Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.3390/ijms23062986 http://scihub22266oqcxt.onion/10.3390/ijms23062986 35328409!8948900!35328409     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=35328409&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\35328409.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Int+J+Mol+Sci 2022 ; 23 (6): ä Nephropedia Template TP {{tp|p=35328409|t=2022. SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights |pdf=|usr=}}{{35328409}} gab.com Text SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=35328409 #FOAvip Severe Acute Respiratory Syndrome CoronaVirus-2 (SARS-CoV-2) is composed of four structural proteins and several accessory non-structural proteins. SARS-CoV-2's most abundant structural protein, Membrane (M) protein, has a pivotal role both during viral infection cycle and host interferon antagonism. This is a highly conserved viral protein, thus an interesting and suitable target for drug discovery. In this paper, we explain the structural nature of M protein homodimer. To do so, we developed and applied a detailed and robust in silico workflow to predict M protein dimeric structure, membrane orientation, and interface characterization. Single Nucleotide Polymorphisms (SNPs) in M protein were retrieved from over 1.2 M SARS-CoV-2 genomes and proteins from the Global Initiative on Sharing All Influenza Data (GISAID) database, 91 of which were located at the predicted dimer interface. Among those, we identified SNPs in Variants of Concern (VOC) and Variants of Interest (VOI). Binding free energy differences were evaluated for dimer interfacial SNPs to infer mutant protein stabilities. A few high-prevalent mutated residues were found to be especially relevant in VOC and VOI. This realization may be a game-changer to structure-driven formulation of new therapeutics for SARS-CoV-2. Twit Text FOAVip SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=35328409 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35328409 #FOAvip English Wikipedia <ref>{{Cite pmid|35328409}}</ref> SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights #MMPMID35328409 Marques-Pereira C; Pires MN; Gouveia RP; Pereira NN; Caniceiro AB; Rosario-Ferreira N; Moreira IS Int J Mol Sci 2022[Mar]; 23 (6): ä PMID35328409show ga Severe Acute Respiratory Syndrome CoronaVirus-2 (SARS-CoV-2) is composed of four structural proteins and several accessory non-structural proteins. SARS-CoV-2's most abundant structural protein, Membrane (M) protein, has a pivotal role both during viral infection cycle and host interferon antagonism. This is a highly conserved viral protein, thus an interesting and suitable target for drug discovery. In this paper, we explain the structural nature of M protein homodimer. To do so, we developed and applied a detailed and robust in silico workflow to predict M protein dimeric structure, membrane orientation, and interface characterization. Single Nucleotide Polymorphisms (SNPs) in M protein were retrieved from over 1.2 M SARS-CoV-2 genomes and proteins from the Global Initiative on Sharing All Influenza Data (GISAID) database, 91 of which were located at the predicted dimer interface. Among those, we identified SNPs in Variants of Concern (VOC) and Variants of Interest (VOI). Binding free energy differences were evaluated for dimer interfacial SNPs to infer mutant protein stabilities. A few high-prevalent mutated residues were found to be especially relevant in VOC and VOI. This realization may be a game-changer to structure-driven formulation of new therapeutics for SARS-CoV-2. |*Mutation[MESH] |*Polymorphism, Single Nucleotide[MESH] |Binding Sites/genetics[MESH] |COVID-19/prevention & control/virology[MESH] |Coronavirus M Proteins/chemistry/*genetics/metabolism[MESH] |Genome, Viral/*genetics[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH]SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insig(epmc).pdf DeepDyve Pubget Overpricing