MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1. - Wikidata - wikimedia - TriplyDB

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

http://www.wikidata.org/entity/Q34681455

about

Ontogeny of recognition specificity and functionality for the broadly neutralizing anti-HIV antibody 4E10 Modeling neutralization kinetics of HIV by broadly neutralizing monoclonal antibodies in genital secretions coating the cervicovaginal mucosa Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield Broad and potent neutralization of HIV-1 by a gp41-specific human antibody A gp41 MPER-specific Llama VHH Requires a Hydrophobic CDR3 for Neutralization but not for Antigen Recognition Structural Basis for Broad Detection of Genogroup II Noroviruses by a Monoclonal Antibody That Binds to a Site Occluded in the Viral Particle Global shape and ligand binding efficiency of the HIV-1-neutralizing antibodies differ from those of antibodies that cannot neutralize HIV-1 Virus neutralisation: new insights from kinetic neutralisation curves Biogenesis of influenza a virus hemagglutinin cross-protective stem epitopes Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)Gene Mining for Proline Based Signaling Proteins in Cell Wall of Arabidopsis thaliana Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.A human antibody to the CD4 binding site of gp120 capable of highly potent but sporadic cross clade neutralization of primary HIV-1.Estimating the probability of polyreactive antibodies 4E10 and 2F5 disabling a gp41 trimer after T cell-HIV adhesion.Flow virometry analysis of envelope glycoprotein conformations on individual HIV virions.HIV-1 Envelope Trimer Design and Immunization Strategies To Induce Broadly Neutralizing Antibodies.Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralization A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus Nef decreases HIV-1 sensitivity to neutralizing antibodies that target the membrane-proximal external region of TMgp41.Cell-cell transmission enables HIV-1 to evade inhibition by potent CD4bs directed antibodies Structure-guided alterations of the gp41-directed HIV-1 broadly neutralizing antibody 2F5 reveal new properties regarding its neutralizing function.Unique C2V3 sequence in HIV-1 envelope obtained from broadly neutralizing plasma of a slow progressing patient conferred enhanced virus neutralization.Designer antigens for elicitation of broadly neutralizing antibodies against HIV.Cell-to-cell transmission can overcome multiple donor and target cell barriers imposed on cell-free HIV.Increased functional stability and homogeneity of viral envelope spikes through directed evolution.MABGEL 1: first phase 1 trial of the anti-HIV-1 monoclonal antibodies 2F5, 4E10 and 2G12 as a vaginal microbicide Receptor binding domain based HIV vaccines.Interaction of the gp120 V1V2 loop with a neighboring gp120 unit shields the HIV envelope trimer against cross-neutralizing antibodies.Heterosubtypic antibodies to influenza A virus have limited activity against cell-bound virus but are not impaired by strain-specific serum antibodies.Structure and immune recognition of trimeric pre-fusion HIV-1 Env.Effects of UVA irradiation, aryl azides, and reactive oxygen species on the orthogonal inactivation of the human immunodeficiency virus (HIV-1).Capacity of Broadly Neutralizing Antibodies to Inhibit HIV-1 Cell-Cell Transmission Is Strain- and Epitope-Dependent Binding of anti-membrane-proximal gp41 monoclonal antibodies to CD4-liganded and -unliganded human immunodeficiency virus type 1 and simian immunodeficiency virus virions Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.Role for the terminal clasp of HIV-1 gp41 glycoprotein in the initiation of membrane fusion Transmembrane domain membrane proximal external region but not surface unit-directed broadly neutralizing HIV-1 antibodies can restrict dendritic cell-mediated HIV-1 trans-infection.Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry.Discrete partitioning of HIV-1 Env forms revealed by viral capture.Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.

P2860

Q21089590-AECB4479-4B6C-499E-A4AB-AD6C4916E9AF Q27322437-FCCADB5D-F7E0-4502-BA25-9CC4C1D858CA Q27654848-9008A260-135B-4EC8-97ED-AFC2ED795AC2 Q27675032-B4A0A8E4-F28B-4D5C-8A3D-AFF90B3763CB Q27675131-F5A313A8-EF30-4F86-9485-83FABD437CE0 Q27676864-5B55BE7F-A62E-4872-B653-4FF132E6DCE1 Q27676892-3ADDA7C0-F961-43AB-9AAA-63F4FC5FF32A Q28250040-955D5F14-50C9-46C7-BA97-50194219C906 Q28487427-952D4EF0-4514-470E-BDC0-F19228F5F958 Q28539672-8CC4BA3C-084A-4B08-9DEE-326C1D08D767 Q28743199-2ACC43CA-AF19-4195-AEAE-AA62A1A7AF89 Q30178311-E6BCF86F-8D68-40D0-A952-3C26753FB267 Q30490942-DCA8275D-E871-403D-864B-F28C66AD47B1 Q31132248-F69919C1-EC3C-4459-9DD9-AD024CAAE30E Q31151010-D4275875-BABA-4B8B-AAFF-F306DBEE4785 Q33680883-21B3E321-5C1F-458A-BB5F-8C329A86E02C Q33753573-40623984-CDB7-491B-98A6-955EFD66E09B Q33946158-B2FF2FED-C721-4005-948A-96EA92299946 Q33954392-48056FC7-A04D-48F7-A790-8113461E7B48 Q34109778-5B6A08A7-E156-427F-90D7-8D752A19ABD9 Q34229664-BE20FD9C-33B7-42A7-8C9D-E7A4EB6DF4EA Q34350894-63833CA2-C19D-48E3-88F6-61DE61BE2CD5 Q34441935-4EC9BB3E-5ACC-406D-B83E-F79DA2685446 Q34511575-1A8EF9B8-F221-4F36-AA2E-DF6B242BA2CD Q34544718-726635F2-B7AD-40BB-B559-E2963174B534 Q34611144-650AA864-20BA-4E9C-9BD3-A79CF6124B9B Q34784621-1CD08C11-CEA9-431C-B581-0C0BA881E811 Q35033862-5685A7CE-934C-45B0-9BBB-BB34023DCA87 Q35102328-2B7C067F-BD7E-4D51-A80C-FB7BEF3D4D5B Q35110992-99865CCC-872C-4AB7-A151-D2ED2D98BB10 Q35142291-104DC14C-D2AA-4D5F-8FD4-2CD34875A2A4 Q35154031-B1811E97-D61C-4C29-99A3-2AA0A584FA8E Q35686912-6AF70B75-342D-4E14-A55C-53FC9E82BFC1 Q35689608-5A02C3FC-9A81-4D25-B8A8-DE87F7AE747E Q35745442-5BD1C23B-61B2-453B-81A4-AFFC723CAB42 Q35842116-7F83CFB0-123A-4BFB-9425-0DF595716BDD Q35842299-8B9503A6-A7B0-410A-907E-5F8B05C91FD9 Q35974165-3A0CDB3E-F51E-4508-9F36-794506E99471 Q36088254-43D97706-437F-47AB-AC37-FE220CFDCD80 Q36100426-52D076C7-60AC-4124-8D08-E9A6874C408B

