Protein knockdown using methyl bestatin-ligand hybrid molecules: Design and synthesis of inducers of ubiquitination-mediated degradation of cellular retinoic acid-binding proteins

Journal of the American Chemical Society

Volumn 132, Issue 16, 2010, Pages 5820-5826

  Itoh, Yukihiro ^a   Ishikawa, Minoru ^a   Naito, Mikihiko ^b   Hashimoto, Yuichi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALL-TRANS RETINOIC ACIDS; BIOLOGICAL RESEARCH; CELL MIGRATION; CELLULAR ASSAYS; CELLULAR INHIBITORS; CHEMICAL TOOLS; HYBRID MOLECULES; IN-CELL; IN-VITRO; NEUROBLASTOMAS; POTENTIAL VALUES; PROTEASOMAL DEGRADATION; RETINOIC ACIDS; SELECTIVE DEGRADATION; SMALL MOLECULES; TARGET PROTEINS; THERAPEUTIC AGENTS; TUMOR METASTASIS; UBIQUITIN LIGASES; UBIQUITINATION;

ACIDS; CELL DEATH; CHELATION; DEGRADATION; LIGANDS; MOLECULES; SYNTHESIS (CHEMICAL); TARGETS;

PROTEINS;

BESTATIN DERIVATIVE; CELLULAR RETINOL BINDING PROTEIN; CELLULAR RETINOL BINDING PROTEIN 1; CELLULAR RETINOL BINDING PROTEIN II; INHIBITOR OF APOPTOSIS PROTEIN 1; LIGAND; METHYL BESTATIN; RETINOIC ACID; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; ( ) N ((2S,3R) 3 AMINO 2 HYDROXY 4 PHENYL BUTYRYL) L LEUCINE METHYL ESTER; (-)-N-((2S,3R)-3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYL)-L-LEUCINE METHYL ESTER; DRUG DERIVATIVE; INHIBITOR OF APOPTOSIS PROTEIN; LEUCINE; RETINOIC ACID RECEPTOR;

APOPTOSIS; ARTICLE; CANCER INHIBITION; CELL ASSAY; CELL MEMBRANE PERMEABILITY; CELL MIGRATION; COMPLEX FORMATION; CONTROLLED STUDY; DRUG MECHANISM; ENZYME ACTIVITY; HUMAN; HUMAN CELL; HYBRID; NEUROBLASTOMA; PROTEIN DEGRADATION; PROTEIN TARGETING; SYNTHESIS; TUMOR CELL; UBIQUITINATION; CANCER INVASION; CELL MOTION; CHEMISTRY; DRUG DESIGN; DRUG EFFECT; METABOLISM; TUMOR CELL LINE;

CELL LINE, TUMOR; CELL MOVEMENT; DRUG DESIGN; HUMANS; INHIBITOR OF APOPTOSIS PROTEINS; LEUCINE; LIGANDS; NEOPLASM INVASIVENESS; RECEPTORS, RETINOIC ACID; TRETINOIN; UBIQUITINATION;

EID: 77952565704     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja100691p     Document Type: Article

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