Evidence map›Paper›PMID 1968466›Full record

ArticleThe Journal of cell biology1990

Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells.

D R Borchelt, M Scott, A Taraboulos, N Stahl, S B Prusiner

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

138 citing papers in PubMed, 504 citations in OpenAlex.

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  7. Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024
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78 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

D R BorcheltDepartment of Neurology, University of California, San Francisco 94143.
M Scott
A Taraboulos
N Stahl
S B Prusiner
University of California, San Francisco · US

Funding

VIRAL DEGENERATIVE DEMENTING DISEASE IN AGING (SUPP)P01AG002132 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 1985 to 2024
$51.7M
TRANSGENIC STUDIES OF SCRAPIE "STRAINS" AND CNS DEGENERATION BY MUTANT PRP GENESP50NS014069 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PRUSINER, STANLEY B · 1994 to 2002
$4.2M
PURIFICATION AND MOLECULAR STRUCTURE OF THE SCRAPIE AGENTP01NS014069 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PRUSINER, STANLEY B · 1985 to 1993
–
NIA NIH HHS AG02132NINDS NIH HHS NS07219NINDS NIH HHS NS14069
6 · The paper itself

Abstract

Both the cellular and scrapie isoforms of the prion protein (PrP) designated PrPc and PrPSc are encoded by a single-copy chromosomal gene and appear to be translated from the same 2.1-kb mRNA. PrPC can be distinguished from PrPSc by limited proteolysis under conditions where PrPC is hydrolyzed and PrPSc is resistant. We report here that PrPC can be released from the surface of both normal-control and scrapie-infected murine neuroblastoma (N2a) cells by phosphatidylinositol-specific phospholipase C (PIPLC) digestion and it can be selectively labeled with sulfo-NHS-biotin, a membrane impermeant reagent. In contrast, PrPSc was neither released by PIPLC nor labeled with sulfo-NHS-biotin. Pulse-chase experiments showed that [35S]methionine was incorporated almost immediately into PrPC while incorporation into PrPSc molecules was observed only during the chase period. While PrPC is synthesized and degraded relatively rapidly (t1/2 approximately 5 h), PrPSc is synthesized slowly (t1/2 approximately 15 h) and appears to accumulate. These results are consistent with several observations previously made on rodent brains where PrP mRNA and PrPC levels did not change throughout the course of scrapie infection, yet PrPSc accumulated to levels exceeding that of PrPC. Our kinetic studies demonstrate that PrPSc is derived from a protease-sensitive precursor and that the acquisition of proteinase K resistance results from a posttranslational event. Whether or not prolonged incubation periods, which are a cardinal feature of prion diseases, reflect the slow synthesis of PrPSc remains to be established.

Indexed as

AnimalsCell LineCell MembraneCell Transformation, ViralElectrophoresis, Polyacrylamide GelImmune SeraImmunoblottingKineticsMethionineMolecular WeightPrionsPrPSc ProteinsViral ProteinsImmune SeraMethioninePrionsPrPSc ProteinsViral Proteins

Identifiers

PMID1968466
PMCPMC2116048
OpenAlexW2167503783

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.