Evidence map›Paper›PMID 31713950›Full record

ReviewJournal of peptide science : an official publication of the European Peptide Society2019

Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.

Stefanie Hackl, Christian F W Becker

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of peptide science : an official publication of the European Peptide Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases.International journal of molecular sciences · 2020
    Review
  6. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019
    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

2 authors at 1 institution in 1 country.

Stefanie HacklUniversity of Vienna, Faculty of Chemistry, Institute of Biological Chemistry, Vienna, Austria.
Christian F W BeckerUniversity of Vienna, Faculty of Chemistry, Institute of Biological Chemistry, Vienna, Austria.ORCID https://orcid.org/0000-0002-8890-7082
University of Vienna · AT

Funding

Wien Kultur
6 · The paper itself

Abstract

Deciphering the pathophysiologic events in prion diseases is challenging, and the role of posttranslational modifications (PTMs) such as glypidation and glycosylation remains elusive due to the lack of homogeneous protein preparations. So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change of cellular prion protein (PrP

Indexed as

Protein FoldingProtein Processing, Post-TranslationalAnimalsHumansPrion DiseasesProtein Aggregation, PathologicalPrPC ProteinsPrPSc ProteinsPrPC ProteinsPrPSc Proteinsglycosylphosphatidylinositol (GPI) anchormembrane interactionprion protein (PrP)protein semisynthesis

Identifiers

PMID31713950
PMCPMC6899880
OpenAlexW2985903850

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.