Ivan E. Collier

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We show that activated collagenase (MMP-1) moves processively on the collagen fibril. The mechanism of movement is a biased diffusion with the bias component dependent on the proteolysis of its substrate, not adenosine triphosphate (ATP) hydrolysis. Inactivation of the enzyme by a single amino acid residue substitution in the active center eliminates the(More)
Remodeling of the extracellular matrix catalyzed by MMPs is central to morphogenetic phenomena during development and wound healing as well as in numerous pathologic conditions such as fibrosis and cancer. We have previously demonstrated that secreted MMP-2 is tethered to the cell surface and activated by MT1-MMP/TIMP-2-dependent mechanism. The resulting(More)
that can become rate-limiting. The activation energy for fibril digestion (101 kcal mol –1) was found to be 4 times that of a helical collagen monomer (26). The high energy of activation for collagenolysis is in good agreement , however, with the apparent energy of activation for collagen fibril unfolding (124 kcal mol –1) measured more recently (27). We(More)
The rate of ultraviolet light (UV)-induced DNA excision repair was determined in embryonic cells derived from a congeneic pair of short-lived (C57BL/10.F) and long-lived (C57BL/10) mice. Excision repair was measured by both bromodeoxyuridine photolysis and arabinofuranosyl cytosine inhibition. No difference in rate of repair was observed between the two(More)
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