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Current Opinion in Clinical Nutrition and Metabolic Care, 2001
The mechanisms of proteolysis remain to be fully defined. This review focuses on recent advances in our understanding of the ubiquitin-proteasome-dependent pathway, which is involved in the control of many major biological functions. The ubiquitinylation/deubiquitinylation system is a complex machinery responsible for the specific tagging and proof ...
Attaix, Didier +3 more
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The mechanisms of proteolysis remain to be fully defined. This review focuses on recent advances in our understanding of the ubiquitin-proteasome-dependent pathway, which is involved in the control of many major biological functions. The ubiquitinylation/deubiquitinylation system is a complex machinery responsible for the specific tagging and proof ...
Attaix, Didier +3 more
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Proteolysis as a Regulatory Mechanism
Annual Review of Genetics, 2004▪ Abstract  Proteases can play key roles in regulation by controlling the levels of critical components of, for example, signal transduction pathways. Proteolytic processing can remove regulatory proteins when they are not needed, while transforming others from the dormant into the biologically active state.
Ehrmann, Michael, Clausen, Tim
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Trends in Genetics, 1999
Our present understanding of intracellular protein degradation developed from an attempt to understand the metabolic stability of proteins in cells. With the unravelling of its complex biochemical machinery has come a realization that protein degradation plays an important role in the most crucial events in the cell cycle, in signal transduction and in
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Our present understanding of intracellular protein degradation developed from an attempt to understand the metabolic stability of proteins in cells. With the unravelling of its complex biochemical machinery has come a realization that protein degradation plays an important role in the most crucial events in the cell cycle, in signal transduction and in
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1977
The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS
R, Mecham, J A, Foster, C, Franzblau
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The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS
R, Mecham, J A, Foster, C, Franzblau
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Proteolysis in the rat lung: hypoxia and evidence for an inhibitor of proteolysis
American Journal of Physiology-Endocrinology and Metabolism, 1981We labeled proteins with [14C]phenylalanine in rats breathing air and assessed the rate of proteolysis in the isolated ventilated lung by measuring the accumulation of [14C]phenylalanine in the medium perfusing the lung. Ventilation with 0% O2 decreased the rate of proteolysis and the ATP content in the lung 60%.
M J, Chiang +3 more
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Intramembrane proteolysis by presenilins
Nature Reviews Molecular Cell Biology, 2000Many neurodegenerative diseases involve the deposition of insoluble amyloid molecules. In Alzheimer's disease, for example, the amyloid beta-peptide (A beta) is the main component of the characteristic senile plaques. Proteolytic enzymes called secretases are involved in generating A beta, and one of these may have been identified as presenilin--a ...
H, Steiner, C, Haass
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The course of proteolysis of lysozyme
Archives of Biochemistry and Biophysics, 1956Abstract The course of proteolysis of lysozyme by chymotrypsin, trypsin, papain at three pH's, and pepsin is reported with tabulation of progressive exposure of 15 N-residue types and 12 C-residue types. A marked similarity in pattern of hydrolysis has been observed.
S W, FOX, T L, HURST
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Stimulation of proteolysis on calmodulin
Life Sciences, 1990The proteolysis of calmodulin by fungal protease (type XIX) was greatly enhanced in the presence of dGTP and MS2 RNA. Whereas, only moderate proteolytic activation on bacterial proteases (type XXVI) was observed in the presence of MS2 RNA. No appreciable proteolysis of calmodulin by bacterial protease (type IX) was observed.
W N, Kuo +5 more
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