Author

O. Demir

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 Biophysics· 1 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 3 Approach:experimental assay· 3 Organism:human· 3 Approach:deep learning· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Organism:mouse· 1

Frequent Co-Authors

R. E. Amaro· 5 shared H. Aihara· 3 shared K. Shi· 3 shared D. A. Harki· 2 shared R. S. Harris· 2 shared S. Banerjee· 2 shared C. Belica· 1 shared C. Durfee· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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5 shared papersBiochemistry

R. E. Amaro

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Targeting N-Myc in Neuroblastoma with Selective Aurora Kinase A Degraders

J. Tang, R. Moorthy, O. Demir, Z. D. Baker, J. A. Naumann, K. F. M. Jones, M. J. Grillo, E. S. Haefner, K. Shi, M. J. Levy, H. Aihara, R. S. Harris, R. E. Amaro, N. M. Levinson, D. A. Harki

This study develops a first-in-class Aurora-A/N-Myc degrader, HLB-0532259, which effectively reduces N-Myc levels and shows tumor reduction in neuroblastoma models.

bioRxiv · Apr 9, 2022Cancer Biology

Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN

N. H. Moeller, K. Shi, O. Demir, S. Banerjee, L. Yin, C. Belica, C. Durfee, R. E. Amaro, H. Aihara

This study determines the structure of SARS-CoV-2 ExoN and its interaction with nsp10, revealing mechanisms of RNA substrate binding and exoribonuclease activity.

bioRxiv · Apr 2, 2021Biochemistry

Discovery of an IKK2 Site that Allosterically Controls Its Activation

S. J. Hotchkiss, M. C. Mulero, G. J. Chan, T. Biswas, S. Polley, C. Ohn, S. Konduri, O. Demir, R. E. Amaro, G. Ghosh

This paper identifies a novel allosteric site on IKK2 that can be targeted by small-molecule inhibitors to block its activity without ATP-competitive off-target effects.

bioRxiv · Jan 27, 2021 · PreprintBiochemistry

Markov State Models and NMR Uncover an Overlooked Allosteric Loop in p53

E. P. Barros, O. Demir, J. Soto, M. J. Cocco, R. E. Amaro

The paper uses Markov state models and NMR to study p53 mutations, revealing a previously overlooked allosteric loop involved in conformational dynamics and mutation-induced inactivation.

bioRxiv · Oct 19, 2020Biophysics

Active site plasticity and possible modes of chemical inhibition of the human DNA deaminase APOBEC3B

K. Shi, O. Demir, M. A. Carpenter, S. Banerjee, D. A. Harki, R. E. Amaro, R. S. Harris, H. Aihara

This study reports structures of APOBEC3B with loop 7 from APOBEC3G, revealing inactive conformations stabilized by small molecules, providing insights for inhibitor design.

bioRxiv · Jan 7, 2019Biochemistry