Results 11 to 20 of about 390,280 (339)
IUCrJ, 2020 Tannerella forsythia is an oral dysbiotic periodontopathogen involved in severe human periodontal disease. As part of its virulence factor armamentarium, at the site of colonization it secretes mirolysin, a metallopeptidase of the unicellular pappalysin ...
Tibisay Guevara +4 more
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Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies
Frontiers in Endocrinology, 2022 The physiological roles of proteolysis are not limited to degrading unnecessary proteins. Proteolysis plays pivotal roles in various biological processes through cleaving peptide bonds to activate and inactivate proteins including enzymes, transcription ...
Daiji Kiyozumi +4 more
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Computational and Structural Biotechnology Journal, 2022 Aureolysin, a secreted metallopeptidase (MP) from the thermolysin family, functions as a major virulence factor in Staphylococcus aureus. No specific aureolysin inhibitors have yet been described, making this an important target for the development of ...
Soraia R. Mendes +7 more
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Microbiome, 2021 Background Proteolysis regulation allows gut microbes to respond rapidly to dynamic intestinal environments by fast degradation of misfolded proteins and activation of regulatory proteins.
Zhixiang Yan +11 more
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Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function
Microbiology Spectrum, 2023 Many CAAX proteins, such as Ras GTPase, undergo a series of posttranslational modifications at their carboxyl terminus (i.e., cysteine prenylation, endoproteolysis of AAX, and carboxylmethylation).
Rajani Ravishankar +6 more
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Phosphorylation Meets Proteolysis [PDF]
Structure, 2012 Phosphorylation is a reversible post-translational modification that regulates many proteins and enzymes, including proteases, as shown by two recent publications. Huang and colleagues and Velázquez-Delgado and Hardy (this issue of Structure) describe how phosphorylation activates the protease activity of the deubiquitinating enzyme DUBA and how it ...
Renatus, Martin, Farady, Christopher J.
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Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit
eLife, 2020 APC/C-mediated proteolysis of cyclin B and securin promotes anaphase entry, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-counteracting phosphatases PP1 and PP2A-B55 ...
James Holder +2 more
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Proteolysis-Driven Oncogenesis [PDF]
Cell Cycle, 2007 An elevated expression of matrix metalloproteinases (MMPs) has been correlated with the growth and metastasis of preexisting tumors. The latest data, however, suggest that MMPs, by promoting genomic instability, are directly involved in the early stages of cell transformation from normalcy to malignancy and in incipient cancer.
Vladislav S, Golubkov, Alex Y, Strongin
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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
M, Staszczak, E, Zdunek
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Nanomechanical in situ monitoring of proteolysis of peptide by Cathepsin B. [PDF]
PLoS ONE, 2009 Characterization and control of proteolysis of peptides by specific cellular protease is a priori requisite for effective drug discovery. Here, we report the nanomechanical, in situ monitoring of proteolysis of peptide chain attributed to protease ...
Taeyun Kwon +9 more
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