Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33 - Wikidata - wikimedia - TriplyDB

Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33

Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33

http://www.wikidata.org/entity/Q27673031

about

Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design Structural Basis of HCV Neutralization by Human Monoclonal Antibodies Resistant to Viral Neutralization Escape Hepatitis C Virus E2 Envelope Glycoprotein Core Structure Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2 Hepatitis C.Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design Optimization of peptide arrays for studying antibodies to hepatitis C virus continuous epitopes.The core domain of hepatitis C virus glycoprotein E2 generates potent cross-neutralizing antibodies in guinea pigs Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2.Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412-423 Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex.Structural basis for penetration of the glycan shield of hepatitis C virus E2 glycoprotein by a broadly neutralizing human antibody.Longitudinal Sequence and Functional Evolution within Glycoprotein E2 in Hepatitis C Virus Genotype 3a Infection Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding Monoclonal Antibodies Directed toward the Hepatitis C Virus Glycoprotein E2 Detect Antigenic Differences Modulated by the N-Terminal Hypervariable Region 1 (HVR1), HVR2, and Intergenotypic Variable Region Antibodies to an interfering epitope in hepatitis C virus E2 can mask vaccine-induced neutralizing activity Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigen.CD81 and hepatitis C virus (HCV) infection.Expression of recombinant glycoproteins in mammalian cells: towards an integrative approach to structural biology.Structural and antigenic definition of hepatitis C virus E2 glycoprotein epitopes targeted by monoclonal antibodies.The past, present and future of neutralizing antibodies for hepatitis C virus.Challenges to the development of vaccines to hepatitis C virus that elicit neutralizing antibodies.HCV E2 core structures and mAbs: something is still missing.HCV glycoprotein structures: what to expect from the unexpected.Role of Conserved E2 Residue W420 in Receptor Binding and Hepatitis C Virus Infection.Viral evasion and challenges of hepatitis C virus vaccine development.Generation and Characterization of Monoclonal Antibodies against a Cyclic Variant of Hepatitis C Virus E2 Epitope 412-422.The dynamic properties of the Hepatitis C Virus E2 envelope protein unraveled by molecular dynamics.Structure-Based Design of Hepatitis C Virus Vaccines that Elicit Neutralizing Antibody Responses to a Conserved Epitope.Monoclonal anti-envelope antibody AP33 protects humanized mice against a patient-derived hepatitis C virus challenge.Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies.The unexpected structures of hepatitis C virus envelope proteins Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis.Screening HCV genotype-specific epitope peptides based on conserved sequence analysis and B cell epitope prediction in HCV E2 region.Escape of Hepatitis C Virus from Epitope I Neutralization Increases Sensitivity of Other Neutralization Epitopes.Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.The Neutralizing Face of Hepatitis C Virus E2 Envelope Glycoprotein.Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.

P2860

Q26801759-18C013C9-27A4-4302-9F58-97073869160C Q27678252-F1E791E7-DF5D-4030-85D0-768CD4C3A707 Q27680704-4CDFABC4-10E6-4E05-9B4F-E6A0C852242F Q27681839-A18F7BE7-76C8-454A-9BDE-D8D7863B0CBE Q28084654-1E59E572-E506-4FE2-9D24-D473F970A38F Q30155145-F0388EE4-4BA6-4C31-9884-EAE6A3AD14F4 Q30374314-9C0E2E48-FBD4-4C5C-A460-A130476C3D7C Q33563569-4C69C9D3-BD45-4A15-9C07-0C3B839CAA47 Q33612608-70C7191A-5D52-410B-925F-50D673D5D627 Q33691856-F4ABB1C7-01C5-4B6D-8068-702D51323B77 Q34047477-1B17BC50-2EC4-404A-AD46-300B8EA51924 Q34262165-DF3CBA42-F513-43EC-B719-DD3D73A60DB1 Q35450992-36C2ABAD-26C0-45A7-915C-CD8E42B593D7 Q35630492-79DB85BD-9A70-4240-A9B5-ADA2A36662B8 Q35942829-D8CCEE60-4B92-4F0C-964A-CC687D038A54 Q36334312-63323D5F-71DF-4E9C-AC01-9CBB020AF893 Q36378193-2C1E43ED-9EC6-4B4C-8A8E-343D2F9DE7B6 Q37417839-6D747D1A-08E6-44DB-BD1E-512CF7458708 Q37611819-D57793FE-1483-4E4A-B503-74E44C59E718 Q38102415-5DD86B7E-2534-4B69-AEA5-48B53E425382 Q38128299-DB93B6F8-C54F-494B-8EC0-40B4B7B9DC23 Q38192357-9C007DC0-71B9-45D2-B32A-651E02AEFEA5 Q38234934-A8A5BD16-7163-48FA-9ABD-9D59AACB7CBE Q38244787-317FDA86-B559-48F5-A658-90322C9F41E3 Q38384140-EEE1AC3B-8E89-4696-A572-0EDF21FD8E0A Q38765582-49C3F039-6954-4ED9-BB18-867209C1DCAB Q38961608-B2D9ABBA-E63F-4D0A-918B-9E20B7696AF2 Q39062848-EF6BF545-75C4-4519-ABA0-384F8E205290 Q39923648-92B42166-1637-4DAD-8490-B9969C5D22D3 Q40088796-9E916FBF-6D28-4A0E-A51E-79D5F61981B1 Q40165519-4342BAAE-21E4-4445-9EA0-73382B1F9C1D Q41619358-E7538361-3701-49B4-81AC-E6F4F1C31121 Q41672624-EC1B64CA-4631-4EFB-9C83-CE190E43FDE4 Q47238536-19F2C8A2-528F-4B2F-8814-14E6523C44D9 Q47335897-A756EBC8-EE1F-4F05-80CB-D907AC7CE0C3 Q52375192-FD2B7945-5FB0-4EE3-8244-5D9195508EF9 Q53683152-B7575E28-FC6C-4D23-A330-617E78648A5C Q55003572-0866D5F6-6EFD-41E1-AA8C-6492B8FB3222 Q55299977-0C3E317C-06AB-45B6-994F-AF0487F37C62 Q55383950-22A447BF-3C42-4D8D-845C-1922E9EC2677

