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Mark Cayabyab

Researcher at Harvard University

Publications -  23
Citations -  1986

Mark Cayabyab is an academic researcher from Harvard University. The author has contributed to research in topics: Simian immunodeficiency virus & Glycoprotein. The author has an hindex of 16, co-authored 22 publications receiving 1918 citations. Previous affiliations of Mark Cayabyab include Beth Israel Deaconess Medical Center & Boston Children's Hospital.

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Journal ArticleDOI

Tyrosine Sulfation of the Amino Terminus of CCR5 Facilitates HIV-1 Entry

TL;DR: The chemokine receptor CCR5, a principal HIV-1 coreceptor, is posttranslationally modified by O-linked glycosylation and by sulfation of its N-terminal tyrosines, a modification common to primate immunodeficiency virus coreceptors.
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The Orphan Seven-Transmembrane Receptor Apj Supports the Entry of Primary T-Cell-Line-Tropic and Dualtropic Human Immunodeficiency Virus Type 1

TL;DR: In this article, Apj and CCR9 were identified as 7TMS proteins that can function as HIV-1 coreceptors, and mRNAs for both proteins were present in phytohemagglutinin- and interleukin-2-activated peripheral blood mononuclear cells.
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Increased CCR5 affinity and reduced CCR5/CD4 dependence of a neurovirulent primary human immunodeficiency virus type 1 isolate.

TL;DR: The results predict the presence of HIV-1 variants with increased CCR5 affinity and reduced dependence on C CR5 and CD4 in the brains of some AIDS patients with central nervous system disease and suggest that R5 variants with increase CCR 5 affinity may represent a pathogenic viral phenotype contributing to the neurodegenerative manifestations of AIDS.
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Adaptation of a CCR5-Using, Primary Human Immunodeficiency Virus Type 1 Isolate for CD4-Independent Replication

TL;DR: A major function of CD4 binding in the entry of primary HIV-1 isolates can be bypassed by changes in the gp120 V1-V2 elements, which allow the envelope glycoproteins to assume a conformation competent for CCR5 binding.