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Volumn 133, Issue 19, 2011, Pages 7528-7535

Determining protease substrate selectivity and inhibition by label-free supramolecular tandem enzyme assays

Author keywords

[No Author keywords available]

Indexed keywords

ACRIDINE ORANGE; ANALYTICAL METHOD; AROMATIC AMINO ACID; CLEAVAGE PRODUCTS; CONTINUOUS MONITORING; CUCURBIT[7]URIL; ENZYMATIC CLEAVAGE; ENZYME ASSAYS; EXOPEPTIDASE ACTIVITY; FLUORESCENT DYES; HIGH AFFINITY; INHIBITION CONSTANTS; LABEL FREE; LABEL-FREE APPROACH; MACROCYCLES; N-TERMINALS; PHENYLALANINE RESIDUES; PROTEASE ACTIVITIES; PROTEASE INHIBITION; REAL TIME; SEQUENCE SPECIFICITY; STEREOSPECIFICITY; SUBSTRATE PEPTIDES; SUBSTRATE SELECTIVITY; THERMOLYSIN;

EID: 79955881748     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja2013467     Document Type: Article
Times cited : (171)

References (81)
  • 57
    • 79955899898 scopus 로고    scopus 로고
    • note
    • 1′ is the position of an amino acid at the C terminus of the cleavage site.
  • 61
    • 0003717374 scopus 로고    scopus 로고
    • M becomes the apparent bimolecular rate constant for the interaction between the substrate and the enzyme, cf.;;; 5th ed.; W. H. Freeman and Company: New York.
    • M becomes the apparent bimolecular rate constant for the interaction between the substrate and the enzyme, cf. Berg, J. M.; Tymoczko, J. L.; Stryer, L. Biochemistry; 5th ed.; W. H. Freeman and Company: New York, 2002.
    • (2002) Biochemistry
    • Berg, J.M.1    Tymoczko, J.L.2    Stryer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.