Evidence map›Paper›PMID 36706363›Full record

ArticleJournal of the American Chemical Society2023

Genetic Perturbation Alters Functional Substates in Alkaline Phosphatase.

Morito Sakuma, Shingo Honda, Hiroshi Ueno, Kazuhito V Tabata, Kentaro Miyazaki, Nobuhiko Tokuriki, Hiroyuki Noji

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. 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
3.2field-weighted citation impact, top 7% 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, 16 citations in OpenAlex.

  1. Review
  2. Article
  3. Widespread promiscuous alkaline phosphatases underscore ancient microbial phosphite utilization.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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 3 institutions in 2 countries.

Morito SakumaDepartment of Applied Chemistry, The University of Tokyo, Tokyo113-8656, Japan.ORCID 0000-0002-8804-9831
Shingo HondaDepartment of Applied Chemistry, The University of Tokyo, Tokyo113-8656, Japan.ORCID 0000-0002-9403-6631
Hiroshi UenoDepartment of Applied Chemistry, The University of Tokyo, Tokyo113-8656, Japan.
Kazuhito V TabataDepartment of Applied Chemistry, The University of Tokyo, Tokyo113-8656, Japan.ORCID 0000-0002-0463-1374
Kentaro MiyazakiInternational Center for Biotechnology, Osaka University, Suita565-0871, Japan.
Nobuhiko TokurikiMichael Smith Laboratories, The University of British Columbia, British ColumbiaV6T1Z4, Canada.ORCID 0000-0002-8235-1829
Hiroyuki NojiDepartment of Applied Chemistry, The University of Tokyo, Tokyo113-8656, Japan.ORCID 0000-0002-8842-6836
The University of Tokyo · JPUniversity of British Columbia · CAOsaka International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes inherently exhibit molecule-to-molecule heterogeneity in their conformational and functional states, which is considered to be a key to the evolution of new functions. Single-molecule enzyme assays enable us to directly observe such multiple functional states or functional substates. Here, we quantitatively analyzed functional substates in the wild-type and 69 single-point mutants of

Indexed as

Alkaline PhosphataseEscherichia coliEscherichia coli ProteinsProtein ConformationMutationAlkaline PhosphataseEscherichia coli Proteins

Identifiers

PMID36706363
PMCPMC9912328
OpenAlexW4318262818

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.