Evidence map›Paper›PMID 27756047›Full record

ReviewCurrent opinion in structural biology2017

Visualizing the nanoscale: protein internal dynamics and neutron spin echo spectroscopy.

David Je Callaway, Zimei Bu

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 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. 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
  3. Article
  4. Article
  5. 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

2 authors.

David Je CallawayDepartment of Chemistry and Biochemistry, City College of New York, PhD Programs in Chemistry and Biochemistry, CUNY, United States.
Zimei BuDepartment of Chemistry and Biochemistry, City College of New York, PhD Programs in Chemistry and Biochemistry, CUNY, United States. Electronic address: dcallaway@ccny.cuny.edu.

Funding

Cellular/Molecular Basis of Development: Research CenterG12MD007603 · NIMHD · CITY COLLEGE OF NEW YORK · PI PEZZANO, MARK · 2012 to 2017
$11.5M
Hormonal Regulation of NHERF1 in BoneR01DK105811 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A · 2016 to 2019
$2.5M
NIDDK NIH HHS R01 DK105811NIMHD NIH HHS G12 MD007603
6 · The paper itself

Abstract

The most complex molecular machines are proteins found within cells. Protein dynamics, in particular dynamics on nanoscales, presents us with a novel paradigm for cell signaling: the idea that proteins and protein complexes can communicate directly within themselves to effect long-range information transfer, via coupled domains and correlated residue clusters. This idea has been little explored, in large part because of a paucity of experimental techniques that can address the necessary questions. Here we review recent progress in developing a promising new approach, neutron spin echo spectroscopy.

Indexed as

NeutronsAllosteric RegulationMovementNanotechnologyProteinsSpectrum AnalysisProteins

Identifiers

PMID27756047
PMCPMC5374024

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.