The DOI matches its Crossref record; 208 of the 208 references it cites were found in a registry or an index.
Protein-Inhibitor Interaction Studies Using NMR
Open accessAbstract
Solution-state NMR has been widely applied to determine the three-dimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.
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“The crystal structure of RT with a hydroxytropolone inhibitor, β-thujaplicinol, showed the inhibitor in the active-site with chelation of two Mn2+ (Figure 5a) and prompted postulation on how RNA/DNA substrate interaction with the inhibitors may occur, providing insight into the mechanism of inhibition [77].”
From Retroviral RNase H: structure, mechanism, and inhibition (2021) · cites this paper as [77]
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Items 201–208 of 208
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Are methyl groups relaxation sinks in small proteins?
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The effects of RNase H inhibitors and nevirapine on the susceptibility of HIV-1 to AZT and 3TC
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Sorted by citations
Retroviral RNase H: structure, mechanism, and inhibition
(2021) · The Enzymes · doi:10.1016/bs.enz.2021.07.007 · Cited by 13
Self-citationKarki, I., Christen, M. T., Spiriti, J., Slack, R. L., Oda, M., Kanaori, K., Zuckerman, D. M., & Ishima, R. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b08323 · Cited by 5
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Metadata
- Authors
- Ishima, R.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Ishima, Rieko
- ORCID
- Ishima, Rieko
- Venue
- Applications of NMR Spectroscopy
- Publisher
- BENTHAM SCIENCE PUBLISHERS
- Published
- 2015-02-09
- Volume
- 1
- Pages
- 143-181
- PMC
- PMC4562695
- OpenAlex
- W654319949
- Cited by
- 13
- References
- 208
- Citations by year
- 2023: 1 · 2021: 3 · 2020: 3 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 3
- FWCI
- 2.81
- Type
- book chapter
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- BENTHAM SCIENCE PUBLISHERS eBooks (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM105401)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- protein-inhibitor interactions, protein-ligand interactions, solution NMR, protein structure determination, protein dynamics, structural biology
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