ReviewJournal of magnetic resonance (San Diego, Calif. : 1997)2019
Protein NMR: Boundless opportunities.
Review in Journal of magnetic resonance (San Diego, Calif. : 1997), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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.
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.
Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026Article
- Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026Review
- Detection of intramolecular protein dynamics on nanosecond-to-microsecond timescales by nanoparticle-assisted NMR spin relaxation (NASR).Nature protocols · 2026Review
- Application of NMR to Large RNAs.Journal of molecular biology · 2025Review
- Resurgence of magnetic resonance techniques in the era of AlphaFold.Biophysical reviews · 2025Review
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Synthesis of aChembiochem : a European journal of chemical biology · 2025Article
- Reformulation of the protein databank for real-time search of geometrical attributes of protein structures.Frontiers in molecular biosciences · 2025Article
- Is there reversible dimerization of albumin in blood plasma? And does it matter?Experimental physiology · 2024Review
- Quantitative Characterization of Chain-Flipping of Acyl Carrier Protein ofJournal of the American Chemical Society · 2024Article
- Protein Interactions inMolecules (Basel, Switzerland) · 2023Article
- Exploiting conformational dynamics to modulate the function of designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2023Article
- Hysteresis behavior in the unfolding/refolding processes of a protein trapped in metallo-cages.Chemical science · 2023Article
- Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble.Scientific reports · 2022Article
- Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins.Journal of biomolecular NMR · 2022Article
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- High ResolutionFrontiers in molecular biosciences · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Over the past approximately three decades, isotope-directed NMR spectroscopy has become a powerful method for determining 3D structures of biological macromolecules and their complexes in solution. From a structural perspective NMR provides an invaluable tool for studying systems that are not amenable to crystallization, including intrinsically disordered proteins and weak complexes. In contrast to both X-ray crystallography and cryo-electron microscopy which afford a largely static view of the systems under consideration, the great power of NMR lies in its ability to quantitatively probe exchange dynamics between interconverting states, and to reveal and characterize at atomic resolution the existence of transient states that may be populated at levels as low as 1%. Such "excited" states play a key role in macromolecular recognition, allostery, signal transduction and macromolecular assembly, including the initial events involved in aggregation and amyloid formation. Optimal application of NMR to such systems of fundamental biological interest requires a sound footing of the physical underpinnings of today's and tomorrow's sophisticated NMR experiments.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.