Evidence map›Paper›PMID 20208177›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2.

Junko Kato, Masato Kato

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In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

2 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Regulation of pyruvate metabolism and human disease.Cellular and molecular life sciences : CMLS · 2014
    Review
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

2 authors at 1 institution in 1 country.

Junko KatoDepartment of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9030, USA.
Masato Kato
The University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial serine phosphatase that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation. In humans, two PDP isoforms (1 and 2) have been identified. PDP1 is composed of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r), whereas PDP2 consists of only a catalytic subunit (PDP2c). Both PDP1c and PDP2c have been crystallized individually and complete X-ray diffraction data sets have been collected to 2.45 and 2.0 A resolution, respectively. The PDP1c crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 65.1, c = 216.1 A. The asymmetric unit is expected to contain one molecule, with a Matthews coefficient V(M) of 2.56 A(3) Da(-1). The PDP2c crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.6, b = 69.1, c = 109.7 A. The asymmetric unit is expected to contain one molecule, with a Matthews coefficient V(M) of 1.91 A(3) Da(-1).

Indexed as

Catalytic DomainCrystallizationCrystallography, X-RayHumansIsoenzymesPyruvate Dehydrogenase (Lipoamide)-PhosphataseIsoenzymesPyruvate Dehydrogenase (Lipoamide)-Phosphatase

Identifiers

PMID20208177
PMCPMC2833053
OpenAlexW2081476974

What OpenQuestion holds

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Registered trials

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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.