Results 51 to 60 of about 5,149,379 (301)
Unbinding of hACE2 and Inhibitors from the Receptor Binding Domain of SARS-CoV-2 Spike Protein [PDF]
, 2021 The first direful biomolecular event leading to COVID-19 disease is the SARS-CoV-2 virus surface spike (S) protein-mediated interaction with the human transmembrane protein, angiotensin-converting enzyme 2 (hACE2). Prevention of this interaction presents
Tusar, Bandyopadhyay, Lokpati, Mishra
core +2 more sources
SARS-CoV-2 receptor binding domain fusion protein efficiently neutralizes virus infection.
PLoS Pathogens, 2021 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the COVID-19 pandemic. Currently, as dangerous mutations emerge, there is an increased demand for specific treatments for SARS-CoV-2 infected patients. The spike glycoprotein
Abigael Eva Chaouat +15 more
doaj +1 more source
Biomedical and Biotechnology Research Journal, 2022 Background: Crocetin, an active constituent derived from Crocus sativus L. and Gardenia jasminoides, has shown to have multiple pharmacological activities such as memory booster, anti-oxidants, anti-inflammatory, and neuroprotective actions.
Dhanashree Sharadchandra Kherade +3 more
doaj +1 more source
Structure and Notch Receptor Binding of the Tandem WWE Domain of Deltex [PDF]
Structure, 2005 Deltex is a cytosolic effector of Notch signaling thought to bind through its N-terminal domain to the Notch receptor. Here we report the structure of the Drosophila Deltex N-terminal domain, which contains two tandem WWE sequence repeats. The WWE repeats, which adopt a novel fold, are related by an approximate two-fold axis of rotation.
Zweifel, Mark E. +2 more
openaire +2 more sources
Mapping of the ligand-binding site on the b ' domain of human PDI: interaction with peptide ligands and the x-linker region [PDF]
, 2009 PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum. PDI consists of four thioredoxin-like domains, of which two contain redox-active catalytic sites (a and a'), and two ...
Freedman, R. B. +15 more
core +1 more source
Botulinum neurotoxin devoid of receptor binding domain translocates active protease. [PDF]
PLoS Pathogens, 2008 Clostridium botulinum neurotoxin (BoNT) causes flaccid paralysis by disabling synaptic exocytosis. Intoxication requires the tri-modular protein to undergo conformational changes in response to pH and redox gradients across endosomes, leading to the ...
Audrey Fischer +3 more
doaj +1 more source
Characterization of the receptor-binding domain of Ebola glycoprotein in viral entry [PDF]
Virologica Sinica, 2011 Ebola virus infection causes severe hemorrhagic fever in human and non-human primates with high mortality. Viral entry/infection is initiated by binding of glycoprotein GP protein on Ebola virion to host cells, followed by fusion of virus-cell membrane also mediated by GP. Using an human immunodeficiency virus (HIV)-based pseudotyping system, the roles
Wang, Jizhen +3 more
openaire +2 more sources
Journal of Lipid Research, 1988 Apolipoprotein B (apoB) is the predominant protein in low density lipoprotein (LDL) and is responsible for LDL binding to the LDL receptor. Although the primary amino acid sequence of human apoB has been determined, little is known about the structural ...
D L Ebert +5 more
doaj +1 more source
FEBS Open Bio, 2020 Botulinum neurotoxins (BoNTs) are one of the most toxic proteins known to humans. Their molecular structure is comprised of three essential domains—a cell binding domain (HC), translocation domain and catalytic domain (light chain) .
Kyle S. Gregory +2 more
doaj +1 more source
Life, 2021 Human receptor gC1qR is a 32 kD protein that mediates the cytoadherence of Plasmodium falciparum-infected erythrocytes (IEs) to human brain microvascular endothelial cells (HBMEC) and platelets.
Rowaida Bakri +3 more
doaj +1 more source