Evidence map›Paper›PMID 1713685›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif.

P Ruff, D W Speicher, A Husain-Chishti

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 148 citations in OpenAlex.

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  9. Erythrocyte scaffolding protein p55/MPP1 functions as an essential regulator of neutrophil polarity.Proceedings of the National Academy of Sciences of the United States of America · 2009
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  18. ELL2, a new member of an ELL family of RNA polymerase II elongation factors.Proceedings of the National Academy of Sciences of the United States of America · 1997
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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

3 authors at 1 institution in 1 country.

P RuffDepartment of Biomedical Research, St. Elizabeth's Hospital, Boston, MA.
D W Speicher
A Husain-Chishti
St. Elizabeth's Hospital · PK

Funding

Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
DOMAIN STRUCTURE OF HUMAN SMOOTH MUSCLE FILAMINR01AR039158 · NIAMS · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1989 to 1993
–
MOLECULAR STUDIES OF RED BLOOD CELL SPECTRINR01HL017411 · NHLBI · HARVARD UNIVERSITY · PI BRANTON, DANIEL · 1985 to 1997
–
NHLBI NIH HHS HL17411NHLBI NIH HHS HL38794NIAMS NIH HHS AR39158
6 · The paper itself

Abstract

The complete amino acid sequence of a 55-kDa erythrocyte membrane protein was deduced from cDNA clones isolated from a human reticulocyte library. This protein, p55, is copurified during the isolation of dematin, an actin-bundling protein of the erythrocyte membrane cytoskeleton. Fractions enriched in p55 also contain protein kinase activity that completely abolishes the actin-bundling property of purified dematin in vitro. The predicted amino acid sequence of p55 does not contain any consensus sequence corresponding to the catalytic domains of protein kinases but does contain a conserved sequence found in the noncatalytic domains of oncogene-encoded tyrosine kinases. This conserved src homology 3 (SH-3) motif appears to suppress the tyrosine kinase activity of various oncoproteins and has also been found in several plasma membrane associated proteins involved in signal transduction. Northern blot analysis indicated that p55 mRNA was constitutively expressed during erythropoiesis and underwent 2-fold amplification after induction of K562 erythroleukemia cells toward the erythropoietic lineage. The abundant expression of p55 mRNA, along with protein 4.1 mRNA, was evident in terminally differentiated human reticulocytes. Although p55 has many features consistent with known peripheral membrane proteins, its tight association with the plasma membrane is reminiscent of an integral membrane protein. This fact may be partly explained by the observation that p55 is the most extensively palmitoylated protein of the erythrocyte membrane.

Indexed as

Genes, srcAmino Acid SequenceBase SequenceCloning, MolecularErythrocyte MembraneGene LibraryHumansLipoproteinsMembrane ProteinsMolecular Sequence DataOncogene Protein pp60(v-src)Palmitic AcidsProto-Oncogene Proteins pp60(c-src)Restriction MappingReticulocytesRNALipoproteinsMembrane ProteinsOncogene Protein pp60(v-src)Palmitic AcidsProto-Oncogene Proteins pp60(c-src)RNA

Identifiers

PMID1713685
PMCPMC52133
OpenAlexW1972414284

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.