Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. - Wikidata - awgldk - TriplyDB

Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific.

Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific.

http://www.wikidata.org/entity/Q33648307

about

Leucine zipper domain is required for Kaposi sarcoma-associated herpesvirus (KSHV) K-bZIP protein to interact with histone deacetylase and is important for KSHV replication Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design Human Oncogenic Herpesvirus and Post-translational Modifications - Phosphorylation and SUMOylation The Modulation of Apoptotic Pathways by Gammaherpesviruses Next-Generation Sequencing in the Understanding of Kaposi's Sarcoma-Associated Herpesvirus (KSHV) Biology Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways Insights into High Affinity Small Ubiquitin-like Modifier (SUMO) Recognition by SUMO-interacting Motifs (SIMs) Revealed by a Combination of NMR and Peptide Array Analysis Determinants of Small Ubiquitin-like Modifier 1 (SUMO1) Protein Specificity, E3 Ligase, and SUMO-RanGAP1 Binding Activities of Nucleoporin RanBP2 MDM2 promotes SUMO-2/3 modification of p53 to modulate transcriptional activity A unique SUMO-2-interacting motif within LANA is essential for KSHV latency Kaposi's sarcoma-associated herpesvirus K-Rta exhibits SUMO-targeting ubiquitin ligase (STUbL) like activity and is essential for viral reactivation The chromatin modification by SUMO-2/3 but not SUMO-1 prevents the epigenetic activation of key immune-related genes during Kaposi's sarcoma associated herpesvirus reactivation Viral manipulation of the cellular sumoylation machinery.Histone demethylase JMJD2A regulates Kaposi's sarcoma-associated herpesvirus replication and is targeted by a viral transcriptional factor.SUMO and KSHV Replication Identification of sumoylated proteins in the silkworm Bombyx mori.HPV E6 proteins target Ubc9, the SUMO conjugating enzyme.Molecular biology of KSHV lytic reactivation.In vivo analysis of protein sumoylation induced by a viral protein: Detection of HCMV pp71-induced Daxx sumoylation K-bZIP Mediated SUMO-2/3 Specific Modification on the KSHV Genome Negatively Regulates Lytic Gene Expression and Viral Reactivation.Post-Translational Modifications of Kaposi's Sarcoma-Associated Herpesvirus Regulatory Proteins - SUMO and KSHV Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100.Changing the ubiquitin landscape during viral manipulation of the DNA damage response.The Epstein-Barr virus miR-BHRF1-1 targets RNF4 during productive infection to promote the accumulation of SUMO conjugates and the release of infectious virus Divergent signaling via SUMO modification: potential for CFTR modulation.The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1γ sumoylation and poly-SUMO chain elongation.Role of IRF4 in IFN-stimulated gene induction and maintenance of Kaposi sarcoma-associated herpesvirus latency in primary effusion lymphoma cells SUMO modification of a heterochromatin histone demethylase JMJD2A enables viral gene transactivation and viral replication.Human pathogens and the host cell SUMOylation system.Sumoylation at the host-pathogen interface.Viral manipulation of cellular protein conjugation pathways: The SUMO lesson.The Latency-Associated Nuclear Antigen of Kaposi's Sarcoma-Associated Herpesvirus Inhibits Expression of SUMO/Sentrin-Specific Peptidase 6 To Facilitate Establishment of Latency.KSHV latent protein LANA2 inhibits sumo2 modification of p53.Manipulation of ubiquitin/SUMO pathways in human herpesviruses infection.Regulation of the tumor suppressor PTEN by SUMO.Modulation of global SUMOylation by Kaposi's sarcoma-associated herpesvirus and its effects on viral gene expression.Viral Interplay with the Host Sumoylation System.Kaposi's sarcoma associated herpesvirus tegument protein ORF75 is essential for viral lytic replication and plays a critical role in the antagonization of ND10-instituted intrinsic immunity.SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.Entropy-driven mechanism of an E3 ligase

