Evidence map›Paper›PMID 38065934›Full record

ArticleNature communications2023

A class of secreted mammalian peptides with potential to expand cell-cell communication.

Amanda L Wiggenhorn, Hind Z Abuzaid, Laetitia Coassolo, Veronica L Li, Julia T Tanzo, Wei Wei, Xuchao Lyu, Katrin J Svensson, Jonathan Z Long

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 18 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Amanda L WiggenhornDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0001-9413-690X
Hind Z AbuzaidDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.
Laetitia CoassoloDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.
Veronica L LiDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.
Julia T TanzoDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.
Wei WeiDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0001-8110-0705
Xuchao LyuDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0003-1967-3902
Katrin J SvenssonDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0001-5376-5128
Jonathan Z LongDepartment of Pathology, Stanford University School of Medicine, Stanford, CA, USA. jzlong@stanford.edu.ORCID 0000-0003-2631-7463
Stanford University · USStanford Medicine · US

Funding

Stanford Islet Research CoreP30DK116074 · NIDDK · STANFORD UNIVERSITY · PI Seung K Kim · 2017 to 2026
$19.5M
Mechanisms controlling fructose uptake and utilizationR01DK125260 · NIDDK · STANFORD UNIVERSITY · PI Katrin Jennifer Svensson · 2020 to 2026
$3.5M
Chemical control of energy metabolism by N-acyl amino acidsR01DK124265 · NIDDK · STANFORD UNIVERSITY · PI LONG, JONATHAN Z · 2020 to 2024
$2.0M
Molecular Pharmacology Training GrantT32GM113854 · NIGMS · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 2015 to 2019
$1.1M
NIDDK NIH HHS P30 DK116074NIDDK NIH HHS R01 DK124265NIDDK NIH HHS R01 DK125260NIGMS NIH HHS T32 GM113854
6 · The paper itself

Abstract

Peptide hormones and neuropeptides are signaling molecules that control diverse aspects of mammalian homeostasis and physiology. Here we provide evidence for the endogenous presence of a sequence diverse class of blood-borne peptides that we call "capped peptides." Capped peptides are fragments of secreted proteins and defined by the presence of two post-translational modifications - N-terminal pyroglutamylation and C-terminal amidation - which function as chemical "caps" of the intervening sequence. Capped peptides share many regulatory characteristics in common with that of other signaling peptides, including dynamic physiologic regulation. One capped peptide, CAP-TAC1, is a tachykinin neuropeptide-like molecule and a nanomolar agonist of mammalian tachykinin receptors. A second capped peptide, CAP-GDF15, is a 12-mer peptide cleaved from the prepropeptide region of full-length GDF15 that, like the canonical GDF15 hormone, also reduces food intake and body weight. Capped peptides are a potentially large class of signaling molecules with potential to broadly regulate cell-cell communication in mammalian physiology.

Indexed as

NeuropeptidesPeptide HormonesAnimalsCell CommunicationMammalsProtein Processing, Post-TranslationalTachykininsNeuropeptidesPeptide HormonesTachykinins

Identifiers

PMID38065934
PMCPMC10709327
OpenAlexW4389481036

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.