Evidence map›Paper›PMID 31500178›Full record

ArticleInternational journal of molecular sciences2019

Crystal Structures of Pyrophosphatase from

Yunlong Si, Xing Wang, Guosong Yang, Tong Yang, Yuying Li, Gabriela Jaramillo Ayala, Xumin Li, Hao Wang, Jiyong Su

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Characterization of a family I inorganic pyrophosphatase from Legionella pneumophila Philadelphia 1.Acta crystallographica. Section F, Structural biology communications · 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

9 authors.

Yunlong SiJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Xing WangJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Guosong YangZhongke Biopharm Co., LTD, East of Beijing, Beijing 101601, China.
Tong YangJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Yuying LiJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Gabriela Jaramillo AyalaJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Xumin LiJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Hao WangJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China.
Jiyong SuJilin Province Key Laboratory on Chemistry and Biology of Natural Drugs in Changbai Mountain, School of Life Sciences, Northeast Normal University, Changchun 130024, China. sujy100@nenu.edu.cn.ORCID 0000-0001-8406-1676

Funding

National Natural Science Foundation of China 31500637Science and Technology Project of Jilin Provincial Department of Education during the Thirteenth Five-Year Plan Period, China JJKH20190287KJ
6 · The paper itself

Abstract

All living things have pyrophosphatases that hydrolyze pyrophosphate and release energy. This energetically favorable reaction drives many energetically unfavorable reactions. An accepted catalytic model of pyrophosphatase shows that a water molecule activated by two divalent cations (M1 and M2) within the catalytic center can attack pyrophosphate in an S

Indexed as

Models, MolecularProtein ConformationAcinetobacter baumanniiAmino Acid SequenceBinding SitesCatalysisCatalytic DomainDiphosphatesEnzyme ActivationHydrolysisPeptidesPhosphorylationProtein BindingPyrophosphatasesStructure-Activity RelationshipDiphosphatesPeptidesPyrophosphatasesAcinetobacter baumanniicatalytic mechanismcrystal structureinorganic pyrophosphataselysine phosphorylationmass spectrometry

Identifiers

PMID31500178
PMCPMC6770254

What OpenQuestion holds

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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.