Conformational selection: Vs. induced fit: Insights into the binding mechanisms of p38α MAP Kinase inhibitors
Chemical Communications, ISSN: 1364-548X, Vol: 56, Issue: 62, Page: 8818-8821
2020
- 8Citations
- 21Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations8
- Citation Indexes8
- CrossRef6
- Captures21
- Readers21
- 21
Article Description
The conformational dynamics of a kinase's activation loop have been challenging to assess due to the activation loop's intrinsic flexibility. To directly probe the conformational equilibrium of the activation loop of mitogen-activated protein kinase p38α, we present an approach based on site-directed spin labeling, electron paramagnetic resonance (EPR) distance restraints, and multilateration. We demonstrate that the activation loop of apo p38α resides in a highly flexible equilibrium state and we reveal that binding of small molecules significantly alters this equilibrium and the populated sub-states. This journal is
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85089162725&origin=inward; http://dx.doi.org/10.1039/d0cc02539a; http://www.ncbi.nlm.nih.gov/pubmed/32749403; https://xlink.rsc.org/?DOI=D0CC02539A; https://dx.doi.org/10.1039/d0cc02539a; https://pubs.rsc.org/en/content/articlelanding/2020/cc/d0cc02539a
Royal Society of Chemistry (RSC)
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