Author

S. Grzesiek

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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Biophysics· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

A. Grahl· 2 shared P. Isaikina· 2 shared T. Maier· 2 shared A. K. Shukla· 1 shared A. Maier· 1 shared A. Ranjan· 1 shared C.-J. Tsai· 1 shared F. Pamula· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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2 shared papersBiophysics

A. Grahl

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4 papers

Recent·Most cited

The molecular basis of Abelson kinase regulation by its αI-helix

J. Paladini, A. Maier, J. M. Habazettl, I. Hertel, R. Sonti, S. Grzesiek

This study identifies how the αI-helix modulates Abl kinase activity through mechanical forces affecting the KD/SH2SH3 interface, with implications for drug response.

bioRxiv · Oct 4, 2023Biophysics

A key GPCR phosphorylation motif discovered in arrestin2-CCR5 phosphopeptide complexes

P. Isaikina, I. Petrovic, R. P. Jakob, P. Sarma, A. Ranjan, M. Baruah, V. Panwalkar, T. Maier, A. K. Shukla, S. Grzesiek

The paper identifies a phosphorylation motif in arrestin2-CCR5 complexes that is essential for stable interactions and functional activation of CCR5.

bioRxiv · Oct 10, 2022 · PreprintBiophysics

Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol

L. A. Abiko, R. Dias Teixeira, S. Engilberge, A. Grahl, S. Grzesiek

The paper identifies dry voids in the β1-adrenergic receptor that cholesterol fills, explaining its allosteric regulation and suggesting new drug development strategies.

bioRxiv · Aug 30, 2021Biophysics

Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist

P. Isaikina, C.-J. Tsai, N. B. Dietz, F. Pamula, A. Grahl, K. N. Goldie, R. Guixa-Gonzalez, G. F. X. Schertler, O. Hartley, H. Stahlberg, T. Maier, X. Deupi, S. Grzesiek

The paper reports the cryo-EM structure of CCR5 bound to a chemokine agonist and Gi protein, revealing its activation mechanism.

bioRxiv · Nov 27, 2020Biophysics