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Study · In vitro (cell-free) · 1997

4 results

Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends.

Safer D, Sosnick TR, Elzinga M

Biochemistry1 May 1997Cited by 84 (Europe PMC)

PMID9153421 (opens in a new tab)DOI10.1021/bi970185v (opens in a new tab)PepBankPUB-09153421
Publisher pagePubMedAsk about this study
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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

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

  1. 01LabIn vitro (cell-free)Mechanism

    In a cell-free system, carbodiimide cross-linking joined Lys-3 of thymosin beta‑4 to Glu-167 of actin and Lys-18 to an N-terminal acidic residue of actin (Asp-1-Glu-4).

    In plain wordsIn lab tests, two specific sites on thymosin beta‑4 were cross-linked to sites on actin, showing where the two proteins touch.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableCarbodiimide cross-links between thymosin beta 4 and actin
    Study

    n: not reported in source

    Cell-free biochemical system with actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    After carbodiimide-mediated cross-linking, Lys-3 of thymosin beta 4 was cross-linked to Glu-167 of actin, and Lys-18 of thymosin beta 4 was cross-linked to one of the the N-terminal acidic residues of actin (Asp-1-Glu-4); the cross-linked actin residues lie within subdomains 3 and 1, respectively.
  2. 02LabIn vitro (cell-free)Mechanism

    In a cell-free system, transglutaminase cross-linking joined Lys-38 of thymosin beta‑4 to Gln-41 of actin, placing the C-terminal region of thymosin beta‑4 near subdomain 2 on the pointed end.

    In plain wordsIn lab tests, the end region of thymosin beta‑4 was cross-linked to a site on actin at the pointed end.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableTransglutaminase cross-link between thymosin beta 4 and actin
    Study

    n: not reported in source

    Cell-free biochemical system with actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    After transglutaminase-mediated cross-linking, Lys-38 of thymosin beta 4 was cross-linked to Gln-41 of actin, placing the C-terminal region of thymosin beta 4 in contact with subdomain 2 on the pointed end; thymosin beta 4 may sterically block actin polymerization at the pointed end as well as the b…

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

    In a cell-free system, circular dichroism showed that free thymosin beta‑4 is mostly unstructured and that up to six more residues may form an alpha-helix on binding actin.

    In plain wordsIn lab tests, free thymosin beta‑4 was mostly unstructured, and a few more residues may form a helix when it binds actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableSecondary structure of free and actin-bound thymosin beta 4 (circular dichroism)
    Study

    n: not reported in source

    Cell-free biochemical system with actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Circular dichroism data indicate that free thymosin beta 4 is predominantly unstructured, containing at most six residues of alpha-helix, and that up to six additional residues may adopt an alpha-helical conformation upon binding actin.

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

    In a cell-free system, NMR data showed that many parts of thymosin beta‑4 are not in tight contact with actin.

    In plain wordsIn lab tests, many parts of thymosin beta‑4 were not in tight contact with actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableContact of thymosin beta 4 with actin (NMR)
    Study

    n: not reported in source

    Cell-free biochemical system with actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    NMR data indicate that many parts of thymosin beta 4 are not in tight contact with actin.

    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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