Evidence map›Paper›PMID 19436320›Full record

ReviewNature reviews. Molecular cell biology2009

Physiological functions of the HECT family of ubiquitin ligases.

Daniela Rotin, Sharad Kumar

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 638 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
638citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

638 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. From Single-Cell Clusters to Causality: ITCH Engagement for CKD Uncovered by Integrative Analysis of MR and MAGMA.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  20. Article

578 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.

Daniela RotinProgram in Cell Biology, The Hospital for Sick Children, Ontario, Canada. drotin@sickkids.ca
Sharad Kumar

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitylation of proteins is carried out by E1, E2 and E3 (ubiquitin ligase) enzymes, and targets them for degradation or for other cellular fates. The HECT enzymes, including Nedd4 family members, are a major group of E3 enzymes that dictate the specificity of ubiquitylation. In addition to ubiquitylating proteins for degradation by the 26S proteasome, HECT E3 enzymes regulate the trafficking of many receptors, channels, transporters and viral proteins. The physiological functions of the yeast HECT E3 ligase Rsp5 are the best known, but the functions of HECT E3 enyzmes in metazoans are now becoming clearer from in vivo studies.

Indexed as

AnimalsEndosomal Sorting Complexes Required for TransportGuanine Nucleotide Exchange FactorsHumansModels, MolecularNedd4 Ubiquitin Protein LigasesProtein ConformationProtein IsoformsSignal TransductionUbiquitinUbiquitinationUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportGuanine Nucleotide Exchange FactorsNedd4 protein, humanNedd4 Ubiquitin Protein LigasesProtein IsoformsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID19436320

What OpenQuestion holds

Textmetadata
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.