P2860

Q24307542-6D0959D8-AE4B-4614-BE88-3E19A8860408 Q24594140-BEAC493B-FB1A-4B07-829D-87BC0F28888C Q26744568-6B62E02C-3E2B-450E-A62E-B2518DDC2247 Q26747452-0B0A5E67-6935-48EF-A65F-9E7C920E9EB5 Q26752599-16BE524B-1202-441A-8968-0A56F755B735 Q26783655-CEB88465-EEC4-4E17-9A87-B2A33DFC714E Q27676009-2C5B6AAD-62F2-4575-837F-21E8B3E0ECFE Q27676384-B1FD0A85-FE5A-4A61-BE59-8F19F4F657AA Q28118946-7BCBF40B-EEDE-4511-BA50-50C70284F97A Q28535343-080CF22B-01DF-4850-8A0E-56B0ADD1A2B1 Q28535568-CBA138D5-9120-4FCA-BF72-A018F4659306 Q33716143-AE45C5B3-5BDE-47B8-9E8B-02F03E7AFEDF Q33910635-F1D3737C-2A31-4BA6-B7F1-3C61C2AAC8BC Q34742661-A69EA34F-CB7E-45D2-98C7-37A582FAEAF6 Q34774847-E2EFB489-9D5B-4C36-ACAA-093701BBD002 Q34833965-0FDDA505-5932-4B83-A6E0-1F24EDA19562 Q35012060-1831DC3E-AFDB-44FD-A148-F87105E34DFA Q35014918-65669008-EE5A-44F2-8DCC-BA1B24BB5AC6 Q35529185-4E10E335-F225-457D-8B01-27832F8A6D4F Q35703276-30E8B7C8-B276-4B38-8583-2907888342A6 Q35755464-B35879BF-3465-433D-92D0-9CBB593A2A88 Q35826788-3D99889B-8280-47EA-9422-93FDBAFF46BA Q35854193-4CB54B92-C306-4F10-929E-BD93312E9BFA Q36348544-D9447825-EC29-401A-BD9D-8D12356EAED7 Q36817048-D3E95C3A-D219-4607-B76B-FF7284A24E63 Q37021805-08C64831-F7F4-432C-8242-24FB3328447C Q37088335-0634EBDE-AAA6-4694-8D9F-B7048EA65FD0 Q37677368-6E21318A-5B10-460F-ABE8-58F410551774 Q37954599-B43A572F-693E-4CF9-9C89-998E7D5DC169 Q38116514-DD783B6C-2B4C-4CB4-8DCC-E570A0958EE7 Q38156888-DE859695-5EAB-4F10-BC8A-CE011B265848 Q38725485-18EC7BEF-D11A-4761-8558-D18D0B7D7B1A Q38917974-7508513D-5609-47A6-A7D0-9F58652B54DD Q38934480-9BB0ACAD-A47D-45BA-B44D-6C50CCC767C1 Q39271041-85F6ADBA-53D5-4D78-9671-074BD23F791B Q40149921-883C2802-3309-4075-ADE4-B3CCD5BCCB50 Q40332996-AD106F2B-90DF-481E-9A1B-6563C481E9CB Q41876173-BD752FB0-DB3F-40A9-B3C2-BE87F15F0A9B Q41983297-33CB157A-649D-44AB-8978-A639FE1D4588 Q42083948-8C3A7FA2-7197-492F-9834-AD271B92304E

P2860

Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific.

http://www.wikidata.org/entity/Q33648307

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@ast

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@en

type

label

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@ast

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@en

prefLabel

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@ast

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@en

P1433

Q33648307-DE04E80B-AEF2-470F-868D-6A7B1A5EDF2C

P1476

Q33648307-0820CB04-C341-4CFA-A1E0-DBA581080034

P2093

Q33648307-00AFE027-A0B5-464F-BE2A-747F98153662

Q33648307-0FC83FEB-3FFD-476A-9507-CCA841E737F7

Q33648307-207B5D5E-8427-4661-9386-F337EDBFA2F7

Q33648307-38C9A533-E35A-4FA3-89A3-6C6E938B72CC

Q33648307-3DD118B2-AE84-4335-A3BC-E815F2F4E151

Q33648307-4035C953-0446-433D-8992-D99B774E77AE

Q33648307-4A429D71-662B-4E4D-BB69-00866D7298C1

Q33648307-C762391C-712E-4DC5-97E6-586284AA91FC

Q33648307-E9319096-4BD7-4156-A480-256E45DBD7E1

P2860

Q33648307-08A4DA41-48A9-4462-83C8-BAE3D2037B5C

Q33648307-0BE5616B-5547-4B28-A056-BAE2620AEE06

Q33648307-1D8830F8-9B9F-4798-9865-4C8FE94D8E56

Q33648307-1DB8460E-08D3-4993-BE4D-DEC6202D1694

Q33648307-1DBCB5C5-5EBF-40D3-BE7E-B9F3DB555ECD

Q33648307-1F1C0485-6783-44EA-97A0-89DEE65BBC97

Q33648307-22981CF2-9769-457B-ADA4-BB0F53315E25

Q33648307-2D561AE9-ECEE-49F8-BD13-D165CCA40874

Q33648307-3494E109-F564-4B18-8F16-BD65658FDFC2

Q33648307-3D530D4A-56DC-40FB-A521-0EB317A1AD9F

P304

Q33648307-505A39B5-690F-44A2-8D53-B122E4C3A420

P31

Q33648307-E890A9F1-58FA-4E4F-8A98-24F8D5D79BC3

P356

Q33648307-362342AB-E246-45EF-9F34-FF4C7391325C

P407

Q33648307-DD2FF523-9A19-44D5-9BD6-9FD940AA9F73

P433

Q33648307-D2C4445A-A7C9-4826-9F21-EF7C8B344F42

P478

Q33648307-115A7C8E-F1E9-4C99-942A-2EB2499A4922

P577

Q33648307-1E707846-E16C-4741-A9AC-30236F26EEF0

P698

Q33648307-2BDCF23E-085E-4DEA-A1C4-14B07E4E1596

P932

Q33648307-6AB39882-7956-43E7-A6CC-BEF711A8139E

P356

JBC.M109.088088

P1433

Journal of Biological Chemistry

P1476

Kaposi's sarcoma-associated he ...... pendent and SUMO-2/3-specific.

@en

P2093

Chun-Yi Wu

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

Hsing-Jien Kung

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

Kit S Lam

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

Latricia D Fitzgerald

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

Mel Campbell

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

Paul A Luciw

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

Pei-Ching Chang

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

Thomas J Ellison

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

Yoshihiro Izumiya

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

P2860

Genome-wide analysis of KAP1 binding suggests autoregulation of KRAB-ZNFs

The mechanisms of PML-nuclear body formation

Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25

Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption

Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies

SUMO-1 modification activates the transcriptional response of p53

Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3

The nucleoporin RanBP2 has SUMO1 E3 ligase activity

The polycomb protein Pc2 is a SUMO E3

Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

P304

5266-5273

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

P31

scholarly article

P356

10.1074/JBC.M109.088088

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

P407

P433

8

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

P478

285

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

P577

2009-12-24T00:00:00Z

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

P698

20034935

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

P932

2820755

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