Evidence map›Paper›PMID 23884624›Full record

ArticleThe European physical journal. E, Soft matter2013

Nanoscale protein dynamics: a new frontier for neutron spin echo spectroscopy.

David J E Callaway, Bela Farago, Zimei Bu

Abstract read
PubMed Publisher
In one paragraph

Article in The European physical journal. E, Soft matter, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  3. Article
  4. Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Editorial on the topical issue "neutron biological physics".The European physical journal. E, Soft matter · 2013
    Article
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

3 authors.

David J E CallawayDepartment of Chemistry, the City College of New York, New York, NY 10031, USA. dcallaway@ccny.cuny.edu
Bela Farago
Zimei Bu

Funding

Struture snd Dynamic Determinants of Ion Channel Assembly by Adapter ProteinsR01HL086496 · NHLBI · RESEARCH INST OF FOX CHASE CAN CTR · PI BU, ZIMEI · 2007 to 2011
$2.1M
NHLBI NIH HHS R01 HL086496
6 · The paper itself

Abstract

Recent studies show that neutron spin echo spectroscopy (NSE) can reveal long-range protein domain motions on nanometer lengthscales and on nanosecond to microsecond timescales. This unique capability of NSE provides new opportunities to understand protein dynamics and functions, such as how binding signals are propagated in a protein to distal sites. Here we review our applications of NSE to the study of nanoscale protein domain motions in a set of cell signaling proteins. We summarize the theoretical framework we have developed, which allows one to interpret the NSE data (Biophys. J. 99, 3473 (2010) and Proc. Natl. Acad. Sci. USA 102, 17646 (2005)). Our theoretical framework uses simple concepts from nonequilibrium statistical mechanics, and does not require elaborate molecular dynamics simulations, complex fits to rotational motion, or elastic network models. It is thus more robust than multiparameter techniques that require untestable assumptions. We also demonstrate our experimental scheme involving deuterium labeling of a protein domain or a subunit in a protein complex. We show that our selective deuteration scheme can highlight and resolve specific domain dynamics from the abundant global translational and rotational motions in a protein. Our approach thus clears significant hurdles to the application of NSE for the study of protein dynamics in solution.

Indexed as

Molecular Dynamics SimulationAnimalsNeutron DiffractionPhosphoproteinsProtein BindingProtein Structure, TertiaryScattering, Small AngleSodium-Hydrogen ExchangersPhosphoproteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

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.