Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
about
Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactionsPhosphorylation of CLK2 at serine 34 and threonine 127 by AKT controls cell survival after ionizing radiationHuman autoimmune sera as molecular probes for the identification of an autoantigen kinase signaling pathwayDifferential effects of hyperphosphorylation on splicing factor SRp55SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elementsStructural analysis of UBL5, a novel ubiquitin-like modifierThe interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)Regulation and substrate specificity of the SR protein kinase Clk/StyThe ER repeat protein YT521-B localizes to a novel subnuclear compartmentSplicing Regulators and Their Roles in Cancer Biology and TherapyKinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein PhosphorylationComparative surface geometry of the protein kinase familyScreening for modulators of spermine tolerance identifies Sky1, the SR protein kinase of Saccharomyces cerevisiae, as a regulator of polyamine transport and ion homeostasis.Digoxin suppresses HIV-1 replication by altering viral RNA processingIdentification of a novel function of CX-4945 as a splicing regulatorDAP-like kinase interacts with the rat homolog of Schizosaccharomyces pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G2/M phase transition.Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCbetaII messenger ribonucleic acidInterplay between the alpharetroviral Gag protein and SR proteins SF2 and SC35 in the nucleus.Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk).Drosophila translational elongation factor-1gamma is modified in response to DOA kinase activity and is essential for cellular viability.The protein kinase Clk/Sty directly modulates SR protein activity: both hyper- and hypophosphorylation inhibit splicing.Multifunctional RNA processing protein SRm160 induces apoptosis and regulates eye and genital development in DrosophilaEmerging functions of SRSF1, splicing factor and oncoprotein, in RNA metabolism and cancer.The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germline cells and is expressed as both nuclear and cytoplasmic isoforms throughout development.In vitro characterization of the RS motif in N-terminal head domain of goldfish germinal vesicle lamin B3 necessary for phosphorylation of the p34cdc2 target serine by SRPK1Utilization of host SR protein kinases and RNA-splicing machinery during viral replicationDifferential effect of CLK SR Kinases on HIV-1 gene expression: potential novel targets for therapy.Htra2-beta 1 stimulates an exonic splicing enhancer and can restore full-length SMN expression to survival motor neuron 2 (SMN2)Stress-responsive maturation of Clk1/4 pre-mRNAs promotes phosphorylation of SR splicing factor.Dissection of darkener of apricot kinase isoform functions in DrosophilaSmall-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phosphorylation-regulated (Dyrk) kinases: development of chemical probe ML315.Superoxide dismutase is regulated by LAMMER kinase in Drosophila and human cells.Pharmacology of Modulators of Alternative Splicing.Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity.CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing.Release of SR Proteins from CLK1 by SRPK1: A Symbiotic Kinase System for Phosphorylation Control of Pre-mRNA Splicing.Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing.Hypoxia leads to significant changes in alternative splicing and elevated expression of CLK splice factor kinases in PC3 prostate cancer cells.
P2860
Q24291592-95BD4257-CACF-43F0-AF6C-00484E49EB40Q24294362-88805C41-7D17-4F7C-859A-019DDAB88BD1Q24316154-FD4532D3-B54C-4C30-9C16-7CCAA68D24C3Q24529916-32278F5C-4382-4E19-9DC2-CA82204CF305Q24548190-D1FF9A4A-A01A-43B5-8F56-8F9788DEAD00Q24644768-10B99D92-231C-4C63-A7C0-C39CEAFA71E9Q24651533-34EF573B-A275-446A-A2B8-1889E3104FC8Q24675674-FE0DC815-4353-4A5E-BAF5-536A174B5D42Q24685879-C3A32BA1-3CA4-4130-AFD4-978EAFDDDDA5Q26798158-45D4C86B-7BC4-4E49-A9AF-252E1107136DQ27654063-EA438DE0-FF7C-4ACA-ABB4-1D4CCE83AD80Q27656514-FEC4AEFA-A230-4124-8368-DA7676AED664Q27937203-CB537E8C-0261-47F9-88FE-625B0EEFB785Q28489086-70761E97-6ED2-42FA-94AF-ACA7B47D31F7Q28537999-7F1D6B5C-6B68-427E-B79E-5286B228D8C5Q28575564-E8B7080B-D052-48F6-9F21-09F4C25F1636Q28577714-F923D3D9-BFFB-45A7-B8FF-BC4305094BFCQ30663968-2FE194C9-5C6D-419F-83EB-06489874166FQ33595525-DBB57A52-D9BA-426B-ACA4-FFBBAFBDA268Q33628402-952C9B99-B4D2-4C08-BDA5-0D7E7F6FA3D3Q33959780-C0AEADAB-7B0E-4992-B473-E3749808B6DEQ34016603-1D8F5E8D-1304-44CE-B0B0-71DFF7DE88A1Q34040857-A64EC4D6-D309-4F6A-A3E1-096904CAFBB3Q34610541-E0BFEEC8-1FCB-4ECE-8CB5-428A7EB0FC81Q34774699-C5BB03F7-43BB-4A33-A20B-54E4CE43AE23Q34983999-96CC8646-DC5B-4747-87EF-7730889330CFQ35143725-42A99C0C-B235-46CB-8158-E606F992B1C3Q35210565-9F43A700-1FCE-4FD2-B8E4-B467284F64A2Q35276828-91B27D01-CE7D-4CB3-AB38-12324967CAA3Q36837033-87D5F92C-A2EF-4E52-8846-D23BF6B45567Q36876032-DB95053C-CCCB-41FC-9863-9EF60D56A24DQ37235751-F2E881FC-23B0-4825-BD86-C23CF7053A3FQ38776406-02D26B1C-0694-4F4B-95E1-7B1E7F1DEA4EQ38910392-C1F2C966-1D38-4B8B-8E44-82E3966DC41BQ39764495-9FDF230C-B9F1-492B-8276-B927C6D0B6F5Q41845300-DBFDCF80-B011-4393-BA20-7E07EE088CD9Q42917564-B3BBC958-3556-425E-8CE3-F766FE818BF2Q54118284-60213661-907B-4A24-9647-32C41F932873
P2860
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
description
1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1997
@ast
im September 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/09/15)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/09/15)
@nl
наукова стаття, опублікована у вересні 1997
@uk
مقالة علمية (نشرت في 15-9-1997)
@ar
name
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@ast
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@en
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@nl
type
label
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@ast
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@en
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@nl
prefLabel
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@ast
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@en
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@nl
P2093
P2860
P921
P1433
P1476
Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
@en
P2093
P2860
P304
P407
P478
326 ( Pt 3)
P577
1997-09-15T00:00:00Z