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Volumn 238, Issue 2, 2004, Pages 77-83

An affinity selection-mass spectrometry method for the identification of small molecule ligands from self-encoded combinatorial libraries: Discovery of a novel antagonist of E. coli dihydrofolate reductase

Author keywords

Affinity selection mass spectrometry; Combinatorial chemistry; Multidimensional chromatography

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; ENZYME INHIBITOR;

EID: 8444221197     PISSN: 13873806     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijms.2003.11.022     Document Type: Article
Times cited : (118)

References (43)
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    • note
    • Mass overlap can be tolerated as MS/MS experiments or independent syntheses can be used to deconvolute isobaric ligands, vide infra.
  • 37
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    • note
    • Pooling libraries allows significantly more compounds to be screened per unit of target and time than screening in a non-multiplexed fashion.
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    • 0019461081 scopus 로고
    • E. coli DHFR was purified to apparent homogeneity as determined by SDS-PAGE according to standard procedures: D.P. Baccanari, D. Stone, L. Kuyper, J. Biol. Chem. 256 (1981) 1738.
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    • 8444236708 scopus 로고    scopus 로고
    • note
    • While discovery libraries are designed to maximize diversity, optimization libraries can be designed to investigate subtle changes in building block and template structure to improve binding affinity and to determine structure-activity relationships.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.