Evidence map›Paper›PMID 30420721›Full record

ArticleScientific reports2018

Crystallographic and kinetic analyses of human IPMK reveal disordered domains modulate ATP binding and kinase activity.

Corey D Seacrist, Raymond D Blind

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Structural Rationalization of IPMK Inhibitor Potency.Journal of medicinal chemistry · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Arg1 frommBio · 2024
    Article
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  13. Article
  14. Review
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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

2 authors at 1 institution in 1 country.

Corey D SeacristDepartment of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Raymond D BlindDepartment of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA. ray.blind@vanderbilt.edu.ORCID http://orcid.org/0000-0002-1358-6309
Vanderbilt University · US

Funding

Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI ALVIN C POWERS · 2012 to 2026
$29.3M
MULTIDISCIPLINARY TRAINING IN MOLECULAR ENDOCRINOLOGYT32DK007563 · NIDDK · VANDERBILT UNIVERSITY · PI Richard M O'Brien · 1988 to 2026
$15.9M
Cancer cell signaling through lipids complexed to proteinsK01CA172957 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI BLIND, RAYMOND DANIEL · 2012 to 2015
$449k
NCI NIH HHS K01 CA172957NIDDK NIH HHS P30 DK020593NIDDK NIH HHS T32 DK007563
6 · The paper itself

Abstract

Inositol polyphosphate multikinase (IPMK) is a member of the IPK-superfamily of kinases, catalyzing phosphorylation of several soluble inositols and the signaling phospholipid PI(4,5)P

Indexed as

Adenosine TriphosphateCrystallographyHumansInositol PhosphatesKineticsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein Structure, SecondarySignal TransductionAdenosine TriphosphateInositol Phosphatesinositol polyphosphate multikinasePhosphotransferases (Alcohol Group Acceptor)

Identifiers

PMID30420721
PMCPMC6232094
OpenAlexW2950060185

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.