Evidence map›Paper›PMID 30287686›Full record

ArticleThe Journal of biological chemistry2018

Oligomerization of the HECT ubiquitin ligase NEDD4-2/NEDD4L is essential for polyubiquitin chain assembly.

Dustin R Todaro, Allison C Augustus-Wallace, Jennifer M Klein, Arthur L Haas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Host E3 ubiquitin ligase ITCH mediatesbioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. DUOX1 in mammalian disease pathophysiology.Journal of molecular medicine (Berlin, Germany) · 2021
    Review
  10. Article
  11. Article
  12. Enzymatic Logic of Ubiquitin Chain Assembly.Frontiers in physiology · 2019
    Review
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

4 authors at 1 institution in 1 country.

Dustin R TodaroFrom the Department of Biochemistry and Molecular Biology and.
Allison C Augustus-WallaceFrom the Department of Biochemistry and Molecular Biology and.
Jennifer M KleinFrom the Department of Biochemistry and Molecular Biology and.
Arthur L HaasFrom the Department of Biochemistry and Molecular Biology and; the Stanley S. Scott Cancer Center, Louisiana State University School of Medicine, New Orleans, Louisiana 70112. Electronic address: ahaas@lsuhsc.edu.
Louisiana State University · US

Funding

Vascular and Cardiac Function Core - "Mentoring in Cardiovascular BiologyP30GM106392 · NIGMS · LSU HEALTH SCIENCES CENTER · PI KAPUSTA, DANIEL R · 2014 to 2018
$5.5M
ATP-UBIQUITIN-DEPENDENT PROTEOLYSISR01GM034009 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI HAAS, ARTHUR L · 1985 to 2011
$3.0M
NIGMS NIH HHS P30 GM106392NIGMS NIH HHS R01 GM034009
6 · The paper itself

Abstract

The NEDD4-2 (neural precursor cell-expressed developmentally down-regulated 4-2) HECT ligase catalyzes polyubiquitin chain assembly by an ordered two-step mechanism requiring two functionally distinct E2∼ubiquitin-binding sites, analogous to the trimeric E6AP/UBE3A HECT ligase. This conserved catalytic mechanism suggests that NEDD4-2, and presumably all HECT ligases, requires oligomerization to catalyze polyubiquitin chain assembly. To explore this hypothesis, we examined the catalytic mechanism of NEDD4-2 through the use of biochemically defined kinetic assays examining rates of

Indexed as

Amino Acid MotifsCatalysisCatalytic DomainHumansKineticsNedd4 Ubiquitin Protein LigasesPolyubiquitinUbiquitinUbiquitin-Protein LigasesNedd4L protein, humanNedd4 Ubiquitin Protein LigasesPolyubiquitinUBE3A protein, humanUbiquitinUbiquitin-Protein LigasesE2E3enzyme kineticsenzyme mechanismHECT domainHECT ligaselinkage specificityoligomerprotein complexprotein degradationprotein-protein interactionstransthiolationubiquitinubiquitin ligase

Identifiers

PMID30287686
PMCPMC6254339
OpenAlexW2895550411

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.