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Study · Not a test of the peptide alone · 2004

3 results

Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.

Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC

The EMBO journal26 Aug 2004Cited by 96 (Europe PMC)

PMID15329672 (opens in a new tab)PMCIDPMC517612 (opens in a new tab)DOI10.1038/sj.emboj.7600372 (opens in a new tab)PepBankPUB-15329672
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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 study3

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

Studies that did not test the peptide alone3

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 lab tests, a hybrid of gelsolin domain 1 and the C-terminal half of thymosin beta4 sequestered actin monomers, severed actin filaments and acted as a leaky barbed end cap.

    In plain wordsIn lab tests, a hybrid protein built from part of thymosin beta4 bound actin monomers and cut actin filaments.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableActin monomer sequestration, filament severing and capping by G1-Tbeta4 hybrid
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap.
    1 context sentence
    Summary · context
    We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4).

    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

    In lab tests, the 2 A structure of the G1-Tbeta4:actin complex showed that the thymosin beta4 part sequesters actin by capping both ends of the actin monomer.

    In plain wordsIn lab tests, the structure of a thymosin beta4 hybrid bound to actin showed it caps both ends of the actin monomer.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableStructure of the G1-Tbeta4:actin complex
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    Resolution
    2 A
    G1-Tbeta4:actin complex

    Source sentences

    Summary
    Here, we present the structure of the G1-Tbeta4:actin complex at 2 A resolution.
    2 context sentences
    Summary · context
    The structure reveals that Tbeta4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tbeta4 and profilin is mediated by a minor overlap in binding sites.
    Summary · context
    We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4).

    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).

  3. 03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    In lab tests, the structure indicated that exchange of actin between thymosin beta4 and profilin is mediated by a minor overlap in binding sites.

    In plain wordsIn lab tests, the structure suggested that actin passes between thymosin beta4 and profilin through a small overlap in binding sites.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableActin exchange between Tbeta4 and profilin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    and that exchange of actin between Tbeta4 and profilin is mediated by a minor overlap in binding sites.
    1 context sentence
    Summary · context
    We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4).

    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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