Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01. - Wikidata - awgldk - TriplyDB

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

http://www.wikidata.org/entity/Q35192782

about

Structural mechanism of trimeric HIV-1 envelope glycoprotein activation Increasing the potency and breadth of an HIV antibody by using structure-based rational design Immune correlates of vaccine protection against HIV-1 acquisition HIV-1 neutralizing antibodies: understanding nature's pathways HIV-1 envelope glycoprotein structure A Chimeric HIV-1 gp120 Fused with Vaccinia Virus 14K (A27) Protein as an HIV Immunogen HIV-1 receptor binding site-directed antibodies using a VH1-2 gene segment orthologue are activated by Env trimer immunization Outer Domain of HIV-1 gp120: Antigenic Optimization, Structural Malleability, and Crystal Structure with Antibody VRC-PG04 Antibody 8ANC195 Reveals a Site of Broad Vulnerability on the HIV-1 Envelope Spike Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env Humanized Immunoglobulin Mice: Models for HIV Vaccine Testing and Studying the Broadly Neutralizing Antibody Problem.Passive immunization against HIV/AIDS by antibody gene transfer.Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120 Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers A human antibody to the CD4 binding site of gp120 capable of highly potent but sporadic cross clade neutralization of primary HIV-1.Abnormal B cell memory subsets dominate HIV-specific responses in infected individuals.Surfactant protein D inhibits HIV-1 infection of target cells via interference with gp120-CD4 interaction and modulates pro-inflammatory cytokine production.Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination.Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection.Neutralizing antibodies inhibit HIV-1 infection of plasmacytoid dendritic cells by an FcγRIIa independent mechanism and do not diminish cytokines production.Potent and broad neutralization of HIV-1 by a llama antibody elicited by immunization.Global panel of HIV-1 Env reference strains for standardized assessments of vaccine-elicited neutralizing antibodies Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41.Unique C2V3 sequence in HIV-1 envelope obtained from broadly neutralizing plasma of a slow progressing patient conferred enhanced virus neutralization.Rapid conformational epitope mapping of anti-gp120 antibodies with a designed mutant panel displayed on yeast Distinct HIV-1 entry phenotypes are associated with transmission, subtype specificity, and resistance to broadly neutralizing antibodies.Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate.Increased functional stability and homogeneity of viral envelope spikes through directed evolution.Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120.HIV-1 envelope glycoprotein variable loops are indispensable for envelope structural integrity and virus entry.Receptor binding domain based HIV vaccines.Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes IgM Repertoire Biodiversity is Reduced in HIV-1 Infection and Systemic Lupus Erythematosus.V3-independent competitive resistance of a dual-X4 HIV-1 to the CXCR4 inhibitor AMD3100 Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer.A mammalian cell based FACS-panning platform for the selection of HIV-1 envelopes for vaccine development Antibody engineering for increased potency, breadth and half-life.HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies.South African HIV-1 subtype C transmitted variants with a specific V2 motif show higher dependence on α4β7 for replication.Neutralization properties of simian immunodeficiency viruses infecting chimpanzees and gorillas.

P2860

Q21131394-12A049CA-95F4-4D4B-8DFE-1193D07DC3D2 Q24631510-D5A12188-EA7D-4B02-9C28-D22A62774DA1 Q26778573-CCECB0C9-04FB-4D58-955B-A5D28DDBA3EB Q27000480-E4F5CBF4-3FAE-439F-A354-E9F7373BB97E Q27011248-B02408DC-F2AA-4E1C-9BB0-911A011E6BDA Q27302081-749F8948-8F67-437A-8D53-F12C27AA2F6B Q27324184-66A94EE7-DC35-436F-BD02-CBF11C292765 Q27675468-9D3A8FF3-6DC0-4A4F-A3DB-36DB04BF20AD Q27683540-B6966525-74BB-4B0D-BB0A-7B79146CF260 Q28256508-03F87735-FBC3-4950-93E9-0F70AA2C337D Q30234773-575A7281-535E-4CAB-A41D-9E079BFD3320 Q30358434-EB014113-E391-492B-9403-F8E6D8854441 Q30524225-5FE9B1BE-611F-44CD-B6D4-CCA30C8099D0 Q30580101-6B544860-815F-4183-A339-CEDC1E463A6C Q31132248-367AAC25-D986-4792-BF6E-5EED1615AD00 Q33808304-8FE97913-1B63-41D4-9698-3241F2FE3F7D Q33921367-D2C48B93-F426-4D80-96AD-F89D0E97D561 Q34022578-04BF2155-D60E-4EA2-9809-9C80DC130B71 Q34034659-45E24B2E-570F-4CC1-AD37-0E03A4EAED6B Q34055377-CB5E9DFB-B221-4B1F-85F9-79FF1378BDF3 Q34284855-54E4ECDD-9EFD-4691-8669-A460B5BB12F2 Q34392963-44DAB469-80D3-4496-B50C-A3577755B489 Q34412302-DBACA749-0298-4D31-B41B-1898E426A22C Q34441935-A58A42CC-E4BF-43CB-AFBA-BEAA59778DCA Q34480254-66B6ED01-5070-4368-BAC8-06D00E7957FC Q34503200-747E7A40-2407-41A9-A886-49C99C19F647 Q34551010-D2276DCF-ADA0-4AFA-9A8B-A909AD80BD3A Q34611144-5DF74DB8-3640-48DA-9995-9E92FA408FE2 Q34885869-08B0F56D-DA42-44D9-A398-0FA14676B7B2 Q34924647-01C999CD-25B5-44FC-9AE2-01773CFCDDF3 Q35033862-B5FCB5FB-CB2B-4A81-99C8-9E8990942E14 Q35034268-087E372A-E9A8-46D4-8DBC-C293C53F0EB4 Q35057901-B9245DFA-138B-4003-BBE3-DF534783EF6D Q35107518-0B02D12C-3995-4830-BC57-D70D5868DB38 Q35217426-6D602FFD-F9EF-4A3F-B202-7FFF1BF039BD Q35298899-ABD0D430-9AAC-4578-A0BE-AF872437883B Q35575206-0375D54B-ABAD-4769-9183-448E264F3054 Q35640998-FD5F0BB6-8CB6-4B39-AD75-2F25090B1C4E Q35672336-B29D5535-C3CB-437C-90D2-D3193C650570 Q35677620-1C33EB9C-33C2-4E37-87C1-C033EA8B2E97

