Dissection of the HIV Vif interaction with human E3 ubiquitin ligase - Test2 - elhamkhani - TriplyDB

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

http://www.wikidata.org/entity/Q41963681

about

Rift Valley fever virus NSs protein functions and the similarity to other bunyavirus NSs proteins Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif.Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex Core binding factor beta plays a critical role by facilitating the assembly of the Vif-cullin 5 E3 ubiquitin ligase.Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Structural insights for HIV-1 therapeutic strategies targeting Vif.Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligase APOBEC3G: a double agent in defense On the solution conformation and dynamics of the HIV-1 viral infectivity factor Identification of a Cullin5-ElonginB-ElonginC E3 complex in degradation of feline immunodeficiency virus Vif-mediated feline APOBEC3 proteins Hydrodynamic and functional analysis of HIV-1 Vif oligomerization.APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif.HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.Dispersed and conserved hydrophobic residues of HIV-1 Vif are essential for CBFβ recruitment and A3G suppression.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation.Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif Identification of a conserved interface of HIV-1 and FIV Vifs with Cullin 5.

P2860

Q26745530-E71673E7-844F-46D9-B087-2BADEA417088 Q27680599-792A3F14-088F-4290-9B56-B341A7D2838D Q27685307-77FAB8A1-774B-4D45-8DBA-EBD605F93A3A Q28482052-883A2C1E-EA2B-4249-818B-997B949EBF41 Q28540150-01640196-4656-4814-AE59-D1D3A07FBB70 Q30496853-147DEA8D-8E13-46C4-A54C-825220B1EB90 Q34034114-B9AFDDFA-ABF8-43DB-9016-CD2BD122D747 Q34039510-9D031444-275C-43CD-889E-1D6214F2278C Q34055413-CE570954-1A43-4244-81FD-B87BE8264794 Q34244067-48DCD69C-A2F7-4AFA-AC6E-8F314289DF6C Q34433647-EABA9ADA-0478-4603-BDAB-8BD1087AB524 Q34695564-136A67F8-03DB-409F-A741-720150845D23 Q34917194-464B3F89-D9A3-494B-9D7D-15A124BAC224 Q35113711-6EFFB8C4-EB56-4D92-B059-7832CFEA1B41 Q35531709-04962AF0-0E6C-4D10-874E-FA26248068C3 Q35827946-9F3FC833-97BA-4CC5-8FA8-559F611ECA56 Q36827236-48FD541C-F066-4C48-A06A-80B66994BF35 Q37153444-F9E16758-3486-448D-94D5-FB26AE140EB4 Q37608208-9273D795-722C-47DE-8B06-438A41FA69A7 Q37644056-0639C82F-4D25-483B-B5C8-7BE2E68731A3 Q37950254-AABB7624-2FA5-4621-903E-66BB55987EE2 Q40459351-214DCD93-3D13-4EB9-9ADD-EDBEAC58A57B Q41897467-18672E24-7E70-4E6F-BA49-4D5792EB4255 Q47269109-81755E2A-E51B-404D-8012-13554AE03BAE

P2860

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

http://www.wikidata.org/entity/Q41963681

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

@en

type

label

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

@en

prefLabel

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

@en

P1433

Q41963681-5EC936BB-9700-43B3-B9BA-924085AA96E9

P1476

Q41963681-1F4ABDC0-3062-4567-AC17-1A0AEBA34348

P2093

Q41963681-4CD06BA7-21AB-4B55-A3DF-FBE1733FA7E9

Q41963681-7748D7B6-3096-4261-9530-410442EA1A6F

Q41963681-A2D6C2B5-6480-4062-AA71-5E372597DA55

Q41963681-A99F4573-05C3-4C5E-91BF-DC50CBFC6108

Q41963681-E08B9254-133E-40D9-8049-C9412007B746

P2860

Q41963681-134D9A9E-7202-4E50-83B8-348CF168E331

Q41963681-1964F686-952F-47BE-968D-EF4704BF3F1E

Q41963681-1F85F1DD-6B11-4025-9F25-EE888B2FCD33

Q41963681-2135992F-D78A-4F99-AE15-F9B5A38FE701

Q41963681-3C904218-0CB4-4031-A5A4-8F0D1AAF753D

Q41963681-6C594C86-6C26-4AE8-ACDE-88885ED3D5CA

Q41963681-7D78F11B-2996-4D25-B438-6B8DEEFAAB4D

Q41963681-7F11B544-B91D-460C-B238-5CED80CD054C

Q41963681-AE0C5ED2-F84E-4377-ABE4-BBACF734FBE8

Q41963681-AFDA4B5B-9DA5-49D0-A0F1-7DF260FEE68E

P304

Q41963681-002E6004-D9E2-4E59-B067-ED0E3EA489C0

P31

Q41963681-33488557-8CD4-47F9-BE63-F446D920E6BC

P356

Q41963681-E021B0C9-47C4-44AA-9998-4151F60691D3

P407

Q41963681-5597B14A-45F7-4E6B-8D4A-FD5AD74684E4

P433

Q41963681-7447E3F1-4C32-4862-81CA-2C334688B781

P478

Q41963681-F75F491C-F731-4BFA-85F0-FF154200F6C8

P577

Q41963681-AD288042-9EF6-4A06-A4E6-B1D8DF9ACB25

P698

Q41963681-DE1EAA2E-2501-4233-A186-6BD6387AA06E

P932

Q41963681-0BAEB515-50DD-48A0-A958-F280AE828EF7

P356

P1433

Journal of Virology

P1476

Dissection of the HIV Vif interaction with human E3 ubiquitin ligase

@en

P2093

Bradford J Stanley

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

Chang Liu

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

Leslie S Wolfe

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

William K Eliason

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

Yong Xiong

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

P2860

Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly

Structure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR Degradation

The SOCS Box Domain of SOCS3: Structure and Interaction with the ElonginBC-Cullin5 Ubiquitin Ligase

Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex

HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation

Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif

Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G.

P304

7135-7139

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

P31

scholarly article

P356

10.1128/JVI.00031-10

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

P407

P433

14

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

P478

84

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

P577

2010-05-12T00:00:00Z

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

P698

20463065

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

P932

2898223

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