Author

P. Barran

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

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Organism:human· 2 Approach:biophysical modeling· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Organism:plant (other)· 1

Frequent Co-Authors

A. Barkhanskiy· 1 shared A. Inga· 1 shared A. Karlen· 1 shared A. Krezel· 1 shared A. Okorokov· 1 shared A. R. Jones· 1 shared A. Theisen· 1 shared B. Bellina· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiochemistry

A. Barkhanskiy

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3 papers

Recent·Most cited

Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability and coordination dynamics of human metallothionein-2 species

M. P. Diaz, A. Barkhanskiy, E. Liggett, P. Barran, A. Krezel

The paper uses IM-MS and molecular dynamics simulations to study conformational stability and coordination dynamics of human metallothionein-2 species.

bioRxiv · Dec 1, 2022Biochemistry

Novel allosteric mechanism of dual p53/MDM2 and p53/MDM4 inhibition by a small molecule

V. Grinkevich, V. Aparna, K. Fawkner, N. Issaeva, V. Andreotti, E. R. Dickinson, E. Hedstrom, C. Spinnler, A. Inga, L.-G. Larsson, A. Karlen, M. Wilhelm, P. Barran, A. Okorokov, G. Selivanova, J. E. Zawacka-Pankau

This paper identifies a novel allosteric mechanism by which RITA and PpIX inhibit p53/MDM2 and p53/MDM4 interactions, offering a new approach for p53 reactivation in cancer therapy.

bioRxiv · Dec 24, 2021Biochemistry

Native Mass Spectrometry Reveals the Conformational Diversity of the UVR8 Photoreceptor

I. S. Camacho, A. Theisen, L. O. Johannissen, L. A. Diaz-Ramos, J. M. Christie, G. I. Jenkins, B. Bellina, P. Barran, A. R. Jones

This study uses native mass spectrometry to show that full-length UVR8 exists in multiple conformational states, unlike truncated versions, and identifies active conformations that bind COP1.

bioRxiv · Jul 18, 2018Biochemistry