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Study · Not a test of the peptide alone · 1994

4 results

Polymerization of actin from the thymosin beta 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1.

Reichert A, Heintz D, Voelter W, Mihelic M, Faulstich H

FEBS letters1 Jun 1994Cited by 9 (Europe PMC)

PMID8034012 (opens in a new tab)DOI10.1016/0014-5793(94)00551-6 (opens in a new tab)PepBankPUB-08034012
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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 study4

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

Studies that did not test the peptide alone4

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 a cell-free system, adding actin trimers triggered rapid filament formation from the actin-thymosin beta‑4 complex.

    In plain wordsIn lab tests, adding actin trimers made filaments form quickly from the thymosin beta‑4-actin complex.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseFilament formation from actin-Tb4 complex with actin trimers
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Rapid formation of filaments from this complex was observed, however, when actin trimers were added.
    1 context sentence
    Title · context
    Polymerization of actin from the thymosin beta 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1.

    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 a cell-free system, adding one equivalent of phalloidin initiated polymerization of actin from the actin-thymosin beta‑4 complex.

    In plain wordsIn lab tests, phalloidin started actin filament formation from the thymosin beta‑4-actin complex.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseFilament formation from actin-Tb4 complex with phalloidin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Polymerization can likewise be initiated by the addition of one equivalent of phalloidin
    1 context sentence
    Title · context
    Polymerization of actin from the thymosin beta 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1.

    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 a cell-free system, cytochalasin B initiated polymerization from the actin-thymosin beta‑4 complex less effectively than phalloidin.

    In plain wordsIn lab tests, cytochalasin B started actin filament formation from the thymosin beta‑4-actin complex, but less well than phalloidin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseFilament formation from actin-Tb4 complex with cytochalasin B
    Study

    n: not reported in source

    Comparator
    Phalloidin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Polymerization can likewise be initiated by the addition of one equivalent of phalloidin or, less effectively, cytochalasin B.
    1 context sentence
    Title · context
    Polymerization of actin from the thymosin beta 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1.

    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).

  4. 04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    In a cell-free system, small amounts of myosin S1 triggered rapid polymerization of the actin-thymosin beta‑4 complex.

    In plain wordsIn lab tests, small amounts of myosin S1 made actin filaments form quickly from the thymosin beta‑4-actin complex.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseFilament formation from actin-Tb4 complex with myosin S1
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Remarkably, rapid polymerization was also observed if small amounts of myosin S1 were added, suggesting that also myosin, a protein functionally connected with polymeric actin, can serve as a nucleation center.
    1 context sentence
    Title · context
    Polymerization of actin from the thymosin beta 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1.

    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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