scholarly journals Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models

1996 ◽  
Vol 5 (2) ◽  
pp. 240-247 ◽  
Author(s):  
Jürgen Bajorath ◽  
Alejandro Aruffo
Keyword(s):  
Cell Surface ◽  
Ligand Binding ◽  
Human Cell ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Cell Surface Receptor ◽  
Molecular Models ◽  
Surface Receptor

In vitro biosynthesis of the human cell surface receptor for transferrin

FEBS Letters ◽  
1983 ◽  
Vol 158 (2) ◽  
pp. 259-264 ◽  
Author(s):  
C. Schneider ◽  
U. Asser ◽  
D.R. Sutherland ◽  
M.F. Greaves
Keyword(s):  
Cell Surface ◽  
Human Cell ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
In Vitro Biosynthesis

A human cell surface receptor activated by free fatty acids and thiazolidinedione drugs

2003 ◽  
Vol 301 (2) ◽  
pp. 406-410 ◽  
Author(s):  
Knut Kotarsky ◽  
Niclas E. Nilsson ◽  
Erik Flodgren ◽  
Christer Owman ◽  
Björn Olde
Keyword(s):  
Fatty Acids ◽  
Cell Surface ◽  
Free Fatty Acids ◽  
Human Cell ◽  
Cell Surface Receptor ◽  
Surface Receptor

Ligand Binding to the Cell-Surface Receptor for Reovirus Type 3 Alters Schwann Cell Growth and Function

1990 ◽  
Vol 605 (1 Myelination a) ◽  
pp. 412-415
Author(s):  
JEFFREY A. COHEN ◽  
WILLIAM V. WILLIAMS ◽  
KENNETH F. MORE ◽  
HARISH SEHDEV ◽  
JAMES G. DAVIES ◽  
...  
Keyword(s):  
Cell Growth ◽  
Schwann Cell ◽  
Cell Surface ◽  
Ligand Binding ◽  
Cell Surface Receptor ◽  
Reovirus Type ◽  
Surface Receptor ◽  
And Function ◽  
Type 3

scholarly journals Designing Short Peptides to Block the Interaction of SARS-CoV-2 and Human ACE2 for COVID-19 Therapeutics

2021 ◽  
Vol 12 ◽  
Author(s):  
Abdul Basit ◽  
Asad Mustafa Karim ◽  
Muhammad Asif ◽  
Tanveer Ali ◽  
Jung Hun Lee ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Affinity ◽  
Human Cell ◽  
De Novo ◽  
Cell Surface Receptor ◽  
Short Peptides ◽  
Potential Candidate ◽  
Binding Interaction ◽  
Surface Receptor ◽  
Binding Residues

To date, the current COVID-19 pandemic caused by SARS-CoV-2 has infected 99.2 million while killed 2.2 million people throughout the world and is still spreading widely. The unavailability of potential therapeutics against this virus urges to search and develop new drugs. SARS-CoV-2 enters human cells by interacting with human angiotensin-converting enzyme 2 (ACE2) receptor expressed on human cell surface through utilizing receptor-binding domain (RBD) of its spike glycoprotein. The RBD is highly conserved and is also a potential target for blocking its interaction with human cell surface receptor. We designed short peptides on the basis of our previously reported truncated ACE2 (tACE2) for increasing the binding affinity as well as the binding interaction network with RBD. These peptides can selectively bind to RBD with much higher affinities than the cell surface receptor. Thus, these can block all the binding residues required for binding to cell surface receptor. We used selected amino acid regions (21–40 and 65–75) of ACE2 as scaffold for the de novo peptide design. Our designed peptide Pep1 showed interactions with RBD covering almost all of its binding residues with significantly higher binding affinity (−13.2 kcal mol−1) than the cell surface receptor. The molecular dynamics (MD) simulation results showed that designed peptides form a stabilized complex with RBD. We suggest that blocking the RBD through de novo designed peptides can serve as a potential candidate for COVID-19 treatment after further clinical investigations.

scholarly journals Effects of Food Mastication on Rat Parotid Gland Adrenergic and Cholinergic Cell Surface Receptors

1993 ◽  
Vol 4 (3) ◽  
pp. 591-597 ◽  
Author(s):  
Dorthea A. Johnson ◽  
H. Lee Cardenas
Keyword(s):  
Cell Surface ◽  
Parotid Gland ◽  
Ligand Binding ◽  
Cell Surface Receptor ◽  
Receptor Density ◽  
Gland Weight ◽  
Surface Receptor ◽  
Muscarinic Cholinergic ◽  
Cholinergic Cell ◽  
Pelleted Diet

Adult male rats were fed diets of differing texture (liquid, powder, standard pelleted, or bulk pelleted) to alter food mastication. After 2 weeks, the parotid glands were removed and adrenergic and muscarinic-cholinergic cell surface receptor density (fM bound/mg protein) and ligand binding dissociation constants (Kd in nM) were determined by radioligand binding techniques on a crude membrane fraction. For all diets, gland weight increased as the requirement for food mastication increased (i.e., liquid < powder < standard pelleted < bulk pelleted). Among the diets, neither beta-two nor alpha-two receptor density was altered. Beta-one receptor density was directly related to dietary mastication. Compared with the standard pelleted diet, beta-one receptor density was reduced 21% for the liquid diet and 7% for the powdered diet; for the bulk-pelleted diet, beta-one receptor density was increased 11%. With respect to alpha-one receptor density, it was not affected by the liquid or powdered diet when compared with the standard pelleted diet, but alpha-one receptors were increased 14% with the bulk-pelleted diet. Muscarinic-cholinergic receptor density for the liquid diet fed rats was 27% less than for the standard-pelleted diet; powdered diet did not differ from standard pelleted, while that for the bulk-pelleted diet was increased 6%. With but minor exceptions, ligand binding affinity was unaffected by the changes in diet texture. These studies demonstrate that dietary mastication as well as affecting parotid gland weight, cell size, and saliva production also influences autonomic cell surface receptor density.

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