Evidence map›Paper›PMID 31820916›Full record

ArticleACS chemical biology2020

A Regulatory Cysteine Residue Mediates Reversible Inactivation of NAD

Yugang Zhang, Miao Wang, Hening Lin

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. 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

3 authors at 2 institutions in 1 country.

Yugang ZhangDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Miao WangDepartment of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.
Hening LinHoward Hughes Medical Institute; Department of Chemistry and Chemical Biology , Cornell University , Ithaca , New York 14853 , United States.ORCID 0000-0002-0255-2701
Cornell University · USHoward Hughes Medical Institute · US

Funding

Metabolite Sensing and Regulation of Protein FunctionR35GM131808 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2019 to 2023
$1.9M
Acquisition of a Hybrid Quadrupole Time of Flight LC-MS/MS System for the CornellS10OD017992 · OD · CORNELL UNIVERSITY · PI ZHANG, SHENG · 2014 to 2014
$600k
NIGMS NIH HHS R35 GM131808NIH HHS S10 OD017992
6 · The paper itself

Abstract

Aldehyde dehydrogenases (ALDHs) are a large family of enzymes that oxidize aldehydes into carboxylic acids. All ALDHs have a conserved catalytic cysteine residue but different cofactor preferences for NAD

Indexed as

Aldehyde DehydrogenaseCatalysisCatalytic DomainCysteineModels, MolecularNADNADPOxidation-ReductionOxidative StressSignal TransductionAldehyde DehydrogenaseCysteineNADNADP

Identifiers

PMID31820916
PMCPMC7175950
OpenAlexW2995671565

What OpenQuestion holds

Textmetadata
LicenceTDM
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.