Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
about
Detection of a novel quiescence-dependent protein kinaseMitotic inactivation of a human SWI/SNF chromatin remodeling complexUltrasensitivity in the mitogen-activated protein kinase cascadeExpression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexesMKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathwayA proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK functionPhosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosisPhosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragmentsMKK3 was involved in larval settlement of the barnacle Amphibalanus amphitrite through activating the kinase activity of p38MAPKConversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical ModificationThe subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers.Dual specificity protein kinase activity of testis-specific protein kinase 1 and its regulation by autophosphorylation of serine-215 within the activation loopReplacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responsesBRAF activates and physically interacts with PAK to regulate cell motilityConformational changes in protein loops and helices induced by post-translational phosphorylation.Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleusPurification of a 12,020-dalton protein that enhances the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase.Induction of acetylcholine receptor gene expression by ARIA requires activation of mitogen-activated protein kinase.Replication protein A (RPA) phosphorylation prevents RPA association with replication centers.Molecular mechanisms of ATP and insulin synergistic stimulation of coronary artery smooth muscle growth.RPA2 is a direct downstream target for ATR to regulate the S-phase checkpoint.Protein phosphatase 2A-dependent dephosphorylation of replication protein A is required for the repair of DNA breaks induced by replication stressHuman cytochrome p450c17: single step purification and phosphorylation of serine 258 by protein kinase a.Engineered single nucleotide polymorphisms in the mosquito MEK docking site alter Plasmodium berghei development in Anopheles gambiae.A novel cross-talk in diacylglycerol signaling: the Rac-GAP beta2-chimaerin is negatively regulated by protein kinase Cdelta-mediated phosphorylationMAP kinase links the fertilization signal transduction pathway to the G1/S-phase transition in starfish eggs.O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin.Dominant mutations of Drosophila MAP kinase kinase and their activities in Drosophila and yeast MAP kinase cascades.Mitogen-activated protein kinase phosphorylates and negatively regulates basic helix-loop-helix-PAS transcription factor BMAL1.Activated MEK suppresses activation of PKR and enables efficient replication and in vivo oncolysis by Deltagamma(1)34.5 mutants of herpes simplex virus 1Identification of novel in vivo Raf-1 phosphorylation sites mediating positive feedback Raf-1 regulation by extracellular signal-regulated kinaseBiochemical and biological analysis of Mek1 phosphorylation site mutants.Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo.Halorhodopsin pumps Cl- and bacteriorhodopsin pumps protons by a common mechanism that uses conserved electrostatic interactions.Protein phosphorylation by semisynthesis: from paper to practice.Involvement of novel autophosphorylation sites in ATM activationAn intrinsic cell cycle checkpoint pathway mediated by MEK and ERK in Drosophila.Identification of novel therapeutic targets in acute leukemias with NRAS mutations using a pharmacologic approachPlk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures
P2860
Q22254205-1D8BC11F-D00D-48A2-AB7D-59B060969F71Q24596960-F8D2C9FE-B773-473F-8293-67A498683967Q24597665-EEE4B4A9-C5E7-4D80-9CFC-560D95FECACDQ24647211-D09D243C-1073-456B-B893-7BB7CB6D1D7EQ24650627-2C4478D2-F1FE-4D0C-BC53-7B40B3D7923EQ24651242-C189790E-E3E2-4864-95E6-3373D976BD5AQ24675701-1EA2D296-C252-4282-96B9-40A8D8BA81C7Q24685922-5BB79DFE-8D25-4849-A950-26B1341DBE8EQ27310997-F1068A39-9359-4A3A-9006-2327DEA6D0AEQ27678617-52C848C5-95B1-4D38-8F1A-718BC375582FQ27679437-3DF8CABB-78F6-4F68-BDF2-1C1B8708923BQ27876231-8EC9851F-D132-4F2C-AFDA-BDA7F5BE5A43Q28141810-1B7045BF-05BA-42B8-A140-064584C9C0D7Q28143168-DC4582EC-1268-4CF8-897D-FBD1628D967EQ28248127-C96C26F4-8EF1-4EFB-B989-4A94AF0235F4Q28469001-1C80A4DE-E813-4CEC-AB9E-D353757A3C83Q29620179-B59C2F2E-853D-4BF6-AFF5-D3750A974433Q30464224-7CA8505B-0828-43F4-B87D-E9FF1BBF229DQ30468691-472988DF-1C9D-4B20-9187-C24AE8D43383Q31048017-9404B01C-8C46-48E7-A3FA-E08229F3A95AQ31833773-1A918300-7E94-4DE8-BA50-80C2B5CB4C07Q33260135-BC52F435-42B8-4370-BB82-F8361C5E43C7Q33496409-EE904E93-A59A-4E02-BA51-854D3D85C73BQ33772407-5576BA4C-81F5-4C3D-9AAE-ACFBC0D8C800Q33830233-5D6219A1-4796-45EC-A130-155C441243DFQ33883417-AB547AF0-DFA2-458D-8ED8-D88BE9CEC60DQ33887095-E164E21A-FDEF-4889-94F3-CA9EA65CB8A8Q33911287-014150D0-1B1C-4533-AE5C-064BD3EA692BQ33969955-13C74795-E916-4C94-AE91-70C364600DABQ34099897-B57C8D8D-90B5-4034-BCC8-9B0A9B830FFAQ34302130-6367771B-5793-4840-86DC-44A4C118DC19Q34407252-2CF15881-FBDB-4B70-9A73-5D8BE109BB32Q34446879-5DEF9293-F7DD-4149-B48D-69D3E52825B2Q34473609-61EE09FF-C69C-4CF7-9DBF-B41671A30ED2Q34581378-59FB0456-C7EC-470A-9ABA-177AAB327C56Q34779578-6E6EFFA6-04F9-4294-9031-CC11FDAB1843Q34972885-B92182AE-3EFF-466D-A337-ACCFBF1F7AADQ34985294-64EED8B6-7191-4D75-B295-E106869358EBQ35592751-E9B46B7C-45C6-44F9-B680-83F9CE2D7855Q36568848-F3277DB7-5C5D-41EB-82E6-6FDBB2CC765A
P2860
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
description
1994 nî lūn-bûn
@nan
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
1994年论文
@zh
1994年论文
@zh-cn
name
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@ast
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@en
type
label
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@ast
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@en
prefLabel
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@ast
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@en
P2860
P356
P1476
Constitutive activation of Mek1 by mutation of serine phosphorylation sites.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.19.8960
P407
P577
1994-09-01T00:00:00Z