Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.
about
Evolutionary history of the vertebrate mitogen activated protein kinases familyCrystal structure of the p38 alpha-MAPKAP kinase 2 heterodimerSpecific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5Interacting JNK-docking sites in MKK7 promote binding and activation of JNK mitogen-activated protein kinasesA walk-through of the yeast mating pheromone response pathwaySpecificity of linear motifs that bind to a common mitogen-activated protein kinase docking grooveMAPKs in development: insights from Dictyostelium signaling pathwaysSelectivity of docking sites in MAPK kinasesIdentification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates.The Structure of the MAP2K MEK6 Reveals an Autoinhibitory DimerCrystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition stateA docking site in MKK4 mediates high affinity binding to JNK MAPKs and competes with similar docking sites in JNK substratesERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Mitogen-activated protein kinase signaling in the heart: angels versus demons in a heart-breaking tale.Computational prediction and experimental verification of new MAP kinase docking sites and substrates including Gli transcription factorsData-driven modeling reconciles kinetics of ERK phosphorylation, localization, and activity states.Novel function of DUSP14/MKP6 (dual specific phosphatase 14) as a nonspecific regulatory molecule for delayed-type hypersensitivity.A mitochondrial kinase complex is essential to mediate an ERK1/2-dependent phosphorylation of a key regulatory protein in steroid biosynthesis.Paradoxical results in perturbation-based signaling network reconstructionCombining docking site and phosphosite predictions to find new substrates: identification of smoothelin-like-2 (SMTNL2) as a c-Jun N-terminal kinase (JNK) substrateMolecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase.The noncatalytic amino terminus of mitogen-activated protein kinase phosphatase 1 directs nuclear targeting and serum response element transcriptional regulation.Characterization of an ERK-binding domain in microphthalmia-associated transcription factor and differential inhibition of ERK2-mediated substrate phosphorylation.Analysis of mitogen-activated protein kinase activation and interactions with regulators and substratesMechanisms of MAPK signalling specificity.Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo.Epitope-guided engineering of monobody binders for in vivo inhibition of Erk-2 signaling.Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.Genome-wide identification of mitogen-activated protein kinase gene family in Gossypium raimondii and the function of their corresponding orthologs in tetraploid cultivated cotton.Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase.Application of a peptide-based assay to characterize inhibitors targeting protein kinases from yeast.The Rab2A GTPase promotes breast cancer stem cells and tumorigenesis via Erk signaling activationSubstrate-dependent control of ERK phosphorylation can lead to oscillationsMapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.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.A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1.MAPK substrate competition integrates patterning signals in the Drosophila embryoCalcineurin modulates growth, stress tolerance, and virulence in Metarhizium acridum and its regulatory network.Identification of a DEF-type docking domain for extracellular signal-regulated kinases 1/2 that directs phosphorylation and turnover of the BH3-only protein BimEL.
P2860
Q21134977-B6E6D677-A747-4C97-A878-620320B4C8A4Q24294617-C36AEA31-DDCB-4F70-8AFA-6A841FE76500Q24294940-A4A8A6F6-A5C8-4446-8D48-B315F9CD439DQ24307753-328AFE40-68E7-4BEA-AB33-0BB64005D378Q24603343-DB3BA6FC-6C85-482D-A661-CF009B6C2E49Q24610682-BA72A300-17DD-4B20-AC06-7591CAA63C5FQ24621902-C5DE8422-26A0-440A-A232-0C51830A2274Q24651580-D13AC606-8D94-433E-AB45-ACD03D3F5934Q25255706-A25D200E-CFE7-43C6-8619-30633AA3E766Q27653414-95C76121-997B-4DB8-B28E-6B8E3F4581AAQ27677567-E6DDDC72-2C8C-4976-8DE7-4D20D10523DEQ28177171-9DEAFA51-FEF8-4B4F-8AD2-720D8034F4CAQ28271104-DB48B853-98C3-44E4-8CCB-28E63EF4A042Q28296128-80AA9F07-EE08-4628-A228-E6AF25CA99C5Q28475319-CBEBDD1B-BA02-407D-9821-111246D2975DQ30746989-4ABC6E10-EFA5-4757-BEF8-8A311188B47BQ33270947-1EC8E4A1-DD04-4CD3-B68F-7874B5152548Q33314909-CFF83CC4-ADDA-4D85-B2E2-84825F05898FQ33803292-420CF7E3-02FA-4FCA-8FE8-2F7BCE5B5857Q34044220-9A07384A-1B72-44FF-9769-BEBC085FFBE0Q34355962-81B52C58-F4B8-4F5B-934C-17B607492F96Q34419558-5A6DD745-6053-405E-81A2-44FA3868D585Q34473579-3067F667-56A9-4F8E-AF5B-A0381F120EE0Q34473595-8E282129-070D-4D8C-A251-64168E5C7876Q34473602-A2C8A766-18D0-457F-8630-979E117D6E3CQ34473609-9277033E-200F-4E7E-8896-17F266689AE9Q34507603-CCD5FD8C-CD33-45B1-B1C7-2EF30DBEF605Q34600125-04BEAC5C-49C0-4D52-B318-C0F9BB5CCA75Q34729226-EEFA4372-76F9-4125-AE38-AFE2A08ED23DQ35049203-59A37902-4761-4D30-A9C9-879E04CC77A5Q35124410-85118E15-885D-4DFC-B6E0-2CE6A1D92EFEQ35464851-DF675EE6-AA89-4FA9-8D6E-C0EE69748B38Q35815838-18FB9BD6-B2F2-491C-950F-C1E6A9592E4EQ35865554-0F12C090-D7A2-42A7-9BB1-E4C5006B0F06Q35991347-D433AE86-89E1-4857-BDF7-2A5EA57547B5Q36283723-D56C4506-161E-456F-890A-51FAF8FB80F6Q36322380-6DAD1FF3-1136-4412-8076-B360BB6CA1DDQ39829894-C2648FE3-9842-4159-9755-368F6DF9E8D8Q40200559-357600D7-0158-432D-86A3-ED1D8E1782C1Q40454938-6565DF39-02BB-4CC3-8C50-E7B822069C14
P2860
Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
name
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@ast
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@en
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@nl
type
label
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@ast
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@en
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@nl
prefLabel
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@ast
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@en
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@nl
P2860
P356
P1433
P1476
Docking sites on mitogen-activ ...... crucial for enzymic activity.
@en
P2093
A Jane Bardwell
Mahsa Abdollahi
P2860
P304
P356
10.1042/BJ20021806
P407
P50
P577
2003-03-01T00:00:00Z