Evidence map›Paper›PMID 30277746›Full record

ArticleBiochemistry2018

Substrate Profile of the Phosphotriesterase Homology Protein from Escherichia coli.

Venkatesh V Nemmara, Dao Feng Xiang, A A Fedorov, E V Fedorov, Jeffrey B Bonanno, Steven C Almo, Frank M Raushel

Open access · greenAbstract read
PubMed Full text at PMC Publisher
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
0.1field-weighted citation impact, top 56% 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, 8 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

7 authors at 2 institutions in 1 country.

Venkatesh V NemmaraDepartment of Chemistry , Texas A&M University , College Station , Texas 77843 , United States.ORCID 0000-0001-6925-869X
Dao Feng XiangDepartment of Chemistry , Texas A&M University , College Station , Texas 77843 , United States.
A A FedorovDepartment of Biochemistry , Albert Einstein College of Medicine , 1300 Morris Park Avenue , Bronx , New York 10461 , United States.
E V FedorovDepartment of Biochemistry , Albert Einstein College of Medicine , 1300 Morris Park Avenue , Bronx , New York 10461 , United States.
Jeffrey B BonannoDepartment of Biochemistry , Albert Einstein College of Medicine , 1300 Morris Park Avenue , Bronx , New York 10461 , United States.
Steven C AlmoDepartment of Biochemistry , Albert Einstein College of Medicine , 1300 Morris Park Avenue , Bronx , New York 10461 , United States.
Frank M RaushelDepartment of Chemistry , Texas A&M University , College Station , Texas 77843 , United States.ORCID 0000-0002-5918-3089
Albert Einstein College of Medicine · USTexas A&M University · US

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI ALMO, STEVEN C. · 2010 to 2015
$34.6M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Novel Biochemical Pathways for the Metabolism of Carbohydrates in the Human gut MicriobiomeR01GM122825 · NIGMS · TEXAS A&M UNIVERSITY · PI RAUSHEL, FRANK M. · 2018 to 2021
$1.3M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS R01 GM122825NIGMS NIH HHS U54 GM093342
6 · The paper itself

Abstract

The phosphotriesterase homology protein (PHP) from Escherichia coli is a member of a family of proteins that is related to phosphotriestrase (PTE), a bacterial enzyme from cog1735 with unusual substrate specificity toward the hydrolysis of synthetic organic phosphates and phosphonates. PHP was cloned, purified to homogeneity, and functionally characterized. The three-dimensional structure of PHP was determined at a resolution of 1.84 Å with zinc and phosphate in the active site. The protein folds as a distorted (β/α)

Indexed as

Catalytic DomainCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydrolasesHydrolysisKineticsModels, MolecularOrganophosphonatesPhosphatesSubstrate SpecificityEscherichia coli ProteinsHydrolasesOrganophosphonatesPhosphatesPHP protein, E coli

Identifiers

PMID30277746
PMCPMC6643279
OpenAlexW2894549732

What OpenQuestion holds

Textmetadata
LicenceTDM
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.