Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A
about
Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylationCdc25B functions as a novel coactivator for the steroid receptorsThe cell cycle-regulatory CDC25A phosphatase inhibits apoptosis signal-regulating kinase 1A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thalianaUltrasensitivity in the Regulation of Cdc25C by Cdk1Sialidase-like Asp-boxes: sequence-similar structures within different protein foldsCrystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5Arsenate reductases in prokaryotes and eukaryotes.Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme.A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii RhodaneseBacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatasesThe crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active siteStructural insights into molecular function of the metastasis-associated phosphatase PRL-3Crystal Structure of the Human Lymphoid Tyrosine Phosphatase Catalytic Domain: Insights into Redox Regulation,Crystal structure of YnjE fromEscherichia coli, a sulfurtransferase with three rhodanese domainsStructure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidationA specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase.Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase.Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function researchInactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transductionEctopic expression of Cdc25A accelerates the G(1)/S transition and leads to premature activation of cyclin E- and cyclin A-dependent kinasesArchaeal protein kinases and protein phosphatases: insights from genomics and biochemistryAn arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristicsPrediction of a ligand-induced conformational change in the catalytic core of Cdc25A.Compound library development guided by protein structure similarity clustering and natural product structureInhibition of a metal-dependent viral RNA triphosphatase by decavanadateOverview of protein structural and functional folds.The N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain.Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactionsChk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 bindingToward a molecular understanding of the interaction of dual specificity phosphatases with substrates: insights from structure-based modeling and high throughput screening.General library-based Monte Carlo technique enables equilibrium sampling of semi-atomistic protein models.The role of protein phosphatases in the regulation of mitogen and stress-activated protein kinases.The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relationsCharacterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin.Sac phosphatase domain proteins.Discordance between the binding affinity of mitogen-activated protein kinase subfamily members for MAP kinase phosphatase-2 and their ability to activate the phosphatase catalytically.Structure and catalytic mechanism of human protein tyrosine phosphatome.Microbial arsenic: from geocycles to genes and enzymes.The catalytic mechanism of protein tyrosine phosphatases revisited.
P2860
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P2860
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@ast
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@en
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@nl
type
label
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@ast
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@en
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@nl
prefLabel
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@ast
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@en
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@nl
P2093
P1433
P1476
Crystal structure of the catal ...... le control phosphatase, Cdc25A
@en
P2093
E B Fauman
H Piwnica-Worms
J P Cogswell
V G Montana
W J Rocque
P304
P356
10.1016/S0092-8674(00)81190-3
P407
P577
1998-05-15T00:00:00Z