Evidence map›Paper›PMID 28708092›Full record

ReviewMolecules (Basel, Switzerland)2017

The Exact Nuclear Overhauser Enhancement: Recent Advances.

Parker J Nichols, Alexandra Born, Morkos A Henen, Dean Strotz, Julien Orts, Simon Olsson, Peter Güntert, Celestine N Chi, Beat Vögeli

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2017. 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
1.3field-weighted citation impact, top 20% 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, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Protein Allostery at Atomic Resolution.Angewandte Chemie (International ed. in English) · 2020
    Article
  12. Article
  13. Article
  14. Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019
    Article
  15. Efficient Stereospecific HMagnetochemistry (Basel, Switzerland) · 2018
    Article
  16. 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

9 authors at 6 institutions in 6 countries.

Parker J NicholsDepartment of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA. parker.nichols@ucdenver.edu.
Alexandra BornDepartment of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA. alexandra.born@ucdenver.edu.
Morkos A HenenDepartment of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA. morkos.henen@ucdenver.edu.
Dean StrotzLaboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich 8093, Switzerland. dean.strotz@phys.chem.ethz.ch.
Julien OrtsLaboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich 8093, Switzerland. julien.orts@phys.chem.ethz.ch.
Simon OlssonDepartment of Mathematics and Computer Science, Freie Universität Berlin, Arnimallee 6, Berlin 14195, Germany. solsson@zedat.fu-berlin.de.
Peter GüntertLaboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich 8093, Switzerland. guentert@em.uni-frankfurt.de.
Celestine N ChiDepartment of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, Uppsala SE-75123, Sweden. chi.celestine@imbim.uu.se.
Beat VögeliDepartment of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA. beat.vogeli@ucdenver.edu.
University of Colorado Anschutz Medical Campus · USETH Zurich · CHFreie Universität Berlin · DEGoethe University Frankfurt · DEMansoura University · EGUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although often depicted as rigid structures, proteins are highly dynamic systems, whose motions are essential to their functions. Despite this, it is difficult to investigate protein dynamics due to the rapid timescale at which they sample their conformational space, leading most NMR-determined structures to represent only an averaged snapshot of the dynamic picture. While NMR relaxation measurements can help to determine local dynamics, it is difficult to detect translational or concerted motion, and only recently have significant advances been made to make it possible to acquire a more holistic representation of the dynamics and structural landscapes of proteins. Here, we briefly revisit our most recent progress in the theory and use of exact nuclear Overhauser enhancements (eNOEs) for the calculation of structural ensembles that describe their conformational space. New developments are primarily targeted at increasing the number and improving the quality of extracted eNOE distance restraints, such that the multi-state structure calculation can be applied to proteins of higher molecular weights. We then review the implications of the exact NOE to the protein dynamics and function of cyclophilin A and the WW domain of Pin1, and finally discuss our current research and future directions.

Indexed as

Amino Acid SequenceCyclophilin AHumansKineticsModels, MolecularMolecular Dynamics SimulationMolecular StructureMotionNIMA-Interacting Peptidylprolyl IsomeraseNuclear Magnetic Resonance, BiomolecularProtein ConformationStructure-Activity RelationshipCyclophilin ANIMA-Interacting Peptidylprolyl Isomeraseallosterybiological macromoleculesconformational spacecorrelated dynamicsdynamicsexact NOENMRproteinsstructure calculationstructure ensemble

Identifiers

PMID28708092
PMCPMC6152122
OpenAlexW2735527796

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.