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11. Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences. Minond D; Lauer-Fields JL; Cudic M; Overall CM; Pei D; Brew K; Moss ML; Fields GB Biochemistry; 2007 Mar; 46(12):3724-33. PubMed ID: 17338550 [TBL] [Abstract][Full Text] [Related]
12. Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases. Lauer-Fields JL; Nagase H; Fields GB J Chromatogr A; 2000 Aug; 890(1):117-25. PubMed ID: 10976799 [TBL] [Abstract][Full Text] [Related]
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14. Monitoring metalloproteinase activity using synthetic fluorogenic substrates. Troeberg L; Nagase H Curr Protoc Protein Sci; 2004 Nov; Chapter 21():21.16.1-21.16.9. PubMed ID: 18429258 [TBL] [Abstract][Full Text] [Related]
15. Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. Hurst DR; Schwartz MA; Ghaffari MA; Jin Y; Tschesche H; Fields GB; Sang QX Biochem J; 2004 Feb; 377(Pt 3):775-9. PubMed ID: 14533979 [TBL] [Abstract][Full Text] [Related]
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18. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. Aimes RT; Quigley JP J Biol Chem; 1995 Mar; 270(11):5872-6. PubMed ID: 7890717 [TBL] [Abstract][Full Text] [Related]
19. Matrix metalloproteinase-1 takes advantage of the induced fit mechanism to cleave the triple-helical type I collagen molecule. O'Farrell TJ; Guo R; Hasegawa H; Pourmotabbed T Biochemistry; 2006 Dec; 45(51):15411-8. PubMed ID: 17176063 [TBL] [Abstract][Full Text] [Related]
20. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. Chung L; Dinakarpandian D; Yoshida N; Lauer-Fields JL; Fields GB; Visse R; Nagase H EMBO J; 2004 Aug; 23(15):3020-30. PubMed ID: 15257288 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]