Evidence map›Paper›PMID 28330605›Full record

ArticleCell chemical biology2017

Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.

Michal Chojnacki, Wissam Mansour, Dharjath S Hameed, Rajesh K Singh, Farid El Oualid, Rina Rosenzweig, Mark A Nakasone, Zanlin Yu, Fabian Glaser, Lewis E Kay and 3 more

Abstract read
In one paragraph

Article in Cell chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022
    Article
  16. Site-specific ubiquitination: Deconstructing the degradation tag.Current opinion in structural biology · 2022
    Review
  17. Review
  18. Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class.Chembiochem : a European journal of chemical biology · 2021
    Review
  19. Review
  20. Review
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

13 authors.

Michal ChojnackiDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel; Department of Medical Biochemistry, Medical University of Łódź, Łódź, Poland.
Wissam MansourDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Dharjath S HameedDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands; Department of Chemical Immunology, Leiden University Medical Center, Einthovenweg 20, 2333 ZC Leiden, the Netherlands.
Rajesh K SinghDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.
Farid El OualidDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands.
Rina RosenzweigDepartments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada; Department of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Mark A NakasoneDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Zanlin YuDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Fabian GlaserThe Technion Bioinformatics Knowledge Unit (BKU) of the Lorry Lokey Interdisciplinary Center for Life Sciences and Engineering, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Lewis E KayDepartments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada.
David FushmanDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA. Electronic address: fushman@umd.edu.
Huib OvaaDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands; Department of Chemical Immunology, Leiden University Medical Center, Einthovenweg 20, 2333 ZC Leiden, the Netherlands. Electronic address: h.ovaa@lumc.nl.
Michael H GlickmanDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel. Electronic address: glickman@tx.technion.ac.il.

Funding

Solution structure and dynamics of polyubiquitin chainsR01GM065334 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI DAVID FUSHMAN · 2002 to 2026
$6.2M
Recognition of non-ubiquitin signals at the proteasomeR01GM095755 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI FUSHMAN, DAVID · 2011 to 2014
$1.4M
Molecular Binding Partners of Non-canonical Ubiquitin ChainsR21NS093454 · NINDS · VIRGINIA COMMONWEALTH UNIVERSITY · PI CROPP, THOMAS ASHTON · 2016 to 2017
$421k
NIGMS NIH HHS R01 GM065334NIGMS NIH HHS R01 GM095755NINDS NIH HHS R21 NS093454
6 · The paper itself

Abstract

Ubiquitin (Ub) signaling is a diverse group of processes controlled by covalent attachment of small protein Ub and polyUb chains to a range of cellular protein targets. The best documented Ub signaling pathway is the one that delivers polyUb proteins to the 26S proteasome for degradation. However, studies of molecular interactions involved in this process have been hampered by the transient and hydrophobic nature of these interactions and the lack of tools to study them. Here, we develop Ub-phototrap (Ub

Indexed as

Binding SitesCross-Linking ReagentsMolecular Docking SimulationNuclear Magnetic Resonance, BiomolecularPolyubiquitinProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUltraviolet RaysCross-Linking ReagentsPolyubiquitinProteasome Endopeptidase ComplexProtein SubunitsSaccharomyces cerevisiae ProteinsUbiquitincrosslinkingproteasomeprotein-protein interactionsubiquitin

Identifiers

PMID28330605
PMCPMC5453731

What OpenQuestion holds

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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.