Evidence map›Paper›PMID 2391360›Full record

ArticleThe Journal of cell biology1990

Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins.

M V de Arruda, S Watson, C S Lin, J Leavitt, P Matsudaira

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 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.4field-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

77 citing papers in PubMed, 210 citations in OpenAlex.

  1. Review
  2. Identification of a novelExperimental and therapeutic medicine · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Getting cells into shape by calcium-dependent actin cross-linking proteins.Frontiers in cell and developmental biology · 2023
    Review
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  9. Article
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  20. Capping protein regulators fine-tune actin assembly dynamics.Nature reviews. Molecular cell biology · 2014
    Review

17 more citing papers are in PubMed but not listed here.

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.

M V de ArrudaWhitehead Institute for Biomedical Research, Cambridge, Massachusetts.
S Watson
C S Lin
J Leavitt
P Matsudaira
Whitehead Institute for Biomedical Research · US

Funding

THE PATHOBIOLOGY OF COLORECTAL CANCERP01CA044704 · NCI · NEW ENGLAND DEACONESS HOSPITAL · PI KOLODNER, RICHARD D · 1987 to 1998
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ROLES OF MICROFILAMENT PROTEINS IN NEOPLASIA/METASTASISR01CA034763 · NCI · PALO ALTO MEDICAL FOUNDATION RES INST · PI LEAVITT, JOHN C · 1986 to 1993
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STRUCTURE AND FUNCTION OF THE INTESTINE BRUSH BORDERR01DK035306 · NIDDK · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI MATSUDAIRA, PAUL T. · 1986 to 1992
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NCI NIH HHS CA-34763NCI NIH HHS CA-44704NIDDK NIH HHS DK-35306
6 · The paper itself

Abstract

Fimbrin is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. The complete protein sequence (630 residues) of chicken intestine fimbrin has been determined from two full-length cDNA clones. The sequence encodes a small amino-terminal domain (115 residues) that is homologous with two calcium-binding sites of calmodulin and a large carboxy-terminal domain (500 residues) consisting of a fourfold-repeated 125-residue sequence. This repeat is homologous with the actin-binding domain of alpha-actinin and the amino-terminal domains of dystrophin, actin-gelation protein, and beta-spectrin. The presence of this duplicated domain in fimbrin links actin bundling proteins and gelation proteins into a common family of actin cross-linking proteins. Fimbrin is also homologous in sequence with human L-plastin and T-plastin. L-plastin is found in only normal or transformed leukocytes where it becomes phosphorylated in response to IL 1 or phorbol myristate acetate. T-plastin is found in cells of solid tissues where it does not become phosphorylated. Neoplastic cells derived from solid tissues express both isoforms. The differences in expression, sequence, and phosphorylation suggest possible functional differences between fimbrin isoforms.

Indexed as

ActinsAmino Acid SequenceAnimalsBase SequenceCalciumCalcium-Binding ProteinsCalmodulinCarrier ProteinsChickensCross ReactionsGene Expression RegulationMembrane GlycoproteinsMicrofilament ProteinsMolecular Sequence DataPhosphoproteinsPhosphorylationActinsCalciumCalcium-Binding ProteinsCalmodulinCarrier ProteinsF-actin-binding proteinsMembrane GlycoproteinsMicrofilament ProteinsPhosphoproteinsplastinvillin

Identifiers

PMID2391360
PMCPMC2116281
OpenAlexW2104282099

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.