Evidence map›Paper›PMID 32535973›Full record

ArticleProtein science : a publication of the Protein Society2020

The long form of pVHL is artifactually modified by serine protease inhibitor AEBSF.

Daniel Tarade, Shelley He, Jonathan St-Germain, Avi Petroff, Anya Murphy, Brian Raught, Michael Ohh

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 94% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. The long form of pVHL is artifactually modified by serine protease inhibitor AEBSF.Protein science : a publication of the Protein Society · 2020
    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

7 authors at 2 institutions in 1 country.

Daniel TaradeDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0001-7029-9640
Shelley HeDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Toronto, Ontario, Canada.
Jonathan St-GermainPrincess Margaret Cancer Centre, University Health Network and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Avi PetroffDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Toronto, Ontario, Canada.
Anya MurphyDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Toronto, Ontario, Canada.
Brian RaughtPrincess Margaret Cancer Centre, University Health Network and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Michael OhhDepartment of Laboratory Medicine & Pathobiology, University of Toronto, Toronto, Ontario, Canada.
University of Toronto · CAUniversity Health Network · CA

Funding

CIHR PJT‐159773
6 · The paper itself

Abstract

von Hippel-Lindau protein (pVHL) is the tumor suppressor responsible for ubiquitylating the hypoxia-inducible factor (HIF) family of transcription factors for degradation under normoxic conditions. There are two major pVHL isoforms with the shorter isoform (pVHL

Indexed as

HumansIsoenzymesProtein DomainsSulfonesVon Hippel-Lindau Tumor Suppressor Protein4-(2-aminoethyl)benzenesulfonylfluorideIsoenzymesSulfonesVHL protein, humanVon Hippel-Lindau Tumor Suppressor ProteinAEBSFgel electrophoresishypoxia-inducible factor (HIF)isoform-specificserine protease inhibitorvon Hippel-Lindau (VHL)

Identifiers

PMID32535973
PMCPMC7380668
OpenAlexW3034412186

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.