Author

A. A. Bobkov

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

Biology Disciplines

Click to filter author papers

Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Assay:protein structure· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 2 Approach:statistical model· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

C. D. Sohl· 2 shared F. M. Marassi· 2 shared J. M. Schiffer· 2 shared W. Im· 2 shared Y. Yao· 2 shared A. E. Aleshin· 1 shared A. Hoang· 1 shared A. Iftikar· 1 shared

Activity by Year

2020-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiochemistry

C. D. Sohl

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Active site remodeling in IDH1 mutants drives distinct kinetic and potential resistance mechanisms

M. Mealka, N. A. Sierra, D. A. Matteo, E. Albekioni, R. Khoury, T. Mai, B. M. Conley, N. J. Coleman, K. A. Sabo, E. A. Komives, A. A. Bobkov, A. L. Cooksy, S. Silletti, J. M. Schiffer, T. Huxford, C. D. Sohl

This study compares the reaction mechanisms of two IDH1 mutants, finding that R132Q has optimized active site conformation for both conventional and neomorphic activity, potentially explaining resistance to inhibitors.

bioRxiv · Jan 10, 2024Biochemistry

Design of novel Cyanovirin-N variants by modulation of binding dynamics through distal mutations

I. C. Kazan, P. Sharma, M. I. Rahman, A. A. Bobkov, R. Fromme, G. Ghirlanda, S. B. Ozkan

The paper introduces an ICDC approach to identify distal mutations that modulate protein function through dynamic allostery, validated on TEM-1 β-lactamase and applied to Cyanovirin-N.

bioRxiv · Dec 21, 2020Biophysics

Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids

A. E. Aleshin, Y. Yao, A. Iftikar, A. A. Bobkov, J. Yu, G. Cadwell, M. Klein, C. Dong, L. A. Bankston, R. C. Liddington, W. Im, G. Powis, F. M. Marassi

This study determines the atomic structure of PLEKHA7's PH domain and reveals its multivalent interaction mechanism with membrane-bound PIPs, providing insights for inhibitor design.

bioRxiv · Nov 25, 2020Biochemistry

An acidic residue buried in the dimer interface of isocitrate dehydrogenase 1 (IDH1) helps regulate catalysis and pH sensitivity

L. A. Luna, Z. Lesecq, K. A. White, A. Hoang, D. A. Scott, O. Zagnitko, A. A. Bobkov, D. L. Barber, J. M. Schiffer, D. G. Isom, C. D. Sohl

This paper identifies an acidic residue in IDH1 that regulates catalysis and pH sensitivity through conformational changes.

bioRxiv · Apr 19, 2020Biochemistry

Conformational states of the cytoprotective protein Bcl-xL

P. Ryzhov, Y. Tian, Y. Yao, A. A. Bobkov, W. Im, F. M. Marassi

This study investigates the conformational states of full-length Bcl-xL in soluble and membrane-anchored forms using NMR, MD simulations, and ITC to understand its structure and ligand binding.

bioRxiv · Mar 25, 2020Biophysics