Evidence map›Paper›PMID 11294893›Full record

ArticleMolecular biology of the cell2001

A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum.

R S Stewart, B Drisaldi, D A Harris

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.4field-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

37 citing papers in PubMed, 125 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Tetherin and its viral antagonists.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011
    Review
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

R S StewartDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
B Drisaldi
D A Harris
Washington University in St. Louis · US

Funding

MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASESR01NS035496 · NINDS · WASHINGTON UNIVERSITY · PI HARRIS, DAVID A · 1996 to 2002
$989k
NEUROPHARMACOLOGY RESEARCH TRAINING PROGRAMT32NS007129 · NINDS · WASHINGTON UNIVERSITY · PI JOHNSON, EUGENE M · 1985 to 2001
$248k
NINDS NIH HHS NS35496NINDS NIH HHS T32 NS007129NINDS NIH HHS T32-NS07129
6 · The paper itself

Abstract

Although there is considerable evidence that PrP(Sc) is the infectious form of the prion protein, it has recently been proposed that a transmembrane variant called (Ctm)PrP is the direct cause of prion-associated neurodegeneration. We report here, using a mutant form of PrP that is synthesized exclusively with the (Ctm)PrP topology, that (Ctm)PrP is retained in the endoplasmic reticulum and is degraded by the proteasome. We also demonstrate that (Ctm)PrP contains an uncleaved, N-terminal signal peptide as well as a C-terminal glycolipid anchor. These results provide insight into general mechanisms that control the topology of membrane proteins during their synthesis in the endoplasmic reticulum, and they also suggest possible cellular pathways by which (Ctm)PrP may cause disease.

Indexed as

Protein Sorting SignalsAnimalsCell LineCell MembraneCricetinaeCysteine EndopeptidasesEndoplasmic ReticulumGlycosylphosphatidylinositolsMembrane ProteinsMiceMultienzyme ComplexesMutagenesisPrionsProteasome Endopeptidase ComplexTumor Cells, Cultured(ctm)PrPCysteine EndopeptidasesGlycosylphosphatidylinositolsMembrane ProteinsMultienzyme ComplexesPrionsProteasome Endopeptidase ComplexProtein Sorting Signals

Identifiers

PMID11294893
PMCPMC32273
OpenAlexW2105134519

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.