Evidence map›Paper›PMID 28330994›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.

Kendra K Frederick, Vladimir K Michaelis, Marc A Caporini, Loren B Andreas, Galia T Debelouchina, Robert G Griffin, Susan Lindquist

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022
    Article
  8. Article
  9. Chemical reviews · 2022
    Review
  10. DNPSOUP: A simulation software package for dynamic nuclear polarization.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. 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
  19. Article
  20. 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

7 authors at 4 institutions in 1 country.

Kendra K FrederickWhitehead Institute for Biomedical Research, Cambridge, MA 02142; kendra.frederick@utsouthwestern.edu.
Vladimir K MichaelisDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Marc A CaporiniBruker BioSpin, Billerica, MA 01821.
Loren B AndreasDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.ORCID 0000-0003-3216-9065
Galia T DebelouchinaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Robert G GriffinDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Susan LindquistWhitehead Institute for Biomedical Research, Cambridge, MA 02142.
Massachusetts Institute of Technology · USBruker (United States) · USHoward Hughes Medical Institute · USWhitehead Institute for Biomedical Research · US

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
High Field DNP in Biological SystemsR01EB002804 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$9.1M
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
Howard Hughes Medical InstituteNIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB002804NIBIB NIH HHS R01 EB003151NIGMS NIH HHS R01 GM025874NIGMS NIH HHS R37 GM025874
6 · The paper itself

Abstract

The yeast prion protein Sup35NM is a self-propagating amyloid. Despite intense study, there is no consensus on the organization of monomers within Sup35NM fibrils. Some studies point to a β-helical arrangement, whereas others suggest a parallel in-register organization. Intermolecular contacts are often determined by experiments that probe long-range heteronuclear contacts for fibrils templated from a 1:1 mixture of

Indexed as

Isotope LabelingModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptide Termination FactorsProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptide Termination FactorsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeamyloiddynamic nuclear polarization[PSI+] prionsolid-state NMRSup35

Identifiers

PMID28330994
PMCPMC5389306
OpenAlexW2603426852

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.