Author

K. Cechova

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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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Assay:fluorescence / live-cell microscopy· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

D. Arac· 2 shared K. Leon· 2 shared R. Vafabakhsh· 2 shared S. J. Bandekar· 2 shared S. P. Kordon· 2 shared A. A. Kossiakoff· 1 shared C. Lan· 1 shared E. E. Dintzner· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiochemistry

D. Arac

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3 papers

Recent·Most cited

Structural analysis and conformational dynamics of a holo-adhesion GPCR reveal interplay between extracellular and transmembrane domains

S. P. Kordon, K. Cechova, S. J. Bandekar, K. Leon, P. Dutka, G. Siffer, A. A. Kossiakoff, R. Vafabakhsh, D. Arac

This study uses cryo-EM and single-molecule FRET to show conformational coupling between the extracellular and transmembrane domains of an aGPCR, revealing how ECR dynamics influence receptor function.

bioRxiv · Feb 25, 2024 · PreprintBiochemistry

The far extracellular CUB domain of the adhesion GPCR ADGRG6/GPR126 is a key regulator of receptor signaling

S. J. Bandekar, E. E. Dintzner, K. Leon, S. P. Kordon, T. Slezak, K. Cechova, R. Vafabakhsh, D. Arac

This study investigates how the CUB domain of ADGRG6 regulates receptor signaling by modulating conformational dynamics of the extracellular region.

bioRxiv · Feb 16, 2024Biochemistry

Kappa but not delta or mu opioid receptors form homodimers at low membrane densities

K. Cechova, C. Lan, M. Macik, N. P. F. Barthes, M. Jung, M. H. Ulbrich

The paper investigates opioid receptor dimerization at different membrane densities and finds that kappa receptors form dimers at physiological densities while delta and mu remain monomeric.

bioRxiv · Mar 22, 2020Biochemistry