Evidence map›Paper›PMID 26456111›Full record

ArticleCell2015

Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus.

Kendra K Frederick, Vladimir K Michaelis, Björn Corzilius, Ta-Chung Ong, Angela C Jacavone, Robert G Griffin, Susan Lindquist

Abstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Article
  7. Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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. Electronic address: kendra.frederick@utsouthwestern.edu.
Vladimir K MichaelisDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Björn CorziliusDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Ta-Chung OngDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Angela C JacavoneDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Robert G GriffinDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Susan LindquistWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Howard Hughes Medical Institute and 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
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
Solid State NMR Studies of Membrane ProteinsR01EB001960 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2017
$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 EB-002026NIBIB NIH HHS EB-002804NIBIB NIH HHS EB-003151NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB001960NIBIB NIH HHS R01 EB002804NIBIB NIH HHS R01 EB003151NIGMS NIH HHS GM-025874NIGMS NIH HHS R01 GM025874NIGMS NIH HHS R37 GM025874
6 · The paper itself

Abstract

Biological processes occur in complex environments containing a myriad of potential interactors. Unfortunately, limitations on the sensitivity of biophysical techniques normally restrict structural investigations to purified systems, at concentrations that are orders of magnitude above endogenous levels. Dynamic nuclear polarization (DNP) can dramatically enhance the sensitivity of nuclear magnetic resonance (NMR) spectroscopy and enable structural studies in biologically complex environments. Here, we applied DNP NMR to investigate the structure of a protein containing both an environmentally sensitive folding pathway and an intrinsically disordered region, the yeast prion protein Sup35. We added an exogenously prepared isotopically labeled protein to deuterated lysates, rendering the biological environment "invisible" and enabling highly efficient polarization transfer for DNP. In this environment, structural changes occurred in a region known to influence biological activity but intrinsically disordered in purified samples. Thus, DNP makes structural studies of proteins at endogenous levels in biological contexts possible, and such contexts can influence protein structure.

Indexed as

Amino Acid SequenceMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide Termination FactorsPrionsProtein FoldingProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID26456111
PMCPMC4621972

What OpenQuestion holds

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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.