Sharath Chandra, G. Asokan, R. Manamohan, M. Ellango, R. Sharma, H. C. Akbar, S. M. D. Krishna Kumar, N. K.
Published in
Applied Biochemistry and Biotechnology
High diversity of digestive proteases is considered to be the key factor in the evolution of polyphagy in Helicoverpa armigera. Serine proteases (SPs) contribute ~85% of the dietary protein digestion in H. armigera. We investigated the dynamics of SP regulation in the polyphagous pest, H. armigera using RNA interference (RNAi). HaTry1, an isoform o...
Bae, Seong Kyeong Lee, Hyunkyoung Heo, Yunwi Pyo, Min Jung Choudhary, Indu Han, Chang Hoon Yoon, Won Duk Kang, Changkeun Kim, Euikyung
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases
BackgroundBecause jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine...
Nafeesa, Zohara Shivalingu, B. R. Neema, K. N. Achar, Raghu Ram Venkatesh, B. K. Hanchinal, Veeresh Priya, B. S. Nanjunda Swamy, S.
Published in
3 Biotech
Upon examination of the fruit extract of Cucumis sativus L. for its pharmacological benefits, it was previously observed that it has potential proteolytic, fibrinogenolytic and procoagulant activities. These properties can be attributed to the presence of the protease. In this regard, the present study comprised of purification and characterization...
Guarino, Carla Hamon, Yveline Croix, Cécile Lamort, Anne-Sophie Dallet-Choisy, Sandrine Marchand-Adam, Sylvain Lesner, Adam Baranek, Thomas Viaud-Massuard, Marie-Claude Lauritzen, Conni
...
Published in
Biochemical pharmacology
Cathepsin C (CatC) is a tetrameric cysteine dipeptidyl aminopeptidase that plays a key role in activation of pro-inflammatory serine protease zymogens by removal of a N-terminal pro-dipeptide sequence. Loss of function mutations in the CatC gene is associated with lack of immune cell serine protease activities and cause Papillon-Lefèvre syndrome (P...
Yeon, Seung Ju Chung, Goo Yong Hong, Jae Sang Hwang, Jin Ha Shin, Hwa Sung
Published in
In Vitro Cellular & Developmental Biology - Animal
Ischemic stroke and cardiovascular disease can occur from blockage of blood vessels by fibrin clots formed naturally in the body. Therapeutic drugs of anticoagulant or thrombolytic agents have been studied; however, various problems have been reported such as side effects and low efficacy. Thus, development of new candidates that are more effective...
Patel, S.
Published in
Allergologia et Immunopathologia
Proteolytic activity is fundamental to survival, so it is not surprising that all living organisms have proteases, especially seine protease. This enzyme in its numerous isoforms and homologues, constitutes the quintessential offence and defence factors, in the form of surface proteins, secreted molecules, gut digestive enzymes, venom in specialise...
Benarafa, Charaf Simon, Hans-Uwe
Published in
Biochemical and biophysical research communications
Neutrophils constitute a crucial component of the innate immune defenses against microbes. Produced in the bone marrow and patrolling in blood vessels, neutrophils are recruited to injured tissues and are immediately active to contain pathogen invasion. Neutrophils undergo programmed cell death by multiple, context-specific pathways, which have con...
Bae, Seong Kyeong Lee, Hyunkyoung Heo, Yunwi Pyo, Min Jung Choudhary, Indu Han, Chang Hoon Yoon, Won Duk Kang, Changkeun Kim, Euikyung
Abstract Background: Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investiga...
Kocadag Kocazorbaz, Ebru Zihnioglu, Figen
Published in
Protein expression and purification
Prolyl oligopeptidase (POP, EC 3.4.21.26) is a cytosolic serine protease that hydrolyses proline containing small peptides. The members of prolyl oligopeptidase family play important roles in many physiological processes such as neurodegenerative diseases, maturation and degradation of peptide hormones. Thus the enzyme has been purified and charact...
Cordier, B Lemberg, M K
Published in
Methods in enzymology
Proteolysis within the membrane is a recent concept in biology. Rhomboid intramembrane serine proteases are conserved in evolution and serve as key switches in diverse cellular pathways ranging from signaling to protein degradation. Since deregulation of intramembrane proteolysis can lead to severe diseases including neurodegenerative disorders, di...
