Evidence map›Paper›PMID 36795942›Full record

ArticleBiochemistry2023

Non-active Site Residue in Loop L4 Alters Substrate Capture and Product Release in d-Arginine Dehydrogenase.

Daniel Ouedraogo, Michael Souffrant, Xin-Qiu Yao, Donald Hamelberg, Giovanni Gadda

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Targeted Mutation of a Non-catalytic Gating Residue Increases the Rate ofJournal of agricultural and food chemistry · 2023
    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

5 authors at 1 institution in 1 country.

Daniel OuedraogoDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States.
Michael SouffrantDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States.
Xin-Qiu YaoDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States.ORCID 0000-0003-2706-2028
Donald HamelbergDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States.ORCID 0000-0002-3785-3037
Giovanni GaddaDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302, United States.ORCID 0000-0002-7508-4195
Georgia State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous studies demonstrate that enzymes undergo multiple conformational changes during catalysis. The malleability of enzymes forms the basis for allosteric regulation: residues located far from the active site can exert long-range dynamical effects on the active site residues to modulate catalysis. The structure of

Indexed as

Amino Acid OxidoreductasesMolecular Dynamics SimulationBinding SitesCatalysisCatalytic DomainFlavinsKineticsProtein ConformationSubstrate SpecificityAmino Acid Oxidoreductasesarginine oxidaseFlavins

Identifiers

PMID36795942
PMCPMC9996824
OpenAlexW4321033173

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.