Increasing the efficiency of ligands for FK506-binding protein 51 by conformational control

Journal of Medicinal Chemistry

Volumn 56, Issue 10, 2013, Pages 3922-3935

  Wang, Yansong ^a,b   Kirschner, Alexander ^a   Fabian, Anne Katrin ^a   Gopalakrishnan, Ranganath ^a,c   Kress, Christoph ^a,d   Hoogeland, Bastiaan ^a   Koch, Uwe ^e   Kozany, Christian ^a   Bracher, Andreas ^f   Hausch, Felix ^a  

^a MAX PLANCK INSTITUTE OF PSYCHIATRY   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c EPFL   (Switzerland)

^d Synchem UG and Company   (Germany)

^e Lead Discovery Center GmbH   (Germany)

^f MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

9,13 IMINO 8H AZOCINO[2,1 A]ISOQUINOLIN 8 ONE, 14 [(3,5 DICHLORO 4 HYDROXYPHENYL)SULFONYL] 5,6,9,10,11,12,13,13ALPHA OCTAHYDRO 1,3 DIMETHOXY; 9,13 IMINO 8H AZOCINO[2,1 A]ISOQUINOLIN 8 ONE, 14 [2 [(2 ETHYL 1 HYDROXYCYCLOHEXYL) 2 OXOACETYL] 5,,9,10,11,12,133ALPHA OCTAHYDRO 1,3 DIMETHOXY; 9,13 IMINO 8H AZOCINO[2,1 A]ISOQUINOLIN 8 ONE, 14 [3,3 DIMETHYL 2 OXOPENTANOYL] 5,6,9,10,11,12,13,13ALPHA OCTAHYDRO 1,3 DIMETHOXY; 9,13 IMINO 8H AZOCINO[2,1ALPHA]ISOQUINOLIN 8 ONE, 14 [(3,5 DICHLOROPHENYL)SULFONYL] 5,6,9,10,11,12,13,13ALPHA OCTAHYDRO 1,3 DI METHOXY; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 51; NITROGEN; PROTEIN P51; SCAFFOLD PROTEIN; SULFONAMIDE; TACROLIMUS; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; ATOM; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYCLIZATION; DRUG PROTEIN BINDING; ENTHALPY; ENTROPY; HYDROGEN BOND; LIGAND BINDING; PHASE TRANSITION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF;

BICYCLO COMPOUNDS; BINDING SITES; CALORIMETRY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRYSTALLOGRAPHY; DRUG DESIGN; HUMANS; IMMUNOSUPPRESSIVE AGENTS; INDICATORS AND REAGENTS; LIGANDS; PROTEIN CONFORMATION; RECEPTORS, GONADOTROPIN; STRUCTURE-ACTIVITY RELATIONSHIP; SULFONAMIDES; TACROLIMUS; TACROLIMUS BINDING PROTEINS;

EID: 84878027311     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400087k     Document Type: Article

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