Author

C. Tempra

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· 5 Biochemistry· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Approach:statistical model· 4 Research Focus:host-pathogen & immune response· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:drug response / drug discovery· 2 Research Focus:cell type annotation· 1

Frequent Co-Authors

M. Javanainen· 4 shared P. Jungwirth· 3 shared A. Olzynska· 2 shared D. Biriukov· 2 shared H. Martinez-Seara· 2 shared L. Cwiklik· 2 shared M. Riopedre-Fernandez· 2 shared P. E. Mason· 2 shared

Activity by Year

2020-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiophysics

M. Javanainen

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Effective Inclusion of Electronic Polarization Improves the Description of Electrostatic Interactions: The prosECCo75 Biomolecular Force Field

R. Nencini, C. Tempra, D. Biriukov, M. Riopedre-Fernandez, V. Cruces Chamorro, J. Polak, P. E. Mason, D. Ondo, J. Heyda, O. H. S. Ollila, P. Jungwirth, M. Javanainen, H. Martinez-Seara

prosECCo75 improves MD simulations by incorporating electronic polarization, enhancing accuracy in modeling electrostatic interactions in biological systems without increasing computational cost.

bioRxiv · May 31, 2024Biophysics

A comparison of lipid diffusive dynamics in monolayers and bilayers in the context of interleaflet coupling

T. Mandal, N. Brandt, C. Tempra, M. Javanainen, B. Fabian, S. Chiantia

This study compares lipid diffusive dynamics in monolayers and bilayers to understand interleaflet coupling mechanisms.

bioRxiv · Apr 26, 2024Biophysics

Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?

F. Scollo, C. Tempra, H. Evci, M. Riopedre-Fernandez, A. Olzynska, M. Javanainen, A. Uday, M. Cebecauer, L. Cwiklik, H. Martinez-Seara, P. Jungwirth, P. Jurkiewicz, M. Hof

The paper investigates whether calmodulin binds to lipids in the cytosolic leaflet of plasma membranes and finds that CaM interacts with PS and PE, with calcium inducing conformational changes and affecting membrane charge and stability.

bioRxiv · Dec 12, 2023Biophysics

Exposure to aldehyde cherry e-liquid flavouring and its vape by-product disrupts pulmonary surfactant biophysical function

A. Martin, C. Tempra, Y. T. Yu, J. Liekkinen, R. Thakker, H. Lee, B. de Santos Moreno, I. Vattulainen, C. Rossios, M. Javanainen, J. Bernardino de la Serna

This study shows that benzaldehyde and its by-product, benzaldehyde propylene glycol acetal, disrupt pulmonary surfactant biophysical function by interacting with surfactant proteins SP-B and SP-C.

bioRxiv · Sep 22, 2023 · PreprintPharmacology & Toxicology

A Stealthy Player in Lipid Experiments? EDTA Binding to Phosphatidylcholine Membranes Probed by Simulations and Monolayer Experiments

K. Vazdar, C. Tempra, A. Olzynska, D. Biriukov, L. Cwiklik, M. Vazdar

This paper shows EDTA anions bind to phosphatidylcholine monolayers, altering surface pressure and highlighting potential interference in lipid experiments.

bioRxiv · Mar 12, 2023Biophysics

The role of alpha-helix on the structure-targeting drug design of amyloidogenic proteins

C. Tempra, C. La Rosa, F. Lolicato

This study investigates how alpha-helix structure influences protein-lipid binding in amyloidogenic proteins, showing that helix content affects contact probability and supports a lipid-chaperon model for membrane interaction.

bioRxiv · Nov 20, 2020Biophysics

Sweet taste of heavy water

N. Ben Abu, P. E. Mason, H. Klein, N. Dubovski, Y. Ben Shoshan-Galeczki, E. Malach, V. Prazienkova, L. Maletinska, C. Tempra, V. C. Chamorro, J. Cvacka, M. Behrens, M. Y. Niv, P. Jungwirth

The paper shows humans can distinguish heavy water (D2O) from normal water by taste, mediated by the TAS1R2/TAS1R3 receptor, while mice cannot.

bioRxiv · May 22, 2020Biochemistry