scholarly journals Human skin barrier structure and function analyzed by cryo-EM and molecular dynamics simulation

2018 ◽  
Vol 203 (2) ◽  
pp. 149-161 ◽  
Author(s):  
Magnus Lundborg ◽  
Ali Narangifard ◽  
Christian L. Wennberg ◽  
Erik Lindahl ◽  
Bertil Daneholt ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Human Skin ◽  
Skin Barrier ◽  
Structure And Function ◽  
Dynamics Simulation ◽  
Barrier Structure ◽  
And Function

Effects of Hydroxydecine® (10-hydroxy-2-decenoic acid) on skin barrier structure and function in vitro and clinical efficacy in the treatment of UV-induced xerosis

2011 ◽  
Vol 21 (6) ◽  
pp. 906-915 ◽  
Author(s):  
Hélène Duplan ◽  
Emmanuel Questel ◽  
Hélène Hernandez-Pigeon ◽  
Marie Florence Galliano ◽  
Antony Caruana ◽  
...  
Keyword(s):  
Clinical Efficacy ◽  
Skin Barrier ◽  
Structure And Function ◽  
Barrier Structure ◽  
Decenoic Acid ◽  
And Function

scholarly journals The Effect of an Emollient Containing Urea, Ceramide NP, and Lactate on Skin Barrier Structure and Function in Older People with Dry Skin

2016 ◽  
Vol 29 (3) ◽  
pp. 135-147 ◽  
Author(s):  
Simon G. Danby ◽  
Kirsty Brown ◽  
Tim Higgs-Bayliss ◽  
John Chittock ◽  
Lujain Albenali ◽  
...  
Keyword(s):  
Older People ◽  
Skin Barrier ◽  
Structure And Function ◽  
Barrier Structure ◽  
Dry Skin ◽  
And Function

scholarly journals Molecular Dynamics of SARS-CoV-2 Nsp1 Structural Changes Associated with Variant Mutations

2021 ◽  
Author(s):  
Shokouh Rezaei ◽  
Yahya Sefidbakht ◽  
Filipe Pereira
Keyword(s):  
Molecular Dynamics ◽  
Conformational Changes ◽  
Structural Changes ◽  
Structure And Function ◽  
Dynamics Simulation ◽  
Structural Protein ◽  
Wild Type ◽  
Deletion Mutations ◽  
And Function

Abstract SARS-CoV-2 non-structural protein 1 (Nsp1) is a virulence factor that inhibits the translation of host mRNAs and interact with viral RNA. Despite the relevance of Nsp1, few studies have been conducted to understand the effect of mutations on Nsp1 structure and function. Here, we provide a molecular dynamics simulation of SARS-CoV-2 Nsp1, wild type and variants. We found that SARS-CoV-2 Nsp1 has a more Rg value than SARS-CoV-1 Nsp1, with indicate an effect on the folding protein. This result suggest that SARS-CoV-2 Nsp1 can more easily approach the active site of the ribosome compared to SARS-CoV-1 Nsp1. In addition, we found that the C-terminal of the SARS-CoV-2 Nsp1, in particular residues 164 to 170, are more flexible than other regions of SARS-CoV-2 Nsp1 and SARS-CoV-1 Nsp1, confirming the role of this region in the interaction with the 40S subunit. Moreover, multiple deletion mutations have been found in the N/C-terminal of the SARS-CoV-2 Nsp1, which seems the effect of SARS-CoV-2 Nsp1 multiple deletions is greater than that of substitutions. Among all deletions, D156-158 and D80-90 may destabilize the protein structure and possibly increase the virulence of the SARS-CoV-2. Overall, our findings reinforce the importance of studying Nsp1 conformational changes in new variants and its effect on virulence of SARS-CoV-2.

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