Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120. (Q42572387)

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scientific article published on 5 June 2013

Language	Label	Description	Also known as
English	Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120.	scientific article published on 5 June 2013

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120. (English)

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

author name string

Tommy Tong

1

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Keiko Osawa

2

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

James E Robinson

3

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Ema T Crooks

4

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

James M Binley

5

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

language of work or name

0 references

publication date

5 June 2013

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Europe PubMed Central

PMC publication ID

2 November 2017

Journal of Virology

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Europe PubMed Central

PMC publication ID

2 November 2017

87

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

16

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

9233-9249

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units

1 reference

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Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.

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Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer

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Structural mechanism of trimeric HIV-1 envelope glycoprotein activation

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Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops

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HIV vaccine development at the turn of the 21st century

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The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.

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Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)

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Direct antibody access to the HIV-1 membrane-proximal external region positively correlates with neutralization sensitivity

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An HIV-1 gp120 envelope human monoclonal antibody that recognizes a C1 conformational epitope mediates potent antibody-dependent cellular cytotoxicity (ADCC) activity and defines a common ADCC epitope in human HIV-1 serum

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

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Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens.

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Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells.

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Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.

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Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target

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Initial B-cell responses to transmitted human immunodeficiency virus type 1: virion-binding immunoglobulin M (IgM) and IgG antibodies followed by plasma anti-gp41 antibodies with ineffective control of initial viremia

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Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity

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In vivo alteration of humoral responses to HIV-1 envelope glycoprotein gp120 by antibodies to the CD4-binding site of gp120.

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Characterizing anti-HIV monoclonal antibodies and immune sera by defining the mechanism of neutralization.

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Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1.

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Antigenic conservation and immunogenicity of the HIV coreceptor binding site

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Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies.

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Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage.

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The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection

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The v3 loop is accessible on the surface of most human immunodeficiency virus type 1 primary isolates and serves as a neutralization epitope.

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

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Additive Effects Characterize the Interaction of Antibodies Involved in Neutralization of the Primary Dualtropic Human Immunodeficiency Virus Type 1 Isolate 89.6

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Association of structural changes in the V2 and V3 loops of the gp120 envelope glycoprotein with acquisition of neutralization resistance in a simian-human immunodeficiency virus passaged in vivo

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Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding

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Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer

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Epitope exposure on functional, oligomeric HIV-1 gp41 molecules

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Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120.

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Synergistic neutralization of human immunodeficiency virus type 1 by combinations of human monoclonal antibodies

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Generation and characterization of monoclonal antibodies to the putative CD4-binding domain of human immunodeficiency virus type 1 gp120.

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Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

28 May 2018

Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

28 May 2018

Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

28 May 2018

Native HIV type 1 virion surface structures: relationships between antibody binding and neutralization or lessons from the viral capture assay

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

16 August 2018

Potent neutralization of primary human immunodeficiency virus clade C isolates with a synergistic combination of human monoclonal antibodies raised against clade B.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

16 August 2018

gp41: HIV's shy protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3754051

1 December 2018

Interactions of human antibodies, epitope exposure, antibody binding and neutralization of primary isolate HIV-1 virions

1 reference

https://pubmed.ncbi.nlm.nih.gov/23740975

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Conformational changes in env oligomer induced by an antibody dependent on the V3 loop base

1 reference

https://pubmed.ncbi.nlm.nih.gov/23740975

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Synergy between human monoclonal antibodies to HIV extends their effective biologic activity against homologous and divergent strains

1 reference

https://pubmed.ncbi.nlm.nih.gov/23740975

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120

1 reference

https://pubmed.ncbi.nlm.nih.gov/23740975

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of antibodies that inhibit HIV gp120 antigen processing and presentation

1 reference

https://pubmed.ncbi.nlm.nih.gov/23740975

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JVI.01145-13

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

ResearchGate publication ID

0 references

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