Evidence map›Paper›PMID 29071441›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017

Kinetic characterization of the inhibition of protein tyrosine phosphatase-1B by Vanadyl (VO

Jason Hon, Michelle S Hwang, Meara A Charnetzki, Issra J Rashed, Patrick B Brady, Sarah Quillin, Marvin W Makinen

Open access · greenAbstract read
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. 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
0.3field-weighted citation impact, top 39% 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, 6 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 1 institution in 1 country.

Jason HonDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Michelle S HwangDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Meara A CharnetzkiDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Issra J RashedDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Patrick B BradyDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Sarah QuillinDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA.
Marvin W MakinenDepartment of Biochemistry and Molecular Biology Center for Integrative Science, The University of Chicago, 929 East 57th Street, Chicago, IL, 60637, USA. makinen@uchicago.edu.
University of Chicago · US

Funding

TRANSGENIC COREP60DK020595 · NIDDK · UNIVERSITY OF CHICAGO · PI BELL, GRAEME I · 1985 to 2012
$25.5M
Pilot and Feasibility ProgramP30DK020595 · NIDDK · UNIVERSITY OF CHICAGO · PI Raghavendra G Mirmira · 2013 to 2026
$20.9M
Variation in Hormone and xenobiotic metabolizing enzyme genes and breast cancerP50CA125183 · NCI · UNIVERSITY OF CHICAGO · PI COX, NANCY · 2006 to 2010
$11.3M
Predoctoral Training Program in Chemistry & BiologyT32GM008720 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 1999 to 2020
$4.7M
Undergraduate Training Program in Chemical & Physical B*T90DK070076 · NIDDK · UNIVERSITY OF CHICAGO · PI KRON, STEPHEN J. · 2006 to 2007
$550k
NCI NIH HHS P50 CA125183NIDDK NIH HHS P30 DK020595NIDDK NIH HHS P60 DK020595NIDDK NIH HHS T90 DK070076NIGMS NIH HHS T32 GM008720
6 · The paper itself

Abstract

Protein tyrosine phosphatases (PTPases) are a prominent focus of drug design studies because of their roles in homeostasis and disorders of metabolism. These studies have met with little success because (1) virtually all inhibitors hitherto exhibit only competitive behavior and (2) a consensus sequence H/V-C-X

Indexed as

Chelating AgentsEnzyme InhibitorsHydrolysisKineticsProtein Tyrosine Phosphatase, Non-Receptor Type 1VanadatesChelating AgentsEnzyme InhibitorsProtein Tyrosine Phosphatase, Non-Receptor Type 1VanadatesBis(acetylacetonato)oxidovanadium(IV)Protein tyrosine phosphatase-1BSteady-state kineticsUncompetitive inhibitionVanadyl (VO2+) chelatesVO(acac)2

Identifiers

PMID29071441
PMCPMC5671894
OpenAlexW2765425512

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.