Evidence map›Paper›PMID 35799812›Full record

ArticleChemical science2022

Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.

Anna J Kiss-Szemán, Pál Stráner, Imre Jákli, Naoki Hosogi, Veronika Harmat, Dóra K Menyhárd, András Perczel

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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 2 countries.

Anna J Kiss-SzemánLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University Budapest - 1117 Hungary dora.k.menyhard@ttk.elte.hu perczel.andras@ttk.elte.hu.ORCID https://orcid.org/0000-0002-3039-0324
Pál StránerMTA-ELTE Protein Modelling Research Group, Eötvös Loránd Research Network Budapest - 1117 Hungary.ORCID https://orcid.org/0000-0003-2240-8501
Imre JákliLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University Budapest - 1117 Hungary dora.k.menyhard@ttk.elte.hu perczel.andras@ttk.elte.hu.ORCID https://orcid.org/0000-0002-5795-6412
Naoki HosogiEM Application Department, EM Business Unit, JEOL Ltd Tokyo 196-8556 Japan.ORCID https://orcid.org/0000-0001-6662-1940
Veronika HarmatLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University Budapest - 1117 Hungary dora.k.menyhard@ttk.elte.hu perczel.andras@ttk.elte.hu.ORCID https://orcid.org/0000-0002-1866-9904
Dóra K MenyhárdLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University Budapest - 1117 Hungary dora.k.menyhard@ttk.elte.hu perczel.andras@ttk.elte.hu.ORCID https://orcid.org/0000-0002-0095-5531
András PerczelLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University Budapest - 1117 Hungary dora.k.menyhard@ttk.elte.hu perczel.andras@ttk.elte.hu.ORCID https://orcid.org/0000-0003-1252-6416
Eötvös Loránd University · HUJEOL (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The first structure of tetrameric mammalian acylaminoacyl peptidase, an enzyme that functions as an upstream regulator of the proteasome through the removal of terminal

Identifiers

PMID35799812
PMCPMC9214879
OpenAlexW4284959607

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.