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Volumn 119, Issue 25, 1997, Pages 5828-5832

Stromelysin inhibitors designed from weakly bound fragments: Effects of linking and cooperativity

Author keywords

[No Author keywords available]

Indexed keywords

ACETOHYDROXAMIC ACID; MATRIX METALLOPROTEINASE; STROMELYSIN; STROMELYSIN INHIBITOR;

EID: 0030829408     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9702780     Document Type: Article
Times cited : (90)

References (19)
  • 18
    • 16944365938 scopus 로고    scopus 로고
    • note
    • In the case of stromelysin, the intrinsic binding energy of the biaryl ligands is that measured in the absence of acetohydroxamic acid. The additional enthalpic interactions between the biaryl and acetohydroxamic acid in the ternary complexes are irrelevant in the linked compounds. Therefore, the additional gains in binding observed for the untethered compounds due to cooperative effects were not included in the intrinsic binding energies, ΔG(A) and ΔG(B).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.