(Q33941033)

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Increased sensitivity to broadly neutralizing antibodies of end-stage disease R5 HIV-1 correlates with evolution in Env glycosylation and charge

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Europe PubMed Central

PubMed publication ID

30 July 2017

Increased sensitivity to broadly neutralizing antibodies of end-stage disease R5 HIV-1 correlates with evolution in Env glycosylation and charge (English)

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Europe PubMed Central

PubMed publication ID

30 July 2017

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Jasminka Sterjovski

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Jasminka Sterjovski

3

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Marianne Jansson

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Marianne Jansson

11

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Adnane Achour

8

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Hannes Uchtenhagen

4

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Hannes Uchtenhagen

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Europe PubMed Central

PubMed publication ID

30 July 2017

Eva Maria Fenyö

10

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Eva Maria Fenyö

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Europe PubMed Central

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30 July 2017

7

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Jan Albert

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Europe PubMed Central

PubMed publication ID

30 July 2017

2

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Johanna Repits

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Europe PubMed Central

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30 July 2017

author name string

Marie Borggren

1

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Europe PubMed Central

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30 July 2017

Melissa J Churchill

5

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Europe PubMed Central

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30 July 2017

Anders Karlsson

6

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Europe PubMed Central

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30 July 2017

Paul R Gorry

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30 July 2017

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publication date

16 June 2011

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Europe PubMed Central

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30 July 2017

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Europe PubMed Central

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30 July 2017

6

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Europe PubMed Central

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30 July 2017

6

1 reference

Europe PubMed Central

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30 July 2017

e20135

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Europe PubMed Central

PubMed publication ID

30 July 2017

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Creative Commons Attribution 4.0 International

16 June 2011

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April 2022 Public Data File from Crossref

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Human anti-HIV-neutralizing antibodies frequently target a conserved epitope essential for viral fitness

1 reference

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1 reference

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Molecular architecture of native HIV-1 gp120 trimers

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Evolution of DC-SIGN use revealed by fitness studies of R5 HIV-1 variants emerging during AIDS progression

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Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity

1 reference

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Very fast empirical prediction and rationalization of protein pKa values

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The host environment drives HIV-1 fitness

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Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1.

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Coevolution of RANTES sensitivity and mode of CCR5 receptor use by human immunodeficiency virus type 1 of the R5 phenotype

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A new cell line-based neutralization assay for primary HIV type 1 isolates

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The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1-->2 mannose residues on the outer face of gp120.

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The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120.

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1 reference

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21 January 2018

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10.1371/JOURNAL.PONE.0020135

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

2011PLoSO...620135B

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

ResearchGate publication ID

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