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Study · In vitro (cell-free) · 2000

3 results

C-terminal variations in beta-thymosin family members specify functional differences in actin-binding properties.

Eadie JS, Kim SW, Allen PG, Hutchinson LM, Kantor JD, Zetter BR

Journal of cellular biochemistry1 Mar 2000Cited by 35 (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

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

  1. 01LabIn vitro (cell-free)Activity measurement

    In actin-binding assays, thymosin beta4 bound actin with lower affinity than thymosin beta15, which bound 2.4-fold more tightly.

    In plain wordsIn lab tests, thymosin beta4 held actin less tightly than thymosin beta15 did.

    Outcome
    DecreaseActin-binding affinity of thymosin beta4 versus thymosin beta15
    Study

    n: not reported in source

    Comparator
    Thymosin beta15
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Affinity ratio, thymosin beta15 vs thymosin beta4
    2.4 fold
    actin binding

    Source sentences

    Summary
    thymosin beta15 binds actin with a 2.4-fold higher affinity than does thymosin beta4.

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

    In actin-binding assays, a thymosin beta4 hybrid with the C-terminal amino acids of thymosin beta15 showed increased actin binding.

    In plain wordsIn lab tests, a thymosin beta4 hybrid with the end of thymosin beta15 bound actin more.

    Outcome
    IncreaseActin binding of thymosin beta4 with thymosin beta15 C-terminal residues
    Study

    n: not reported in source

    Comparator
    Thymosin beta4
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Similarly, replacement of the thymosin beta4 C-terminal amino acids with those of thymosin beta15 led to increased actin binding.

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

    In actin-binding assays, a thymosin beta15 hybrid with the 10 C-terminal amino acids of thymosin beta4 had lower actin-binding affinity than thymosin beta15.

    In plain wordsIn lab tests, a thymosin beta15 hybrid with the end of thymosin beta4 bound actin less than thymosin beta15 did.

    Outcome
    DecreaseActin-binding affinity of thymosin beta15 with thymosin beta4 C-terminal residues
    Study

    n: not reported in source

    Comparator
    Thymosin beta15
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Replacement of the 10 C-terminal amino acids of thymosin beta15 with those of thymosin beta4 did, however, reduce the actin-binding affinity of the hybrid relative to thymosin beta15.

    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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