Evidence map›Paper›PMID 23351377›Full record

ReviewBMB reports2013

Biochemistry and structure of phosphoinositide phosphatases.

Young Jun Kim, Nusrat Jahan, Young Yil Bahk

Open access · goldAbstract readReview
In one paragraph

Review in BMB reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Striking a balance: PIPExploration of neuroprotective therapy · 2021
    Article
  3. Review
  4. 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

3 authors at 1 institution in 1 country.

Young Jun KimDepartment of Biotechnology, Konkuk University, Chungju, Korea.
Nusrat Jahan
Young Yil Bahk
Konkuk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoinositides are the phosphorylated derivatives of phosphatidylinositol, and play a very significant role in a diverse range of signaling processes in eukaryotic cells. A number of phosphoinositide-metabolizing enzymes, including phosphoinositide-kinases and phosphatases are involved in the synthesis and degradation of these phospholipids. Recently, the function of various phosphatases in the phosphatidylinositol signaling pathway has been of great interest. In the present review we summarize the structural insights and biochemistry of various phosphatases in regulating phosphoinositide metabolism.

Indexed as

AnimalsDual-Specificity PhosphatasesHumansInositol Polyphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein Structure, TertiaryProtein Tyrosine Phosphatases, Non-ReceptorPTEN PhosphohydrolaseDual-Specificity PhosphatasesInositol Polyphosphate 5-PhosphatasesmyotubularinPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein Tyrosine Phosphatases, Non-ReceptorPTEN PhosphohydrolaseTPTE2 protein, human

Identifiers

PMID23351377
PMCPMC4133831
OpenAlexW2063016013

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.