Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria

The high‐affinity binding of tissue inhibitors of metalloproteinases (TIMPs) to matrix metalloproteinases (MMPs) is essential for regulation of the turnover of the extracellular matrix during development, wound healing, and progression of inflammatory diseases, such as cancer, atherosclerosis, and a...

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Veröffentlicht in:	Biopolymers 2008-11, Vol.89 (11), p.960-968
Hauptverfasser:	Van Doren, Steven R., Wei, Shuo, Gao, Guanghua, DaGue, Beverly B., Palmier, Mark O., Bahudhanapati, Harinath, Brew, Keith
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Amino Acid Motifs Aminoacyltransferases - metabolism Animals Chromatography, Liquid Escherichia coli - enzymology Escherichia coli Proteins Gene Expression Humans Matrix Metalloproteinase 12 - chemistry Matrix Metalloproteinase 12 - metabolism Matrix Metalloproteinase Inhibitors MMP inhibitor MS/MS sequencing N-acetylation Protein Binding Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Tissue Inhibitor of Metalloproteinase-1 - chemistry Tissue Inhibitor of Metalloproteinase-1 - isolation & purification Tissue Inhibitor of Metalloproteinase-1 - metabolism
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