Evidence map›Paper›PMID 27576687›Full record

ArticleThe Journal of biological chemistry2016

N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways.

Yiming Wang, Qing Shao, Carol K Hall

Erratum issuedAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Anatomy of a selectively coassembled β-sheet peptide nanofiber.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Article
  10. Thermodynamic phase diagram of amyloid-β (16-22) peptide.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP(120-144).Protein science : a publication of the Protein Society · 2018
    Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Yiming WangFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina, 27695-7905.
Qing ShaoFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina, 27695-7905.
Carol K HallFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina, 27695-7905 hall@ncsu.edu.

Funding

Biotechnology Research Partnerships Renewal: Aggregation of Therapeutic ProteinsR01EB006006 · NIBIB · UNIVERSITY OF COLORADO · PI RANDOLPH, THEODORE W · 2006 to 2017
$7.2M
COMPUTER SIMULATION STUDIES OF PROTEIN AGGREGATIONR01GM056766 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI HALL, CAROL K · 1999 to 2009
$1.4M
NIBIB NIH HHS R01 EB006006NIGMS NIH HHS R01 GM056766
6 · The paper itself

Abstract

The prion diseases are a family of fatal neurodegenerative diseases associated with the misfolding and accumulation of normal prion protein (PrP

Indexed as

Protein AggregatesAmyloidAnimalsArvicolinaeCricetinaeHumansMesocricetusProtein Structure, SecondaryPrPC ProteinsAmyloidProtein AggregatesPrPC Proteinsamino acid substitutionamyloid corediscontinuous molecular dynamicsfibrilkineticsprion diseaseprotein aggregationthermodynamics

Identifiers

PMID27576687
PMCPMC5063992

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.