Author

L. Geris

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· 2 Bioengineering· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:statistical model· 3 Organism:mouse· 2 Research Focus:protein folding & dynamics· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

F. Rapino· 2 shared M. Joiret· 2 shared P. Close· 2 shared A. A. Pitsillides· 1 shared A. Chavli· 1 shared A. Pastore· 1 shared C. Verfaillie· 1 shared F. Luyten· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiophysics

F. Rapino

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Robotics-driven manufacturing of cartilaginous microtissues for the bio-assembly of skeletal implants

I. Decoene, G. Nasello, R. F. Madeiro, G. Nilsson Hall, A. Pastore, I. Van Hoven, S. Ribeiro Viseu, C. Verfaillie, L. Geris, F. Luyten, I. Papantoniou

This paper develops a robotic system for automated manufacturing of cartilaginous microtissues, showing improved control and differentiation into cartilage and bone.

bioRxiv · Jan 9, 2023 · PreprintBioengineering

In silico, in vitro, and in vivo models reveal EPHA2 as a target for decreasing inflammation and pathological endochondral ossification in osteoarthritis.

M. N. Ferrao Blanco, R. Lesage, N. Kops, N. Fahy, F. T. Bekedam, A. Chavli, Y. M. Bastiaansen-Jenniskens, L. Geris, M. G. Chambers, A. A. Pitsillides, R. Narcisi, G. J. V. M. van Osch

This study identifies EPHA2 as a therapeutic target for osteoarthritis by showing its inhibition reduces inflammation and pathological endochondral ossification in both in vitro and in vivo models.

bioRxiv · Jun 12, 2022Pharmacology & Toxicology

A simple geometrical model of the electrostatic environment around the catalytic center of the ribosome

M. Joiret, F. Rapino, P. Close, L. Geris

The paper develops a geometrical model to estimate the electrostatic potential and field around the ribosome's peptidyl transferase center and assesses its role in peptide bond formation.

bioRxiv · Mar 7, 2022 · PreprintBiophysics

Ribosome Exit Tunnel Electrostatics

M. Joiret, F. Rapino, P. Close, L. Geris

This paper develops a quantitative electrostatic model of the ribosome exit tunnel to analyze its impact on protein elongation rates and forces on nascent polypeptides.

bioRxiv · Oct 20, 2020 · PreprintBiophysics