P2860

Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33

http://www.wikidata.org/entity/Q27673031

description

2012 nî lūn-bûn

@nan

2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@ast

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@en

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@nl

type

label

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@ast

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@en

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@nl

prefLabel

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@ast

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@en

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@nl

P1433

Q27673031-FFD5DDCF-2273-4208-B651-50036C6CEF71

P1476

Q27673031-3BCA6C95-3ED3-41D6-9886-2CE9A0B661EA

P2093

Q27673031-17824FA5-5E14-4CBE-BF23-B59DFEA9AB8D

Q27673031-1C78473E-45C1-44DC-81DA-EE085818EBD7

Q27673031-844AEF76-C2E4-45CE-BA34-92986F2FF6A3

Q27673031-A1451D53-424F-4FEA-8227-BF65C1557B8C

Q27673031-BA58697D-C9DB-4FBF-A07F-81C5A23F5C97

Q27673031-DA4A0917-71CC-497B-89FE-94A5E23B249B

P2860

Q27673031-12C86AC9-ACEA-4A6D-813A-BC2DBC7E9D7C

Q27673031-21A118AE-B0C2-4539-B4C1-3E911DFC386E

Q27673031-38751CCE-5BA6-4FFE-812B-A5C0DEB3D4BD

Q27673031-44CE697E-8B9C-4F9A-910D-050492AD2FE8

Q27673031-6B33BFD0-CE84-48D0-ACA0-826EBCEC212E

Q27673031-891AA36C-29C6-46B5-B5F4-F586A4310E76

Q27673031-C29EC787-C44A-4C0F-8D8E-E1EF39A1E062

Q27673031-E943B83A-DD1B-4EDF-A810-CB468E649AAD

Q27673031-EA4E1C7E-6314-452F-891B-B82B9F24E08A

Q27673031-F839D4B8-3B22-4556-A257-F6DC3FF16AFE

P304

Q27673031-FEB63936-403C-4692-BB54-1421EA2407CF

P31

Q27673031-FBEC4E47-D55C-451C-83EE-89DB0C163266

P356

Q27673031-46861E99-11AA-40FD-85CD-0275351FD5C1

P433

Q27673031-F578EF0A-DA17-4C07-A20F-78A3521946B1

P478

Q27673031-3F1DB77A-9C38-4530-B4F3-168F16EB2FA6

P50

Q27673031-A5FD7116-AB99-4823-B5D2-DD01C94C9B11

Q27673031-EC16034D-57E9-445D-AAB2-EB60EA455202

P577

Q27673031-85871D40-760C-4D42-A58F-2FE556753816

P698

Q27673031-F89B0258-CE8D-464E-A196-A755781CF895

P921

Q27673031-2D1DD741-8CA6-4024-A17E-9E4BC1FD2B61

P932

Q27673031-32F873D8-08AB-48C4-9C84-2ECE9180D6E2

P356

P1433

Journal of Virology

P1476

Structure of Hepatitis C Virus ...... in Complex with Antibody AP33

@en

P2093

Erick Giang

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

Justin B Robbins

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

Leopold Kong

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

Mansun Law

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

Robyn L Stanfield

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

Travis Nieusma

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

P2860

Monoclonal Antibody AP33 Defines a Broadly Neutralizing Epitope on the Hepatitis C Virus E2 Envelope Glycoprotein

In vitro selection of a neutralization-resistant hepatitis C virus escape mutant

Identification and Characterization of Broadly Neutralizing Human Monoclonal Antibodies Directed against the E2 Envelope Glycoprotein of Hepatitis C Virus

Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1

Characterization of the hepatitis C virus E2 epitope defined by the broadly neutralizing monoclonal antibody AP33.

HIV-1 and influenza antibodies: seeing antigens in new ways

Mutations within a conserved region of the hepatitis C virus E2 glycoprotein that influence virus-receptor interactions and sensitivity to neutralizing antibodies.

Antibodies, viruses and vaccines.

Structure-based antigen design: a strategy for next generation vaccines.

Functional analysis of hepatitis C virus E2 glycoproteins and virus-like particles reveals structural dissimilarities between different forms of E2.

P304

13085-8

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

P31

scholarly article

P356

10.1128/JVI.01939-12

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

P433

23

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

P478

86

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

P50

Ian Andrew Wilson

P577

2012-12-01T00:00:00Z

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

P698

22973046

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

P921

P932

3497658

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