Evidence map›Paper›PMID 25740212›Full record

ArticleScientific reports2015

Structure of human dipeptidyl peptidase 10 (DPPY): a modulator of neuronal Kv4 channels.

Gustavo Arruda Bezerra, Elena Dobrovetsky, Alma Seitova, Sofiya Fedosyuk, Sirano Dhe-Paganon, Karl Gruber

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

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  13. decorate: differential epigenetic correlation test.Bioinformatics (Oxford, England) · 2020
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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

6 authors at 4 institutions in 3 countries.

Gustavo Arruda BezerraInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50/3, A-8010 Graz, Austria.
Elena DobrovetskyDepartment of Physiology and Structural Genomics Consortium, University of Toronto, MaRS Centre, South Tower, 101 College St., Suite 700, Toronto, ON, M5G 1L7, Canada.
Alma SeitovaDepartment of Physiology and Structural Genomics Consortium, University of Toronto, MaRS Centre, South Tower, 101 College St., Suite 700, Toronto, ON, M5G 1L7, Canada.
Sofiya FedosyukMax F. Perutz Laboratories, Medical University of Vienna, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria.
Sirano Dhe-PaganonDepartment of Physiology and Structural Genomics Consortium, University of Toronto, MaRS Centre, South Tower, 101 College St., Suite 700, Toronto, ON, M5G 1L7, Canada.
Karl GruberInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50/3, A-8010 Graz, Austria.
University of Graz · ATUniversity of Toronto · CAMedical University of Vienna · ATStructural Genomics Consortium · CA

Funding

CIHRWellcome Trust
6 · The paper itself

Abstract

The voltage-gated potassium channel family (Kv) constitutes the most diverse class of ion channels in the nervous system. Dipeptidyl peptidase 10 (DPP10) is an inactive peptidase that modulates the electrophysiological properties, cell-surface expression and subcellular localization of voltage-gated potassium channels. As a consequence, DPP10 malfunctioning is associated with neurodegenerative conditions like Alzheimer and fronto-temporal dementia, making this protein an attractive drug target. In this work, we report the crystal structure of DPP10 and compare it to that of DPP6 and DPP4. DPP10 belongs to the S9B serine protease subfamily and contains two domains with two distinct folds: a β-propeller and a classical α/β-hydrolase fold. The catalytic serine, however, is replaced by a glycine, rendering the protein enzymatically inactive. Difference in the entrance channels to the active sites between DPP10 and DPP4 provide an additional rationale for the lack of activity. We also characterize the DPP10 dimer interface focusing on the alternative approach for designing drugs able to target protein-protein interactions.

Indexed as

Models, MolecularProtein ConformationCatalytic DomainDipeptidyl-Peptidases and Tripeptidyl-PeptidasesGlycosylationHumansNeuronsProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationShal Potassium ChannelsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDPP10 protein, humanShal Potassium Channels

Identifiers

PMID25740212
PMCPMC4350108
OpenAlexW2007416922

What OpenQuestion holds

Textmetadata
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.