Author

R. D. Blind

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 4 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

P. Chapagain· 2 shared A. T. Hale· 1 shared C. D. Seacrist· 1 shared D. Desmarini· 1 shared D. Uredi· 1 shared E. A. Stivision· 1 shared G. A. Sowd· 1 shared H. Wang· 1 shared

Activity by Year

2018-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersPharmacology & Toxicology

P. Chapagain

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Author profile →

4 papers

Recent·Most cited

Design, synthesis and cellular characterization of a new class of IPMK kinase inhibitors

Y. Zhou, P. Chapagain, D. Desmarini, D. Uredi, L. E. Rameh Plant, J. T. Djordjevic, R. D. Blind, X. Wang

This study designs, synthesizes, and characterizes a new class of IPMK kinase inhibitors, showing reduced glioblastoma cell growth and a novel InsP5 metabolic signature.

bioRxiv · May 9, 2024Pharmacology & Toxicology

X-ray crystallographic analyses of 14 IPMK inhibitor complexes

H. Wang, R. D. Blind, S. B. Shears

The paper reports 14 new X-ray crystal structures of human IPMK complexed with inhibitors, revealing structural features like water molecules and an unoccupied pocket.

bioRxiv · May 9, 2024 · PreprintBiochemistry

IPMK regulates HDAC3 activity and histone H4 acetylation in human cells.

G. A. Sowd, E. A. Stivision, P. Chapagain, A. T. Hale, J. C. Poland, L. E. Rameh, R. D. Blind

This study shows IPMK regulates HDAC3 activity and histone H4 acetylation in human cells through inositol phosphate production.

bioRxiv · Apr 29, 2024 · PreprintBiochemistry

Crystallographic and kinetic analyses of human IPMK reveal disordered domains modulate ATP binding and kinase activity.

C. D. Seacrist, R. D. Blind

This study shows that disordered domains in IPMK modulate ATP binding and kinase activity through structural and kinetic analyses of a variant lacking these domains.

bioRxiv · Oct 3, 2018Biochemistry