Evidence map›Paper›PMID 27683242›Full record

ArticleJournal of bioenergetics and biomembranes2016

Kinetic and mutational studies of the adenosine diphosphate ribose hydrolase from Mycobacterium tuberculosis.

Suzanne F O'Handley, Puchong Thirawatananond, Lin-Woo Kang, Jennifer E Cunningham, J Alfonso Leyva, L Mario Amzel, Sandra B Gabelli

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2016. 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
0.9field-weighted citation impact, top 22% 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, 4 citations in OpenAlex.

  1. Visualization of mutagenic nucleotide processing byProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. 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

7 authors at 5 institutions in 3 countries.

Suzanne F O'HandleySchool of Chemistry and Materials Science, Rochester Institute of Technology, Rochester, NY, 14623, USA.
Puchong ThirawatananondDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Lin-Woo KangDepartment of Biological Sciences, Konkuk University, Seoul, South Korea.
Jennifer E CunninghamSchool of Chemistry and Materials Science, Rochester Institute of Technology, Rochester, NY, 14623, USA.
J Alfonso LeyvaDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
L Mario AmzelDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Sandra B GabelliDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA. gabelli@jhmi.edu.
Johns Hopkins Medicine · USRochester Institute of Technology · USJohns Hopkins University · USKonkuk University · KRPontificia Universidad Javeriana · CO

Funding

Tumor Antigens for Individual Signatures and TherapyP50CA062924 · NCI · JOHNS HOPKINS UNIVERSITY · PI JAFFEE, ELIZABETH M. · 1993 to 2022
$54.6M
Structure, Function and Mechanism of Nudix HydrolasesR01GM066895 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI AMZEL, L. MARIO · 2003 to 2006
$1.1M
Nudix Hydrolases and HAD Superfamily PhosphatasesR15GM066715 · NIGMS · ROCHESTER INSTITUTE OF TECHNOLOGY · PI O'HANDLEY, SUZANNE FREEMAN · 2003 to 2006
$339k
NCI NIH HHS P50 CA062924NIGMS NIH HHS R01 GM066895NIGMS NIH HHS R15 GM066715
6 · The paper itself

Abstract

Mycobacterium tuberculosis represents one of the world's most devastating infectious agents - with one third of the world's population infected and 1.5 million people dying each year from this deadly pathogen. As part of an effort to identify targets for therapeutic intervention, we carried out the kinetic characterization of the product of gene rv1700 of M. tuberculosis. Based on its sequence and its structure, the protein had been tentatively identified as a pyrophosphohydrolase specific for adenosine diphosphate ribose (ADPR), a compound involved in various pathways including oxidative stress response and tellurite resistance. In this work we carry out a kinetic, mutational and structural investigation of the enzyme, which provides a full characterization of this Mt-ADPRase. Optimal catalytic rates were achieved at alkaline pH (7.5-8.5) with either 0.5-1 mM Mg

Indexed as

Adenosine Diphosphate RiboseAmino Acid SequenceBinding SitesCatalysisHydrolasesKineticsMutationMycobacterium tuberculosisPyrophosphatasesSequence Homology, Amino AcidSubstrate SpecificityAdenosine Diphosphate RiboseADPribose pyrophosphataseHydrolasesPyrophosphatasesADPRaseADP-riboseADP-ribose hydrolaseMycobacterium tuberculosisNudix

Identifiers

PMID27683242
PMCPMC5489420
OpenAlexW2523944938

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.