Evidence map›Paper›PMID 19639158›Full record

ArticlePhysical chemistry chemical physics : PCCP2009

Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation.

Anna Pavlova, Evan R McCarney, Dylan W Peterson, Frederick W Dahlquist, John Lew, Songi Han

Abstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Efficient assignment and NMR analysis of an intact virus using sequential side-chain correlations and DNP sensitization.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Anomalously Rapid Hydration Water Diffusion Dynamics Near DNA Surfaces.Journal of the American Chemical Society · 2015
    Article
  11. Hydration water mobility is enhanced around tau amyloid fibers.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  12. Probing water density and dynamics in the chaperonin GroEL cavity.Journal of the American Chemical Society · 2014
    Article
  13. Review
  14. Overhauser Dynamic Nuclear Polarization-Enhanced NMR Relaxometry.Microporous and mesoporous materials : the official journal of the International Zeolite Association · 2013
    Article
  15. Article
  16. 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

6 authors at 1 institution in 1 country.

Anna PavlovaDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA.
Evan R McCarney
Dylan W Peterson
Frederick W Dahlquist
John Lew
Songi Han
University of California, Santa Barbara · US

Funding

MECHANISTIC STUDIES OF BACTERIAL CHEMOTAXISR01GM059544 · NIGMS · UNIVERSITY OF OREGON · PI DAHLQUIST, FREDERICK W. · 1999 to 2018
$4.8M
NIGMS NIH HHS R01 GM059544
6 · The paper itself

Abstract

We present a generally applicable approach for monitoring protein aggregation by detecting changes in surface hydration water dynamics and the changes in solvent accessibility of specific protein sites, as protein aggregation proceeds in solution state. This is made possible through the Overhauser dynamic nuclear polarization (DNP) of water interacting with stable nitroxide spin labels tethered to specific proteins sites. This effect is highly localized due to the magnetic dipolar nature of the electron-proton spin interaction, with >80% of their interaction occurring within 5 A between the unpaired electron of the spin label and the proton of water. We showcase our tool on the aggregation of tau proteins, whose fibrillization is linked to neurodegenerative disease pathologies known as taupathies. We demonstrate that the DNP approach to monitor local changes in hydration dynamics with residue specificity and local contrast can distinguish specific and neat protein-protein packing leading to fibers from non-specific protein agglomeration or precipitation. The ability to monitor tau assembly with local, residue-specific, resolution, under ambient conditions and in solution state will help unravel the mechanism and structural characteristics of the gradual process of tau aggregation into amyloid fibers, which remains unclear to this day.

Indexed as

Amino Acid SubstitutionAmyloidElectron Spin Resonance SpectroscopyHumansPeptide FragmentsProtein BindingProtein IsoformsProteinsRecombinant ProteinsSpin Labelstau ProteinsWaterAmyloidPeptide FragmentsProtein IsoformsProteinsRecombinant ProteinsSpin Labelstau ProteinsWater

Identifiers

PMID19639158
PMCPMC3153360
OpenAlexW2006087142

What OpenQuestion holds

Textmetadata
LicenceTDM
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.