Evidence map›Paper›PMID 20462492›Full record

ArticleStructure (London, England : 1993)2010

The Prp19 WD40 domain contains a conserved protein interaction region essential for its function.

Craig W Vander Kooi, Liping Ren, Ping Xu, Melanie D Ohi, Kathleen L Gould, Walter J Chazin

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

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  8. Topology of the U12-U6ACS omega · 2020
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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

6 authors at 3 institutions in 1 country.

Craig W Vander KooiDepartment of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA. craig.vanderkooi@uky.edu
Liping Ren
Ping Xu
Melanie D Ohi
Kathleen L Gould
Walter J Chazin
Vanderbilt University · USHoward Hughes Medical Institute · USUniversity of Kentucky · US

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Structural Biology of U-box E3 Ubiquitin LigasesR01GM075156 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2005 to 2013
$2.4M
Multifaceted Approaches for Studying the Structure and Function of SpliceosomesDP2OD004483 · OD · VANDERBILT UNIVERSITY · PI OHI, MELANIE DIANE · 2008 to 2008
$2.3M
Howard Hughes Medical InstituteNCRR NIH HHS P20 RR020171NCRR NIH HHS P20RR020171NIGMS NIH HHS R01 GM075156NIGMS NIH HHS R01GM075156NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32GM08320NIH HHS 1DP2OD004483NIH HHS DP2 OD004483
6 · The paper itself

Abstract

Prp19 is a member of the WD40 repeat family of E3 ubiquitin ligases and a conserved eukaryotic RNA splicing factor essential for activation and stabilization of the spliceosome. To understand the role of the WD40 repeat domain of Prp19 we have determined its structure using X-ray crystallography. The domain has a distorted seven bladed WD40 architecture with significant asymmetry due to irregular packing of blades one and seven into the core of the WD40 domain. Structure-based mutagenesis identified a highly conserved surface centered around blade five that is required for the physical interaction between Prp19 and Cwc2, another essential splicing factor. This region is found to be required for Prp19 function and yeast viability. Experiments in vitro and in vivo demonstrate that two molecules of Cwc2 bind to the Prp19 tetramer. These coupled structural and functional studies provide a model for the functional architecture of Prp19.

Indexed as

Amino Acid MotifsCrystallography, X-RayEukaryotaMutagenesisProteinsProtein Structure, TertiaryRNA SplicingSaccharomyces cerevisiaeSpliceosomesUbiquitin-Protein LigasesX-RaysProteinsUbiquitin-Protein Ligases

Identifiers

PMID20462492
PMCPMC2871033
OpenAlexW2054502896

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.