Evidence map›Paper›PMID 2307701›Full record

ArticleThe Journal of cell biology1990

Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and nonerythroid tissues.

T K Tang, Z Qin, T Leto, V T Marchesi, E J Benz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 122 citations in OpenAlex.

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  15. The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  16. A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
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  20. Structural protein 4.1 is located in mammalian centrosomes.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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

5 authors at 1 institution in 1 country.

T K TangDepartment of Internal Medicine, School of Medicine, Yale University, New Haven, Connecticut 06510.
Z Qin
T Leto
V T Marchesi
E J Benz
Yale University · US

Funding

THALASSEMIC GLOBIN GENE EXPRESSION IN HUMAN RED CELLSR01HL024385 · NHLBI · YALE UNIVERSITY · PI BENZ, EDWARD J · 1985 to 2011
$3.6M
REPETITIVE DNA SEQUENCESP01AM028376 · AM · YALE UNIVERSITY · PI FORGET, BERNARD G · 1985 to 1985
–
STRUCTURE AND FUNCTION OF ERYTHROCYTE MEMBRANE PROTEINSP50GM021714 · NIGMS · YALE UNIVERSITY · PI MARCHESI, VINCENT · 1985 to 1989
–
NHLBI NIH HHS HL24385NIADDK NIH HHS AM28376NIGMS NIH HHS GM21714
6 · The paper itself

Abstract

Immunologically cross-reactive isoforms of the cytoskeletal element protein 4.1 have been identified in many tissues in which they exhibit heterogeneity of molecular weight, abundance, and intracellular localization. To examine the basis for isoform production in erythroid and nonerythroid tissues, we have compared the structure and expression of cDNAs isolated from human erythroid and nonerythroid sources. We have encountered cDNAs representing many distinct mRNA sequences. These exhibit complete nucleotide sequence homology along most of their lengths. Differences were confined to five sequence blocks designated Motifs I-V, which were present or absent in each mRNA moiety. Motif I was expressed only in erythroid cells; it encodes 21 amino acids in a well-characterized spectrin/actin binding domain. Motif II, located near the COOH terminus of the 80-kD "erythroid" protein 4.1 molecule is present in the vast majority of transcripts from both erythroid and nonerythroid cells. Motifs IV and V alter the 5' untranslated region: simultaneous insertion of Motif IV and deletion of Motif V in the untranslated region inserts a new initiator methionine and establishes a contiguous open reading frame encoding a novel 135-kD protein 4.1 molecule. By immunochemical analysis we have identified the longer isoform in cells. Our results are most consistent with tissue-specific alternative mRNA splicing of transcripts of the protein 4.1 gene to yield numerous isoforms. These isoforms exhibit tissue specificity and alter strategic portions of the molecule. Moreover, we describe a novel high molecular weight form of protein 4.1 that arises by splicing events which allow translation at an upstream site.

Indexed as

Cytoskeletal ProteinsGenesNeuropeptidesAmino Acid SequenceBase SequenceCell LineDNA, NeoplasmErythrocyte MembraneGene LibraryHumansMembrane ProteinsMolecular Sequence DataNucleic Acid HybridizationOligonucleotide ProbesOrgan SpecificityPeptidesCytoskeletal ProteinsDNA, Neoplasmerythrocyte membrane band 4.1 proteinerythrocyte membrane protein band 4.1-like 1Membrane ProteinsNeuropeptidesOligonucleotide ProbesPeptidesRNA, Messenger

Identifiers

PMID2307701
PMCPMC2116033
OpenAlexW2136889117

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.