메뉴 건너뛰기




Volumn 18, Issue 24, 2008, Pages 6332-6335

Carbonic anhydrase inhibitors: 2-Substituted-1,3,4-thiadiazole-5-sulfamides act as powerful and selective inhibitors of the mitochondrial isozymes VA and VB over the cytosolic and membrane-associated carbonic anhydrases I, II and IV

Author keywords

Carbonic anhydrase; Isozyme VA and VB; Isozyme selective inhibitor; Mitochondria; Sulfamide

Indexed keywords

1,3,4 THIADIAZOLE 5 SULFAMIDE; ACETAZOLAMIDE; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE I; CARBONATE DEHYDRATASE II; CARBONATE DEHYDRATASE INHIBITOR; CARBONATE DEHYDRATASE IV; CARBONIC ANHYDRASE VA; CARBONIC ANHYDRASE VB; ISOENZYME; MITOCHONDRIAL ENZYME; SULFAMIDE DERIVATIVE; TOPIRAMATE; UNCLASSIFIED DRUG; ZONISAMIDE;

EID: 56249097203     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.10.093     Document Type: Article
Times cited : (37)

References (42)
  • 2
    • 56249105151 scopus 로고    scopus 로고
    • Supuran C.T., Scozzafava A., and Conway J. (Eds), CRC Press, Boca Raton (FL), USA and references cited therein
    • In: Supuran C.T., Scozzafava A., and Conway J. (Eds). Carbonic Anhydrase-Its Inhibitors and Activators (2004), CRC Press, Boca Raton (FL), USA 1-376 and references cited therein
    • (2004) Carbonic Anhydrase-Its Inhibitors and Activators , pp. 1-376
  • 27
    • 56249128663 scopus 로고    scopus 로고
    • note
    • 6) δ 7.14 (s, 2H), 3.5 (s, 3H), 3.16 (s, 1H).
  • 30
    • 56249115268 scopus 로고    scopus 로고
    • Di Fiore, A.; Monti, S. M.; Hilvo, M.; Parkkila, S.; Romano, V.; Scaloni, A.; Pedone, C.; Scozzafava, A.; Supuran, C.T.; De Simone, G. Proteins 2008, in press.
    • Di Fiore, A.; Monti, S. M.; Hilvo, M.; Parkkila, S.; Romano, V.; Scaloni, A.; Pedone, C.; Scozzafava, A.; Supuran, C.T.; De Simone, G. Proteins 2008, in press.
  • 42
    • 0015239422 scopus 로고    scopus 로고
    • note
    • 2 concentrations ranged from 1.7 to 17 mM for the determination of the kinetic parameters and inhibition constants. For each inhibitor at least six traces of the initial 5-10% of the reaction have been used for determining the initial velocity. The uncatalyzed rates were determined in the same manner and subtracted from the total observed rates. Stock solutions of inhibitor (10 mM) were prepared in distilled-deionized water with 10-20% (v/v) DMSO (which is not inhibitory at these concentrations) and dilutions up to 0.1 nM were done thereafter with distilled-deionized water. Inhibitor and enzyme solutions were preincubated together for 15 min at room temperature prior to assay, in order to allow for the formation of the E-I complex. The inhibition constants were obtained by non-linear least-squares methods using PRISM 3, and represent the mean from at least three different determinations.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.