Evidence map›Paper›PMID 29796789›Full record

ArticleJournal of biomolecular NMR2018

Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules.

Maureen Leninger, William M Marsiglia, Alexej Jerschow, Nathaniel J Traaseth

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Exploiting conformational dynamics to modulate the function of designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020
    Article
  8. Article
  9. Exchangeable deuterons introduce artifacts in amideJournal of biomolecular NMR · 2019
    Article
  10. Chemical Exchange.Methods in enzymology · 2019
    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

4 authors.

Maureen LeningerDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA.
William M MarsigliaDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA.
Alexej JerschowDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA.
Nathaniel J TraasethDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA. traaseth@nyu.edu.ORCID http://orcid.org/0000-0002-1185-6088

Funding

Mechanisms of Allostery and Molecular Recognition in the Small Multidrug Resistance FamilyR01AI108889 · NIAID · NEW YORK UNIVERSITY · PI Nathaniel J. Traaseth · 2014 to 2026
$5.4M
Isolating CEST from MT Asymmetry in MRIR01EB016045 · NIBIB · NEW YORK UNIVERSITY · PI JERSCHOW, ALEXEJ · 2013 to 2016
$1.4M
FGF Receptor Structure, Dynamics and FunctionR01GM117118 · NIGMS · NEW YORK UNIVERSITY · PI TRAASETH, NATHANIEL J. · 2017 to 2020
$1.3M
Acquisition of a Cryoprobe for a 600 MHz NMR SpectrometerS10OD016343 · OD · NEW YORK UNIVERSITY · PI KROGSGAARD, MICHELLE, TRAASETH, NATHANIEL J. · 2014 to 2014
$360k
Mechanisms of resistance and activation conferred by kinases displaying hinge and gate-keeper mutationsF99CA212474 · NCI · NEW YORK UNIVERSITY · PI MARSIGLIA, WILLIAM M · 2016 to 2017
$89k
National Science Foundation MCB1506420NCI NIH HHS F99 CA212474NIAID NIH HHS R01 AI108889NIBIB NIH HHS R01 EB016045NIGMS NIH HHS R01 GM117118NIH HHS F99CA212474NIH HHS OD016343NIH HHS R01AI108889NIH HHS R01EB016045NIH HHS R01GM117118NIH HHS S10 OD016343
6 · The paper itself

Abstract

Exchange between conformational states is required for biomolecular catalysis, allostery, and folding. A variety of NMR experiments have been developed to quantify motional regimes ranging from nanoseconds to seconds. In this work, we describe an approach to speed up the acquisition of chemical exchange saturation transfer (CEST) experiments that are commonly used to probe millisecond to second conformational exchange in proteins and nucleic acids. The standard approach is to obtain CEST datasets through the acquisition of a series of 2D correlation spectra where each experiment utilizes a single saturation frequency to

Indexed as

Molecular Dynamics SimulationMolecular ConformationMotionNuclear Magnetic Resonance, BiomolecularPhospholipase C gammaProteinssrc Homology DomainsTime FactorsPhospholipase C gammaProteinsCESTFast data acquisitionProteinsSensitivity enhancementSolution NMR

Identifiers

PMID29796789
PMCPMC5989009

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.