Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation - Wikidata - wikimedia - TriplyDB

Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation

Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation

http://www.wikidata.org/entity/Q27654063

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Phosphorylation mechanism and structure of serine-arginine protein kinases Regulation of pol III transcription by nutrient and stress signaling pathways Clks 1, 2 and 4 prevent chromatin breakage by regulating the Aurora B-dependent abscission checkpoint.Comparative surface geometry of the protein kinase family Structure and functional characterization of the atypical human kinase haspin Specific CLK Inhibitors from a Novel Chemotype for Regulation of Alternative Splicing Crystal Structures of ABL-Related Gene (ABL2) in Complex with Imatinib, Tozasertib (VX-680), and a Type I Inhibitor of the Triazole Carbothioamide Class The Cryptosporidium parvum Kinome Structures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate Recognition Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic gluconeogenesis Identification of CLK1 Inhibitors by a Fragment-linking Based Virtual Screening.Biophysical characterization of recombinant proteins: a key to higher structural genomics success Structural and evolutionary divergence of eukaryotic protein kinases in Apicomplexa.Rapid determination of multiple linear kinase substrate motifs by mass spectrometry Clk/STY (cdc2-like kinase 1) and Akt regulate alternative splicing and adipogenesis in 3T3-L1 pre-adipocytes Pharmacophore and 3D-QSAR characterization of 6-arylquinazolin-4-amines as Cdc2-like kinase 4 (Clk4) and dual specificity tyrosine-phosphorylation-regulated kinase 1A (Dyrk1A) inhibitors Differential effect of CLK SR Kinases on HIV-1 gene expression: potential novel targets for therapy.Benzobisthiazoles Represent a Novel Scaffold for Kinase Inhibitors of CLK Family Members.Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phosphorylation-regulated (Dyrk) kinases: development of chemical probe ML315.N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases.Functional divergence and evolutionary turnover in mammalian phosphoproteomes.Uncovering the global host cell requirements for influenza virus replication via RNAi screening.A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics.Role of Host Genes in Influenza Virus Replication.Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates.Ancestral resurrection reveals evolutionary mechanisms of kinase plasticity.A triple exon-skipping luciferase reporter assay identifies a new CLK inhibitor pharmacophore.Molecular structures of cdc2-like kinases in complex with a new inhibitor chemotype.Advancements in Host-Based Interventions for Influenza Treatment Identification of Plant Homologues of Dual Specificity Yak1-Related Kinases

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Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation

http://www.wikidata.org/entity/Q27654063

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2009 nî lūn-bûn

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2009 թուականի Մարտին հրատարակուած գիտական յօդուած

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2009 թվականի մարտին հրատարակված գիտական հոդված

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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J.STR.2008.12.023

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Kinase Domain Insertions Defin ...... in SR Protein Phosphorylation

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Alex N Bullock

http://www.w3.org/2001/XMLSchema#string

Ann L Amos

http://www.w3.org/2001/XMLSchema#string

Benjamin E Turk

http://www.w3.org/2001/XMLSchema#string

Evangelos Papagrigoriou

http://www.w3.org/2001/XMLSchema#string

Frank H Niesen

http://www.w3.org/2001/XMLSchema#string

Gourisankar Ghosh

http://www.w3.org/2001/XMLSchema#string

Judit E Debreczeni

http://www.w3.org/2001/XMLSchema#string

Kunde Guo

http://www.w3.org/2001/XMLSchema#string

Peter Rellos

http://www.w3.org/2001/XMLSchema#string

Sanjan Das

http://www.w3.org/2001/XMLSchema#string

P2860

The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B

The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing

A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators

SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells

The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution

A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1

Inhibition of cyclin-dependent kinases, GSK-3beta and CK1 by hymenialdisine, a marine sponge constituent

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b

SR protein kinase 1 is resilient to inactivation

Structural analysis identifies imidazo[1,2-b]pyridazines as PIM kinase inhibitors with in vitro antileukemic activity

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10.1016/J.STR.2008.12.023

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3

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19278650

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phosphorylation

structural biology

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2667211

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