Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein - Wikidata - wikimedia - TriplyDB

Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein

Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein

http://www.wikidata.org/entity/Q24673603

about

Inhibition of hepatitis C virus replication by a specific inhibitor of serine-arginine-rich protein kinase Serine-arginine protein kinases: a small protein kinase family with a large cellular presence The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2 Hepatitis B virus morphogenesis Virus strategies for passing the nuclear envelope barrier Centronuclear myopathy in mice lacking a novel muscle-specific protein kinase transcriptionally regulated by MEF2 Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically.Screening and identification of interacting proteins with hepatitis B virus core protein in leukocytes and cloning of new gene C1.Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity Phosphoacceptors threonine 162 and serines 170 and 178 within the carboxyl-terminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication.A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro.Phosphorylation state-dependent interactions of hepadnavirus core protein with host factors A theoretical study of SRPK interaction with the flexible domains of hepatitis B capsids.C-terminal substitution of HBV core proteins with those from DHBV reveals that arginine-rich 167RRRSQSPRR175 domain is critical for HBV replication.Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.An RS motif within the Epstein-Barr virus BLRF2 tegument protein is phosphorylated by SRPK2 and is important for viral replication.Human papillomavirus type 1 E1^E4 protein is a potent inhibitor of the serine-arginine (SR) protein kinase SRPK1 and inhibits phosphorylation of host SR proteins and of the viral transcription and replication regulator E2 Analyses of phosphorylation events in the rubella virus capsid protein: role in early replication events An efficient proteomics method to identify the cellular targets of protein kinase inhibitors.Utilization of host SR protein kinases and RNA-splicing machinery during viral replication Regulation of multiple stages of hepadnavirus replication by the carboxyl-terminal domain of viral core protein in trans.HBV life cycle: entry and morphogenesis.Role of peroxisome proliferator-activated receptor gamma coactivator 1alpha in AKT/PKB-mediated inhibition of hepatitis B virus biosynthesis.Whole-Chain Tick Saliva Proteins Presented on Hepatitis B Virus Capsid-Like Particles Induce High-Titered Antibodies with Neutralizing Potential Nuclear import of hepatitis B virus capsids and release of the viral genome.A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.Cyclin-dependent kinase 2 phosphorylates s/t-p sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids.Hepatitis B virus-cell interactions and pathogenesis.Functional interplay between viral and cellular SR proteins in control of post-transcriptional gene regulation.HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acids Phosphorylation events during viral infections provide potential therapeutic targets.Host factors involved in hepatitis B virus maturation, assembly, and egress.Hepatitis B core-based virus-like particles to present heterologous epitopes.Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Pharmacology of Modulators of Alternative Splicing.Presence and utility of intrinsically disordered regions in kinases.Nuclear localization of the duck hepatitis B virus capsid protein: detection and functional implications of distinct subnuclear bodies in a compartment associated with RNA synthesis and maturation.Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization.

P2860

Q24314907-F5BAE413-235D-4DC7-96E1-0C26D16759F2 Q24323291-CE9B5115-AEDE-43D5-B379-2A5C86ECB110 Q24324040-96A3DE88-0C25-4489-800E-D323AE66F020 Q24563883-A338A22F-97DE-4761-A033-7D1E60E2DA38 Q26866395-A54A2673-8467-41AB-8001-CACF197FF475 Q28589432-067FF3D6-B3DB-4E37-AD93-59DB958D3FC3 Q33245399-65573B8C-2775-4858-8530-9A2C71D5ACC9 Q33831725-002DCBB4-31F0-459D-A395-363758C0C744 Q33868098-992580D8-6D0A-4185-A49B-89CD4F5BF689 Q33966563-DB2E5F32-59F3-4E25-988B-385083D02F73 Q34059140-907A10C1-6636-487B-BF4B-A84EB918D24C Q34082677-4BC872D2-2195-48AD-A608-839A6207B0AB Q34117726-87A42383-4F52-4E6C-B51C-91578D071A57 Q34203795-7B2F58E8-3559-40FD-82D0-826D3335F0AB Q34387651-DA90601E-FE71-4C28-9D9D-AB3A57214B8C Q34426465-825D2929-DEF6-4081-A383-37C3406C371A Q34551462-5F329298-D549-4905-8071-6B8507E71F44 Q34593811-DFFC0843-AB53-498D-B327-6701D03C415A Q34717767-9F350EDE-2939-415D-BB76-1FC0F8F10973 Q34787933-42911FFF-78F8-4110-B5A0-D69E2962C368 Q34983999-2CE5B5FE-3350-4FB1-8976-8C801366A416 Q35076767-1BCE2DC9-D154-402F-BF0B-4DD341594CD3 Q35259698-18D6539F-BAF5-4E07-97CE-71DAEE4F26F9 Q35531347-A8BA39F0-AC2A-477E-87C2-0D84020E841E Q35767564-6BC26A95-E954-40F5-9572-694546E6B102 Q35813985-80AF4DDF-FAD9-48AD-8F03-56D48638375D Q36217707-3B99BC46-B44B-409C-A613-1C6E853B5E97 Q36363961-72E4F304-0CED-4FB5-AA82-0283F11CBE8C Q37095435-D0227C46-7B0B-4184-A81B-5EE163C63720 Q37394282-B5BA69C8-C9F3-402B-B495-AFB4F8239BD9 Q37498902-7C6D1DE0-067E-42D7-8327-8C7CF0EE70E3 Q37960427-609744F6-9716-4C60-91D4-C8831256DADC Q38042329-6072AB6E-A27F-4F99-AEF3-3269951C0A70 Q38081969-24EFDC19-C1E0-4CFF-A0A9-EB1C3B0C2A9D Q38541052-F0E35435-9717-45F6-9458-8413407AAE1D Q38629145-37A5EB4F-A6CC-4BC8-B857-00E8FF792166 Q38776406-C15EEA1E-BBFD-455E-A288-7AFFA15A3905 Q38968261-428A2B36-A167-43B9-A032-D03DC3F139DE Q39699826-1F898909-EE7E-44DE-B69E-B4CC3E85142C Q39960878-5E17816F-A259-4C92-9276-D7C7A53F4CF3

