Evidence map›Paper›PMID 16388587›Full record

ArticleBiochemistry2006

The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases.

Craig W Vander Kooi, Melanie D Ohi, Joshua A Rosenberg, Michael L Oldham, Marcia E Newcomer, Kathleen L Gould, Walter J Chazin

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

55 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Wheat E3 ligasePhysiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Article
  3. Increased PRP19 in Hepatocyte Impedes B Cell Function to Promote Hepatocarcinogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  4. Review
  5. Review
  6. E3 ubiquitin ligases in nasopharyngeal carcinoma and implications for therapies.Journal of molecular medicine (Berlin, Germany) · 2023
    Article
  7. Review
  8. Review
  9. Article
  10. The roles of E3 ligases in Hepatocellular carcinoma.American journal of cancer research · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020
    Review
  18. TheFrontiers in plant science · 2020
    Article
  19. Review
  20. 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

7 authors at 4 institutions in 1 country.

Craig W Vander KooiDepartment of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232, USA.
Melanie D Ohi
Joshua A Rosenberg
Michael L Oldham
Marcia E Newcomer
Kathleen L Gould
Walter J Chazin
Howard Hughes Medical Institute · USHarvard University · USLouisiana State University · USVanderbilt University · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
VIRUSES, NUCLEIC ACIDS, GROWTH, AND CANCERT32CA009385 · NCI · VANDERBILT UNIVERSITY · PI RULEY, HENRY EARL · 1985 to 2007
$4.1M
Structural Biology of U-box E3 Ubiquitin LigasesR01GM075156 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2005 to 2013
$2.4M
S100 PROTEINS: STRUCTURAL BASIS OF FUNCTIONAL PROPERTIESR01GM062112 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2000 to 2009
$2.1M
ENZYMATIC ACTIVATION OF LIPOPHILIC SIGNALING MOLECULESR01GM055420 · NIGMS · VANDERBILT UNIVERSITY · PI NEWCOMER, MARCIA E. · 1996 to 2004
$951k
NCI NIH HHS T32 CA009385NCI NIH HHS T32CA09385NIEHS NIH HHS P30 ES000267NIGMS NIH HHS R01 GM055420NIGMS NIH HHS R01 GM062112NIGMS NIH HHS R01 GM075156NIGMS NIH HHS R01GM55420NIGMS NIH HHS R01GM62112NIGMS NIH HHS R01GM75156NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32GM08320
6 · The paper itself

Abstract

Prp19 is an essential splicing factor and a member of the U-box family of E3 ubiquitin ligases. Prp19 forms a tetramer via a central coiled-coil domain. Here, we show the U-box domain of Prp19 exists as a dimer within the context of the Prp19 tetramer. A high-resolution structure of the homodimeric state of the Prp19 U-box was determined by X-ray crystallography. Mutation of the U-box dimer interface abrogates U-box dimer formation and is lethal in vivo. The structure of the U-box dimer enables construction of a complete model of Prp19 providing insights into how the tetrameric protein functions as an E3 ligase. Finally, comparison of the Prp19 U-box homodimer with the heterodimeric complex of BRCA1/BARD1 RING-finger domains uncovers a common architecture for a family of oligomeric U-box and RING-finger E3 ubiquitin ligases, which has mechanistic implications for E3 ligase-mediated polyubiquitination and E4 polyubiquitin ligases.

Indexed as

Amino Acid SequenceBinding SitesCarrier ProteinsCrystallography, X-RayDimerizationDNA Repair EnzymesHumansModels, ChemicalMolecular Sequence DataNuclear ProteinsPolyubiquitinProtein Structure, TertiaryRNA, Small NuclearRNA Splicing FactorsSubstrate SpecificityUbiquitin-Conjugating EnzymesCarrier ProteinsDNA Repair EnzymesNuclear ProteinsPolyubiquitinPRPF19 protein, humanRNA, Small NuclearRNA Splicing FactorsUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID16388587
PMCPMC2570371
OpenAlexW2000945872

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.