Tyrosine-sulfated V2 peptides inhibit HIV-1 infection via coreceptor mimicry
Open Access
- 1 August 2016
- journal article
- Published by Elsevier in EBioMedicine
- Vol. 10, 45-54
Abstract
No abstract availableKeywords
Funding Information
- Division of Intramural Research (293FS, AI058072, AI013225)
- National Institutes of Health (293FS, AI058072, AI013225)
- International AIDS Vaccine Initiative (293FS, AI058072, AI013225)
- National Institute of Allergy and Infectious Diseases (293FS, AI058072, AI013225)
This publication has 49 references indexed in Scilit:
- Identification of the platelet-derived chemokine CXCL4/PF-4 as a broad-spectrum HIV-1 inhibitorProceedings of the National Academy of Sciences, 2012
- Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loopsProceedings of the National Academy of Sciences, 2012
- Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimerProceedings of the National Academy of Sciences, 2011
- Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9Nature, 2011
- Broad neutralization coverage of HIV by multiple highly potent antibodiesNature, 2011
- Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structureProceedings of the National Academy of Sciences, 2010
- Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1Proceedings of the National Academy of Sciences, 2010
- Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobilityProceedings of the National Academy of Sciences, 2009
- Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120Science, 2009
- Molecular architecture of native HIV-1 gp120 trimersNature, 2008