Bourenkov, Gleb

Structure of TPR Domain–Peptide Complexes

Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 1,188

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.

Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature

Protease and Inhibitor MechanismsBlood Coagulation and Thrombosis Mechanisms

Cited by 619

Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods

Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., et al. (1999) · Structure

Metalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

Cited by 286

CASK Functions as a Mg2+-independent neurexin kinase

Mukherjee, K., Sharma, M., Urlaub, H., Bourenkov, G. P., Jahn, R., Südhof, T. C., & Wahl, M. C. (2008) · Cell

Protein Kinase Regulation and GTPase SignalingNeuroscience and Neuropharmacology Research

Cited by 271

Profiling cellular diversity in sponges informs animal cell type and nervous system evolution

Musser, J. M., Schippers, K. J., Nickel, M., Mizzon, G., Kohn, A. B., Pape, C., Ronchi, P., Papadopoulos, N., Tarashansky, A. J., Hammel, J. U., et al. (2021) · Science

Marine Invertebrate Physiology and EcologyMarine Sponges and Natural Products

Cited by 242

Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen-activated protein kinase signaling to late endosomes

Kurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences

Protein Kinase Regulation and GTPase SignalingCellular transport and secretion

Cited by 95

Structural basis for receptor selectivity and inverse agonism in S1P5 receptors

Lyapina, E., Marin, E., Gusach, A., Orekhov, P., Gerasimov, A., Luginina, A., Vakhrameev, D., Ergasheva, M., Kovaleva, M., Khusainov, G., et al. (2022) · Nature Communications

Sphingolipid Metabolism and SignalingReceptor Mechanisms and Signaling

Cited by 26

Structural basis for receptor selectivity and inverse agonism in S1P 5 receptors

Lyapina, E., Marin, E., Gusach, A., Orekhov, P., Gerasimov, A., Luginina, A., Vakhrameev, D., Ergasheva, M., Kovaleva, M., Khusainov, G., et al. (2022) · Nature Communications

Sphingolipid Metabolism and SignalingReceptor Mechanisms and Signaling

Cited by 26

A novel subgroup of light-driven sodium pumps with an additional Schiff base counterion

Podoliak, E., Lamm, G. H. U., Alekseev, A., Marin, E., Schellbach, A. V., Fedotov, D. A., Stetsenko, A., Maliar, N., Bourenkov, G., Balandin, T., et al. (2023) · Nature Communications

Photoreceptor and optogenetics researchReceptor Mechanisms and Signaling

Cited by 18

CryoRhodopsins: a comprehensive characterization of a group of microbial rhodopsins from cold environments

Lamm, G. H. U., Marin, E., Alekseev, A., Schellbach, A. V., Stetsenko, A., Bourenkov, G., Borshchevskiy, V., Asido, M., Agthe, M., Engilberge, S., et al. (2024) · Science Advances

Photoreceptor and optogenetics researchReceptor Mechanisms and Signaling

Cited by 7

CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments

Lamm, G. H. U., Marin, E., Alekseev, A., Schellbach, A. V., Stetsenko, A., Haro-Moreno, J. M., Bourenkov, G., Borshchevskiy, V., Asido, M., Agthe, M., et al. (2025) · Science Advances

Photoreceptor and optogenetics researchReceptor Mechanisms and Signaling

Cited by 7