Evidence map›Paper›PMID 25702872›Full record

ArticleMolecular cell2015

Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

Ryan T Vander Linden, Casey W Hemmis, Benjamin Schmitt, Ada Ndoja, Frank G Whitby, Howard Robinson, Robert E Cohen, Tingting Yao, Christopher P Hill

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 118 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Assembly and disassembly of branched ubiquitin chains.Frontiers in molecular biosciences · 2023
    Review
  17. Review
  18. Article
  19. Review
  20. Article

9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Ryan T Vander Linden *Department of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112-5650 USA.
Casey W Hemmis *Department of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112-5650 USA.
Benjamin SchmittDepartment of Biochemistry and Molecular Biology Colorado State University, Fort Collins, CO 80523 USA.
Ada NdojaDepartment of Biochemistry and Molecular Biology Colorado State University, Fort Collins, CO 80523 USA.
Frank G WhitbyDepartment of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112-5650 USA.
Howard RobinsonBiology Department Brookhaven National Laboratory, Upton, NY, 11973 USA.
Robert E CohenDepartment of Biochemistry and Molecular Biology Colorado State University, Fort Collins, CO 80523 USA.
Tingting YaoDepartment of Biochemistry and Molecular Biology Colorado State University, Fort Collins, CO 80523 USA.
Christopher P HillDepartment of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112-5650 USA.
Colorado State University · USUniversity of Utah · USBrookhaven National Laboratory · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Structures of Proteasome ActivatorsR01GM059135 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 1999 to 2012
$3.4M
Regulation of a Deubiquitinating Enzyme in Proteolysis and Chromatin RemodelingR01GM098401 · NIGMS · COLORADO STATE UNIVERSITY · PI YAO, TINGTING · 2011 to 2021
$2.9M
Linkage-specific recognition of polyubiquitinR01GM097452 · NIGMS · COLORADO STATE UNIVERSITY · PI COHEN, ROBERT · 2011 to 2014
$1.1M
NCI NIH HHS P30 CA042014NCI NIH HHS P30CA042014NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NCRR NIH HHS P41 RR012408NCRR NIH HHS P41RR012408NIBIB NIH HHS P30 EB009998NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS P50 GM082545NIGMS NIH HHS R01 GM059135NIGMS NIH HHS R01 GM097452NIGMS NIH HHS R01 GM098401
6 · The paper itself

Abstract

The UCH37 deubiquitylase functions in two large and very different complexes, the 26S proteasome and the INO80 chromatin remodeler. We have performed biochemical characterization and determined crystal structures of UCH37 in complexes with RPN13 and NFRKB, which mediate its recruitment to the proteasome and INO80, respectively. RPN13 and NFRKB make similar contacts to the UCH37 C-terminal domain but quite different contacts to the catalytic UCH domain. RPN13 can activate UCH37 by disrupting dimerization, although physiologically relevant activation likely results from stabilization of a surface competent for ubiquitin binding and modulation of the active-site crossover loop. In contrast, NFRKB inhibits UCH37 by blocking the ubiquitin-binding site and by disrupting the enzyme active site. These findings reveal remarkable commonality in mechanisms of recruitment, yet very different mechanisms of regulating enzyme activity, and provide a foundation for understanding the roles of UCH37 in the unrelated proteasome and INO80 complexes.

Indexed as

Models, MolecularProtein Structure, SecondaryProtein Structure, TertiaryAmino Acid SequenceBinding SitesCatalytic DomainCrystallography, X-RayDNA-Binding ProteinsEnzyme ActivationHumansIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMolecular Sequence DataMultiprotein ComplexesProteasome Endopeptidase ComplexProtein BindingADRM1 protein, humanDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMultiprotein ComplexesNFRKB protein, humanProteasome Endopeptidase ComplexUbiquitinUbiquitin ThiolesteraseUCHL5 protein, human

Identifiers

PMID25702872
PMCPMC4355076
OpenAlexW1990283498

What OpenQuestion holds

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Registered trials

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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.