Characterization of the in vitro Binding of [3H] DP-5,6-ADTN to Rat Striatal Membranes

1986 ◽  
pp. 405-406
Author(s):  
T. B. A. Mulder ◽  
C. J. Grol ◽  
D. Dijkstra ◽  
A. S. Horn
Keyword(s):  
In Vitro Binding ◽  
Vitro Binding

Characterization of anti oLHβ-antibodies acting as contraceptives in rhesus monkeys. I. In vitro binding properties

1982 ◽  
Vol 4 (5) ◽  
pp. 295-311 ◽  
Author(s):  
Yukio Yamamoto ◽  
Glen L. Gunsalus ◽  
Kalyan Sundaram ◽  
Rosemarie B. Thau
Keyword(s):  
Rhesus Monkeys ◽  
Binding Properties ◽  
In Vitro Binding ◽  
Vitro Binding

scholarly journals Characterization of Influenza Virus PB1 Protein Binding to Viral RNA: Two Separate Regions of the Protein Contribute to the Interaction Domain

1999 ◽  
Vol 73 (1) ◽  
pp. 631-637 ◽  
Author(s):  
Susana González ◽  
Juan Ortín
Keyword(s):  
Influenza Virus ◽  
Experimental Approach ◽  
Viral Rna ◽  
Deletion Mutants ◽  
Interaction Domain ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
In Vitro Interaction

ABSTRACT The interaction of the PB1 subunit of the influenza virus polymerase with the viral RNA (vRNA) template has been studied in vitro. The experimental approach included the in vitro binding of labeled model vRNA to PB1 protein immobilized as an immunoprecipitate, as well as Northwestern analyses. The binding to model vRNA was specific, and an apparent Kd of about 2 × 10−8 M was determined. Although interaction with the isolated 3′ arm of the panhandle was detectable, interaction with the 5′ arm was prominent and the binding was optimal with a panhandle analog structure (5′+3′ probe). When presented with a panhandle analog mixed probe, PB1 was able to retain the 3′ arm as efficiently as the 5′ arm. The sequences of the PB1 protein involved in vRNA binding were identified by in vitro interaction tests with PB1 deletion mutants. Two separate regions of the PB1 protein sequence proved positive for binding: the N-terminal 83 amino acids and the C-proximal sequences located downstream of position 493. All mutants able to interact with model vRNA were capable of binding the 5′ arm more efficiently than the 3′ arm of the panhandle. Taken together, these results suggest that two separate regions of the PB1 protein constitute a vRNA binding site that interacts preferentially with the 5′ arm of the panhandle structure.

Molecular characterization of the lam locus and sequences involved in regulation by the AmdR protein of Aspergillus nidulans

1992 ◽  
Vol 12 (1) ◽  
pp. 337-346
Author(s):  
I B Richardson ◽  
M E Katz ◽  
M J Hynes
Keyword(s):  
Aspergillus Nidulans ◽  
Regulatory Gene ◽  
Regulatory Elements ◽  
Specific Factor ◽  
Carbon And Nitrogen ◽  
In Vitro Binding ◽  
Vitro Binding

The lam locus of Aspergillus nidulans consists of two divergently transcribed genes, lamA and lamB, involved in the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. The lamB gene and the region between the two genes have been sequenced, and the start points of transcription have been determined. Within the lam locus are two sequences with homology to elements, required for AmdR regulation, found in the 5' regions of the coregulated genes amdS and gatA. In vitro and in vivo assays were used to investigate the lam and gatA regulatory elements. One of the three gatA elements and one of the two lam elements were shown to bind AmdR protein in vivo and activate transcription. With a gel shift mobility assay, in vitro binding of AmdR protein to the functional gatA element was detected. Both the functional gatA and lam boxes contain within them a CAAT sequence. In vitro binding analysis indicates that a CCAAT-specific factor(s) binds at these sequences, adjacent to or overlapping the AmdR protein-binding site.

scholarly journals Molecular characterization of the lam locus and sequences involved in regulation by the AmdR protein of Aspergillus nidulans.

1992 ◽  
Vol 12 (1) ◽  
pp. 337-346 ◽  
Author(s):  
I B Richardson ◽  
M E Katz ◽  
M J Hynes
Keyword(s):  
Aspergillus Nidulans ◽  
Regulatory Gene ◽  
Regulatory Elements ◽  
Specific Factor ◽  
Carbon And Nitrogen ◽  
In Vitro Binding ◽  
Vitro Binding

The lam locus of Aspergillus nidulans consists of two divergently transcribed genes, lamA and lamB, involved in the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. The lamB gene and the region between the two genes have been sequenced, and the start points of transcription have been determined. Within the lam locus are two sequences with homology to elements, required for AmdR regulation, found in the 5' regions of the coregulated genes amdS and gatA. In vitro and in vivo assays were used to investigate the lam and gatA regulatory elements. One of the three gatA elements and one of the two lam elements were shown to bind AmdR protein in vivo and activate transcription. With a gel shift mobility assay, in vitro binding of AmdR protein to the functional gatA element was detected. Both the functional gatA and lam boxes contain within them a CAAT sequence. In vitro binding analysis indicates that a CCAAT-specific factor(s) binds at these sequences, adjacent to or overlapping the AmdR protein-binding site.

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>

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