Evidence map›Paper›PMID 27486686›Full record

ArticleJournal of proteome research2016

Quantitative Proteomic Analysis Reveals Similarities between Huntington's Disease (HD) and Huntington's Disease-Like 2 (HDL2) Human Brains.

Tamara Ratovitski, Raghothama Chaerkady, Kai Kammers, Jacqueline C Stewart, Anialak Zavala, Olga Pletnikova, Juan C Troncoso, Dobrila D Rudnicki, Russell L Margolis, Robert N Cole and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

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  15. Polyglutamine Repeats in Viruses.Molecular neurobiology · 2019
    Review
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4 · The record

Corrections and comments

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

11 authors at 2 institutions in 1 country.

Tamara RatovitskiDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Raghothama ChaerkadyMass Spectrometry and Proteomics Facility, Department of Biological Chemistry, Johns Hopkins University School of Medicine , 733 North Broadway Street, Suite 371 BRB, Baltimore, Maryland 21205, United States.
Kai KammersDepartment of Biostatistics, Johns Hopkins Bloomberg School of Public Health , Baltimore, Maryland 21205, United States.
Jacqueline C StewartDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Anialak ZavalaDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Olga PletnikovaDepartment of Pathology, Johns Hopkins University School of Medicine , Baltimore, Maryland 21287, United States.
Juan C TroncosoDepartment of Pathology, Johns Hopkins University School of Medicine , Baltimore, Maryland 21287, United States.
Dobrila D RudnickiDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Russell L MargolisDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Robert N ColeMass Spectrometry and Proteomics Facility, Department of Biological Chemistry, Johns Hopkins University School of Medicine , 733 North Broadway Street, Suite 371 BRB, Baltimore, Maryland 21205, United States.
Christopher A RossDivision of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine , 600 North Wolfe Street, CMSC 8-121, Baltimore, Maryland 21287, United States.
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

'T V ASSESSMENT - MEMORY DISORDERED PATIENTS'P50AG005146 · NIA · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 1985 to 2019
$37.6M
Validation of Novel Pathogenic Post-Translational Modifications of Huntingtin, and of Modifying Enzymes as Therapeutic Targets for Huntington's DiseaseR01NS086452 · NINDS · JOHNS HOPKINS UNIVERSITY · PI ROSS, CHRISTOPHER A · 2014 to 2023
$6.2M
The Huntington's Disease iPS ConsortiumRC2NS069422 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI FINKBEINER, STEVEN M, GUSELLA, JAMES F · 2009 to 2010
$3.8M
Genomic and functional analysis of transcriptome changes in Huntington's DiseaseR01NS076631 · NINDS · UNIVERSITY OF IOWA · PI DAVIDSON, BEVERLY L., ROSS, CHRISTOPHER A · 2013 to 2017
$3.2M
Immortalized Human Strital Precursors as a Cell Model of HDR21NS083365 · NINDS · JOHNS HOPKINS UNIVERSITY · PI ROSS, CHRISTOPHER A · 2013 to 2014
$443k
NIA NIH HHS P50 AG005146NINDS NIH HHS R01 NS076631NINDS NIH HHS R01 NS086452NINDS NIH HHS R21 NS083365NINDS NIH HHS RC2 NS069422
6 · The paper itself

Abstract

The pathogenesis of HD and HDL2, similar progressive neurodegenerative disorders caused by expansion mutations, remains incompletely understood. No systematic quantitative proteomics studies, assessing global changes in HD or HDL2 human brain, were reported. To address this deficit, we used a stable isotope labeling-based approach to quantify the changes in protein abundances in the cortex of 12 HD and 12 control cases and, separately, of 6 HDL2 and 6 control cases. The quality of the tissues was assessed to minimize variability due to post mortem autolysis. We applied a robust median sweep algorithm to quantify protein abundance and performed statistical inference using moderated test statistics. 1211 proteins showed statistically significant fold changes between HD and control tissues; the differences in selected proteins were verified by Western blotting. Differentially abundant proteins were enriched in cellular pathways previously implicated in HD, including Rho-mediated, actin cytoskeleton and integrin signaling, mitochondrial dysfunction, endocytosis, axonal guidance, DNA/RNA processing, and protein transport. The abundance of 717 proteins significantly differed between control and HDL2 brain. Comparative analysis of the disease-associated changes in the HD and HDL2 proteomes revealed that similar pathways were altered, suggesting the commonality of pathogenesis between the two disorders.

Indexed as

AlgorithmsBlotting, WesternBrainCase-Control StudiesChoreaCognition DisordersDementiaHeredodegenerative Disorders, Nervous SystemHumansHuntington DiseaseIsotope LabelingMetabolic Networks and PathwaysProteinsProteomicsProteinshuman brainHuntington’s diseaseiTRAQneurodegenerative disorderproteomicsTMT

Identifiers

PMID27486686
PMCPMC5555151
OpenAlexW2496120585

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.