(Q53811747)

20 May 2018

title

Tyrosine phosphorylation induced by C4 peptide constructs from HIV Gp120. (English)

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20 May 2018

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Liu M

1

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20 May 2018

Zeng J

series ordinal

2

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20 May 2018

Robey FA

series ordinal

3

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20 May 2018

publication date

1 January 1999

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20 May 2018

published in

Peptides

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20 May 2018

volume

20

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20 May 2018

issue

2

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20 May 2018

page(s)

185-191

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20 May 2018

Human immunodeficiency virus (HIV) envelope binds to CXCR4 independently of CD4, and binding can be enhanced by interaction with soluble CD4 or by HIV envelope deglycosylation.

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Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway

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

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Participation of tyrosine phosphorylation in the cytopathic effect of human immunodeficiency virus-1

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The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus

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Tyrosyl Phosphorylation and Activation of MAP Kinases by p56lck

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Reversal of the inhibitory effects of HIV-gp120 on CD4+ T cells by stimulation through the CD28 pathway

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7 January 2021

CD4-independent association between HIV-1 gp120 and CXCR4: functional chemokine receptors are expressed in human neurons

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7 January 2021

Human immunodeficiency virus gp120 and derived peptides activate protein tyrosine kinase p56lck in human CD4 T lymphocytes

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7 January 2021

Interaction of HIV gp120 and anti-CD4 antibodies with the CD4 molecule on human CD4+ T cells inhibits the binding activity of NF-AT, NF-kappa B and AP-1, three nuclear factors regulating interleukin-2 gene enhancer activity

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Role of tumour necrosis factor-alpha (TNF-alpha) in the induction of HIV-1 gp120-mediated CD4+ T cell anergy

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T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV

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Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor

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gp120 envelope glycoproteins of human immunodeficiency viruses competitively antagonize signaling by coreceptors CXCR4 and CCR5

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CD4-independent binding of SIV gp120 to rhesus CCR5.

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Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110K viral protein and the T4 molecule

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Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA

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7 January 2021

A conformational switch is associated with receptor affinity in peptides derived from the CD4-binding domain of gp120 from HIV I.

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Primary structure elements responsible for the conformational switch in the envelope glycoprotein gp120 from human immunodeficiency virus type 1: LPCR is a motif governing folding

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Automated synthesis of N-bromoacetyl-modified peptides for the preparation of synthetic peptide polymers, peptide-protein conjugates, and cyclic peptides

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Peptomers as Vaccine Candidates

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7 January 2021

A synthetic conformational epitope from the C4 domain of HIV Gp120 that binds CD4.

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A Helical Epitope in the C4 Domain of HIV Glycoprotein 120

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7 January 2021

The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human T lymphocytes

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Interaction of human immunodeficiency virus glycoprotein 160 with CD4 in Jurkat cells increases p56lck autophosphorylation and kinase activity

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The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck

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Identifiers

DOI

1 reference

20 May 2018

PubMed ID

10422873

1 reference

20 May 2018