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.

suck abstract from ncbi


suck pdf from google scholar
unlimited free pdf from europmc33149560    free
PDF from PMC    free
html from PMC    free
PDF vom PMID33149560 :   free
PDF vom PMID33149560 :   free

suck abstract from ncbi

Nephropedia Template TP Text

Twit Text FOAVip

Twit Text #

English Wikipedia

  • Targeting the GRP78-Dependant SARS-CoV-2 Cell Entry by Peptides and Small Molecules #MMPMID33149560
  • Allam L; Ghrifi F; Mohammed H; El Hafidi N; El Jaoudi R; El Harti J; Lmimouni B; Belyamani L; Ibrahimi A
  • Bioinform Biol Insights 2020[]; 14 (ä): 1177932220965505 PMID33149560show ga
  • The global burden of infections and the rapid spread of viral diseases show the need for new approaches in the prevention and development of effective therapies. To this end, we aimed to explore novel inhibitor compounds that can stop replication or decrease the viral load of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), for which there is currently no approved treatment. Besides using the angiotensin-converting enzyme (ACE2) receptor as a main gate, the CoV-2 can bind to the glucose-regulating protein 78 (GRP78) receptor to get into the cells to start an infection. Here, we report potential inhibitors comprising small molecules and peptides that could interfere with the interaction of SARS-CoV-2 and its target cells by blocking the recognition of the GRP78 cellular receptor by the viral Spike protein. These inhibitors were discovered through an approach of in silico screening of available databases of bioactive peptides and polyphenolic compounds and the analysis of their docking modes. This process led to the selection of 9 compounds with optimal binding affinities to the target sites. The peptides (satpdb18674, satpdb18446, satpdb12488, satpdb14438, and satpdb28899) act on regions III and IV of the viral Spike protein and on its binding sites in GRP78. However, 4 polyphenols such as epigallocatechin gallate (EGCG), homoeriodictyol, isorhamnetin, and curcumin interact, in addition to the Spike protein and its binding sites in GRP78, with the ATPase domain of GRP78. Our work demonstrates that there are at least 2 approaches to block the spread of SARS-CoV-2 by preventing its fusion with the host cells via GRP78.
  • ä

  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    1177932220965505 ä.14 2020