Results 161 to 170 of about 31,301 (210)
Advanced Science, EarlyView.Radiotherapy triggers LTβR N‐glycosylation, enhancing its overall protein stability and nuclear retention. This accumulation drives TRIM28‐mediated PCBP2 SUMOylation, suppressing pyroptosis and conferring gastric cancer radioresistance. Therapeutically, a targeted nanoplatform (cRGD‐Lipo@EMD) effectively disrupts this regulatory axis, offering a highly
Weijie Zang +8 more
wiley +1 more source
Advanced Science, EarlyView.Our experimental evidence supports a model in which ALO targets the HSPA8‐CMA‐ATP6V1A axis to induce lysosomal hyperacidification and initiate osmotic and lipidomic stress. These changes are associated with LMP and loss of lysosomal integrity in prostate cancer cells.
Bingzheng An +8 more
wiley +1 more source
Proteolysis in the rat lung: hypoxia and evidence for an inhibitor of proteolysis
American Journal of Physiology-Endocrinology and Metabolism, 1981 We 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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2021
Proteostasis integrates biological pathways controlling biogenesis, trafficking, folding, and degradation of proteins. This book focuses on two protein breakdown/degradation processes (proteolysis), which are part of a normally functioning proteostatic system: the ubiquitin-proteasome system and autophagy.
Niki Chondrogianni +2 more
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Proteostasis integrates biological pathways controlling biogenesis, trafficking, folding, and degradation of proteins. This book focuses on two protein breakdown/degradation processes (proteolysis), which are part of a normally functioning proteostatic system: the ubiquitin-proteasome system and autophagy.
Niki Chondrogianni +2 more
openaire +2 more sources
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
openaire +4 more sources
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
openaire +4 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways
New Phytologist, 2017 Proteases can either digest target proteins or perform the so-called 'limited proteolysis' by cleaving polypeptide chains at specific site(s). Autophagy and the ubiquitin-proteasome system (UPS) are two main mechanisms carrying out digestive proteolysis.
Elena A Minina +2 more
exaly +2 more sources
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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