Evidence map›Paper›PMID 17349955›Full record

ArticleMolecular cell2007

Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes.

Christian Schlieker, Wilhelm A Weihofen, Evelyne Frijns, Lisa M Kattenhorn, Rachelle Gaudet, Hidde L Ploegh

Abstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
–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

78 citing papers in PubMed.

  1. Article
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  5. Review
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  8. DALI shines a light on remote homologs: One hundred discoveries.Protein science : a publication of the Protein Society · 2023
    Article
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  12. Review
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  15. Article
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  18. Review
  19. Article
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18 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

6 authors.

Christian SchliekerDepartment of Biology, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, MA 02142, USA.
Wilhelm A Weihofen
Evelyne Frijns
Lisa M Kattenhorn
Rachelle Gaudet
Hidde L Ploegh

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR 15301
6 · The paper itself

Abstract

All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the suicide substrate. The Ub core participates in an extensive hydrophobic interaction with an exposed beta hairpin loop of M48(USP). This Ub binding mode contributes to Ub specificity and is distinct from that observed in other deubiquitinating enzymes. Both the arrangement of active-site residues and the architecture of the interface with Ub lead us to classify this domain as the founding member of a previously unknown class of deubiquitinating enzymes.

Indexed as

Amino Acid SequenceBinding SitesCatalysisCrystallography, X-RayCysteine EndopeptidasesModels, MolecularMolecular Sequence DataMuromegalovirusMutationProtein FoldingProtein Structure, SecondarySubstrate SpecificityUbiquitinCysteine EndopeptidasesUbiquitin

Identifiers

PMID17349955
PMCPMC7110467

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.