Evidence map›Paper›PMID 21942715›Full record

ArticleJournal of proteome research2011

Proteomic dissection of the von Hippel-Lindau (VHL) interactome.

Yanlai Lai, Meihua Song, Kevin Hakala, Susan T Weintraub, Yuzuru Shiio

Abstract read
In one paragraph

Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 44 citations in OpenAlex.

  1. Rescuing the Function of Missense-Mutated Tumor SuppressorbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Interaction with p53 explains a pro-proliferative function for VHL in cancer.Journal of molecular medicine (Berlin, Germany) · 2020
    Article
  9. The long form of pVHL is artifactually modified by serine protease inhibitor AEBSF.Protein science : a publication of the Protein Society · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Metastatic Renal Cell Cancer-Systemic Therapy.Indian journal of surgical oncology · 2018
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

5 authors at 2 institutions in 1 country.

Yanlai LaiThe University of Texas Health Science Center , San Antonio, TX 78229-3900, USA.
Meihua Song
Kevin Hakala
Susan T Weintraub
Yuzuru Shiio
The University of Texas Health Science Center at San Antonio · USThe University of Texas Health Science Center · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
Analysis of the VHL-HIF hydroxylase pathwayR01CA125020 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI SHIIO, YUZURU · 2007 to 2011
$1.1M
NCI NIH HHS CA054174NCI NIH HHS CA125020NCI NIH HHS P30 CA054174NCI NIH HHS R01 CA125020
6 · The paper itself

Abstract

The von Hippel-Lindau (VHL) tumor suppressor gene encodes a component of a ubiquitin ligase complex containing elongin B, elongin C, cullin 2, and Rbx1, which acts as a negative regulator of hypoxia inducible factor (HIF). VHL ubiquitinates and degrades the alpha subunits of HIF, and this is proposed to suppress tumorigenesis and tumor angiogenesis. Several lines of evidence also suggest important roles for HIF-independent VHL functions in the maintenance of primary cilium, extracellular matrix formation, and tumor suppression. We undertook a series of proteomic analyses to gain a comprehensive picture of the VHL-interacting proteins. We found that the ARF tumor suppressor interacts with VHL30, a longer VHL isoform, but not with VHL19, a shorter VHL isoform. ARF was found to release VHL30 from the E3 ligase complex, promoting the binding of VHL30 to a protein arginine methyltransferase, PRMT3. Our analysis of the VHL19 interactome also uncovered that VHL19 displays an affinity to collagens and their biosynthesis enzymes.

Indexed as

Protein Interaction MappingArginineCell Line, TumorCollagenCullin ProteinsElonginHEK293 CellsHumansMethylationProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein-Arginine N-MethyltransferasesProtein BindingProtein IsoformsProteomicsTranscription FactorsTumor Suppressor Protein p14ARFArginineCollagenCUL2 protein, humanCullin ProteinsELOB protein, humanELOC protein, humanElonginPRMT3 protein, humanProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein-Arginine N-MethyltransferasesProtein IsoformsTP53 protein, humanTranscription FactorsTumor Suppressor Protein p14ARFTumor Suppressor Protein p53Ubiquitin-Protein Ligase ComplexesVon Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID21942715
PMCPMC3208728
OpenAlexW2028489196

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.