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Study · In vitro (cell-free) · 2012

2 results

How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly.

Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L

The EMBO journal23 Dec 2011Cited by 49 (Europe PMC)

PMID22193718 (opens in a new tab)PMCIDPMC3280557 (opens in a new tab)DOI10.1038/emboj.2011.461 (opens in a new tab)PepBankPUB-22193718
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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

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Mechanism

    In 1:1 complexes with actin, Thymosin-β4 inhibits actin assembly by sequestering actin monomers.

    In plain wordsIn lab tests, Thymosin-β4 binds actin units one to one and stops them from building filaments.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableActin assembly by Thymosin-β4
    Study

    n: not reported in source

    actin-thymosin complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    in their 1:1 stoichiometric complexes with actin, they either inhibit assembly by sequestering actin monomers like Thymosin-β4
    1 context sentence
    Summary · context
    We combined mutational, functional or structural analysis by X-ray crystallography, SAXS (small angle X-ray scattering) and NMR on Thymosin-β4, Ciboulot, TetraThymosinβ and the long WH2 domain of WASP-interacting protein.

Studies that did not test the peptide alone1

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

    At physiological ionic strength, a single salt bridge with actin next to the LKKT/V motif induces G-actin sequestration in isolated long βT and WH2 domains.

    In plain wordsIn lab tests, one salt bridge with actin makes long beta-thymosin and WH2 domains hold actin units in place.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableG-actin sequestration by a single salt bridge
    Study

    n: not reported in source

    actin-thymosin complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    At physiological ionic strength, a single salt bridge with actin located next to their central LKKT/V motif induces G-actin sequestration in both isolated long βT and WH2 domains.
    1 context sentence
    Summary · context
    We combined mutational, functional or structural analysis by X-ray crystallography, SAXS (small angle X-ray scattering) and NMR on Thymosin-β4, Ciboulot, TetraThymosinβ and the long WH2 domain of WASP-interacting protein.

    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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