The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
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A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phaseMAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent mannerThe prolyl isomerase Pin1 in breast development and cancer1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptidesCks confers specificity to phosphorylation-dependent CDK signaling pathwaysCks1 is required for G(1) cyclin-cyclin-dependent kinase activity in budding yeastThree different binding sites of Cks1 are required for p27-ubiquitin ligationCyclin-dependent kinase-associated proteins Cks1 and Cks2 are essential during early embryogenesis and for cell cycle progression in somatic cellsThe APC/C recruits cyclin B1-Cdk1-Cks in prometaphase before D box recognition to control mitotic exitProlyl isomerase Pin1-mediated conformational change and subnuclear focal accumulation of Runx2 are crucial for fibroblast growth factor 2 (FGF2)-induced osteoblast differentiation.Utilizing the peptidyl-prolyl cis-trans isomerase pin1 as a probe of its phosphorylated target proteins. Examples of binding to nuclear proteins in a human kidney cell line and to tau in Alzheimer's diseased brain.CKS1At overexpression in Arabidopsis thaliana inhibits growth by reducing meristem size and inhibiting cell-cycle progression.Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.Oncogenic potential of a C.elegans cdc25 gene is demonstrated by a gain-of-function allele.Cks overexpression enhances chemotherapeutic efficacy by overriding DNA damage checkpoints.The biochemistry of mitosisA Synthetic Dosage Lethal Genetic Interaction Between CKS1B and PLK1 Is Conserved in Yeast and Human Cancer Cells.Targeting Conformational Activation of CDK2 Kinase.Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.The Prozone Effect Accounts for the Paradoxical Function of the Cdk-Binding Protein Suc1/CksLoss of cks1 homeostasis deregulates cell division cycle.The CDK subunit CKS2 counteracts CKS1 to control cyclin A/CDK2 activity in maintaining replicative fidelity and neurodevelopment.Cks1: Structure, Emerging Roles and Implications in Multiple CancersDifferential regulation of cellular senescence and differentiation by prolyl isomerase Pin1 in cardiac progenitor cellsDeterminants for activation of the atypical AGC kinase Greatwall during M phase entry.Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.CDK1 structures reveal conserved and unique features of the essential cell cycle CDK.The cyclin dependent kinase subunit Cks1 is required for infection-associated development of the rice blast fungus Magnaporthe oryzae.Expression profiling of genes and proteins in HaCaT keratinocytes: proliferating versus differentiated state.Multisite phosphorylation networks as signal processors for Cdk1.Regulatory dephosphorylation of CDK at G₂/M in plants: yeast mitotic phosphatase cdc25 induces cytokinin-like effects in transgenic tobacco morphogenesisInvolvement of the dehydroleucodine alpha-methylene-gamma-lactone function in GVBD inhibition in Bufo arenarum oocytes.p13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope.Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function.Molecular and biochemical characterization of the parvulin-type PPIases in Lotus japonicus.CKS Proteins Promote Checkpoint Recovery by Stimulating Phosphorylation of Treslin.Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase.Functional modules in the Arabidopsis core cell cycle binary protein-protein interaction network.Systematic localization of the Arabidopsis core cell cycle proteins reveals novel cell division complexes.
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P2860
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
@en
type
label
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
@en
prefLabel
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
@en
P2093
P2860
P356
P1476
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
@en
P2093
P2860
P304
36839-36842
P356
10.1074/JBC.274.52.36839
P407
P577
1999-12-01T00:00:00Z