Page last updated: 2024-08-22

vanadates and flupenthixol

vanadates has been researched along with flupenthixol in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ambudkar, SV; Dey, S; Gottesman, MM; Pastan, I; Ramachandra, M	1
Dey, S; Ghosh, P; Maki, N; Moitra, K	1

Other Studies

2 other study(ies) available for vanadates and flupenthixol

Article	Year
Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein. Proceedings of the National Academy of Sciences of the United States of America, 1997, Sep-30, Volume: 94, Issue:20 Topics: 3T3 Cells; Affinity Labels; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; Biological Transport; Cell Line; Cyclosporine; Flupenthixol; Humans; Insecta; Iodine Radioisotopes; Mice; Models, Biological; Prazosin; Radioligand Assay; Vanadates; Vinblastine	1997
Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein. The Journal of biological chemistry, 2006, Apr-21, Volume: 281, Issue:16 Topics: Adenosine Diphosphate; Adenosine Triphosphate; Allosteric Site; Animals; ATP Binding Cassette Transporter, Subfamily B; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; Catalytic Domain; Cell Line; Cell Membrane; Flupenthixol; Humans; Hydrolysis; Insecta; Ligands; Molecular Conformation; Prazosin; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Thioxanthenes; Time Factors; Trypsin; Vanadates	2006

Article

Year

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein.

Proceedings of the National Academy of Sciences of the United States of America, 1997, Sep-30, Volume: 94, Issue:20

Topics: 3T3 Cells; Affinity Labels; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; Biological Transport; Cell Line; Cyclosporine; Flupenthixol; Humans; Insecta; Iodine Radioisotopes; Mice; Models, Biological; Prazosin; Radioligand Assay; Vanadates; Vinblastine

1997

Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein.

The Journal of biological chemistry, 2006, Apr-21, Volume: 281, Issue:16

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Allosteric Site; Animals; ATP Binding Cassette Transporter, Subfamily B; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Binding Sites; Catalytic Domain; Cell Line; Cell Membrane; Flupenthixol; Humans; Hydrolysis; Insecta; Ligands; Molecular Conformation; Prazosin; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Thioxanthenes; Time Factors; Trypsin; Vanadates

2006