Evidence map›Paper›PMID 17951556›Full record

ArticleMolecular & cellular proteomics : MCP2008

Functional dissection of a HECT ubiquitin E3 ligase.

Jin-Ying Lu, Yu-Yi Lin, Jiang Qian, Sheng-Ce Tao, Jian Zhu, Cecile Pickart, Heng Zhu

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Developments and Applications of Functional Protein Microarrays.Molecular & cellular proteomics : MCP · 2020
    Review
  4. Article
  5. Article
  6. Ubiquitination as a Key Regulator of Endosomal Signaling by GPCRs.Frontiers in cell and developmental biology · 2019
    Review
  7. Article
  8. Article
  9. Protein Array-based Approaches for Biomarker Discovery in Cancer.Genomics, proteomics & bioinformatics · 2017
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Overview of protein microarrays.Current protocols in protein science · 2013
    Review
  19. Review
  20. Proteomic identification of protein ubiquitination events.Biotechnology & genetic engineering reviews · 2013
    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

7 authors at 3 institutions in 3 countries.

Jin-Ying LuDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Yu-Yi Lin
Jiang Qian
Sheng-Ce Tao
Jian Zhu
Cecile Pickart
Heng Zhu
Johns Hopkins University · USHigh Throughput Biology (United States) · USJohns Hopkins Medicine · US

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
MECHANISM OF INSERTION SEQUENCE TRANSLOCATIONR01GM028470 · NIGMS · YALE UNIVERSITY · PI GRINDLEY, NIGEL DAVID · 1985 to 2005
$1.6M
Application of Bioinformatics to Retinal Gene RegulationR03EY015684 · NEI · JOHNS HOPKINS UNIVERSITY · PI QIAN, JIANG · 2004 to 2006
$487k
MECHANISM OF INSERTION SEQUENCE TRANSLOCATIONR37GM028470 · NIGMS · YALE UNIVERSITY · PI GRINDLEY, NIGEL D · 1991 to 2000
$453k
NCRR NIH HHS U54 RR020839NCRR NIH HHS U54RR020839NEI NIH HHS EY015684NEI NIH HHS R03 EY015684NIGMS NIH HHS GM28470NIGMS NIH HHS R01 GM028470NIGMS NIH HHS R37 GM028470
6 · The paper itself

Abstract

Ubiquitination is one of the most prevalent protein post-translational modifications in eukaryotes, and its malfunction is associated with a variety of human diseases. Despite the significance of this process, the molecular mechanisms that govern the regulation of ubiquitination remain largely unknown. Here we used a combination of yeast proteome chip assays, genetic screening, and in vitro/in vivo biochemical analyses to identify and characterize eight novel in vivo substrates of the ubiquitinating enzyme Rsp5, a homolog of the human ubiquitin-ligating enzyme Nedd4, in yeast. Our analysis of the effects of a deubiquitinating enzyme, Ubp2, demonstrated that an accumulation of Lys-63-linked polyubiquitin chains results in processed forms of two substrates, Sla1 and Ygr068c. Finally we showed that the localization of another newly identified substrate, Rnr2, is Rsp5-dependent. We believe that our approach constitutes a paradigm for the functional dissection of an enzyme with pleiotropic effects.

Indexed as

EndopeptidasesEndosomal Sorting Complexes Required for TransportHumansLysinePolyubiquitinProtein Processing, Post-TranslationalProteomeReproducibility of ResultsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitin-Protein Ligase ComplexesEndopeptidasesEndosomal Sorting Complexes Required for TransportLysinePolyubiquitinProteomeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsubiquitin-Nalpha-protein hydrolaseUbiquitin-Protein Ligase Complexes

Identifiers

PMID17951556
PMCPMC2861892
OpenAlexW2141721028

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.