Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41 - Wikidata - wikimedia - TriplyDB

Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41

Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41

http://www.wikidata.org/entity/Q27666159

about

Structural mechanism of trimeric HIV-1 envelope glycoprotein activation The molecular basis of HIV entry The Antibody Response against HIV-1 HIV-1 envelope glycoprotein structure Complexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41 Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing A gp41 MPER-specific Llama VHH Requires a Hydrophobic CDR3 for Neutralization but not for Antigen Recognition Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains Molecular dynamics studies of the inhibitor C34 binding to the wild-type and mutant HIV-1 gp41: inhibitory and drug resistant mechanism Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery.Synthetic Fab fragments that bind the HIV-1 gp41 heptad repeat regions.Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting.Characterization of neutralizing profiles in HIV-1 infected patients from whom the HJ16, HGN194 and HK20 mAbs were obtained.Particle conformation regulates antibody access to a conserved GII.4 norovirus blockade epitope.Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acid-modified peptide fusion inhibitor.Identification of a new epitope for HIV-neutralizing antibodies in the gp41 membrane proximal external region by an Env-tailored phage display library.Synergy in monoclonal antibody neutralization of HIV-1 pseudoviruses and infectious molecular clones.Sub-inhibitory concentrations of human α-defensin potentiate neutralizing antibodies against HIV-1 gp41 pre-hairpin intermediates in the presence of serum.Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti-HIV-1 drugs.IGHV1-69 B cell chronic lymphocytic leukemia antibodies cross-react with HIV-1 and hepatitis C virus antigens as well as intestinal commensal bacteria.Structure and immune recognition of trimeric pre-fusion HIV-1 Env.Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1.HIV-1 VACCINES. Diversion of HIV-1 vaccine-induced immunity by gp41-microbiota cross-reactive antibodies.Recombinant antibodies for diagnostics and therapy against pathogens and toxins generated by phage display.Swapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infection Statistical inference of a convergent antibody repertoire response to influenza vaccine Role of human immunodeficiency virus type 1 envelope structure in the induction of broadly neutralizing antibodies.Computer-Aided Approaches for Targeting HIVgp41.Conformational plasticity of the Ebola virus matrix protein.Restricted, canonical, stereotyped and convergent immunoglobulin responses.Designed protein mimics of the Ebola virus glycoprotein GP2 α-helical bundle: stability and pH effects.Evaluation of ligand-based NMR screening methods to characterize small molecule binding to HIV-1 glycoprotein-41.Structure-activity relationship studies of indole-based compounds as small molecule HIV-1 fusion inhibitors targeting glycoprotein 41.A novel gene therapy strategy using secreted multifunctional anti-HIV proteins to confer protection to gene-modified and unmodified target cells.The C34 Peptide Fusion Inhibitor Binds to the Six-Helix Bundle Core Domain of HIV-1 gp41 by Displacement of the C-Terminal Helical Repeat Region.A novel view of modelling interactions between synthetic and biological polymers via docking.Adsorption and folding dynamics of MPER of HIV-1 gp41 in the presence of DPC micelle.Novel neutralising antibodies targeting the N-terminal helical region of the transmembrane envelope protein p15E of the porcine endogenous retrovirus (PERV).Multi-Donor Longitudinal Antibody Repertoire Sequencing Reveals the Existence of Public Antibody Clonotypes in HIV-1 Infection.

P2860

Q21131394-3D26D6FD-1144-4D59-87E4-2F02CA70EFC1 Q26863686-827EFAAC-4BB5-4D83-8D66-06E0209CD5CD Q27000889-CF367DCE-6B3F-43B4-B82B-9527F0EDECFC Q27011248-99BBD2D4-33C8-462A-9311-298298CF4B8B Q27303525-1D1A8A45-EF81-4096-9C64-A5D210A25EC3 Q27671696-495B97A0-9299-4A90-A008-7827D1041CEA Q27676864-49AB4416-E6A7-428F-BC51-8CD6742DEEE0 Q27684503-67D03244-DDE9-42CA-B7F3-48E568009535 Q28544927-BE8FAF69-A7F8-4565-90B4-B002FCEC81B3 Q30155145-D871BFB4-31AA-4113-AF9B-455736F3B0FC Q30912819-963B19C2-9490-4A0D-95E0-8A42DCFDA5EC Q34021319-6141282C-796D-4315-94D6-E8AB602EEDC5 Q34042758-D5D5E71F-FFBB-46E7-8583-671FA896D9B2 Q34053295-E657A53B-B7B1-45EC-A6DA-564605EAF6D3 Q34059136-4AFEE1C8-71C9-4024-A358-165C80BA12C7 Q34189558-259786EC-CD2B-4D23-8FD5-9D331FC710FA Q34488183-60AB6821-280D-4335-9CD7-B0A46CC8C1E4 Q34762224-78CCCE39-1476-4023-8CE3-8055B8B31070 Q34778515-FA1E94CA-E231-47AC-A93C-66BE6B1329FC Q34793125-3658892D-77B8-4C21-9244-92C96A7315AF Q35116369-4D1DC187-B7F4-457B-A60E-3887528D3B47 Q35142291-BAB3D197-D397-4085-91BD-9B7931ADF1D7 Q35603504-1F176B1C-7AF0-418C-8805-E75C5FC73E54 Q35728947-4C3C159E-E8C5-4514-AF32-21AA74954D97 Q36023082-F5E608E0-CC8B-4358-B602-D237FFCABD2D Q36036157-CF0E1F30-D802-4731-882A-47D64A98A9BD Q36965474-8B93B208-E301-4024-AC04-CE3C1057F695 Q38046828-75DDCD9F-40AF-4F74-AF86-8C34C84426D4 Q38111393-EB7134E5-EB4F-407F-AAB7-9ED3B34BBF52 Q38243508-05C4E786-8154-43DA-A7EB-965687B6C89E Q38551067-DC94514B-D8E6-4C11-9768-15885E5E6B4A Q38666508-78EC9CC3-1BD9-4495-A0F1-1C7F10F3DC63 Q38673747-0AD019EE-3EB2-4E13-B330-C0CBEA95810E Q38992313-3ED2C587-ABBB-4BEB-8B97-A8D55CAAD9D3 Q39048904-951A0EE7-5DDD-4E18-8170-F7BC69B39B58 Q40387378-096807EC-8DA4-4BE1-8FB6-4097CBF3B1B0 Q44536459-1F356CC6-DB1C-4D35-BC50-D2CDD5FCA252 Q46917279-469CA2D9-A413-4CB7-8564-FBC76903B4DE Q50943628-40608469-B961-49FE-88DA-2F5DE292D599 Q55347049-C21FCC22-7C6A-4F5C-8B19-32A3431D144A

