Evidence for common structural determinants of human immunodeficiency virus type 1 coreceptor activity provided through functional analysis of CCR5/CXCR4 chimeric coreceptors (Q39605336)

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scientific article published on December 2001

Language	Label	Description	Also known as
English	Evidence for common structural determinants of human immunodeficiency virus type 1 coreceptor activity provided through functional analysis of CCR5/CXCR4 chimeric coreceptors	scientific article published on December 2001

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

Evidence for common structural determinants of human immunodeficiency virus type 1 coreceptor activity provided through functional analysis of CCR5/CXCR4 chimeric coreceptors (English)

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

author name string

Pontow S

1

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

Ratner L

2

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

language of work or name

0 references

publication date

1 December 2001

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

Journal of Virology

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Europe PubMed Central

PMC publication ID

13 September 2017

75

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

23

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

11503-11514

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

Molecular interactions of cyclam and bicyclam non-peptide antagonists with the CXCR4 chemokine receptor

1 reference

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1 reference

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Inhibition of HIV infection by bicyclams, highly potent and specific CXCR4 antagonists

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N-linked glycosylation of CXCR4 masks coreceptor function for CCR5-dependent human immunodeficiency virus type 1 isolates

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Viral entry through CXCR4 is a pathogenic factor and therapeutic target in human immunodeficiency virus type 1 disease

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Multiple charged and aromatic residues in CCR5 amino-terminal domain are involved in high affinity binding of both chemokines and HIV-1 Env protein.

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Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease

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Highly potent RANTES analogues either prevent CCR5-using human immunodeficiency virus type 1 infection in vivo or rapidly select for CXCR4-using variants.

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Effect of mutations in the second extracellular loop of CXCR4 on its utilization by human and feline immunodeficiency viruses.

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Determinants for sensitivity of human immunodeficiency virus coreceptor CXCR4 to the bicyclam AMD3100

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CXCR4 sequences involved in coreceptor determination of human immunodeficiency virus type-1 tropism. Unmasking of activity with M-tropic Env glycoproteins

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T-cell-line-tropic human immunodeficiency virus type 1 that is made resistant to stromal cell-derived factor 1alpha contains mutations in the envelope gp120 but does not show a switch in coreceptor use

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Alanine substitutions of polar and nonpolar residues in the amino-terminal domain of CCR5 differently impair entry of macrophage- and dualtropic isolates of human immunodeficiency virus type 1.

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A Tyrosine-Rich Region in the N Terminus of CCR5 Is Important for Human Immunodeficiency Virus Type 1 Entry and Mediates an Association between gp120 and CCR5

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Molecular uncoupling of C-C chemokine receptor 5-induced chemotaxis and signal transduction from HIV-1 coreceptor activity

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HIV-1 entry and macrophage inflammatory protein-1beta-mediated signaling are independent functions of the chemokine receptor CCR5.

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Change in coreceptor use correlates with disease progression in HIV-1--infected individuals

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Identifiers

10.1128/JVI.75.23.11503-11514.2001

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

ResearchGate publication ID

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