Author

Y. B. Slonimskiy

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· 6 Biophysics· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Research Focus:protein folding & dynamics· 7 Assay:protein structure· 5 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

E. G. Maksimov· 11 shared N. N. Sluchanko· 11 shared T. Friedrich· 6 shared N. A. Egorkin· 4 shared A. B. Rubin· 3 shared G. V. Tsoraev· 3 shared K. E. Klementiev· 3 shared K. M. Boyko· 3 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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11 shared papersBiochemistry

E. G. Maksimov

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11 papers

Recent·Most cited

Structural framework for the understanding spectroscopic and functional signatures of the cyanobacterial Orange Carotenoid Protein families

N. N. Sluchanko, E. G. Maksimov, Y. B. Slonimskiy, L. A. Varfolomeeva, A. Y. Bukhanko, N. A. Egorkin, G. V. Tsoraev, M. G. Khrenova, B. Ge, S. Qin, K. M. Boyko, V. O. Popov

The paper presents the first crystal structures of OCP2 from different cyanobacteria and compares them with OCP1 and OCP3 to correlate structural features with spectroscopic and functional properties.

bioRxiv · Aug 20, 2023Biochemistry

Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP

F. D. Kornilov, Y. B. Slonimskiy, D. A. Lunegova, N. A. Egorkin, A. G. Savitskaya, S. Y. Kleymenov, E. G. Maksimov, S. A. Goncharuk, K. S. Mineev, N. N. Sluchanko

This paper determines the structure of AstaP, a carotenoid-binding protein, and explains its ligand promiscuity through structural and biochemical analyses.

bioRxiv · Dec 26, 2022 · PreprintBiochemistry

Nanocontainer derived from silkworm carotenoprotein for carotenoid extraction and presentation in biotechnology and biomedical applications

N. N. Sluchanko, Y. B. Slonimskiy, N. A. Egorkin, L. A. Varfolomeeva, S. Y. Kleymenov, M. E. Minyaev, A. M. Moysenovich, E. Y. Parshina, T. Friedrich, E. G. Maksimov, K. M. Boyko, V. O. Popov

This study characterizes the structure and function of BmCBP, a silkworm carotenoprotein, showing its ability to bind and deliver carotenoids for biomedical applications.

bioRxiv · Jun 28, 2022 · PreprintBiochemistry

Crystal structure and functional peculiarities of a primordial Orange Carotenoid Protein (OCPX)

Y. B. Slonimskiy, A. O. Zupnik, L. A. Varfolomeeva, K. M. Boyko, E. G. Maksimov, N. N. Sluchanko

The paper presents the first crystal structure of OCPX and compares it with OCP1, revealing structural and functional differences that explain its unique photoprotection mechanism.

bioRxiv · Jun 14, 2022 · PreprintBiochemistry

Microalgal protein AstaP is a potent carotenoid solubilizer and delivery module with a broad carotenoid binding repertoire

Y. B. Slonimskiy, N. A. Egorkin, T. N. Friedrich, E. G. Maksimov, N. N. Sluchanko

This study characterizes AstaP, a microalgal protein that efficiently solubilizes and delivers multiple carotenoids, showing its potential as an antioxidant nanocarrier.

bioRxiv · Aug 5, 2021Biochemistry

Soluble cyanobacterial carotenoprotein as a robust antioxidant nanocarrier and delivery module

E. G. Maksimov, A. V. Zamaraev, E. Y. Parshina, Y. B. Slonimskiy, T. A. Slastnikova, A. A. Abdrakhmanov, P. A. Babaev, S. S. Efimova, O. S. Ostroumova, A. V. Stepanov, A. V. Ryabova, T. G. Friedrich, N. N. Sluchanko

This paper demonstrates a cyanobacterial carotenoprotein (CTDH) that efficiently delivers carotenoids to liposomes and mammalian cells, providing antioxidant protection against oxidative stress.

bioRxiv · Oct 30, 2019Biophysics

Radioprotective role of cyanobacterial phycobilisomes

K. E. Klementiev, E. G. Maksimov, D. A. Gvozdev, G. V. Tsoraev, F. F. Protopopov, I. V. Elanskaya, S. M. Abramov, M. Y. Dyakov, V. K. Ilyin, N. A. Nikolaeva, Y. B. Slonimskiy, N. N. Sluchanko, V. M. Lebedev, A. V. Spassky, T. Friedrich, , A. B. Rubin

The paper investigates the radioprotective role of cyanobacterial phycobilisomes by exposing Synechocystis sp. PCC6803 to ionizing radiation and space flight, revealing their potential role in stress response and recovery.

bioRxiv · Mar 13, 2018Biophysics

Functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCP

Y. B. Slonimskiy, E. G. Maksimov, E. P. Lukashev, M. Moldenhauer, C. M. Jeffries, D. I. Svergun, T. Friedrich, N. N. Sluchanko

The paper investigates the functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCP, revealing distinct binding properties despite similar structural conformations.

bioRxiv · Jan 15, 2018Biochemistry

The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components

E. G. Maksimov, N. N. Sluchanko, Y. B. Slonimskiy, A. V. Stepanov, E. A. Shirshin, G. V. Tsoraev, K. E. Klementiev, O. V. Slatinskaya, E. P. Lukashev, T. Friedrich, V. Z. Paschenko, A. B. Rubin

This study identifies two novel photocycle intermediates in the Orange Carotenoid Protein (OCP) using time-resolved spectroscopy, revealing asynchronous changes in carotenoid and protein components.

bioRxiv · Jul 23, 2017Biophysics

The Unique Protein-To-Protein Carotenoid Transfer Mechanism

E. G. Maksimov, N. N. Sluchanko, Y. B. Slonimskiy, K. S. Mironov, K. E. Klementiev, M. Moldenhauer, T. Friedrich, D. A. Los, V. Z. Paschenko, A. B. Rubin

The paper demonstrates a unique protein-to-protein carotenoid transfer mechanism using COCP to assemble photoactive OCP from photoinactive species.

bioRxiv · Apr 13, 2017Biophysics

Deletion of the short N-terminal extension in OCP reveals the main site for the FRP binding

N. N. Sluchanko, Y. B. Slonimskiy, M. Moldenhauer, T. Friedrich, E. G. Maksimov

The paper identifies the main site of OCP-FRP interactions by analyzing structural and functional similarities between the NTE and FRP.

bioRxiv · Mar 13, 2017Biophysics