P2860

Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41

http://www.wikidata.org/entity/Q27666159

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

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

name

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@ast

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@en

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@nl

type

label

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@ast

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@en

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@nl

prefLabel

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@ast

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@en

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@nl

P1433

Q27666159-0684884C-1FBC-4D28-8987-4393E7DAD3EA

P1476

Q27666159-A801C89B-0D3F-4024-9137-6B7B0A62C834

P2093

Q27666159-211DB4B8-215A-4888-9C48-D3E52827FC5E

Q27666159-2923424C-20EC-4A62-8BBC-8754C015D553

Q27666159-30C89CDD-FDC9-4D13-A41C-29C2CE6C3A94

Q27666159-43200CF3-3DC8-4F28-95FF-0404F5D33C3D

Q27666159-5D631675-FDB6-4D74-B868-C1F7B49595D6

Q27666159-61F6B155-748E-42AC-B4E9-6536143E6AC6

Q27666159-737BB8DB-FA21-4EE5-A8AE-FD4CDC7A5BE1

Q27666159-BBDEDB9A-DE56-4F04-964B-3299E9B6AF61

Q27666159-BBEEEA54-BD1C-45D5-B6D9-44B2AA849179

Q27666159-ED0AE21A-F6B1-4D1B-BE1B-07B183AEB4C3

P2860

Q27666159-00D894DE-66CC-4D6E-8614-6468990D5BAF

Q27666159-14514087-CC22-4C8B-BCD8-054FA57AB70E

Q27666159-176DC9C5-C135-4B57-AD02-9D601FDC4C60

Q27666159-1A143AD5-6222-413D-BD52-E4E1F83D87D0

Q27666159-1EC67CB2-30C7-4F95-BA62-AAF52B140C81

Q27666159-23802F96-428F-4EAE-BFCD-6ED2CECFA80D

Q27666159-28188149-5BE8-4189-9E3B-2FF944F836CA

Q27666159-34CBA373-70F0-498B-AC95-B82D4E4B5EC5

Q27666159-399883BA-BA19-4BE6-BD07-2FADD577FCBA

Q27666159-3B6E418C-FD2C-49E6-8465-F2EB68E180C7

P304

Q27666159-7D8DCC15-0A7C-40A4-8107-067AC56D93F9

P31

Q27666159-7A050BBA-73F7-4A48-895C-A01350F8E5C4

P3181

Q27666159-5D8E463B-1FF2-4A58-9A42-A229E46C44CF

P356

Q27666159-0102E803-D948-4210-82A4-D3B7A4855D1D

P433

Q27666159-8ABD1B9E-4CA7-4F70-AC02-9694D93A150D

P478

Q27666159-4C29BA01-821D-4083-AB5D-D13313C5BEB5

P50

Q27666159-31A4C9C9-0C8B-46C1-8D4E-F555C8B909FB

Q27666159-473F519C-1C59-4BAD-A83B-71A982F2EE56

Q27666159-4B6B796B-D48B-4EDF-B9F6-0A944595AF88

Q27666159-CE0A9D3D-54E2-40D8-8C67-641D6F7F0425

P577

Q27666159-DC77D304-46EB-4B0A-8A01-B0BEC332015F

P5875

Q27666159-8272A8B7-328A-4747-9E39-AB192EFF374C

P698

Q27666159-6475D15E-49EA-48D4-AE0A-EA26D97DF709

P921

Q27666159-3B2FB7C9-833F-4B83-ABC6-6CD90DD27CC0

Q27666159-428A22E5-A3B7-4672-A508-FD04045B8C86

P932

Q27666159-DF431DA9-AA2D-4EC7-8E15-D23AB36F88A6

P3181

P356

JOURNAL.PPAT.1001195

P1433

P1476

Crystal Structure and Size-Dep ...... served Heptad Repeat 1 of gp41

@en

P2093

Andreas Hinz

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

Charles Sabin

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

Chiara Silacci

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

David Lutje Hulsik

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

Davide Corti

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

Fabrizia Vanzetta

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

Gloria Agatic

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

Mike S Seaman

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

Robin Weiss

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

Victor Buzon

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

P2860

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

HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes

Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41

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

Viral membrane fusion

Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket

Short constrained peptides that inhibit HIV-1 entry

Core structure of gp41 from the HIV envelope glycoprotein

Atomic structure of the ectodomain from HIV-1 gp41

Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues

P304

e1001195

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

P31

scholarly article

P3181

1047439

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

P356

10.1371/JOURNAL.PPAT.1001195

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

P433

11

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

P478

6

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

P50

Antonio Lanzavecchia

Federica Sallusto

Gabriella Scarlatti

P577

2010-11-18T00:00:00Z

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

P5875

49652053

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

P698

21124990

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

P921

crystal structure

P932

2987821

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