84D5-D85A640D5CB4Q34968461-CDDFC6F9-6FCF-4829-A098-5A1192DF163DQ35015415-105EFBEA-A056-43F8-A4A8-0DB081A5A383Q35122900-44257E55-05E5-4A55-8AB5-6F4FF06BC578Q35157014-20C357E7-7D9C-453D-91C4-C7BC7AE7E18BQ35597254-090DB6BC-F3C0-47BB-8C72-02941A7FB13FQ35777940-57A5B12E-790F-4EB9-8788-9B42EB5E0519Q35865554-B80EB72F-C6DD-4C95-AF6B-D6C74880AE34Q35891699-1786E5C8-0212-4BEC-9095-73E35144C6F1Q35991347-61311D87-B577-43AF-A26E-F58BDB18C5A8Q36283723-E8EB55F6-3A27-47A3-817B-45DDA357E353Q36331194-43397BF2-CBED-413C-8C98-6E5B245297F4Q36419214-4B63B68C-F811-4F43-8A69-B80BE7962CCFQ36755114-E42D0708-D557-47EA-9C36-22E6DB87A3EAQ37161124-3062FCC5-AC3C-417E-A969-01EA9FD9FB21Q37194952-4572F997-2C5C-44F8-908F-822FE47E716CQ37201320-95DB5964-A0D6-4793-BC37-682B3CACBB0FQ37483222-24D5A3D7-FAB3-463C-8DE5-266C4F89BF29Q37583522-86AABDB2-8CFE-4CD2-819F-18DF043EA4C4Q37633627-601D8A81-C8E6-4A8B-AD6B-4D6E04197A00Q38151621-45D2994F-8197-4E9E-92C6-361C7CEA74C6Q38789563-119B9FAA-950A-4B77-82EC-B83686332768Q40435051-4C0AC4E3-EEE0-4A23-85C7-5367081E3171Q42276390-BE5AB4DA-3EB9-4D71-850A-3FBC45CEC3A9Q46178714-E774B7D0-A1DE-4989-9D33-D579425E0CA1Q47159538-021871D8-EC43-4C7E-88C2-FC3F5D82B3EBQ47250549-1DBC4376-8048-41D6-B8A9-B782317AF553Q47279069-9E3F91BB-B91B-4D58-8BD2-22B7BBB21EFE
P2860
Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին 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
Specificity of linear motifs t ...... protein kinase docking groove
@ast
Specificity of linear motifs t ...... protein kinase docking groove
@en
Specificity of linear motifs t ...... protein kinase docking groove
@nl
type
label
Specificity of linear motifs t ...... protein kinase docking groove
@ast
Specificity of linear motifs t ...... protein kinase docking groove
@en
Specificity of linear motifs t ...... protein kinase docking groove
@nl
altLabel
Specificity of Linear Motifs T ...... Protein Kinase Docking Groove
@en
prefLabel
Specificity of linear motifs t ...... protein kinase docking groove
@ast
Specificity of linear motifs t ...... protein kinase docking groove
@en
Specificity of linear motifs t ...... protein kinase docking groove
@nl
P2093
P2860
P3181
P1433
P1476
Specificity of linear motifs t ...... protein kinase docking groove
@en
P2093
András Zeke
Anita Alexa
Attila Reményi
Gergő Gógl
Hagen Blankenburg
János Varga
Mario Albrecht
Tünde Bárkai
Ágnes Garai
P2860
P3181
P356
10.1126/SCISIGNAL.2003004
P407
P577
2012-10-09T00:00:00Z