Activity enhancement of the synthetic syrbactin proteasome inhibitor hybrid and biological evaluation in tumor cells

Biochemistry

Volumn 51, Issue 34, 2012, Pages 6880-6888

  Archer, Crystal R ^b,c   Groll, Michael ^d   Stein, Martin L ^d   Schellenberg, Barbara ^e   Clerc, Jérôme ^f   Kaiser, Markus ^f   Kondratyuk, Tamara P ^a   Pezzuto, John M ^a,c   Dudler, Robert ^e   Bachmann, André S ^a,b,c  

^a UNIVERSITY OF HAWAII AT HILO   (United States)

^b UNIVERSITY OF HAWAII   (United States)

^c UNIVERSITY OF HAWAII   (United States)

^d TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^e UNIVERSITY OF ZURICH   (Switzerland)

^f UNIVERSITY OF DUISBURG ESSEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVITY ENHANCEMENT; BIOLOGICAL EVALUATION; COVALENT BINDING; DRUG DEVELOPMENT; ETHER BOND; HYBRID MOLECULES; IN-VITRO; INHIBITORY EFFECT; MULTIPLE MYELOMA; NATURAL COMPOUNDS; NATURAL PRODUCT INHIBITORS; NEUROBLASTOMAS; OVARIAN CANCER CELLS; PROTEASOME INHIBITORS; PROTEASOMES; STRUCTURE ACTIVITY RELATIONSHIPS; TOTAL SYNTHESIS; TUMOR CELLS; X-RAY STRUCTURE;

MOLECULES;

CELL CULTURE;

CASPASE; CHYMOTRYPSIN; GLIDOBACTIN A; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LACTAM DERIVATIVE; LIGAND; NATURAL PRODUCT; PROTEASOME; PROTEASOME INHIBITOR; SYRBACTIN; SYRINGOLIN A; SYRINGOLIN A GLIDOBACTIN A HYBRID MOLECULE; TRYPSIN; UNCLASSIFIED DRUG;

ANTIPROLIFERATIVE ACTIVITY; ARTICLE; BINDING AFFINITY; CANCER CELL CULTURE; CANCER INHIBITION; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; CRYSTALLIZATION; DRUG BINDING SITE; DRUG EFFICACY; DRUG MECHANISM; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG SCREENING; DRUG SYNTHESIS; ENZYME ACTIVITY; ENZYME INHIBITION; EUKARYOTE; HUMAN; HUMAN CELL; IN VITRO STUDY; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ANTINEOPLASTIC AGENTS; CELL LINE, TUMOR; CELL PROLIFERATION; DRUG DESIGN; HUMANS; NEOPLASMS; PEPTIDES, CYCLIC; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEASOME INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84867496886     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300841r     Document Type: Article

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