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The Journal of Biological Chemistry|July 5, 1993
Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2A Y Strongin, B L Marmer, G A Grant, et al.
Biophysical Journal|September 22, 2001
Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusionI E Collier, S Saffarian, B L Marmer, et al.
The Journal of Biological Chemistry|April 25, 1987
The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion productsG A Grant, A Z Eisen, B L Marmer, et al.
The Journal of Biological Chemistry|March 10, 1995
Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteaseA Y Strongin, I Collier, G Bannikov, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1989
Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2G I Goldberg, B L Marmer, G A Grant, et al.
Nature Structural Biology|November 1, 1995
Crystal structure of the haemopexin-like C-terminal domain of gelatinase AA M Libson, A G Gittis, I E Collier, et al.
Kidney International|January 1, 1993
Human 92 kDa type IV collagenase: functional analysis of fibronectin and carboxyl-end domainsA Y Strongin, I E Collier, P A Krasnov, et al.
Matrix (Stuttgart, Germany). Supplement|January 1, 1992
Mosaic structure of the secreted ECM metalloproteases and interaction of the type IV collagenases with inhibitorsG I Goldberg, I E Collier, A Z Eisen, et al.
The Journal of Biological Chemistry|October 15, 1989
SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophagesS M Wilhelm, I E Collier, B L Marmer, et al.
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