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Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase
Matrix metalloproteases are secreted by mammalian cells as zymogens and, upon activation, initiate tissue remodeling by proteolytic degradation of collagens and proteoglycans. Activation of theExpand
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SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages.
We have reported that SV40-transformed human lung fibroblasts secrete a 92-kDa metalloprotease which is not detectable in the parental cell line IMR-90. We now present the complete structure of thisExpand
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Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in MycobacteriumExpand
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H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen.
H-ras-transformed human bronchial epithelial cells (TBE-1) secrete a single major extracellular matrix metalloprotease which is not found in the normal parental cells. The enzyme is secreted in aExpand
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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.
Simian virus 40 (SV40)-transformed human lung fibroblasts secrete both 72-kDa type IV collagenase and a closely related 92-kDa type IV collagenase that was not detected in the parental cell line. TheExpand
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The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase
The crystal structure of the phosphoglycerate dehydrogenase from Eschehchia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. TheExpand
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Tissue cooperation in a proteolytic cascade activating human interstitial collagenase.
We present a cascade of proteolytic events catalyzed by the proteases secreted by cultured keratinocytes and fibroblasts that results in the activation of interstitial procollagenase. Cultured humanExpand
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Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2.
Human 72-kDa type IV collagenase (72T4Cl) is secreted as a proenzyme that can form a specific stoichiometric complex with the tissue inhibitor of metalloproteases TIMP-2 via interaction with theExpand
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The ACT Domain: A Small Molecule Binding Domain and Its Role as a Common Regulatory Element*
  • G. A. Grant
  • Chemistry, Medicine
  • Journal of Biological Chemistry
  • 10 November 2006
The ACT domain is a structural motif in proteins of 70–80 amino acids that is one of a growing number of different intracellular small molecule binding domains that function in the control ofExpand
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Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.
We have determined the complete sequence of the cDNA clone representing the full size human skin collagenase mRNA. Collagenase is synthesized in preproenzyme form, Mr 54,092, with a 19 amino acidExpand
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