Author

G. Anderluh

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· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell-cell communication· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

A. Sakanovic· 2 shared U. Krengel· 2 shared A. Gucek· 1 shared A. Verkhratsky· 1 shared B. Bozic· 1 shared B. Rituper· 1 shared D. Grosser· 1 shared E. Lasic· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

A. Sakanovic

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Insight into glycosphingolipid crypticity: Crystal structure of the anti-tumor antibody 14F7 and recognition of NeuGc GM3 ganglioside

K. Bjerregaard-Andersen, H. Johannesen, F. Abraha, A. Sakanovic, D. Grosser, U. Coskun, G. Anderluh, S. Oscarson, E. Moreno, M. Grzybek, U. Krengel

This paper presents the crystal structure of the 14F7 antibody bound to NeuGc GM3 and shows how membrane composition and curvature influence its binding.

bioRxiv · Sep 18, 2020Biochemistry

Redistribution of cholesterol from vesicle to plasmalemma controls fusion pore geometry

B. Rituper, A. Gucek, M. Lisjak, U. Gorska, A. Sakanovic, S. Trkov Bobnar, E. Lasic, M. Bozic, P. S. Abbineni, J. Jorgacevski, M. Kreft, A. Verkhratsky, F. M. Platt, G. Anderluh, M. Stenovec, , R. Zorec

The paper shows that cholesterol redistribution from vesicles to the plasmalemma constricts the fusion pore, while depletion widens it, proposing a cholesterol-dependent mechanism for pore geometry regulation.

bioRxiv · Apr 6, 2020 · PreprintCell Biology

Crystal structures reveal that Lewis-x and fucose bind to secondary cholera toxin binding site - in contrast to fucosyl-GM1

J. B. Heim, V. Hodnik, J. E. Heggelund, G. Anderluh, U. Krengel

The paper reports crystal structures and SPR data showing Lewis-x and fucose bind to a secondary cholera toxin binding site, distinct from the GM1 binding site.

Scientific Reports · Aug 22, 2019Peer-reviewedBiochemistry