Evidence map›Paper›PMID 36680395›Full record

ArticleFEBS open bio2023

Destabilization of vitelline membrane outer layer protein 1 homolog (VMO1) by C-mannosylation.

Satoshi Yoshimoto, Takehiro Suzuki, Naoki Otani, Daisuke Takahashi, Kazunobu Toshima, Naoshi Dohmae, Siro Simizu

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Satoshi YoshimotoDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Naoki OtaniDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Daisuke TakahashiDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Kazunobu ToshimaDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Siro SimizuDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.ORCID 0000-0003-2949-2427
Keio University · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C-mannosylation is a rare type of protein glycosylation whereby a single mannose is added to the first tryptophan in the consensus sequence Trp-Xaa-Xaa-Trp/Cys (in which Xaa represents any amino acid). Its consensus sequence is mainly found in proteins containing a thrombospondin type-1 repeat (TSR1) domain and in type I cytokine receptors. In these proteins, C-mannosylation affects protein secretion, intracellular localization, and protein stability; however, the role of C-mannosylation in proteins that are not type I cytokine receptors and/or do not contain a TSR1 domain is less well explored. In this study, we focused on human vitelline membrane outer layer protein 1 homolog (VMO1). VMO1, which possesses two putative C-mannosylation sites, is a 21-kDa secreted protein that does not contain a TSR1 domain and is not a type I cytokine receptor. Mass spectrometry analyses revealed that VMO1 is C-mannosylated at Trp

Indexed as

MannoseVitelline MembraneGlycosylationHumansProtein TransportReceptors, CytokineMannoseReceptors, CytokineC-mannosylationmass spectrometryprotein stabilitysecretionVMO1

Identifiers

PMID36680395
PMCPMC9989928
OpenAlexW4317679821

What OpenQuestion holds

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Registered trials

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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.