Evidence map›Paper›PMID 19557014›Full record

ReviewCell death and differentiation2010

Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions.

B Yang, S Kumar

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

130 citing papers in PubMed, 241 citations in OpenAlex.

  1. Trial
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  14. Update on the Pathogenesis of Keloid Formation.JID innovations : skin science from molecules to population health · 2024
    Review
  15. Article
  16. Article
  17. Article
  18. Regulation of the intestinal NaAmerican journal of physiology. Cell physiology · 2024
    Article
  19. Novel Therapeutic Avenues for Hypertrophic Cardiomyopathy.American journal of cardiovascular drugs : drugs, devices, and other interventions · 2023
    Review
  20. Article

70 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

B YangCarver College of Medicine, University of Iowa, Iowa City, IA 52242, USA. baoli-yang@uiowa.edu
S Kumar
Centre for Cancer Biology · AUUniversity of Iowa · US

Funding

PHENOTYPE AND GENETICS IN OROFACIAL CLEFT FAMILIESP50DE016215 · NIDCR · UNIVERSITY OF IOWA · PI LOVETT, MICHAEL · 2004 to 2008
$10.1M
ROLE OF ENAC IN NA EXCRETION--INNER MEDULLARY COLLECTING DUCT AND EPITHELIUMP50DK052617 · NIDDK · UNIVERSITY OF IOWA · PI YANG, BAOLI · 1997 to 2007
$7.1M
NIAMS NIH HHS AR052647NIDCR NIH HHS DE16215NIDCR NIH HHS P50 DE016215NIDDK NIH HHS DK52617NIDDK NIH HHS P50 DK052617
6 · The paper itself

Abstract

The Nedd4 (neural precursor cell-expressed developmentally downregulated gene 4) family of ubiquitin ligases (E3s) is characterized by a distinct modular domain architecture, with each member consisting of a C2 domain, 2-4 WW domains, and a HECT-type ligase domain. Of the nine mammalian members of this family, Nedd4 and its close relative, Nedd4-2, represent the ancestral ligases with strong similarity to the yeast, Rsp5. In Saccharomyces cerevisiae Rsp5 has a key role in regulating the trafficking, sorting, and degradation of a large number of proteins in multiple cellular compartments. However, in mammals the Nedd4 family members, including Nedd4 and Nedd4-2, appear to have distinct functions, thereby suggesting that these E3s target specific proteins for ubiquitylation. In this article we focus on the biology and emerging functions of Nedd4 and Nedd4-2, and review recent in vivo studies on these E3s.

Indexed as

14-3-3 ProteinsEndosomal Sorting Complexes Required for TransportEpithelial Sodium ChannelsImmediate-Early ProteinsNedd4 Ubiquitin Protein LigasesNeuromuscular JunctionProtein Serine-Threonine KinasesPTEN PhosphohydrolaseSaccharomyces cerevisiae ProteinsSerum-Glucocorticoid Regulated KinasesSodium ChannelsUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases14-3-3 ProteinsEndosomal Sorting Complexes Required for TransportEpithelial Sodium ChannelsImmediate-Early ProteinsNedd4 Ubiquitin Protein LigasesProtein Serine-Threonine KinasesPTEN PhosphohydrolaseRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerum-Glucocorticoid Regulated KinasesSodium ChannelsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID19557014
PMCPMC2818775
OpenAlexW2015709967

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.