Journal of Dr. NTR University of Health Sciences, 2019 Cathepsins are a class of globular lysosomal proteases known to be responsible for protein degradation. In addition to proteolysis they have many biological roles such as apoptosis wound healing angiogenesis, proenzymatic activation, bone remodelling and
K Ajay Benarji +4 more
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Family C1 cysteine proteases: Biological diversity or redundancy? [PDF]
, 2003 Recent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes.
Brömme D. +4 more
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IGF-I receptor phosphorylation is impaired in cathepsin X-deficient prostate cancer cells [PDF]
, 2012 The cysteine-type peptidase cathepsin X is highly upregulated in several cancers and presumably promotes tumor invasion through bypassing cellular senescence. Here, we present first evidence that the underlying mechanism may involve the regulation of the
Bunsen, Thea +3 more
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Zymography of proteases in honey bees (Apis Mellifera) infected with Nosema ceranae [PDF]
Veterinarski GlasnikNosemosis is one of the most important honey bee diseases and is caused by two fungal species of the genus Nosema, i.e., Nosema apis and Nosema ceranae.
Doghuzlu Mohammad Afrasiabi +5 more
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FEBS Open Bio, 2022 For a long time, lysosomes were purely seen as organelles in charge of garbage disposal within the cell. They destroy any cargo delivered into their lumen with a plethora of highly potent hydrolytic enzymes, including various proteases. In case of damage
Thomas Reinheckel, Martina Tholen
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Peptide synthesis by recombinant Fasciola hepatica cathepsin L1 [PDF]
, 2006 Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5%
Ciarán Ó'Fágáin +16 more
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DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes [PDF]
, 2018 DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima, is synthesized by the fat body and the ovary and functions as yolk protein precursor. Functionally, DmCatD is involved in vitellin proteolysis.
Arrese, Estela L. +8 more
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Importance of lysosomal cysteine proteases in lung disease
Respiratory Research, 2000 The human lysosomal cysteine proteases are a family of 11 proteases whose members include cathepsins B, C, H, L, and S. The biology of these proteases was largely ignored for decades because of their lysosomal location and the belief that their function ...
Chapman Harold A, Wolters Paul J
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Autophagy is activated and involved in cell death with participation of cathepsins during stress-induced microspore embryogenesis in barley [PDF]
, 2018 Microspores are reprogrammed towards embryogenesis by stress. Many microspores die after this stress, limiting the efficiency of microspore embryogenesis. Autophagy is a degradation pathway that plays critical roles in stress response and cell death.
Berenguer, Eduardo +4 more
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The Role of DmCatD, a Cathepsin D-Like Peptidase, and Acid Phosphatase in the Process of Follicular Atresia in Dipetalogaster maxima (Hemiptera: Reduviidae), a Vector of Chagas' Disease [PDF]
, 2015 In this work, we have investigated the involvement of DmCatD, a cathepsin D-like peptidase, and acid phosphatase in the process of follicular atresia of Dipetalogaster maxima, a hematophagous insect vector of Chagas' disease. For the studies, fat bodies,
Canavoso, Lilian Etelvina +3 more
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