P2860

Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein

http://www.wikidata.org/entity/Q24673603

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@ast

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@en

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@nl

type

label

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@ast

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@en

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@nl

prefLabel

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@ast

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@en

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@nl

P1433

Q24673603-D8C14502-4AC0-463C-8D9F-149B4B652B47

P1476

Q24673603-6BCC8D91-E595-4446-AE1D-0B88C1B40FB7

P2093

Q24673603-1117A459-CCEC-4036-8381-2791197DBF90

Q24673603-1422F123-6349-46F2-9DA4-07EA2B7240C5

Q24673603-1D35F54F-F3EE-418A-AE10-1A20C39CE999

Q24673603-6AF98F6D-948B-4A3E-B783-8CC04A340D22

Q24673603-9F5F621F-A5E0-4CD4-8C69-6E3E32DFF2A9

Q24673603-A5F5AC62-6491-4651-B6A4-B5A295469459

Q24673603-ABF1BB3B-6AAC-42F4-8D9E-A907CE4BD8A9

P2860

Q24673603-0404EC14-686E-4E02-844B-034963A01B6B

Q24673603-100BADEC-B6C9-4C38-82C3-6B71B88D18EA

Q24673603-2083FAC1-3A96-4290-9681-C1F0414203C9

Q24673603-25025769-EE6C-44ED-8E5B-BE5429BB818C

Q24673603-2D369896-B07E-4BCE-AF4E-6AAC278CED28

Q24673603-359261F9-1A3E-483A-B3A8-953C21C00427

Q24673603-398A24BF-A929-482A-B7BB-F86A2C737101

Q24673603-4036198B-B022-49A3-8615-C0C1844717A0

Q24673603-41F26434-DD86-446A-BD44-E11C7F2AB1C6

Q24673603-42875AFD-F35C-4F03-BCE0-D4C92906AB33

P304

Q24673603-72CF67E2-82E7-478D-A653-49C3CEC62D6C

P31

Q24673603-9D84A280-A422-4850-9A00-9EED104AB38C

P356

Q24673603-AFC249D9-9A3C-4434-9E7F-96729F8C91AD

P407

Q24673603-0F10D9BA-CCBB-462C-A1AB-86B901F14136

P433

Q24673603-E9B4B19C-D733-41E9-A445-F328E14D9799

P478

Q24673603-362BEC37-3ACB-44BF-8056-79A760D9156C

P50

Q24673603-84AAAEFD-190F-4F22-8897-5A7C01936100

P577

Q24673603-9FED0217-4C6A-4969-8ADD-806F96CB8616

P698

Q24673603-94B636E3-2F0C-442A-B748-B6ABE03BCD65

P921

Q24673603-342C3DC9-848D-471E-B172-F496F42D2178

Q24673603-E75AC1EF-051D-4043-ADF0-4CE57B88B574

P932

Q24673603-43024A28-9100-49C0-8D89-ED06B98D1FB7

P356

JVI.76.16.8124-8137.2002

P1433

Journal of Virology

P1476

Identification of SRPK1 and SR ...... hepatitis B virus core protein

@en

P2093

Alexander Kurtenbach

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

Axel Ullrich

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

Henrik Daub

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

Josef Wissing

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

Julia Dennenmoser

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

Peter Habenberger

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

Stephanie Blencke

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

P2860

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

A serine kinase regulates intracellular localization of splicing factors in the cell cycle

Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae

SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors

The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C

Characteristics of a human cell line transformed by DNA from human adenovirus type 5

Use of an oriented peptide library to determine the optimal substrates of protein kinases

Identification of in-gel digested proteins by complementary peptide mass fingerprinting and tandem mass spectrometry data obtained on an electrospray ionization quadrupole time-of-flight mass spectrometer.

Hepatitis B virus HBx protein deregulates cell cycle checkpoint controls

Phosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase.

P304

8124-8137

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

P31

scholarly article

P356

10.1128/JVI.76.16.8124-8137.2002

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

P407

P433

16

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

P478

76

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

P50

P577

2002-08-01T00:00:00Z

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

P698

12134018

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

P921

phosphorylation

P932

155132

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