P2860

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

http://www.wikidata.org/entity/Q35192782

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին 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

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@ast

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@en

type

label

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@ast

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@en

prefLabel

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@ast

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@en

P1433

Q35192782-06E24228-1D2A-4717-955D-2B472A5DFF54

P1476

Q35192782-7A07B1C3-B350-4139-8D21-BB6577C9A26D

P2093

Q35192782-06BB5C9F-8C39-4BA2-B02C-D9866BF832EE

Q35192782-12EA064E-60EE-45E0-B5A6-582EE3D381A8

Q35192782-630552A8-2D83-4392-9B34-C7EE71A24980

Q35192782-68247B95-8C07-4BC5-B9AB-80489BEDF61E

Q35192782-838BC56A-2CA9-488F-A17C-DDB68D863666

Q35192782-96117594-C619-4BB4-BA8F-45FCE13F94E0

Q35192782-ABB4C35E-C4D8-413B-B5D8-E043BEE7DE9B

Q35192782-C0DBED2A-7701-4A3E-888F-8D699D015C27

Q35192782-C2599AAB-9339-40E9-B543-D2148C27EA76

Q35192782-D51DFDB8-A108-4593-ACDC-A6AFB5FF3CF8

P2860

Q35192782-00C4EF6E-0DC3-4F88-B4F5-14CC41BCA2E9

Q35192782-0321076E-BF00-4BA3-A00A-6EE0C919AD4D

Q35192782-0DAA1A4E-D14E-43FE-AFDE-DF54BAE88EB3

Q35192782-125495A6-A06A-45D9-8DD3-9D54122CCA1C

Q35192782-13295AE4-D2A0-4E79-9919-7308CD93167B

Q35192782-14E85BF0-6592-442E-BB32-B4E23DDF95E0

Q35192782-17289253-B3AB-4512-A84B-1E8CD1FDCEB6

Q35192782-1B6DD8E4-6294-4B4C-8E6D-9E5421656D8C

Q35192782-1F73C99E-F532-4940-9D8A-ECF72DF825C3

Q35192782-20ECA342-5A42-48E6-B378-0905B20F5D76

P304

Q35192782-8779D53F-9B5F-4748-8CAE-0888CE3614A4

P31

Q35192782-3728613E-23F3-4155-8F86-1F6CDE731033

P356

Q35192782-6E36C78F-F887-4A35-9954-F71BF181C38F

P407

Q35192782-3FF99077-243D-47D7-BCEA-BDAEA43A6BEF

P433

Q35192782-16C5E5E2-E308-485A-AF24-80CF78E00D0E

P478

Q35192782-ED0C5F96-1C47-45EB-B160-53B24C84B291

P50

Q35192782-8519A32F-178F-406F-9E4C-24109A7CC602

Q35192782-BE3665F1-49B4-4E6D-9898-2873A1E66E7E

Q35192782-EE7C1150-FA19-4ED8-BACD-3D6DBE3E3B75

Q35192782-FDD319D1-A703-4A11-8C01-ABD4EB60D3DD

P577

Q35192782-83D9FC7E-847A-4F81-A8F5-683A51FD4AF4

P5875

Q35192782-FB53D637-ED64-4DC0-9F0E-24C0A4804609

P698

Q35192782-0999E946-DE7A-4967-B8C0-C2B2F5A0DB6D

P921

Q35192782-4BF3D6A7-BCAF-4ABF-BE3D-5266A389EE70

P932

Q35192782-74F416E8-6AE7-42D8-A7C3-585A79B05D9B

P356

P1433

Journal of Virology

P1476

Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.

@en

P2093

Dennis R Burton

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

Javier Guenaga

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

Krisha McKee

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

Laura M Walker

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

Mark K Louder

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

Richard T Wyatt

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

Sijy O'Dell

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

Stephen D Schmidt

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

Xueling Wu

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

Yu Feng

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

P2860

The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and Immunogens

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

Identification of a major co-receptor for primary isolates of HIV-1

Energetics of the HIV gp120-CD4 binding reaction

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Molecular architecture of native HIV-1 gp120 trimers

Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity

Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01

Core structure of gp41 from the HIV envelope glycoprotein

Atomic structure of the ectodomain from HIV-1 gp41

P304

8954-8967

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

P31

scholarly article

P356

10.1128/JVI.00754-11

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

P407

P433

17

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

P478

85

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

P50

Julie Ledgerwood

Barney S. Graham

P577

2011-06-29T00:00:00Z

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

P5875

51454068

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

P698

21715490

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

P921

P932

3165784

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