Evidence map›Paper›PMID 25436519›Full record

ArticleNature chemical biology2015

Intrinsic disorder drives N-terminal ubiquitination by Ube2w.

Vinayak Vittal, Lei Shi, Dawn M Wenzel, K Matthew Scaglione, Emily D Duncan, Venkatesha Basrur, Kojo S J Elenitoba-Johnson, David Baker, Henry L Paulson, Peter S Brzovic and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 83 citations in OpenAlex.

  1. Pooled it
  2. Molecular biology of the cell · 2026
    Article
  3. Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026
    Article
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023
    Review
  13. Article
  14. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022
    Review
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Vinayak VittalDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Lei Shi1] Department of Biochemistry, University of Washington, Seattle, Washington, USA. [2] Howard Hughes Medical Institute, University of Washington, Seattle, Washington, USA.
Dawn M WenzelDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
K Matthew Scaglione1] Department of Neurology, University of Michigan Medical School, Ann Arbor, Michigan, USA. [2] Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin, USA. [3] Neuroscience Research Center, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Emily D DuncanDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Venkatesha BasrurDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA.
Kojo S J Elenitoba-JohnsonDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA.
David Baker1] Department of Biochemistry, University of Washington, Seattle, Washington, USA. [2] Howard Hughes Medical Institute, University of Washington, Seattle, Washington, USA.
Henry L PaulsonDepartment of Neurology, University of Michigan Medical School, Ann Arbor, Michigan, USA.
Peter S BrzovicDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
Rachel E KlevitDepartment of Biochemistry, University of Washington, Seattle, Washington, USA.
University of Washington · USUniversity of Michigan–Ann Arbor · USHoward Hughes Medical Institute · US

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
Structural and Functional Characterization of BRCA1/BARD1R01GM088055 · NIGMS · UNIVERSITY OF WASHINGTON · PI KLEVIT, RACHEL E · 2009 to 2020
$6.5M
Integrating Quality Control: Studies of CHIP in Age-related NeurodegenerationR01AG034228 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PAULSON, HENRY L · 2009 to 2013
$1.5M
Unconventional Interactions of Human Ubiquitin Conjugating EnzymesR01GM098503 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRZOVIC, PETER S · 2012 to 2016
$1.5M
Protein fate in neurodegeneration: Investigations of novel regulatory mechanismsR00NS073936 · NINDS · MEDICAL COLLEGE OF WISCONSIN · PI SCAGLIONE, KENNETH MATTHEW · 2014 to 2016
$741k
Protein fate in neurodegeneration: Investigations of novel regulatory mechanismsK99NS073936 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCAGLIONE, KENNETH MATTHEW · 2012 to 2013
$197k
NIA NIH HHS R01 AG034228NIGMS NIH HHS 2T32 GM007270NIGMS NIH HHS R01 GM088055NIGMS NIH HHS R01 GM098503NIGMS NIH HHS T32 GM007270NINDS NIH HHS K99 NS073936NINDS NIH HHS R00 NS073936
6 · The paper itself

Abstract

Ubiquitination of the αN-terminus of protein substrates has been reported sporadically since the early 1980s. However, the identity of an enzyme responsible for this unique ubiquitin (Ub) modification has only recently been elucidated. We show the Ub-conjugating enzyme (E2) Ube2w uses a unique mechanism to facilitate the specific ubiquitination of the α-amino group of its substrates that involves recognition of backbone atoms of intrinsically disordered N termini. We present the NMR-based solution ensemble of full-length Ube2w that reveals a structural architecture unlike that of any other E2 in which its C terminus is partly disordered and flexible to accommodate variable substrate N termini. Flexibility of the substrate is critical for recognition by Ube2w, and either point mutations in or the removal of the flexible C terminus of Ube2w inhibits substrate binding and modification. Mechanistic insights reported here provide guiding principles for future efforts to define the N-terminal ubiquitome in cells.

Indexed as

HumansMagnetic Resonance SpectroscopyModels, MolecularPoint MutationProtein BindingProtein ConformationSubstrate SpecificityUbiquinoneUbiquitinationUbiquitin-Conjugating EnzymesUBE2W protein, humanUbiquinoneUbiquitin-Conjugating Enzymes

Identifiers

PMID25436519
PMCPMC4270946
OpenAlexW2136623638

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.