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Study · Not a test of the peptide alone · 1992

2 results

G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin beta 4.

Vancompernolle K, Goethals M, Huet C, Louvard D, Vandekerckhove J

The EMBO journal1 Dec 1992Cited by 63 (Europe PMC)

PMID1464307 (opens in a new tab)DOI10.1002/j.1460-2075.1992.tb05579.x (opens in a new tab)PepBankPUB-01464307
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

  1. 01LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    In peptide mimetic studies, the actin-binding site of thymosin beta‑4 extends over 20 residues in the NH2-terminus and holds a conserved hexapeptide motif that forms the major contact site with actin.

    In plain wordsIn lab tests with peptide fragments, the actin-binding site of thymosin beta‑4 lies at its NH2 end. A short motif makes the main contact.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableActin-binding site location and structure
    Study

    n: not reported in source

    Peptide mimetics with actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Both sites are functionally similar and extend over 20 residues and are located in the NH2-terminus of the polypeptides.
    1 context sentence
    Summary · context
    They can be dissected into two functional entities: a conserved hexapeptide motif (LKHAET or LKKTET), which forms the major contact site through electrostatic interactions with actin, and a non-conserved NH2-terminal segment preceding the motif, which exerts the inhibitory activity on actin polymeri…

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

  2. 02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    Introducing a glutamic acid at the third position of the binding motif of the peptides converted the inhibitory phenotype into an F-actin stimulatory property.

    In plain wordsIn lab tests, changing one amino acid in the binding motif turned a peptide that blocks actin assembly into one that promotes F-actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableEffect of glutamic acid substitution in the binding motif on actin polymerization
    Study

    n: not reported in source

    Peptide mimetics with actin in vitro
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The introduction of a glutamic acid at the third position in the motif, creating LKEAET or LKETET sequences, which are similar to those found in some F-actin binding proteins, converts the peptide's inhibitory phenotype into an F-actin stimulatory property.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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