Evidence map›Paper›PMID 24485763›Full record

ArticleChemistry & biology2014

Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.

Kendra K Frederick, Galia T Debelouchina, Can Kayatekin, Tea Dorminy, Angela C Jacavone, Robert G Griffin, Susan Lindquist

Abstract read
In one paragraph

Article in Chemistry & biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
  13. Michler's hydrol blue elucidates structural differences in prion strains.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Classifying the Binding Modes of Disordered Proteins.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020
    Review
  18. Review
  19. Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Kendra K FrederickWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Galia T DebelouchinaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Francis Bitter Magnet Labaratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Can KayatekinWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Tea DorminyDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Angela C JacavoneDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Francis Bitter Magnet Labaratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Robert G GriffinDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Francis Bitter Magnet Labaratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Susan LindquistWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: lindquist_admin@wi.mit.edu.

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Solid State NMR Studies of Peptides and ProteinsR01EB003151 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2004 to 2015
$6.5M
THE FUNCTION OF HEAT SHOCK RESPONSE IN DROSOPHILAR01GM025874 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI WHITESELL, LUKE J · 1985 to 2016
$4.7M
CHAPERONE PROTEIN AND PROTEIN CONFORMATIONAL SWITCHESR37GM025874 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI LINDQUIST, SUSAN L. · 1997 to 2006
$2.7M
NIBIB NIH HHS EB002026NIBIB NIH HHS EB003151NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB003151NIGMS NIH HHS GM025874NIGMS NIH HHS R01 GM025874NIGMS NIH HHS R37 GM025874
6 · The paper itself

Abstract

Yeast prions are self-templating protein-based mechanisms of inheritance whose conformational changes lead to the acquisition of diverse new phenotypes. The best studied of these is the prion domain (NM) of Sup35, which forms an amyloid that can adopt several distinct conformations (strains) that produce distinct phenotypes. Using magic-angle spinning nuclear magnetic resonance spectroscopy, we provide a detailed look at the dynamic properties of these forms over a broad range of timescales. We establish that different prion strains have distinct amyloid structures, with many side chains in different chemical environments. Surprisingly, the prion strain with a larger fraction of rigid residues also has a larger fraction of highly mobile residues. Differences in mobility correlate with differences in interaction with the prion-partitioning factor Hsp104 in vivo, perhaps explaining strain-specific differences in inheritance.

Indexed as

Amino Acid SequenceAmyloidBinding SitesMolecular ChaperonesMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide Termination FactorsPrionsProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidMolecular ChaperonesPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID24485763
PMCPMC4030713

What OpenQuestion holds

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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.