Evidence map›Paper›PMID 28643003›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2018

Recent developments in solution nuclear magnetic resonance (NMR)-based molecular biology.

Joshua J Ziarek, Diego Baptista, Gerhard Wagner

Abstract readReview
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2018. 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
–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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Distance-Dependence of Photo-CIDNP in Biomimetic Tryptophan-Flavin Diads.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Metabolomics and NMR.Handbook of experimental pharmacology · 2023
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Chemical tools for membrane protein structural biology.Current opinion in structural biology · 2019
    Review
  16. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    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

3 authors.

Joshua J ZiarekDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA.
Diego BaptistaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA. gerhard_wagner@hms.harvard.edu.

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
Roles of Eukaryotic Translation Initiation Factors in Gene ExpressionR01CA200913 · NCI · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2016 to 2020
$2.3M
Deciphering GPCR signal transduction through NMR structure and dynamics studiesK99GM115814 · NIGMS · HARVARD MEDICAL SCHOOL · PI ZIAREK, JOSHUA JAMES · 2015 to 2016
$180k
NCI NIH HHS R01 CA200913NIGMS NIH HHS K99 GM115814NIGMS NIH HHS P01 GM047467
6 · The paper itself

Abstract

Visualizing post-translational modifications, conformations, and interaction surfaces of protein structures at atomic resolution underpins the development of novel therapeutics to combat disease. As computational resources expand, in silico calculations coupled with experimentally derived structures and functional assays have led to an explosion in structure-based drug design (SBDD) with several compounds in clinical trials. It is increasingly clear that "hidden" transition-state structures along activation trajectories can be harnessed to develop novel classes of allosteric inhibitors. The goal of this mini-review is to empower the clinical researcher with a general knowledge of the strengths and weaknesses of nuclear magnetic resonance (NMR) spectroscopy in molecular medicine. Although NMR can determine protein structures at atomic resolution, its unrivaled strength lies in sensing subtle changes in a nuclei's chemical environment as a result of intrinsic conformational dynamics, solution conditions, and binding interactions. These can be recorded at atomic resolution, without explicit structure determination, and then incorporated with static structures or molecular dynamics simulations to produce a complete biological picture.

Indexed as

Magnetic Resonance SpectroscopyDrug DiscoveryConformational dynamicsIntegral membrane proteinsIntrinsically disordered proteinsLow-gamma nuclei detection

Identifiers

PMID28643003
PMCPMC5742078

What OpenQuestion holds

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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.