Author

C. Aponte-Santamaria

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 8

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:mechanistic / dynamical model· 5 Research Focus:protein folding & dynamics· 4 Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Approach:deep learning· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Approach:statistical model· 2

Frequent Co-Authors

F. Graeter· 2 shared F. Grater· 2 shared M. Brosz· 2 shared A. Alexander-Katz· 1 shared A. J. Lay· 1 shared A. Sandoval-Perez· 1 shared B. Geiger· 1 shared B. L. de Groot· 1 shared

Activity by Year

2022-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 9 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiophysics

F. Graeter

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

O-glycans Expand Lubricin and Attenuate its Viscosity and Shear Thinning

S. Boushehri, H. Holey, M. Brosz, P. Gumbsch, L. Pastewka, C. Aponte-Santamaria, F. Graeter

This study uses molecular dynamics simulations to show that O-glycans in lubricin increase its conformational extension, reduce viscosity, but weaken shear thinning at high shear rates.

bioRxiv · Dec 7, 2023 · PreprintBiophysics

Mechanical forces control the valency of the malaria adhesin VAR2CSA by exposing cryptic glycan binding sites

R. Roessner, N. Michelarakis, F. Gräter, C. Aponte-Santamaria

This study shows mechanical forces increase VAR2CSA's binding avidity by converting it from monovalent to multivalent through conformational changes exposing additional CSA binding sites.

bioRxiv · Jul 31, 2023Biophysics

Structure and dynamics of cholesterol-mediated aquaporin-0 arrays and implications for lipid rafts

P.-L. Chiu, J. D. Orjuela, B. L. de Groot, C. Aponte-Santamaria, T. Walz

This study determines the structure of AQP0 tetramers in sphingomyelin/cholesterol membranes and shows how cholesterol stabilizes their arrangement through hydrophobic interactions and avidity effects.

bioRxiv · May 16, 2023Biophysics

Energetics and kinetics of membrane permeation of photoresists for bioprinting

L. Diedrich, M. Brosz, T. Abele, S. Steinke, F. Grater, K. Gopfrich, C. Aponte-Santamaria

This study investigates how photoresists interact with lipid membranes using simulations and assays, finding permeability varies widely and is influenced by membrane properties.

bioRxiv · Mar 27, 2023Biophysics

The interplay between adsorption and aggregation of von Willebrand factor chains in shear flows

H. Amaya-Espinosa, A. Alexander-Katz, C. Aponte-Santamaria

This study uses Brownian dynamics simulations to investigate how shear flow affects VWF chain adsorption, aggregation, and extension, revealing their interplay in hemostasis.

bioRxiv · Dec 26, 2022Biophysics

Dynamic Disulfide Bond Topologies in von-Willebrand-Factor's C4-Domain Undermine Platelet Binding

F. Kutzki, D. Butera, A. J. Lay, D. M. Maag, J. Chiu, H.-G. Woon, T. Kubar, M. Elstner, C. Aponte-Santamaria, P. Hogg, F. Graeter

This study quantifies disulfide bond topologies in vWF-C4 domain and shows their impact on platelet binding through integrin.

bioRxiv · Aug 20, 2022 · PreprintBiophysics

How talin allosterically activates vinculin

F. Franz, R. Tapia-Rojo, S. E. Winograd-Katz, R. Boujemaa-Paterski, W. Li, T. Unger, S. Albeck, C. Aponte-Santamaria, S. Garcia-Manyes, O. Medalia, B. Geiger, F. Grater

This study identifies an allosteric network in vinculin regulated by talin, showing how force and binding dynamics control focal adhesion formation.

bioRxiv · Aug 1, 2022 · PreprintBiophysics

Thermodynamic stabilization of the von Willebrand Factor A1 domain due to loss-of-function disease-related mutations.

A. Sandoval-Perez, V. Mejia-Restrepo, C. Aponte-Santamaria

This study investigates how mutations G1324A and G1324S in the vWF A1 domain affect its thermodynamic stability and conformational flexibility, leading to reduced platelet adhesion in type 2M von Willebrand disease.

bioRxiv · Mar 10, 2022Biophysics