Metalloproteinase inhibitor 1

[1]. V Knäuper, et al. Biochemical characterization of human collagenase-3. J Biol Chem. 1996 Jan 19;271(3):1544-50. [Content Brief]

[2]. Soo Youn Lee, et al. TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling. Biochem J. 2014 May 1;459(3):565-76. [Content Brief]

[3]. J C Gasson, et al. Molecular characterization and expression of the gene encoding human erythroid-potentiating activity. Nature. 1985;315(6022):768-71. [Content Brief]

[4]. Ki-Kyung Jung, et al. Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. EMBO J. 2006 Sep 6;25(17):3934-42. [Content Brief]

[5]. A J Docherty, et al. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature. 1985 Nov;318(6041):66-9. [Content Brief]

[6]. L Chesler, et al. Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1. Blood. 1995 Dec 15;86(12):4506-15. [Content Brief]

[7]. A Osthues, et al. Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid. FEBS Lett. 1992 Jan 13;296(1):16-20. [Content Brief]

[8]. Moran Grossman, et al. The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function. Biochemistry. 2010 Jul 27;49(29):6184-92. [Content Brief]

[9]. Shalini Iyer, et al. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1. J Biol Chem. 2007 Jan 5;282(1):364-71. [Content Brief]

[10]. Jyotica Batra, et al. Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure. J Biol Chem. 2012 May 4;287(19):15935-46. [Content Brief]

[11]. M O'Shea, et al. Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13. Biochemistry. 1992 Oct 27;31(42):10146-52. [Content Brief]

[12]. V Knäuper, et al. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem. 1997 Mar 21;272(12):7608-16. [Content Brief]