Sulfotyrosine dipeptide: Synthesis and evaluation as HIV-entry inhibitor.

Tong Ju, Duoyi Hu, Shi-Hua Xiang, Jiantao Guo

Abstract read

In one paragraph

Article in Bioorganic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.7field-weighted citation impact, top 28% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 6 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Tong JuDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, United States.

Duoyi HuNebraska Center for Virology, School of Veterinary Medicine and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States.

Shi-Hua XiangNebraska Center for Virology, School of Veterinary Medicine and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States. Electronic address: sxiang2@unl.edu.

Jiantao GuoDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, United States. Electronic address: jguo4@unl.edu.

University of Nebraska–Lincoln · US

Funding

Nebraska Center for VirologyP30GM103509 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2012 to 2014

$3.3M

NIGMS NIH HHS P30 GM103509

6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) is responsible for the worldwide AIDS pandemic. Due to the lack of prophylactic HIV-1 vaccine, drug treatment of the infected patients becomes essential to reduce the viral load and to slow down progression of the disease. Because of drug resistance, finding new antiviral agents is necessary for AIDS drug therapies. The interaction of gp120 and co-receptor (CCR5/CXCR4) mediates the entry of HIV-1 into host cells, which has been increasingly exploited in recent years as the target for new antiviral agents. A conserved co-receptor binding site on gp120 that recognizes sulfotyrosine (sTyr) residues represents a structural target to design novel HIV entry inhibitors. In this work, we developed an efficient synthesis of sulfotyrosine dipeptide and evaluated it as an HIV-1 entry inhibitor.

Indexed as

Anti-HIV AgentsCell Line, TumorCell ProliferationDipeptidesDose-Response Relationship, DrugHIV-1HumansMolecular Docking SimulationMolecular StructureStructure-Activity RelationshipTyrosineAnti-HIV AgentsDipeptidesTyrosinetyrosine O-sulfateAntiviral therapygp120HIV entry inhibitorProtein sulfationSulfopeptideSulfotyrosineSulfotyrosine dipeptide

Identifiers

PMID27475281

DOI10.1016/j.bioorg.2016.07.012

PMCPMC5922769

OpenAlexW2480588073

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.