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Study · Not a test of the peptide alone · 2007

3 results

Models of the actin-bound forms of the beta-thymosins.

Xue B, Aguda AH, Robinson RC

Annals of the New York Academy of Sciences27 Apr 2007Cited by 8 (Europe PMC)

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. 01Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoMechanism

    Models of beta-thymosin:actin complexes show that the beta-thymosins interact with actin throughout their length and that all conserved residues are in this interface.

    In plain wordsIn computer models, beta-thymosins, the family that includes thymosin beta‑4, touched actin along their whole length.

    Outcome
    Not applicableBeta-thymosin interaction with actin along the sequence
    Study

    n: not reported in source

    computer models of beta-thymosin:actin complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The models reveal that the beta-thymosins interact with actin throughout their length and that all the conserved residues are functional in this interface.

    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. 02Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoMechanism

    The beta-thymosin:actin models are consistent with the actin monomer sequestering and actin filament binding properties of beta-thymosins.

    In plain wordsIn computer models, the predicted beta-thymosin binding fits what is known about how these peptides hold and bind actin.

    Outcome
    Not applicableConsistency with actin monomer sequestering and filament binding
    Study

    n: not reported in source

    computer models of beta-thymosin:actin complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In particular, the models are consistent with the actin monomer sequestering and actin filament binding properties of beta-thymosins.

    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. 03Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoMechanism

    The models predict competition of thymosin-beta4 with DNase I or profilin in binding actin, while allowing ternary complexes at higher concentrations.

    In plain wordsIn computer models, thymosin beta‑4 was predicted to compete with DNase I or profilin for actin, while all three could bind together at higher concentrations.

    Outcome
    Not applicablePredicted competition of thymosin-beta4 with DNase I or profilin for actin
    Study

    n: not reported in source

    computer models of beta-thymosin:actin complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The models also correctly predict competition between thymosin-beta4 with DNase I or profilin in binding actin while allowing ternary complexes at higher concentrations.

    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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