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Study · Not a test of the peptide alone · 2006

2 results

Solution structure of Ser14Gly-humanin, a potent rescue factor against neuronal cell death in Alzheimer's disease.

Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M

Biochemical and biophysical research communications23 Aug 2006Cited by 18 (Europe PMC)

PMID16945331 (opens in a new tab)DOI10.1016/j.bbrc.2006.08.087 (opens in a new tab)PepBankPUB-16945331
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 study2

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

Studies that did not test the peptide alone2

In this study, Humanin 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 Humanin.

  1. 01LabNot a test of Humanin aloneIn vitro (cell-free)Other

    By NMR in aqueous solution, the S14G analog of humanin is a flexible peptide with turn-like structures distributed over residues Pro3 to Glu15.

    In plain wordsIn lab tests, the S14G humanin analog was flexible in water, with turn-like shapes over much of its sequence.

    Peptide
    Humanin
    Outcome
    Not applicableSolution structure of S14G-humanin in water
    Study

    n: not reported in source

    NMR in aqueous solution and 30% TFE
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In aqueous solution the NMR data show that S14G-HN is a flexible peptide with turn-like structures in its conformational ensemble distributed over an extensive part of its sequence from Pro3 to Glu15.
    1 context sentence
    Summary · context
    The NMR solution study of Ser14Gly-humanin (S14G-HN), a 1000-fold more potent derivative of humanin (HN), is reported.

    In this study, Humanin 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 Humanin.

  2. 02LabNot a test of Humanin aloneIn vitro (cell-free)Other

    By NMR in 30% TFE, the S14G analog of humanin formed an alpha-helical structure spanning residues Phe6 to Thr13.

    In plain wordsIn lab tests, the S14G humanin analog formed a helix in a lipid-like solvent.

    Peptide
    Humanin
    Outcome
    Not applicableSolution structure of S14G-humanin in 30% TFE
    Study

    n: not reported in source

    NMR in aqueous solution and 30% TFE
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In the more lipophilic environment of 30% TFE, an alpha-helical structure spanning residues Phe6 to Thr13 is identified.

    In this study, Humanin 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 Humanin.

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, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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