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Rieko Ishima

Researcher at University of Pittsburgh

Publications -  90
Citations -  3761

Rieko Ishima is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: HIV-1 protease & Protease. The author has an hindex of 31, co-authored 85 publications receiving 3546 citations. Previous affiliations of Rieko Ishima include University of Missouri & Ontario Institute for Cancer Research.

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Protein dynamics from NMR

TL;DR: This review surveys recent investigations of conformational fluctuations of proteins in solution using NMR techniques to illustrate that studies of protein dynamics provide insights into protein–protein interactions, target recognition, ligand binding, and enzyme function.
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Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function.

TL;DR: A working model of the flap-opening mechanism in free HIV-1 protease which involves a transition from a semi-open to an open conformation that is facilitated by interaction of the Phe53 ring with the substrate is presented.
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Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.

TL;DR: The NMR-derived structure of the homodimeric core domain of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions, is presented, revealing the molecular assembly of two active sites within the dimeric kinase.
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Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations.

TL;DR: This paper has obtained nearly complete backbone and many sidechain signal assignments of a fully active free‐protease construct that is stabilized against autoproteolysis by three point mutations, and characterized the secondary structure and fast (sub‐ns) dynamics of the flaps of the free protease in solution.
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Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach.

TL;DR: Relaxation compensated constant-time Carr–Purcell–Meiboom–Gill relaxation dispersion experiments for amide protons are presented that detect μs-ms time-scale dynamics of protein backbone amide sites.