Evidence map›Paper›PMID 35102896›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.

Shimeng Liu, Wenyue Wu, Qi Zhao, Han Liang, Shiyou Che, Hao Zhang, Ruihua Liu, Qionglin Zhang, Mark Bartlam

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. 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
–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

2 citing papers in PubMed.

  1. Article
  2. Sumner's legacy: a century of urease crystals and recent structural advances.Critical reviews in biochemistry and molecular biology
    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

9 authors.

Shimeng LiuCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.ORCID 0000-0002-4733-1566
Wenyue WuCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Qi ZhaoCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Han LiangCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Shiyou CheCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Hao ZhangCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Ruihua LiuCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.
Qionglin ZhangCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.ORCID 0000-0002-1016-1874
Mark BartlamCollege of Life Sciences, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Protein Science, Nankai University, 38 Tongyan Road, Tianjin 300350, People's Republic of China.ORCID 0000-0001-5173-5080

Funding

National Key Research and Development Program of China 2020YFC1807000National Natural Science Foundation of China 31800627National Natural Science Foundation of China 31870053
6 · The paper itself

Abstract

Klebsiella pneumoniae is an opportunistic pathogen that mostly affects those with weakened immune systems. Urease is a vital enzyme that can hydrolyze urea to ammonia and carbon dioxide as a source of nitrogen for growth. Urease is also a K. pneumoniae virulence factor that enables survival of the bacterium under nutrient-limiting conditions. UreF, an important nickel-binding urease accessory protein, is involved in the insertion of Ni

Indexed as

Bacterial ProteinsCircular DichroismCrystallography, X-RayKlebsiella pneumoniaeModels, MolecularProtein ConformationUreaseBacterial ProteinsUreaseUreF protein, bacteriacrystal structureKlebsiella pneumoniaeureaseUreF

Identifiers

PMID35102896
PMCPMC8805216

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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.