Evidence map›Paper›PMID 24060756›Full record

ArticleNature communications2013

Analysing the substrate multispecificity of a proton-coupled oligopeptide transporter using a dipeptide library.

Keisuke Ito, Aya Hikida, Shun Kawai, Vu Thi Tuyet Lan, Takayasu Motoyama, Sayuri Kitagawa, Yuko Yoshikawa, Ryuji Kato, Yasuaki Kawarasaki

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  7. Orphan lysosomal solute carrier MFSD1 facilitates highly selective dipeptide transport.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  19. Article
  20. Proton movement and coupling in the POT family of peptide transporters.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

9 authors at 2 institutions in 1 country.

Keisuke Ito1] Department of Food and Nutritional Sciences, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, Yada 52-1, Suruga-ku, Shizuoka 422-8526, Japan [2] School of Food and Nutritional Sciences, University of Shizuoka, Yada 52-1, Suruga-ku, Shizuoka 422-8526, Japan [3].
Aya Hikida
Shun Kawai
Vu Thi Tuyet Lan
Takayasu Motoyama
Sayuri Kitagawa
Yuko Yoshikawa
Ryuji Kato
Yasuaki Kawarasaki
University of Shizuoka · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide uptake systems that involve members of the proton-coupled oligopeptide transporter (POT) family are conserved across all organisms. POT proteins have characteristic substrate multispecificity, with which one transporter can recognize as many as 8,400 types of di/tripeptides and certain peptide-like drugs. Here we characterize the substrate multispecificity of Ptr2p, a major peptide transporter of Saccharomyces cerevisiae, using a dipeptide library. The affinities (Ki) of di/tripeptides toward Ptr2p show a wide distribution range from 48 mM to 0.020 mM. This substrate multispecificity indicates that POT family members have an important role in the preferential uptake of vital amino acids. In addition, we successfully establish high performance ligand affinity prediction models (97% accuracy) using our comprehensive dipeptide screening data in conjunction with simple property indices for describing ligand molecules. Our results provide an important clue to the development of highly absorbable peptides and their derivatives including peptide-like drugs.

Indexed as

Gene Expression Regulation, FungalProtonsBiological TransportDipeptidesKineticsMembrane Transport ProteinsPeptide LibraryProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityDipeptidesMembrane Transport ProteinsPeptide LibraryProtonsPTR2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID24060756
PMCPMC3791473
OpenAlexW2049485506

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.