Author

G. Kozlov

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· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Organism:bacteria (other)· 1 Organism:human· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

K. Gehring· 3 shared J. Xie· 2 shared R. Fakih· 2 shared X. Wei· 2 shared Y. Chen· 2 shared A. Rohaim· 1 shared A. Saran· 1 shared A. Shahsavan· 1 shared

Activity by Year

2021-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiochemistry

K. Gehring

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Author profile →

5 papers

Recent·Most cited

Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15

L. Mahbub, G. Kozlov, P. Zong, S. Tetteh, T. Nethramangalath, C. Knorn, J. Jiang, A. Shahsavan, E. Lee, L. Yue, L. Runnels, K. Gehring

This study identifies ARL15 as a GTPase that binds CNNM2 and inhibits TRPM7-mediated divalent cation uptake, revealing molecular interactions and competitive regulation with PRL2.

bioRxiv · Jan 19, 2023Biochemistry

Structural basis for feedforward control in the PINK1/parkin pathway

V. Sauve, G. Sung, E. MacDougall, G. Kozlov, A. Saran, R. Fakih, E. A. Fon, K. Gehring

The paper elucidates how phospho-ubiquitin binds to parkin's RING domains to activate the PINK1/parkin pathway through a feedforward mechanism.

bioRxiv · Aug 16, 2021Biochemistry

Crystal structure of a bacterial CNNM magnesium transporter

Y. S. Chen, G. Kozlov, J. Armitano, B. J. Moeller, R. Fakih, A. Rohaim, B. Roux, J. E. Burke, K. Gehring

The paper determines the crystal structure of an archaeal CNNM protein bound to Mg2+-ATP, revealing its transmembrane fold and suggesting it functions as a cation transporter.

bioRxiv · Feb 11, 2021Biophysics

Paip2 associates with PABPC1 on mRNA, and may facilitate PABPC1 dissociation from mRNA upon deadenylation

J. Xie, X. Wei, G. Kozlov, Y. Chen, M. Menade

This study identifies Paip2 as a protein that interacts with PABPC1 on mRNA and may help PABPC1 detach from mRNA during deadenylation.

bioRxiv · Feb 7, 2021 · PreprintBiochemistry

Poly(A) binding protein is required for mRNP remodeling to form P-bodies in mammalian cells

J. Xie, Y. Chen, X. Wei, G. Kozlov

The paper shows PABPC1 is essential for P-body formation despite not being present in P-bodies, and demonstrates GW182's role in mediating this process.

bioRxiv · Feb 7, 2021 · PreprintBiochemistry