Evidence map›Paper›PMID 26033855›Full record

ArticleProteomics. Clinical applications2016

Mass spectrometric phosphoproteome analysis of HIV-infected brain reveals novel phosphorylation sites and differential phosphorylation patterns.

Lerna Uzasci, Sungyoung Auh, Robert J Cotter, Avindra Nath

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Article in Proteomics. Clinical applications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Lerna UzasciSection of Infections of the Nervous System, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
Sungyoung AuhClinical Neurosciences Program, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
Robert J CotterThe Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Avindra NathSection of Infections of the Nervous System, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
National Institutes of Health · USJohns Hopkins Medicine · US

Funding

Neuropathogenesis of Retroviral InfectionsZIANS003130 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI NATH, AVINDRA · 2011 to 2025
$73.7M
Role of HIV Tat protein in pathogenesis of HIV dementiaR01NS039253 · NINDS · UNIVERSITY OF KENTUCKY · PI SCHNAAR, RONALD L · 1999 to 2014
$4.5M
Intramural NIH HHSNINDS NIH HHS R01 NS039253NINDS NIH HHS R01NS039253
6 · The paper itself

Abstract

purposeTo map the phosphoproteome and identify changes in the phosphorylation patterns in the HIV-infected and uninfected brain. EXPERIMENTAL

designParietal cortex from individuals with and without HIV infection were lysed and trypsinized. The peptides were labeled with iTRAQ reagents, combined, phospho-enriched by titanium dioxide chromatography, and analyzed by LC-MS/MS with high resolution.

resultsOur phosphoproteomic workflow resulted in the identification of 112 phosphorylated proteins and 17 novel phosphorylation sites in all the samples that were analyzed. The phosphopeptide sequences were searched for kinase substrate motifs, which revealed potential kinases involved in important signaling pathways. The site-specific phosphopeptide quantification showed that peptides from neurofilament medium polypeptide, myelin basic protein, and 2'-3'-cyclic nucleotide-3' phosphodiesterase have relatively higher phosphorylation levels during HIV infection. CONCLUSIONS AND CLINICAL RELEVANCE: This study has enriched the global phosphoproteome knowledge of the human brain by detecting novel phosphorylation sites on neuronal proteins and identifying differentially phosphorylated brain proteins during HIV infection. Kinases that lead to unusual phosphorylations could be therapeutic targets for the treatment of HIV-associated neurocognitive disorders.

Indexed as

ProteomicsBrainEncephalitis, ViralHIV InfectionsHumansMass SpectrometryPhosphoproteinsPhosphorylationPhosphoproteinsDrug targetHIV-associated neurocognitive disordersPhosphorylationProtein kinase AProteomics

Identifiers

PMID26033855
PMCPMC5101124
OpenAlexW1549821174

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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.