P2860

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

http://www.wikidata.org/entity/Q34681455

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին 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

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@ast

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@en

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@nl

type

label

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@ast

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@en

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@nl

prefLabel

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@ast

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@en

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@nl

P1433

Q34681455-6CF962DA-06C3-4402-9688-8EB5D24038D6

P1476

Q34681455-D3A7EE96-EBA8-437A-BF2F-153D4FF89A22

P2093

Q34681455-1FF58C23-F889-4F54-9EFD-D9D7492AB503

Q34681455-2BB168D6-9A31-44CF-B615-2C69CDC6FE01

Q34681455-759268D7-6E0B-42CD-A700-39019C3B8DCA

Q34681455-7CA53E21-E065-4955-979B-2A2F35E9C0E6

Q34681455-C92341F5-A631-4942-8AFE-74BDA1259D67

Q34681455-D24902DB-2D8E-42C6-A73D-ABCB307159B7

Q34681455-E95B0EE3-9883-4300-AF59-A4F3BAA13B81

P2860

Q34681455-075F5854-DC08-424B-8AF0-AEBD7E688E18

Q34681455-091BA565-49A7-4EDD-9CEA-9B0A19000FBD

Q34681455-09DE3B2E-663B-405E-B4CF-1A93B675818E

Q34681455-131F2E4A-5C60-4277-9B9E-AA7C97D298BE

Q34681455-162BA8E7-0427-4F3C-96DD-ED4678405746

Q34681455-1A61AC65-0A63-41A2-A3F3-DE76F969CB87

Q34681455-2116A54B-12F7-474D-92F9-10DC870A11A4

Q34681455-21701DF0-9798-499B-A90C-8E0CA62E5583

Q34681455-24C1A7BD-BF1D-48A3-A098-1B9E522B9F98

Q34681455-28F9131A-4110-463D-8E1A-B06DC4CF50B2

P304

Q34681455-59BD71D4-5794-48EF-8F56-1837AA2DFDA2

P31

Q34681455-0F9C72DA-7240-478B-9C80-7FB2AAA1AEF3

P356

Q34681455-80D5F28A-609D-4231-99EE-ADDFFEACD447

P407

Q34681455-6DC30063-30B8-4D08-9784-2864987BBBED

P433

Q34681455-378FE077-EF93-438C-864A-81AFEACCE2F2

P478

Q34681455-90546F61-E473-4A2F-A628-7AAB0A642178

P50

Q34681455-1A8C6B3F-6D1F-47EB-87F6-165E95AB3A71

Q34681455-1CF283D6-0385-4053-91D0-3EAC8CCD023B

Q34681455-93B9B954-B001-4F7A-B516-F9A9EA5B41A9

Q34681455-C9594A9B-9628-4F72-AF6D-FEEBD5E040A5

P577

Q34681455-E9CC32B1-B62B-4791-BE94-D3ED0B1F23C9

P5875

Q34681455-12453F81-3157-488F-887C-4549963CED2B

P698

Q34681455-8E66C0DE-8E4D-45D1-8DF9-62E3C21C8154

P921

Q34681455-A3944F1C-A62F-48FE-9D8C-23CC852DFF4A

P932

Q34681455-E7128DBB-F3B6-4DF8-AD50-54E57DA0C4D1

P356

P1433

Journal of Experimental Medicine

P1476

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.

@en

P2093

Anders Krarup

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

Axel M Mann

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

Claudia R Ruprecht

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

Irene A Abela

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

Livia Berlinger

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

Peter Rusert

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

Roland R Regoes

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

P2860

Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions

Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies

Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro

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

HIV traffics through a specialized, surface-accessible intracellular compartment during trans-infection of T cells by mature dendritic cells

A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies

Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins

Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120

Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility

Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies

P304

439-454

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

P31

scholarly article

P356

10.1084/JEM.20101907

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

P407

P433

3

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

P478

208

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

P50

Alexandra Trkola

Huldrych F Günthard

Oliver F Brandenberg

P577

2011-02-28T00:00:00Z

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

P5875

50226846

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

P698

21357743

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

P921

P932

3058584

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