Comparing protein structures with RINspector automation in Cytoscape

по Brysbaert, Guillaume, Mauri, Théo, Lensink, Marc F.
Опубликовано в: F1000Res (2018)

The Inclusion of Water Molecules in Residue Interaction Networks Identifies Additional Central Residues

по Brysbaert, Guillaume, Blossey, Ralf, Lensink, Marc F.
Опубликовано в: Front Mol Biosci (2018)

Identification of Specific Lipid-binding Sites in Integral Membrane Proteins

по Lensink, Marc F., Govaerts, Cédric, Ruysschaert, Jean-Marie
Опубликовано 2010

Structures of C-mannosylated anti-adhesives bound to the type 1 fimbrial FimH adhesin

по de Ruyck, Jerome, Lensink, Marc F., Bouckaert, Julie
Опубликовано в: IUCrJ (2016)

Relating destabilizing regions to known functional sites in proteins

по Dessailly, Benoît H, Lensink, Marc F, Wodak, Shoshana J
Опубликовано 2007

On the ability of molecular dynamics simulation and continuum electrostatics to treat interfacial water molecules in protein-protein complexes

по Copie, Guillaume, Cleri, Fabrizio, Blossey, Ralf, Lensink, Marc F.
Опубликовано в: Sci Rep (2016)

CLUB-MARTINI: Selecting Favourable Interactions amongst Available Candidates, a Coarse-Grained Simulation Approach to Scoring Docking Decoys

по Hou, Qingzhen, Lensink, Marc F., Heringa, Jaap, Feenstra, K. Anton
Опубликовано в: PLoS One (2016)

Molecular docking as a popular tool in drug design, an in silico travel

по de Ruyck, Jerome, Brysbaert, Guillaume, Blossey, Ralf, Lensink, Marc F
Опубликовано в: Adv Appl Bioinform Chem (2016)

RINspector: a Cytoscape app for centrality analyses and DynaMine flexibility prediction

по Brysbaert, Guillaume, Lorgouilloux, Kevin, Vranken, Wim F, Lensink, Marc F
Опубликовано в: Bioinformatics (2018)

Identification of Novel Interaction Partners of Ets-1: Focus on DNA Repair

по Brysbaert, Guillaume, de Ruyck, Jérôme, Aumercier, Marc, Lensink, Marc F.
Опубликовано в: Genes (Basel) (2019)

LigASite—a database of biologically relevant binding sites in proteins with known apo-structures

по Dessailly, Benoit H., Lensink, Marc F., Orengo, Christine A., Wodak, Shoshana J.
Опубликовано 2008

Computational characterization of the binding mode between oncoprotein Ets‐1 and DNA‐repair enzymes

по de Ruyck, Jerome, Brysbaert, Guillaume, Villeret, Vincent, Aumercier, Marc, Lensink, Marc F.
Опубликовано в: Proteins (2018)

Targeting Dynamical Binding Processes in the Design of Non-Antibiotic Anti-Adhesives by Molecular Simulation—The Example of FimH

по Krammer, Eva-Maria, de Ruyck, Jerome, Roos, Goedele, Bouckaert, Julie, Lensink, Marc F.
Опубликовано в: Molecules (2018)

Asymmetrical diversification of the receptor-ligand interaction controlling self-incompatibility in Arabidopsis

по Chantreau, Maxime, Poux, Céline, Lensink, Marc F, Brysbaert, Guillaume, Vekemans, Xavier, Castric, Vincent
Опубликовано в: eLife (2019)

On the Molecular Basis of D-Bifunctional Protein Deficiency Type III

по Mehtälä, Maija L., Lensink, Marc F., Pietikäinen, Laura P., Hiltunen, J. Kalervo, Glumoff, Tuomo
Опубликовано 2013

Probing the Conformation of FhaC with Small-Angle Neutron Scattering and Molecular Modeling

по Gabel, Frank, Lensink, Marc F., Clantin, Bernard, Jacob-Dubuisson, Françoise, Villeret, Vincent, Ebel, Christine
Опубликовано 2014

Coiled-Coil Antagonism Regulates Activity of Venus Flytrap-Domain-Containing Sensor Kinases of the BvgS Family

по Lesne, Elodie, Dupré, Elian, Lensink, Marc F., Locht, Camille, Antoine, Rudy, Jacob-Dubuisson, Françoise
Опубликовано в: mBio (2018)

O-GlcNAcylation Prediction: An Unattained Objective

по Mauri, Theo, Menu-Bouaouiche, Laurence, Bardor, Muriel, Lefebvre, Tony, Lensink, Marc F, Brysbaert, Guillaume
Опубликовано в: Adv Appl Bioinform Chem (2021)

FlexPepDock lessons from CAPRI peptide–protein rounds and suggested new criteria for assessment of model quality and utility

по Marcu, Orly, Dodson, Emma‐Joy, Alam, Nawsad, Sperber, Michal, Kozakov, Dima, Lensink, Marc F., Schueler‐Furman, Ora
Опубликовано в: Proteins (2017)

Assembly of B4GALT1/ST6GAL1 heteromers in the Golgi membranes involves lateral interactions via highly charged surface domains

по Khoder-Agha, Fawzi, Harrus, Deborah, Brysbaert, Guillaume, Lensink, Marc F., Harduin-Lepers, Anne, Glumoff, Tuomo, Kellokumpu, Sakari
Опубликовано в: J Biol Chem (2019)