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Hemodynamic Regulation of Metallopeptidases within the Vasculature
Protein & Peptide Letters, 2004Hemodynamic forces associated with blood flow play a vital role in the endothelial regulation of vascular tone, remodeling and the initiation and progression of vascular diseases such as atherosclerosis and hypertension. Crucial elements in endothelium-mediated events within the blood vessel are bioactive peptide signals and their associated hydrolytic
Philip M, Cummins +2 more
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Natural Inhibitors of Snake Venom Metallopeptidases
, 2015 Jonas Perales +2 more
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Mitochondrial metallopeptidase OMA1 in cancer
Our understanding of the roles that mitochondria play in cellular physiology has evolved drastically-from a mere cellular energy supplier to a crucial regulator of metabolic and signaling processes, particularly in the context of development and progression of human diseases such as cancers.Gunjan, Purohit +2 more
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Selective cleavage of pepsin by molybdenum metallopeptidase
Biochemical and Biophysical Research Communications, 2012In this study, the cleavage of protein by molybdenum cluster is reported for the first time. The protein target used is porcine pepsin. The data presented in this study show that pepsin is cleaved to at least three fragments with molecular weights of ∼23, ∼19 and ∼16 kDa when the mixture of the protein and ammonium heptamolybdate tetrahydrate ((NH(4 ...
Sudarat, Yenjai +3 more
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Metallopeptidase Inhibitors of Tetanus Toxin: A Combinatorial Approach
Journal of Medicinal Chemistry, 1999The bacterial protein tetanus toxin (TeNt), which belongs to the family of zinc endopeptidases, cleaves synaptobrevin, an essential synaptic protein component of the neurotransmitter exocytosis apparatus, at a single peptide bond (Gln76-Phe77). This protease activity is a particularly attractive target for designing potent and selective synthetic ...
Martin, Loïc +5 more
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The Journal of Physical Chemistry B, 2010
In this comparative DFT study, the hydrolysis of a peptide bond (Phe1-Phe2) by the following three types of catalysts has been studied: (1) beta-secretase (BACE2), (2) matrix metalloproteinase (MMP) and insulin degrading enzyme (IDE), and (3) [Pd(H(2)O)(4)](2+) (I(MPC)) and [Pd(2)(mu-OH)([18]aneN(6))](3+) (I(DPC)).
Ram Prasad, Bora +4 more
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In this comparative DFT study, the hydrolysis of a peptide bond (Phe1-Phe2) by the following three types of catalysts has been studied: (1) beta-secretase (BACE2), (2) matrix metalloproteinase (MMP) and insulin degrading enzyme (IDE), and (3) [Pd(H(2)O)(4)](2+) (I(MPC)) and [Pd(2)(mu-OH)([18]aneN(6))](3+) (I(DPC)).
Ram Prasad, Bora +4 more
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Inactivation of neurotensin and neuromedin N by Zn metallopeptidases
Peptides, 2006The two related peptides neurotensin (NT) and neuromedin N (NN) are efficiently inactivated by peptidases in vitro. Whereas NT is primarily degraded by a combination of three Zn metallo-endopeptidases, namely endopeptidases 24.11, 24.15 and 24.16, in all systems examined, NN is essentially inactivated by the Zn metallo-exopeptidase aminopeptidase M. In
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