Evidence map›Paper›PMID 35897808›Full record

ArticleInternational journal of molecular sciences2022

Functional Versatility of the Human 2-Oxoadipate Dehydrogenase in the L-Lysine Degradation Pathway toward Its Non-Cognate Substrate 2-Oxopimelic Acid.

Natalia S Nemeria, Balint Nagy, Roberto Sanchez, Xu Zhang, João Leandro, Attila Ambrus, Sander M Houten, Frank Jordan

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Natalia S NemeriaDepartment of Chemistry, Rutgers University-Newark, Newark, NJ 07102-1811, USA.
Balint NagyDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 1082 Budapest, Hungary.ORCID 0000-0003-3669-7041
Roberto SanchezIcahn Institute for Data Science and Genomic Technology, Icahn School of Medicine at Mount Sinai, New York, NY 10029-6501, USA.
Xu ZhangDepartment of Chemistry, Rutgers University-Newark, Newark, NJ 07102-1811, USA.
João LeandroIcahn Institute for Data Science and Genomic Technology, Icahn School of Medicine at Mount Sinai, New York, NY 10029-6501, USA.
Attila AmbrusDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 1082 Budapest, Hungary.ORCID 0000-0001-6014-3175
Sander M HoutenIcahn Institute for Data Science and Genomic Technology, Icahn School of Medicine at Mount Sinai, New York, NY 10029-6501, USA.
Frank JordanDepartment of Chemistry, Rutgers University-Newark, Newark, NJ 07102-1811, USA.ORCID 0000-0003-1354-718X
Icahn School of Medicine at Mount Sinai · USRutgers, The State University of New Jersey · USSemmelweis University · HU

Funding

STRUCTURE AND MECHANISM OF YEAST PYRUVATE DECARBOXYLASER01GM050380 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 1993 to 2013
$3.0M
Novel Treatment Options for Glutaric AciduriaR21HD088775 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI DEVITA, ROBERT J, HOUTEN, SANDER MICHEL · 2017 to 2018
$466k
Mechanistic Issues Related to Aging on Human 2-Oxoglutarate Dehydrogenase ComplexR15GM116077 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 2015 to 2015
$369k
Genetic validation of DHTKD1 as a therapeutic target for the treatment of Glutaric Aciduria type 1R03HD092878 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI HOUTEN, SANDER MICHEL · 2017 to 2018
$170k
Eunice Kennedy Shriver National Institute of Child Health and Human Development R03HD092878, R21HD088775Hungarian Brain Research program 2 2017-1.2.1-NKP-2017-00002NICHD NIH HHS R03 HD092878NICHD NIH HHS R21 HD088775NIGMS NIH HHS R01 GM050380NIGMS NIH HHS R15 GM116077NIH HHS GM050380, R15-GM116077Semmelweis University STIA-OTKA-2021, TKP2021-EGA-25, TKP2021-EGA-25
6 · The paper itself

Abstract

The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+H

Indexed as

Amino Acid Metabolism, Inborn ErrorsKetoglutarate Dehydrogenase ComplexHumansLysineNADOxidation-ReductionDHTKD1 protein, humanKetoglutarate Dehydrogenase ComplexLysineNAD2-oxoadipate dehydrogenase2-oxoadipate dehydrogenase complex2-oxopimelate substrateE1a promiscuityH2O2 productionL-lysine degradation pathwayrare E1a variants

Identifiers

PMID35897808
PMCPMC9367764
OpenAlexW4288038101

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.