Evidence map›Paper›PMID 22954596›Full record

Trial reportJournal of proteomics2012

A label-free proteome analysis strategy for identifying quantitative changes in erythrocyte membranes induced by red cell disorders.

Esther N Pesciotta, Sira Sriswasdi, Hsin-Yao Tang, Philip J Mason, Monica Bessler, David W Speicher

Abstract readClinical Trial
In one paragraph

Trial report in Journal of proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Role of channels in the ObioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. CRISPR/Cas9 knockouts reveal genetic interaction between strain-transcendent erythrocyte determinants ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors.

Esther N PesciottaDivision of Hematology, Department of Pediatrics, Children's Hospital of Philadelphia, University of Pennsylvania, Philadelphia, PA, USA.
Sira Sriswasdi
Hsin-Yao Tang
Philip J Mason
Monica Bessler
David W Speicher

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
CHANGES IN THE RBC PROTEOME DURING HEALTH AND DISEASER01DK084188 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI ABDULMALIK, OSHEIZA Y · 2010 to 2014
$2.0M
NCI NIH HHS CA010815NCI NIH HHS P30 CA010815NHLBI NIH HHS HL38794NHLBI NIH HHS R01 HL038794NIDDK NIH HHS DK084188NIDDK NIH HHS R01 DK084188
6 · The paper itself

Abstract

Red blood cells have been extensively studied but many questions regarding membrane properties and pathophysiology remain unanswered. Proteome analysis of red cell membranes is complicated by a very wide dynamic range of protein concentrations as well as the presence of proteins that are very large, very hydrophobic, or heterogeneously glycosylated. This study investigated the removal of other blood cell types, red cell membrane extraction, differing degrees of fractionation using 1-D SDS gels, and label-free quantitative methods to determine optimized conditions for proteomic comparisons of clinical blood samples. The results showed that fractionation of red cell membranes on 1-D SDS gels was more efficient than low-ionic-strength extractions followed by 1-D gel fractionation. When gel lanes were sliced into 30 uniform slices, a good depth of analysis that included the identification of most well-characterized, low-abundance red cell membrane proteins including those present at 500 to 10,000 copies per cell was obtained. Furthermore, the size separation enabled detection of changes due to proteolysis or in vivo protein crosslinking. A combination of Rosetta Elucidator quantitation and subsequent statistical analysis enabled the robust detection of protein differences that could be used to address unresolved questions in red cell disorders. This article is part of a Special Issue entitled: Integrated omics.

Indexed as

Erythrocyte MembraneErythrocytes, AbnormalFemaleHematologic DiseasesHumansMaleMembrane ProteinsProteomeProteomicsMembrane ProteinsProteome

Identifiers

PMID22954596
PMCPMC3508302

What OpenQuestion holds

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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.