Lack of adaptation to human tetherin in HIV-1 group O and P. - Wikidata - wikimedia - TriplyDB

Lack of adaptation to human tetherin in HIV-1 group O and P.

Lack of adaptation to human tetherin in HIV-1 group O and P.

http://www.wikidata.org/entity/Q30407564

about

How SAMHD1 changes our view of viral restriction The role of BST-2/Tetherin in host protection and disease manifestation Vpu Protein: The Viroporin Encoded by HIV-1 Impacts of humanized mouse models on the investigation of HIV-1 infection: illuminating the roles of viral accessory proteins in vivo Vpu and BST2: Still Not There Yet?Differential sensitivities of tetherin isoforms to counteraction by primate lentiviruses.Pandemic HIV-1 Vpu overcomes intrinsic herd immunity mediated by tetherin.Vpu-Mediated Counteraction of Tetherin Is a Major Determinant of HIV-1 Interferon Resistance.Differential Control of BST2 Restriction and Plasmacytoid Dendritic Cell Antiviral Response by Antagonists Encoded by HIV-1 Group M and O Strains.Efficient Vpu-Mediated Tetherin Antagonism by an HIV-1 Group O Strain.HIV-1 Group P is unable to antagonize human tetherin by Vpu, Env or Nef.Efficient SIVcpz replication in human lymphoid tissue requires viral matrix protein adaptation Eastern chimpanzees, but not bonobos, represent a simian immunodeficiency virus reservoir.Reacquisition of Nef-mediated tetherin antagonism in a single in vivo passage of HIV-1 through its original chimpanzee host Human tetherin exerts strong selection pressure on the HIV-1 group N Vpu protein.Non-M variants of human immunodeficiency virus type 1.Tetherin can restrict cell-free and cell-cell transmission of HIV from primary macrophages to T cells.Simian-Human immunodeficiency viruses expressing chimeric subtype B/C Vpu proteins demonstrate the importance of the amino terminal and transmembrane domains in the rate of CD4(+) T cell loss in macaques.Genetic characterization of natural variants of Vpu from HIV-1 infected individuals from Northern India and their impact on virus release and cell death.Nef proteins of epidemic HIV-1 group O strains antagonize human tetherin.A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release Interplay between HIV-1 and Host Genetic Variation: A Snapshot into Its Impact on AIDS and Therapy Response.Host restriction factors in retroviral infection: promises in virus-host interaction.Filamin A Is Involved in HIV-1 Vpu-mediated Evasion of Host Restriction by Modulating Tetherin Expression.A comparative mutational analysis of HIV-1 Vpu subtypes B and C for the identification of determinants required to counteract BST-2/Tetherin and enhance viral egress.Functional antagonism of rhesus macaque and chimpanzee BST-2 by HIV-1 Vpu is mediated by cytoplasmic domain interactions.Preservation of tetherin and CD4 counter-activities in circulating Vpu alleles despite extensive sequence variation within HIV-1 infected individuals.The Envelope Gene of Transmitted HIV-1 Resists a Late Interferon Gamma-Induced Block.Targeting frameshifting in the human immunodeficiency virus.Various plus unique: Viral protein U as a plurifunctional protein for HIV-1 replication The Potency of Nef-Mediated SERINC5 Antagonism Correlates with the Prevalence of Primate Lentiviruses in the Wild.Determinants in HIV-2 Env and tetherin required for functional interaction.Experimental adaptive evolution of SIVcpz to pandemic HIV-1 using a humanized mouse model.Inhibiting the Ins and Outs of HIV Replication: Cell-Intrinsic Antiretroviral Restrictions at the Plasma Membrane.Preadaptation of Simian Immunodeficiency Virus SIVsmm Facilitated Env-Mediated Counteraction of Human Tetherin by Human Immunodeficiency Virus Type 2

P2860

Q24605899-9B12FC45-11B0-43A4-BA33-B4669403EB21 Q26752737-DC384C07-A88E-4D90-8097-496B0A07A17E Q26801489-B6F7DD05-24E4-47DA-B08F-256EC3FB53EA Q26851152-A5094B39-EE34-4FBE-BC0A-11A97D87FF5A Q28730708-D080B96B-2729-4E71-82BF-7BB238544716 Q30360141-6753F7E6-CDAE-4116-9787-C03DA2DDCE4A Q30376824-1434E89B-3727-4970-8292-41200BDBB661 Q30391895-60D699C8-71A0-4486-A72B-997E595BF60D Q30392459-D36EC955-51E5-43E4-9406-62AEA111ED9E Q30397332-931BF9A2-7B64-40FD-90BC-897073D67965 Q30410687-DF341FF4-22F1-4D0C-A832-617740E3586D Q30415403-7C993772-C051-491A-8D4F-5E414450671D Q30419742-03AA3C7C-A6C4-4081-9491-4F7359404A4A Q30421288-6C035310-633B-4F05-B9E4-AB4AC72C6D36 Q30425799-D011C537-5424-4A86-BE62-555C5D056072 Q30432689-CC88DFFA-CD54-4FF7-A0A4-EEB0679A3137 Q31172123-806A47F1-88DF-409C-94E1-D6B84DC9032B Q33926191-9177F6CC-8B84-4E58-8356-629C9B4CAA39 Q34651035-152FEE1C-90CF-4B05-AFAF-D2DBEE1B0AEC Q34761549-606CC55B-90EA-44A7-ABA9-BD5328527F82 Q34929498-8FEA551E-EFB8-449E-A31D-790A34EAC3EA Q35993707-8568CE5F-75C2-4E3F-B245-9DD2A47EAACA Q36548179-51EE6728-1A75-4252-881B-410913A7AA70 Q36594734-5309719A-CEA4-41D8-8938-1907B6E03410 Q37141248-1CC5FE10-8A5A-47F2-B084-F5548A622C3C Q37336745-BE50853F-0DED-422C-B289-3BC7DB8B6B78 Q37510562-6D8DAC03-6084-40B1-99DD-0A41656B6E2A Q37707466-2ED300AE-FBEF-43B3-814E-46857BF88F04 Q37992096-73A5564F-0C9B-4918-9F44-E4B24A65524B Q38739273-934B5519-B6F5-4AA0-85C3-AB218BC78F99 Q40580241-3B5B44E2-CEED-4AF1-9387-9A8D7F721659 Q41065951-318A7EB0-422A-45AA-85B9-C7A3E20EB49F Q46246548-DF72A932-4258-488D-ACAF-1990AB1AD9F2 Q47550785-066C692B-3DBA-427F-B18D-5E1A2DA3A446 Q57093831-C3FD1910-996B-4B0B-A55C-986549EF4F23

