Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Cedrix J. Dongmo Foumthuim"'
Autor:
Alvise Spanò, Lorenzo Fanton, Davide Pizzolato, Jacopo Moi, Francesco Vinci, Alberto Pesce, Cedrix J. Dongmo Foumthuim, Achille Giacometti, Marta Simeoni
Publikováno v:
BMC Bioinformatics, Vol 24, Iss 1, Pp 1-14 (2023)
Abstract Background Residue Interaction Networks (RINs) map the crystallographic description of a protein into a graph, where amino acids are represented as nodes and non-covalent bonds as edges. Determination and visualization of a protein as a RIN
Externí odkaz:
https://doaj.org/article/bb74bffdfc374ba2a92c98afae915d0e
Autor:
Carlos Sequeiros-Borja, Aravind Selvaram Thirunavukarasu, Cedrix J. Dongmo Foumthuim, Jan Brezovsky
An aqueous environment is necessary for life as we know it, and water is required for almost all biochemical processes at a molecular level. Proteins employ water molecules in many ways. Hence, proteins need to transport water molecules across their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3ee5e7e8a34da2ce8ca6eaa3b139bb2
https://doi.org/10.1101/2023.05.24.542065
https://doi.org/10.1101/2023.05.24.542065
Using molecular dynamics and thermodynamic integration, we report on the solvation process in water and in cyclohexane of seven polypeptides (GLY, ALA, ILE, ASN, LYS, ARG, GLU). The polypeptides are selected to cover the full hydrophobic scale while
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::073de77ee59d332fbed6f09e700e02e4
http://arxiv.org/abs/2301.12709
http://arxiv.org/abs/2301.12709
Autor:
Giulia Moro, Cedrix J. Dongmo Foumthuim, Marco Spinaci, Ettore Martini, Dafne Cimino, Eleonora Balliana, Peter Lieberzeit, Flavio Romano, Achille Giacometti, Rui Campos, Karolien De Wael, Ligia Maria Moretto
Publikováno v:
Analytica chimica acta
There is an urgent need for sensing strategies to screen perfluoroalkyl substances (PFAS) in aqueous matrices. These strategies must be applicable in large-scale monitoring plans to face the ubiquitous use of PFAS, their wide global spread, and their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1c50d1c9a672e14a1a1b2c60c4bde3c
https://pubmed.ncbi.nlm.nih.gov/35397910
https://pubmed.ncbi.nlm.nih.gov/35397910
Autor:
Cedrix J. Dongmo Foumthuim, Rita Grandori, Sara La Manna, Alessandra Corazza, Miguel A. Soler, Daniela Marasco, Giacinto Scoles, Cristina Cantarutti, Sara Fortuna, M Cristina Vargas, Mireille Dumoulin, Carlo Santambrogio
Herein, we compared the ability of linear and cyclic peptides generated in silico to target different protein sites: internal pockets and solvent-exposed sites. We selected human lysozyme (HuL) as a model target protein combined with the computationa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::357730b784dcef91fe0ef1f7eb71ea33
https://hdl.handle.net/11368/2999240
https://hdl.handle.net/11368/2999240
Autor:
Manuel Carrer, Giuseppe Graziano, Maurine Houvet, Cedrix J. Dongmo Foumthuim, Achille Giacometti, Tatjana Škrbić
Using thermodynamics integration, we study the solvation free energy of 18 amino acid side chain equivalents in solvents with different polarity, ranging from the most polar water to the most non-polar cyclohexane. The amino acid side chain equivalen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b346b6f689d2951c6d251bc947d2d95
http://arxiv.org/abs/2010.06332
http://arxiv.org/abs/2010.06332
Publikováno v:
Molecular BioSystems. 13:2625-2637
Hydrophobic surfaces are known to adsorb and unfold proteins, a process that has been studied only for a few proteins. Here we address the interaction of β2-microglobulin, a paradigmatic protein for the study of amyloidogenesis, with hydrophobic sur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58234627c3ebb28e2cff2ba67e96b049
https://doi.org/10.1039/c7mb00464h
https://doi.org/10.1039/c7mb00464h
Autor:
Federico Fogolari, Gennaro Esposito, Alessandra Corazza, Cedrix J. Dongmo Foumthuim, Ornela Maloku
Entropy calculation is an important step in the postprocessing of molecular dynamics trajectories or predictive models. In recent years the nearest neighbor method has emerged as a powerful method to deal in a flexible way with the dimensionality of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5476a44ee023f64780acade8006d813
http://hdl.handle.net/10278/3745093
http://hdl.handle.net/10278/3745093
Autor:
Alessandra Corazza, Anna Russo, Cedrix J. Dongmo Foumthuim, Daniela Marasco, Abimbola Feyisara Adedeji, Alessandro Laio, Alex Rodriguez, Cristina Cantarutti, Miguel A. Soler, Sara Fortuna, Giacinto Scoles, Loredana Casalis, Elena Ambrosetti
The oriented immobilization of proteins, key for the development of novel responsive biomaterials, relies on the availability of effective probes. These are generally provided by standard approaches based on in vivo maturation and in vitro selection
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::322f1452c2b9196ac7e327b14c4cf4cc
https://hdl.handle.net/11368/2894503
https://hdl.handle.net/11368/2894503
Autor:
Federico Fogolari, Cedrix J. Dongmo Foumthuim, Sara Fortuna, Alessandra Corazza, Miguel A. Soler, Gennaro Esposito
The estimation of rotational and translational entropies in the context of ligand binding has been the subject of long-time investigations. The high dimensionality (six) of the problem and the limited amount of sampling often prevent the required res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a043364683642cdce06d55609a98a5ef
http://hdl.handle.net/10278/3745089
http://hdl.handle.net/10278/3745089