Author

Rieko Ishima

University of PittsburghORCID 0000-0002-3418-0922Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Alexander B. TayloriD· 1 shared Andrew P. HinckiD· 1 shared Ari M. SelzeriD· 1 shared Carlos Jaime CamachoiD· 1 shared Caroline S. HilliD· 1 shared Chang‐Hyeock ByeoniD· 1 shared Cynthia S. HinckiD· 1 shared Daniel J. BernardiD· 1 shared

Activity by Year

2018-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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1 shared paperBiophysics

Alexander B. TaylorORCID

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3 papers

Recent·Most cited

Structures of TGF-beta with betaglycan and the signaling receptors reveal the mechanism whereby betaglycan potentiates receptor complex assembly and signaling

Łukasz Wieteska, Alexander B. Taylor, Emma K. Punch, Jonathan A. Coleman, Isabella O. Conway, Yeu‐Farn Lin, Chang‐Hyeock Byeon, Cynthia S. Hinck, Troy C. Krzysiak, Rieko Ishima, Fernando López‐Casillas, Peter Cherepanov, Daniel J. Bernard, Caroline S. Hill, Andrew P. Hinck

This study determines the structure of TGF-beta bound to betaglycan and its signaling receptors, revealing mechanisms of ligand selectivity and signal potentiation.

Nature Communications · Feb 26, 2025Peer-reviewedBiophysics

An SH3-binding allosteric modulator stabilizes the global conformation of the AML-associated Src-family kinase, Hck

Ari M. Selzer, Gabriella Gerlach, Giancarlo Gonzalez-Areizaga, Thomas E. Wales, Stephanie Y. Cui, Prema C. Iyer, John R. Engen, Carlos Jaime Camacho, Rieko Ishima, Thomas E. Smithgall

This study identifies PDA1 as an SH3-binding allosteric modulator that stabilizes Hck conformation, potentially enhancing combination therapy with ATP-site inhibitors.

Journal of Biological Chemistry · Dec 13, 2024Peer-reviewedPharmacology & Toxicology

An inhibitor-interaction intermediate of HIV-1 protease, revealed by Isothermal Titration Calorimetry and NMR spectroscopy

Shahid N Khan, John D Persons, Michel Guerrero, Tatiana V. Ilina, Masayuki Oda, Rieko Ishima

The paper investigates entropy-enthalpy compensation in HIV-1 protease mutants using ITC and NMR, revealing an inhibitor-bound intermediate pathway.

bioRxiv · Sep 4, 2018 · PreprintBiochemistry