Evidence map›Paper›PMID 8617195›Full record

ArticleThe EMBO journal1996

The actin binding site of thymosin beta 4 mapped by mutational analysis.

M Van Troys, D Dewitte, M Goethals, M F Carlier, J Vandekerckhove, C Ampe

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Review
  3. PIPCommunications biology · 2022
    Article
  4. Article
  5. Cloning, Expression and Effects ofInternational journal of molecular sciences · 2019
    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

6 authors.

M Van TroysDepartment of Biochemistry, University of Ghent, Belgium.
D Dewitte
M Goethals
M F Carlier
J Vandekerckhove
C Ampe

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants. The N-terminal part (residues 1-16) and a hexapeptide motif (residues 17-22) form separate structural entities. In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments. Quantitative data on the activity of the variants and circular dichroism experiments allow to present a model in which the N-terminal part needs to adopt an alpha-helix for actin binding and interacts through a patch of hydrophobic residues (6M-I-F12) on one side of this helix. Also, electrostatic contacts between actin and lysine residues 18, in the motif, and 14, in the N-terminal alpha-helix, appear important for binding. The residues critical for contacting actin are conserved throughout the beta-thymosin family and in addition to this we identify a similar pattern in the C-terminal headpiece of villin and dematin.

Indexed as

PhosphoproteinsProtein Structure, SecondaryActinsAmino Acid SequenceAnimalsBinding, CompetitiveBinding SitesBlood ProteinsCalcium-Binding ProteinsCarrier ProteinsChickensCircular DichroismConserved SequenceCross-Linking ReagentsGenetic VariationHumansActinsBlood ProteinsCalcium-Binding ProteinsCarrier ProteinsCross-Linking ReagentsDMTN protein, humanMembrane ProteinsMicrofilament ProteinsPeptide FragmentsPhosphoproteinsRecombinant ProteinsThymosinThymosin beta(4)villin

Identifiers

PMID8617195
PMCPMC449934

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.