scholarly journals In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles.

1991 ◽  
Vol 10 (12) ◽  
pp. 3735-3742 ◽  
Author(s):  
J.P. Beltzer ◽  
M. Spiess
Keyword(s):  
Plasma Membrane ◽  
Asialoglycoprotein Receptor ◽  
Coated Vesicles ◽  
In Vitro Binding ◽  
Vitro Binding

scholarly journals Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane

2009 ◽  
Vol 184 (3) ◽  
pp. 451-462 ◽  
Author(s):  
Jian-Jiang Hao ◽  
Yin Liu ◽  
Michael Kruhlak ◽  
Karen E. Debell ◽  
Barbara L. Rellahan ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Membrane Association ◽  
Erm Proteins ◽  
Cytoskeletal Remodeling ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Hydrolysis Of

Mechanisms controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma membrane, are incompletely understood. In lymphocytes, chemokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma membrane and dephosphorylation. SDF-1–mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibitors. Conversely, reduction of phosphatidylinositol 4,5-bisphosphate (PIP2) levels by activation of PLC, expression of active PLC mutants, or acute targeting of phosphoinositide 5-phosphatase to the plasma membrane promotes release and dephosphorylation of moesin and ezrin. Although expression of phosphomimetic moesin (T558D) or ezrin (T567D) mutants enhances membrane association, activation of PLC still relocalizes them to the cytosol. Similarly, in vitro binding of ERM proteins to the cytoplasmic tail of CD44 is also dependent on PIP2. These results demonstrate a new role of PLCs in rapid cytoskeletal remodeling and an additional key role of PIP2 in ERM protein biology, namely hydrolysis-mediated ERM inactivation.

Localization of “in vitro” binding of the fungal toxin fusicoccin to plasma-membrane-rich fractions from corn coleoptiles

1977 ◽  
Vol 9 (3) ◽  
pp. 291-299 ◽  
Author(s):  
U. Dohrmann ◽  
R. Hertel ◽  
P. Pesci ◽  
S.M. Cocucci ◽  
E. Marrè ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fungal Toxin ◽  
In Vitro Binding ◽  
Vitro Binding

In Vivo and in Vitro Binding of IgA to the Plasma Membrane of Hepatocytes

1978 ◽  
Vol 8 (6) ◽  
pp. 543-549 ◽  
Author(s):  
U. HOPF ◽  
P. BRANDTZAEG ◽  
T. H. HUTTEROTH ◽  
K. H. MEYER ZUM BUSCHENFELDE
Keyword(s):  
Plasma Membrane ◽  
In Vitro Binding ◽  
Vitro Binding

In vitro binding specificity of glycosylated dextrans to the asialoglycoprotein receptor of primary hepatocytes

1995 ◽  
Vol 3 (6) ◽  
pp. 339-345 ◽  
Author(s):  
David A. Anderson ◽  
Stefan Vansteenkiste ◽  
Etienne H. Schacht ◽  
Sankya K. Sen ◽  
Len W. Seymour
Keyword(s):  
Binding Specificity ◽  
Asialoglycoprotein Receptor ◽  
Primary Hepatocytes ◽  
In Vitro Binding ◽  
Vitro Binding

Discovery of New AKT1 Inhibitors by Combination of In silico Structure Based Virtual Screening Approaches and Biological Evaluations

2019 ◽  
Author(s):  
Filip Fratev ◽  
Denisse A. Gutierrez ◽  
Renato J. Aguilera ◽  
suman sirimulla
Keyword(s):  
Virtual Screening ◽  
Success Rate ◽  
Protein Interactions ◽  
In Silico ◽  
Biological Data ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Screening Protocol ◽  
Screening Approaches

AKT1 is emerging as a useful target for treating cancer. Herein, we discovered a new set of ligands that inhibit the AKT1, as shown by in vitro binding and cell line studies, using a newly designed virtual screening protocol that combines structure-based pharmacophore and docking screens. Taking together with the biological data, the combination of structure based pharamcophore and docking methods demonstrated reasonable success rate in identifying new inhibitors (60-70%) proving the success of aforementioned approach. A detail analysis of the ligand-protein interactions was performed explaining observed activities.<br>

Sign in / Sign up

Export Citation Format

Share Document