Page last updated: 2024-08-17

aspartic acid and (3h)2-carbomethoxy-3-(4-fluorophenyl)tropane

aspartic acid has been researched along with (3h)2-carbomethoxy-3-(4-fluorophenyl)tropane in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's5 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chen, N; Reith, ME; Vaughan, RA1
Chen, N; Dutta, AK; Maiti, S; Reith, ME; Zhen, J1
Bondi, CD; Kozikowski, AP; Kulkarni, SS; Newman, AH; Pan, S; Surratt, CK; Ukairo, OT1
Ambrosio, E; Crespo, JA; Del Olmo, N; García-Lecumberri, C; Higuera-Matas, A; Miguéns, M; Montoya, GL1
Chen, N; Dutta, AK; Kharkar, P; Mishra, M; Reith, ME; Schmitt, KC; Zhen, J1

Other Studies

5 other study(ies) available for aspartic acid and (3h)2-carbomethoxy-3-(4-fluorophenyl)tropane

ArticleYear
The role of conserved tryptophan and acidic residues in the human dopamine transporter as characterized by site-directed mutagenesis.
    Journal of neurochemistry, 2001, Volume: 77, Issue:4

    Topics: Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Carrier Proteins; Cell Line; Cocaine; Conserved Sequence; Dopamine; Dopamine Plasma Membrane Transport Proteins; Humans; Kinetics; Mazindol; Membrane Glycoproteins; Membrane Transport Proteins; Models, Molecular; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Protein Structure, Secondary; Radioligand Assay; Recombinant Proteins; Transfection; Tritium; Tryptophan

2001
Interaction between a hydroxypiperidine analogue of 4-(2-benzhydryloxy-ethyl)-1-(4-fluorobenzyl)piperidine and Aspartate 68 in the human dopamine transporter.
    European journal of pharmacology, 2004, Dec-03, Volume: 506, Issue:1

    Topics: Animals; Aspartic Acid; Benzhydryl Compounds; Binding Sites; Binding, Competitive; Biological Transport; Cell Line; Cell Membrane; Cerebral Cortex; Cocaine; Corpus Striatum; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dose-Response Relationship, Drug; Humans; Male; Membrane Glycoproteins; Membrane Transport Proteins; Models, Molecular; Mutation; Nerve Tissue Proteins; Norepinephrine; Piperazines; Piperidines; Protein Binding; Rats; Rats, Sprague-Dawley; Serotonin; Stereoisomerism; Synaptosomes; Tritium

2004
Recognition of benztropine by the dopamine transporter (DAT) differs from that of the classical dopamine uptake inhibitors cocaine, methylphenidate, and mazindol as a function of a DAT transmembrane 1 aspartic acid residue.
    The Journal of pharmacology and experimental therapeutics, 2005, Volume: 314, Issue:2

    Topics: Amino Acid Substitution; Animals; Aspartic Acid; Benztropine; Binding, Competitive; CHO Cells; Cocaine; Cricetinae; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Humans; Immunohistochemistry; Kinetics; Ligands; Mazindol; Membrane Glycoproteins; Membrane Transport Proteins; Methylphenidate; Microscopy, Confocal; Models, Molecular; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Transfection

2005
Differential cocaine-induced modulation of glutamate and dopamine transporters after contingent and non-contingent administration.
    Neuropharmacology, 2008, Volume: 55, Issue:5

    Topics: Amino Acid Transport System X-AG; Animals; Aspartic Acid; Autoradiography; Behavior, Animal; Cocaine; Conditioning, Operant; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Extinction, Psychological; Male; Multivariate Analysis; Protein Binding; Random Allocation; Rats; Rats, Inbred Lew; Reinforcement, Psychology; Self Administration; Time Factors; Tritium

2008
Interaction of cocaine-, benztropine-, and GBR12909-like compounds with wild-type and mutant human dopamine transporters: molecular features that differentially determine antagonist-binding properties.
    Journal of neurochemistry, 2008, Volume: 107, Issue:4

    Topics: Animals; Asparagine; Aspartic Acid; Benztropine; Binding, Competitive; Cell Line, Transformed; Cocaine; Dopamine Plasma Membrane Transport Proteins; Dopamine Uptake Inhibitors; Drug Interactions; Humans; Leucine; Models, Molecular; Mutation; Piperazines; Protein Binding; Protein Structure, Tertiary; Sodium; Structure-Activity Relationship; Transfection; Tritium; Tryptophan

2008