Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. - sprookjes - yvandenbroek - TriplyDB

Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120.

Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120.

http://www.wikidata.org/entity/Q36132925

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Advances in structure-based vaccine design Structural insights on the role of antibodies in HIV-1 vaccine and therapy A Blueprint for HIV Vaccine Discovery HIV-1 neutralizing antibodies: understanding nature's pathways Antibodies in HIV-1 vaccine development and therapy Antigenic properties of the human immunodeficiency virus envelope glycoprotein gp120 on virions bound to target cells Molecular evolution of broadly neutralizing Llama antibodies to the CD4-binding site of HIV-1 HIV-1 receptor binding site-directed antibodies using a VH1-2 gene segment orthologue are activated by Env trimer immunization Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors Restricting HIV-1 pathways for escape using rationally designed anti–HIV-1 antibodies Multidonor Analysis Reveals Structural Elements, Genetic Determinants, and Maturation Pathway for HIV-1 Neutralization by VRC01-Class Antibodies Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies Recurrent Potent Human Neutralizing Antibodies to Zika Virus in Brazil and Mexico.Recent advances on the use of structural biology for the design of novel envelope immunogens of HIV-1 Generation of Long-Lived Bone Marrow Plasma Cells Secreting Antibodies Specific for the HIV-1 gp41 Membrane-Proximal External Region in the Absence of Polyreactivity.Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues Broadly Neutralizing Antibodies as Treatment: Effects on Virus and Immune System Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination.The Antibody Germline/Maturation Hypothesis, Elicitation of Broadly Neutralizing Antibodies Against HIV-1 and Cord Blood IgM Repertoires Elicitation of HIV-1-neutralizing antibodies against the CD4-binding site.Global panel of HIV-1 Env reference strains for standardized assessments of vaccine-elicited neutralizing antibodies Evolution of cross-neutralizing antibody specificities to the CD4-BS and the carbohydrate cloak of the HIV Env in an HIV-1-infected subject.HIV-1 antibody 3BNC117 suppresses viral rebound in humans during treatment interruption.Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo.Envelope variants circulating as initial neutralization breadth developed in two HIV-infected subjects stimulate multiclade neutralizing antibodies in rabbits.A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein.Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved.A mammalian cell based FACS-panning platform for the selection of HIV-1 envelopes for vaccine development Analysis of immunoglobulin transcripts and hypermutation following SHIV(AD8) infection and protein-plus-adjuvant immunization

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Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120.

http://www.wikidata.org/entity/Q36132925

description

2012 nî lūn-bûn

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name

Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Proceedings of the National Academy of Sciences of the United States of America

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Structural basis for germ-line ...... 4-binding site of HIV-1 gp120.

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Anthony P West

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Ron Diskin

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P2860

Few and far between: how HIV may be evading antibody avidity

High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells

Increasing the potency and breadth of an HIV antibody by using structure-based rational design

Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1

IMGT/V-QUEST: the highly customized and integrated system for IG and TR standardized V-J and V-D-J sequence analysis

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

Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope

Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding

Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing

Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

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Pamela J. Bjorkman

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