Evidence map›Paper›PMID 30231198›Full record

ArticleBiochemistry2018

Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.

Ting Yao, Yiyou Huang, Meng Zhang, Yujuan Chen, Hairun Pei, Jianyou Shi, Huanchen Wang, Yousheng Wang, Hengming Ke

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 92% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 at 3 institutions in 2 countries.

Ting YaoBeijing Advanced Innovation Center for Food Nutrition and Human Health , Beijing Technology and Business University , Beijing 100048 , China.
Yiyou HuangDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center , The University of North Carolina , Chapel Hill , North Carolina 27599-7260 , United States.
Meng ZhangBeijing Advanced Innovation Center for Food Nutrition and Human Health , Beijing Technology and Business University , Beijing 100048 , China.
Yujuan ChenBeijing Advanced Innovation Center for Food Nutrition and Human Health , Beijing Technology and Business University , Beijing 100048 , China.
Hairun PeiBeijing Advanced Innovation Center for Food Nutrition and Human Health , Beijing Technology and Business University , Beijing 100048 , China.
Jianyou ShiDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center , The University of North Carolina , Chapel Hill , North Carolina 27599-7260 , United States.
Huanchen WangLaboratory of Signal Transduction, National Institute of Environmental Health Sciences , National Institutes of Health , 111 Alexander Drive , Research Triangle Park , North Carolina 27709 , United States.
Yousheng WangBeijing Advanced Innovation Center for Food Nutrition and Human Health , Beijing Technology and Business University , Beijing 100048 , China.
Hengming KeDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center , The University of North Carolina , Chapel Hill , North Carolina 27599-7260 , United States.ORCID 0000-0001-8864-7279
Beijing Technology and Business University · CNUniversity of North Carolina at Chapel Hill · USNational Institutes of Health · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI David Darr · 1985 to 2026
$201.5M
Inositol SignallingZIAES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 2009 to 2023
$31.3M
REGULATION OF INOSITOL LIPID SIGNALLING MECHANISMSZ01ES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 1990 to 2008
$4.3M
Substrate specificity and inhibitor selectivity of PDER01GM059791 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KE, HENGMING · 2000 to 2013
$3.0M
Intramural NIH HHS Z01 ES080046Intramural NIH HHS ZIA ES080046NCI NIH HHS P30 CA016086NIGMS NIH HHS R01 GM059791
6 · The paper itself

Abstract

The cAMP signaling system plays important roles in the physiological processes of pathogen yeast Candida albicans, but its functional mechanism has not been well illustrated. Here, we report the enzymatic characterization and crystal structures of C. albicans phosphodiesterase 2 (caPDE2) in the unliganded and 3-isobutyl-1-methylxanthine-complexed forms. caPDE2 is a monomer in liquid and crystal states and specifically hydrolyzes cAMP with a K

Indexed as

Candida albicansCrystallography, X-RayCyclic Nucleotide Phosphodiesterases, Type 2Fungal ProteinsProtein DomainsProtein Structure, SecondaryStructure-Activity RelationshipCyclic Nucleotide Phosphodiesterases, Type 2Fungal Proteins

Identifiers

PMID30231198
PMCPMC9364965
OpenAlexW2890690413

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.