Synthesis, in vitro binding profile, and autoradiographic analysis of [3H]-cis-3-[(2-methoxybenzyl)amino]-2-phenylpiperidine, a highly potent and selective nonpeptide substance P receptor antagonist radioligand

1993 ◽  
Vol 36 (21) ◽  
pp. 3197-3201 ◽  
Author(s):  
Terry Rosen ◽  
Thomas F. Seeger ◽  
Stafford McLean ◽  
Manoj C. Desai ◽  
Karen J. Guarino ◽  
...  
Keyword(s):  
Substance P ◽  
Receptor Antagonist ◽  
Binding Profile ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Substance P Receptor ◽  
Autoradiographic Analysis

Synthesis, in vitro binding profile, and CNS penetrability of the highly potent 5-HT3 receptor antagonist [3H]-4-(2-methoxyphenyl)-2-[4(5)-methyl-5(4)-imidazolylmethyl]thiazole

1990 ◽  
Vol 33 (11) ◽  
pp. 3020-3023 ◽  
Author(s):  
Terry Rosen ◽  
Thomas F. Seeger ◽  
Stafford McLean ◽  
Arthur A. Nagel ◽  
Jefferey L. Ives ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Binding Profile ◽  
In Vitro Binding ◽  
Vitro Binding

Mechanistic insights into a novel chromone-appended Cu(ii) anticancer drug entity: in vitro binding profile with DNA/RNA substrates and cytotoxic activity against MCF-7 and HepG2 cancer cells

2015 ◽  
Vol 44 (22) ◽  
pp. 10330-10342 ◽  
Author(s):  
Imtiyaz Yousuf ◽  
Farukh Arjmand ◽  
Sartaj Tabassum ◽  
Loic Toupet ◽  
Rais Ahmad Khan ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Mtt Assay ◽  
Rna Binding ◽  
Ros Generation ◽  
Binding Studies ◽  
Binding Profile ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Mcf 7

DNA/RNA binding studies, the MTT assay and ROS generation by complex 1.

Autoradiographic analysis of the in vivo distribution of 3H-imipramine and 3H-desipramine in brain: Comparison to in vitro binding patterns

1991 ◽  
Vol 38 (3) ◽  
pp. 621-631 ◽  
Author(s):  
Gary E. Duncan ◽  
Ian A. Paul ◽  
Jonathan B. Fassberg ◽  
Kelly R. Powell ◽  
Walter E. Stumpf ◽  
...  
Keyword(s):  
In Vitro Binding ◽  
In Vivo Distribution ◽  
Vitro Binding ◽  
Autoradiographic Analysis

Tritiated kappa receptor antagonist norbinaltorphimine: Synthesis and in vitro binding in three different tissues

Life Sciences ◽  
1999 ◽  
Vol 66 (1) ◽  
pp. 43-49 ◽  
Author(s):  
Á. Márki ◽  
F. Ötvös ◽  
G. Tóth ◽  
S. Hosztafi ◽  
A. Borsodi
Keyword(s):  
Receptor Antagonist ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Kappa Receptor ◽  
Different Tissues

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>

scholarly journals ADP-ribosylation of integrin α7 modulates the binding of integrin α7β1 to laminin

2004 ◽  
Vol 385 (1) ◽  
pp. 309-317 ◽  
Author(s):  
Zhefeng ZHAO ◽  
Joanna GRUSZCZYNSKA-BIEGALA ◽  
Anna ZOLKIEWSKA
Keyword(s):  
C2c12 Myotubes ◽  
Post Translational Modification ◽  
Integrin Β1 ◽  
Adp Ribosylation ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
C2c12 Skeletal Muscle Cells ◽  
Adp Ribosyltransferase

The extracellular domain of integrin α7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 skeletal muscle cells. The effect of ADP-ribosylation on the structure or function of integrin α7β1 has not been explored. In the present study, we show that ADP-ribosylation of integrin α7 takes place exclusively in differentiated myotubes and that this post-translational modification modulates the affinity of α7β1 dimer for its ligand, laminin. ADP-ribosylation in the 37-kDa ‘stalk’ region of α7 that takes place at micromolar NAD+ concentrations increases the binding of the α7β1 dimer to laminin. Increased in vitro binding of integrin α7β1 to laminin after ADP-ribosylation of the 37-kDa fragment of α7 requires the presence of Mn2+ and it is not observed in the presence of Mg2+. In contrast, ADP-ribosylation of the 63-kDa N-terminal region comprising the ligand-binding site of α7 that occurs at approx. 100 μM NAD+ inhibits the binding of integrin α7β1 to laminin. Furthermore, incubation of C2C12 myotubes with NAD+ increases the expression of an epitope on integrin β1 subunit recognized by monoclonal antibody 9EG7. We discuss our results based on the current models of integrin activation. We also hypothesize that ADP-ribosylation may represent a mechanism of regulation of integrin α7β1 function in myofibres in vivo when the continuity of the membrane is compromised and NAD+ is available as a substrate for ecto-ADP-ribosylation.

IC-P-199: Comparing [3 H]MK-6240 and [3 H]AV-1451(T-807) In In vitro Binding Studies in Brain Tissues

2016 ◽  
Vol 12 ◽  
pp. P144-P144
Author(s):  
Zhizhen Zeng ◽  
Patricia J. Miller ◽  
Brett M. Connolly ◽  
Stacey S. O’Malley ◽  
Idriss Bennacef ◽  
...  
Keyword(s):  
Binding Studies ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Brain Tissues
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