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Study · Not a test of the peptide alone · 2001

4 results

Identification of an extracellular segment of the oxytocin receptor providing agonist-specific binding epitopes.

Hawtin SR, Howard HC, Wheatley M

The Biochemical journal1 Mar 2001Cited by 13 (Europe PMC)

PMID11171127 (opens in a new tab)PMCIDPMC1221676 (opens in a new tab)DOI10.1042/0264-6021:3540465 (opens in a new tab)PepBankPUB-11171127
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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, Oxytocin 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 Oxytocin.

  1. 01LabNot a test of Oxytocin aloneIn vitro (cells)Mechanism

    A 12-residue segment in the distal N-terminus of the human oxytocin receptor provides epitopes required for agonist binding.

    In plain wordsIn cells, one short part of the human oxytocin receptor is needed for oxytocin-type agonists to bind.

    Peptide
    Oxytocin
    Outcome
    Not applicableAgonist binding to the oxytocin receptor N-terminus
    Study

    humann: not reported in source

    Truncated and chimaeric oxytocin receptor constructs
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Using truncated and chimaeric receptor constructs, we establish that a small 12-residue segment in the distal portion of the N-terminus of the human OTR provides important epitopes which are required for agonist binding.

    In this study, Oxytocin 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 Oxytocin.

  2. 02LabNot a test of Oxytocin aloneIn vitro (cells)Mechanism

    The distal N-terminal segment of the oxytocin receptor has a role in agonist-induced receptor signalling.

    In plain wordsIn cells, the same part of the oxytocin receptor helps the signal that follows agonist binding.

    Peptide
    Oxytocin
    Outcome
    Not applicableReceptor signalling after agonist binding
    Study

    humann: not reported in source

    Truncated and chimaeric oxytocin receptor constructs
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    It does, however, have a role in agonist-induced OTR signalling.

    In this study, Oxytocin 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 Oxytocin.

  3. 03LabNot a test of Oxytocin aloneIn vitro (cells)Mechanism

    Substituting the V1a receptor N-terminus into a truncated oxytocin receptor fully restored agonist binding and intracellular signalling.

    In plain wordsIn cells, swapping in the vasopressin receptor end piece fully restored agonist binding and signalling in a damaged oxytocin receptor.

    Peptide
    Oxytocin
    Outcome
    IncreaseRestoration of agonist binding by V1a receptor N-terminus
    Study

    humann: not reported in source

    Truncated and chimaeric oxytocin receptor constructs
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    We show that the V(1a)R N-terminus present in V(1a)R(N)-OTR fully restored both agonist binding and intracellular signalling to a dysfunctional truncated OTR construct.

    In this study, Oxytocin 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 Oxytocin.

  4. 04LabNot a test of Oxytocin aloneIn vitro (cells)Mechanism

    The N-terminal segment does not contribute to receptor-selective agonism between the oxytocin receptor and the V1a receptor.

    In plain wordsIn cells, this receptor end piece does not decide whether an agonist acts on the oxytocin or the vasopressin receptor.

    Peptide
    Oxytocin
    Outcome
    No significant changeReceptor-selective agonism between OTR and V1aR
    Study

    humann: not reported in source

    Truncated and chimaeric oxytocin receptor constructs
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The N-terminal segment does not, however, contribute to receptor-selective agonism between the OTR and the V(1a)R.

    In this study, Oxytocin 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 Oxytocin.

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

    11 Oct 2026, 20:03 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 02:51 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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