Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates (Q27629806)

2

object named as

R Wyatt

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Peter D. Kwong

1

object named as

P D Kwong

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author name string

S Majeed

3

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J Robinson

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R W Sweet

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W A Hendrickson

Isolation of a T-Lymphotropic Retrovirus from a Patient at Risk for Acquired Immune Deficiency Syndrome (AIDS)

7

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publication date

15 December 2000

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published in

Structure

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volume

8

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issue

12

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page(s)

1329-39

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cites work

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The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates

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HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5

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CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1

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Core structure of gp41 from the HIV envelope glycoprotein

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Atomic structure of the ectodomain from HIV-1 gp41

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

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Energetics of the HIV gp120-CD4 binding reaction

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The antigenic structure of the HIV gp120 envelope glycoprotein

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The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and Immunogens

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The V3 domain of the HIV-1 gp120 envelope glycoprotein is critical for chemokine-mediated blockade of infection

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A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding

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Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry

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Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates.

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11188697

1 reference

Consolidated OpenCitations Corpus – April 2017