Evidence map›Paper›PMID 32627744›Full record

ArticleActa crystallographica. Section F, Structural biology communications2020

Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase.

Youzhong Guo, Weihua Qiu, Thomas E Roche, Marvin L Hackert

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

Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 49% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Oxidative medicine and cellular longevity · 2021
    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

4 authors at 3 institutions in 1 country.

Youzhong GuoDepartment of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298, USA.
Weihua QiuDepartment of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298, USA.
Thomas E RocheDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
Marvin L HackertDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
Virginia Commonwealth University · USKansas State University · USThe University of Texas at Austin · US

Funding

Virginia Commonwealth University 147019Welch Foundation F-1219
6 · The paper itself

Abstract

Mammalian pyruvate dehydrogenase (PDH) activity is tightly regulated by phosphorylation and dephosphorylation, which is catalyzed by PDH kinase isomers and PDH phosphatase isomers, respectively. PDH phosphatase isomer 1 (PDP1) is a heterodimer consisting of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). Here, the crystal structure of bovine PDP1c determined at 2.1 Å resolution is reported. The crystals belonged to space group P3

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalytic DomainCattleCrystallography, X-RayDimerizationManganeseProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein DomainsPyruvate Dehydrogenase (Lipoamide)-PhosphataseRecombinant ProteinsSequence AlignmentWaterManganesePyruvate Dehydrogenase (Lipoamide)-PhosphataseRecombinant ProteinsWatercis-peptidepyruvate dehydrogenasepyruvate dehydrogenase phosphatase

Identifiers

PMID32627744
PMCPMC7336360
OpenAlexW3038178196

What OpenQuestion holds

Textmetadata
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.