Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
about
Centrosome-associated regulators of the G(2)/M checkpoint as targets for cancer therapyCaenorhabditis elegans cyclin B3 is required for multiple mitotic processes including alleviation of a spindle checkpoint-dependent block in anaphase chromosome segregationRegulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and EGG-5 during the oocyte-to-embryo transitionFeedback Regulation of Kinase Signaling Pathways by AREs and GREsThe final link: tapping the power of chemical genetics to connect the molecular and biologic functions of mitotic protein kinasesTuning a Three-Component Reaction For Trapping Kinase Substrate ComplexesChemical genetic screen for AMPKα2 substrates uncovers a network of proteins involved in mitosisChemical genetic identification of NDR1/2 kinase substrates AAK1 and Rabin8 Uncovers their roles in dendrite arborization and spine developmentMST3 kinase phosphorylates TAO1/2 to enable Myosin Va function in promoting spine synapse developmentThe cell proliferation antigen Ki-67 organises heterochromatinDDK dependent regulation of TOP2A at centromeres revealed by a chemical genetics approachModulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogenCell cycle-regulated membrane binding of NuMA contributes to efficient anaphase chromosome separation.Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling.The serine/threonine kinase Par1b regulates epithelial lumen polarity via IRSp53-mediated cell-ECM signaling.Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells.A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1.Protein kinases display minimal interpositional dependence on substrate sequence: potential implications for the evolution of signalling networksDepletion of nucleoporins from HeLa nuclear pore complexes to facilitate the production of ghost pores for in vitro reconstitutionPhosphoproteomics for the massesProteogenomic convergence for understanding cancer pathways and networks.Evidence toward a dual phosphatase mechanism that restricts Aurora A (Thr-295) phosphorylation during the early embryonic cell cycle.Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosisFinding the middle ground: how kinetochores power chromosome congression.Generation and characterization of an analog-sensitive PERK allele.Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic functionKinase-Catalyzed Biotinylation.Global discovery of high-NaCl-induced changes of protein phosphorylationPhosphorylation-dependent kinase-substrate cross-linkingHyperphosphorylation by cyclin B/CDK1 in mitosis resets CUX1 DNA binding clock at each cell cycle.Emerging technologies to map the protein methylome.Expanding applications of chemical genetics in signal transduction.Changes in Ect2 localization couple actomyosin-dependent cell shape changes to mitotic progressionIn vivo conditions to identify Prkci phosphorylation targets using the analog-sensitive kinase method in zebrafish.The retroviral restriction ability of SAMHD1, but not its deoxynucleotide triphosphohydrolase activity, is regulated by phosphorylationNup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region.Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.The generality of kinase-catalyzed biotinylation.
P2860
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P2860
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@ast
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@en
type
label
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@ast
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@en
prefLabel
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@ast
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates.
@en
P2860
P356
P1476
Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
@en
P2093
Justin D Blethrow
Kevan M Shokat
P2860
P304
P356
10.1073/PNAS.0708966105
P407
P577
2008-01-30T00:00:00Z