Evidence map›Paper›PMID 9245787›Full record

ArticleThe Journal of cell biology1997

Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein.

D J Roof, A Hayes, M Adamian, A H Chishti, T Li

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

57 citing papers in PubMed, 127 citations in OpenAlex.

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  7. The Role of Liquid-Liquid Phase Separation in Actin Polymerization.International journal of molecular sciences · 2023
    Review
  8. Review
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  11. Self-construction of actin networks through phase separation-induced abLIM1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 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

5 authors at 2 institutions in 1 country.

D J RoofBerman-Gund Laboratory for the Study of Retinal Degenerations, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts 02114, USA.
A Hayes
M Adamian
A H Chishti
T Li
Tufts University · USHarvard University · US

Funding

FUNCTIONAL STUDIES OF RED BLOOD CELL DEMATINR01HL051445 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHISHTI, ATHAR H. · 1994 to 2010
$1.9M
Functional Studies of Erythrocyte DematinR56HL051445 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHISHTI, ATHAR H. · 2008 to 2008
$393k
INTRACELLULAR ASSEMBLY OF PHOTORECEPTOR PROTEINSR01EY011692 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI ROOF, DOROTHY J · 1996 to 1999
–
NEI NIH HHS EY11692NHLBI NIH HHS HL51445NHLBI NIH HHS R01 HL051445NHLBI NIH HHS R56 HL051445
6 · The paper itself

Abstract

Molecules that couple the actin-based cytoskeleton to intracellular signaling pathways are central to the processes of cellular morphogenesis and differentiation. We have characterized a novel protein, the actin-binding LIM (abLIM) protein, which could mediate such interactions between actin filaments and cytoplasmic targets. abLIM protein consists of a COOH-terminal cytoskeletal domain that is fused to an NH2-terminal domain consisting of four double zinc finger motifs. The cytoskeletal domain is approximately 50% identical to erythrocyte dematin, an actin-bundling protein of the red cell membrane skeleton, while the zinc finger domains conform to the LIM motif consensus sequence. In vitro expression studies demonstrate that abLIM protein can bind to F-actin through the dematin-like domain. Transcripts corresponding to three distinct isoforms have a widespread tissue distribution. However, a polypeptide corresponding to the full-length isoform is found exclusively in the retina and is enriched in biochemical extracts of retinal rod inner segments. abLIM protein also undergoes extensive phosphorylation in light-adapted retinas in vivo, and its developmental expression in the retina coincides with the elaboration of photoreceptor inner and outer segments. Based on the composite primary structure of abLIM protein, actin-binding capacity, potential regulation via phosphorylation, and isoform expression pattern, we speculate that abLIM may play a general role in bridging the actin-based cytoskeleton with an array of potential LIM protein-binding partners. The developmental time course of abLIM expression in the retina suggests that the retina-specific isoform may have a specialized role in the development or elaboration of photoreceptor inner and outer segments.

Indexed as

PhosphoproteinsZinc FingersActinsAmino Acid SequenceAnimalsBase SequenceBlood ProteinsBrain ChemistryCloning, MolecularConserved SequenceCytoskeletal ProteinsDNA, ComplementaryHumansLIM Domain ProteinsMiceMicrofilament ProteinsABLIM1 protein, humanActinsBlood ProteinsCytoskeletal ProteinsDMTN protein, humanDmtn protein, mouseDNA, ComplementaryLIM Domain ProteinsMicrofilament ProteinsPhosphoproteinsRecombinant Fusion Proteins

Identifiers

PMID9245787
PMCPMC2141644
OpenAlexW2059603567

What OpenQuestion holds

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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.