Aloin isoforms (A and B) selectively inhibits proteolytic and deubiquitinating activity of papain like protease (PLpro) of SARS-CoV-2 in vitro

Autor: Devin S. M. Lewis, Joanna Ho, Savannah Wills, Anasha Kawall, Avini Sharma, Krishna Chavada, Maximilian C. C. J. C. Ebert, Stefania Evoli, Ajay Singh, Srujana Rayalam, Vicky Mody, Shashidharamurthy Taval

Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-11 (2022)

Abstract The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that

Externí odkaz: https://doaj.org/article/b2e36b295fd24a44a89fca39420fb8d0

Molecular simulations of β-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites

Autor: Bruno Rizzuti, Stefania Evoli, Rita Guzzi

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 82:2609-2619

The interaction of saturated fatty acids of different length (C8:0 to C18:0) with β-lactoglobulin (βLG) was investigated by molecular dynamics simulation and docking approaches. The results show that the presence of such ligands in the hydrophobic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2950173da69eb70140300bd3c980546f
https://doi.org/10.1002/prot.24625

Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation

Autor: Bruno Rizzuti, Rita Guzzi, Stefania Evoli

Publikováno v: JBIC. Journal of biological inorganic chemistry
18 (2013): 739–749. doi:10.1007/s00775-013-1017-1
info:cnr-pdr/source/autori:Evoli, Stefania; Guzzi, Rita; Rizzuti, Bruno/titolo:Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation/doi:10.1007%2Fs00775-013-1017-1/rivista:JBIC. Journal of biological inorganic chemistry (Print)/anno:2013/pagina_da:739/pagina_a:749/intervallo_pagine:739–749/volume:18

The spectroscopic, thermal, and functional properties of blue copper proteins can be modulated by mutations in the metal binding loop. Molecular dynamics simulation was used to compare the conformational properties of azurin and two chimeric variants

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be6ae90beb51c51b82b7df66220e101f
https://doi.org/10.1007/s00775-013-1017-1

Molecular simulations of β-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites

Autor: Stefania, Evoli, Rita, Guzzi, Bruno, Rizzuti

Publikováno v: Proteins. 82(10)

The interaction of saturated fatty acids of different length (C8:0 to C18:0) with β-lactoglobulin (βLG) was investigated by molecular dynamics simulation and docking approaches. The results show that the presence of such ligands in the hydrophobic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7468c2ebaa22b6ea4c9075abb3d9a943
https://pubmed.ncbi.nlm.nih.gov/24916607