Structure-based calculation of binding affinities of alpha 2A-adrenoceptor agonists.
Balogh
Balázs
B
Department of Organic Chemistry, Semmelweis University, Hogyes E. u. 7. 1095 Budapest, Hungary.
Hetényi
Csaba
C
Keseru
Miklós György
MG
Mátyus
Péter
P
D058647:Adrenergic alpha-2 Receptor Agonists; D000316:Adrenergic alpha-Agonists / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000187:drug effects / Q000235:genetics; D002417:Cattle; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding / Q000187:drug effects / Q000235:genetics; D011487:Protein Conformation; D018341:Receptors, Adrenergic, alpha-2 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012243:Rhodopsin / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
C547768:ADRA2A protein, human; D058647:Adrenergic alpha-2 Receptor Agonists; D000316:Adrenergic alpha-Agonists; D008024:Ligands; D018341:Receptors, Adrenergic, alpha-2; D012243:Rhodopsin