H
Hideaki Nagase
Researcher at University of Oxford
Publications - 302
Citations - 37777
Hideaki Nagase is an academic researcher from University of Oxford. The author has contributed to research in topics: Matrix metalloproteinase & ADAMTS. The author has an hindex of 91, co-authored 299 publications receiving 35655 citations. Previous affiliations of Hideaki Nagase include University of Nebraska Medical Center & University of Southampton.
Papers
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Journal ArticleDOI
Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Robert Visse,Hideaki Nagase +1 more
TL;DR: This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.
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Structure and function of matrix metalloproteinases and TIMPs
TL;DR: The members of the MMP family are introduced and their domain structure and function, proenyme activation, the mechanism of inhibition by TIMPs and their significance in physiology and pathology are discussed.
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Tissue inhibitors of metalloproteinases: evolution, structure and function.
TL;DR: The evolution of TIMPs, the recently elucidated high-resolution structures of TIMP and their complexes with metalloproteinases, and the results of mutational and other studies of structure-function relationships that have enhanced understanding of the mechanism and specificity of the inhibition of MMPs by TIMPs are highlighted.
Journal Article
Activation mechanisms of matrix metalloproteinases.
TL;DR: Recent progress made to elucidate the activation mechanisms of pro-matrixins are described which include extracellular stepwise activation common to most proMMPs, cell surface activation of progelatinase A and procollagenase 3, and intracellular activation of prostromelysin 3 and pro-membrane-type-1 MMP.
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The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity
Keith Brew,Hideaki Nagase +1 more
TL;DR: Tissue inhibitors of metalloproteinases (TIMPs) are widely distributed in the animal kingdom and the human genome contains four paralogous genes encoding TIMPs 1 to 4, and their range of activities has now been found to be broader as it includes the inhibition of several of the disintegrin-metallop proteinases, ADAMs and ADAMTSs.