Evidence map›Paper›PMID 25234227›Full record

ReviewNaunyn-Schmiedeberg's archives of pharmacology2015

Modulation of cytoskeletal dynamics by mammalian nucleoside diphosphate kinase (NDPK) proteins.

Natasha T Snider, Peter J Altshuler, M Bishr Omary

Open access · greenAbstract readReview
In one paragraph

Review in Naunyn-Schmiedeberg's archives of pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Comprehensive analysis of theTranslational cancer research · 2020
    Article
  5. Structure, Folding and Stability of Nucleoside Diphosphate Kinases.International journal of molecular sciences · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. 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.

Natasha T SniderDepartment of Molecular & Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA, nsnider@umich.edu.
Peter J Altshuler
M Bishr Omary
University of Michigan–Ann Arbor · US

Funding

Regulation and Dynamics of Keratins in Digestive OrgansR01DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1997 to 2015
$4.5M
Keratin sumoylation and its function during hepatocyte stress and liver diseaseK01DK093776 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SNIDER, NATASHA T · 2011 to 2015
$586k
NIDDK NIH HHS K01 DK093776NIDDK NIH HHS R01 DK052951
6 · The paper itself

Abstract

Nucleoside diphosphate kinase (NDPK) proteins comprise a family of ten human isoforms that participate in the regulation of multiple cellular processes via enzymatic and nonenzymatic functions. The major enzymatic function of NDPKs is the generation of nucleoside triphosphates, such as guanosine triphosphate (GTP). Mechanisms behind the nonenzymatic NDPK functions are not clear but likely involve context-dependent signaling roles of NDPK within multi-protein complexes. This is most evident for NDPK-A, which is encoded by the human NME1 gene, the first tumor metastasis suppressor gene to be identified. Understanding which protein interactions are most relevant for the biological and metastasis-related functions of NDPK will be important in the potential utilization of NDPK as a disease target. Accumulating evidence suggests that NDPK interacts with and affects various components and regulators of the cytoskeleton, including actin-binding proteins, intermediate filaments, and cytoskeletal attachment structures (adherens junctions, desmosomes, and focal adhesions). We review the existing literature on this topic and highlight outstanding questions and potential future directions that should clarify the impact of NDPK on the different cytoskeletal systems.

Indexed as

AnimalsCytoskeletal ProteinsCytoskeletonHumansNucleoside-Diphosphate KinaseCytoskeletal ProteinsNucleoside-Diphosphate Kinase

Identifiers

PMID25234227
PMCPMC4308521
OpenAlexW1965656525

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.