P2860

Lack of adaptation to human tetherin in HIV-1 group O and P.

http://www.wikidata.org/entity/Q30407564

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Lack of adaptation to human tetherin in HIV-1 group O and P.

@ast

Lack of adaptation to human tetherin in HIV-1 group O and P.

@en

type

label

Lack of adaptation to human tetherin in HIV-1 group O and P.

@ast

Lack of adaptation to human tetherin in HIV-1 group O and P.

@en

prefLabel

Lack of adaptation to human tetherin in HIV-1 group O and P.

@ast

Lack of adaptation to human tetherin in HIV-1 group O and P.

@en

P1433

Q30407564-4306A24E-D861-4838-A4E5-A5184D9157A1

P1476

Q30407564-E5829A62-7E47-40DC-BE88-B7A3E39DF1F4

P2093

Q30407564-38FA6732-2A58-4E7A-98E0-F389F7A5ACCB

Q30407564-5499B109-1AC1-4A4E-9C16-2A817FE62C6F

Q30407564-6CE6D414-C31F-4B05-BA35-AE91F22C1C0C

Q30407564-9C77D008-216C-48BF-8DFA-A247938C69C5

Q30407564-9CD98228-7BE4-4A20-92AC-E239C3FC289F

P2860

Q30407564-0206B17A-E757-47F3-ADA6-571FEB5CD9E5

Q30407564-0A1DD853-C878-46AC-9C71-087DDA95BBBF

Q30407564-0BA601A8-20D7-4DDF-AE67-CCEDDDE467F3

Q30407564-18A6CD80-9637-4CC8-976A-37129AF2EA6E

Q30407564-1BB36BAD-0114-4061-A018-91CBE648180D

Q30407564-1C5F0435-C4AC-43B4-B5B5-BB14A786F0AF

Q30407564-21996608-B477-4214-B171-F8C0FC47E73D

Q30407564-23E0DBCD-0DB2-420B-BE0B-88BB5AE1D0DD

Q30407564-23F201A9-D93B-4465-A062-B765CFB9E098

Q30407564-25B521CF-7498-472D-9D0F-62B6F4F12245

P2888

Q30407564-8A095A81-C8ED-4533-8FD4-2313AE6683DE

P304

Q30407564-C6BF466F-4865-4B9C-AA61-54BE1D170C04

P31

Q30407564-07BAC560-738C-41AA-8A79-F41C51AB795D

P356

Q30407564-BEA271E0-5E54-4EA3-ABA4-84C28367BFA4

P478

Q30407564-D4DBCCCE-6BD3-465B-97D7-BAC3140EF958

P577

Q30407564-B68FAD9A-E0DB-4C78-8E52-F358B329879A

P5875

Q30407564-C24EC407-014B-4A02-B169-B73D273CA115

P6179

Q30407564-2EB9F26C-ED82-4469-9943-85C4BEC94ABF

P698

Q30407564-CDF1C103-C539-4B9F-ADC6-ED6FA0307418

P932

Q30407564-45D5A4DC-C1BC-441A-8425-60DBBCC3604A

P356

P1433

P1476

Lack of adaptation to human tetherin in HIV-1 group O and P.

@en

P2093

Colin M Exline

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

Kevin G Haworth

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

Lisa A Lopez

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

Paula M Cannon

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

Su Jung Yang

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

P2860

HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation

The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu

Species-specific activity of SIV Nef and HIV-1 Vpu in overcoming restriction by tetherin/BST2

Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes

Simian Immunodeficiency Virus Infection of Chimpanzees

A new human immunodeficiency virus derived from gorillas

Origin of HIV-1 in the chimpanzee Pan troglodytes troglodytes

Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism

Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments

The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation

P2888

P304

78

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

P31

scholarly article

P356

10.1186/1742-4690-8-78

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

P478

8

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

P577

2011-09-28T00:00:00Z

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

P5875

51678174

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

P6179

1041357683

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

P698

21955466

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

P932

3192746

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