Evidence map›Paper›PMID 27856737›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3.

Estela Puchulu-Campanella, Francesco M Turrini, Yen-Hsing Li, Philip S Low

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Trial
  2. Review
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  5. Review
  6. Rapid degradation of protein tyrosine phosphatase 1B in sickle cells: Possible contribution to sickle cell membrane weakening.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
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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

4 authors at 2 institutions in 2 countries.

Estela Puchulu-CampanellaPurdue Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907.ORCID 0000-0002-3951-3925
Francesco M TurriniDepartment of Oncology, University of Turin, 10126 Turin, Italy.
Yen-Hsing LiPurdue Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907.
Philip S LowPurdue Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907; plow@purdue.edu.
Purdue University West Lafayette · USUniversity of Turin · IT

Funding

Studies of Erythrocyte Membrane StructureR01GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1985 to 2020
$5.4M
ERYTHROCYTE MEMBRANE STRUCTURER37GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1999 to 2008
$3.5M
NIGMS NIH HHS R01 GM024417NIGMS NIH HHS R37 GM024417
6 · The paper itself

Abstract

Src homology 2 (SH2) domains are composed of weakly conserved sequences of ∼100 aa that bind phosphotyrosines in signaling proteins and thereby mediate intra- and intermolecular protein-protein interactions. In exploring the mechanism whereby tyrosine phosphorylation of the erythrocyte anion transporter, band 3, triggers membrane destabilization, vesiculation, and fragmentation, we discovered a SH2 signature motif positioned between membrane-spanning helices 4 and 5. Evidence that this exposed cytoplasmic sequence contributes to a functional SH2-like domain is provided by observations that: (i) it contains the most conserved sequence of SH2 domains, GSFLVR; (ii) it binds the tyrosine phosphorylated cytoplasmic domain of band 3 (cdb3-PO

Indexed as

Anion Exchange Protein 1, ErythrocyteBinding SitesConserved SequenceCytoplasmCytoskeletonErythrocyte MembraneErythrocytesModels, MolecularPhosphorylationProtein BindingProtein Interaction Domains and MotifsProtein Structure, Secondarysrc Homology DomainsAnion Exchange Protein 1, Erythrocyteanion exchanger 1erythrocyte glycolysisregulation of transport proteinsSH2 domain motiftyrosine phosphorylation

Identifiers

PMID27856737
PMCPMC5137735
OpenAlexW2550981335

What OpenQuestion holds

Textmetadata
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.