Results 261 to 270 of about 118,840 (299)

Structure of the periodontium in cathepsin C‐deficient mice

European Journal of Oral Sciences, 2006
Papillon–Lefevre syndrome is characterized by increased susceptibility to early‐onset periodontitis and is caused by mutations in the cathepsin C gene. How deficiency of the enzyme relates to an increased periodontal infection risk is still not entirely clear.
de Haar, S.F., Tigchelaar-Gutter, W., Everts, V., Beertsen, W.   +3 more
openaire   +5 more sources

[6] Cathepsin C from beef spleen

1955
Publisher Summary Cathepsin C, a proteinase obtained from beef spleen and other tissues, catalyzes the hydrolysis of the amide bond of glycyl-L- phenylalaninamide (GPA) to form glycyl-L-phenylalanine and ammonia, which m a y be determined by the Conway microdiffusion technique.
G. de la Haba, P.S. Cammarata, J.S. Fruton   +2 more
openaire   +1 more source

Involvement of Fenneropenaeus chinensis Cathepsin C in antiviral immunity

Fish & Shellfish Immunology, 2012
Cathepsin C (Cath C) is a lysosomal cysteine protease that belongs to the papain superfamily. Cath C is capable of activating many chymotrypsin-like serine proteases and is reported to be a central coordinator for the activation of many serine proteinases in immune and inflammatory cells.
Shuai, Wang, Li-Jie, Shi, Ning, Liu, An-Jing, Chen, Xiao-Fan, Zhao, Jin-Xing, Wang   +5 more
openaire   +2 more sources

Cathepsin C activity as related to some histochemical substrates

Histochemie, 1965
Hog kidney homogenate was fractionated initially following the steps presented by De La Haba et al. (1959) for the purification of cathepsin C from beef spleen. The preparation was further fractionated by gel filtration using Sephadex G 200, starch gel and immunoelectrophoresis. The following enzymes were identified in the fractions obtained: Cathepsin
T, Vanha-Perttula, V K, Hopsu, V, Sonninen, G G, Glenner   +3 more
openaire   +2 more sources

Action of cathepsins C and D in protein hydrolysis

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 1. 1. Partially purified cathepsin D (EC 3.4.4.23) and cathepsin C (EC 3.4.4.9) were used in combination with activator and inhibitor to investigate the hydrolysis of hemoglobin. 2. 2. In the presence of iodoacetamide, which inhibits cathepsin C, acid-denatured hemoglobin was only slightly hydrolyzed, owing to the action of cathepsin
F L, Huang, A L, Tappel
openaire   +2 more sources

Therapeutic Utility and Medicinal Chemistry of Cathepsin C Inhibitors

Current Topics in Medicinal Chemistry, 2010
The lysosomal cysteine protease cathepsin C (Cat C), also known as dipeptidyl peptidase I, activates a number of granule-associated serine proteases with pro-inflammatory and immune functions by removal of their inhibitory N-terminal dipeptides. Thus, Cat C is a therapeutic target for the treatment of a number of inflammatory and autoimmune diseases ...
Daniel, Guay, Christian, Beaulieu, M David, Percival   +2 more
openaire   +2 more sources

Specificity of cathepsin C

Biochimica et Biophysica Acta, 1961
R J, PLANTA, M, GRUBER
openaire   +2 more sources

Prothrombin activation with cathepsin C

Biochimica et Biophysica Acta, 1963
G M, PURCELL, M I, BARNHART
openaire   +2 more sources

Cathepsin C: A chloride-requiring enzyme

Biochemical and Biophysical Research Communications, 1966
J K, McDonald, T J, Reilly, B B, Zeitman, S, Ellis   +3 more
openaire   +2 more sources

Characterization and function analysis of cathepsin C in Marsupenaeus japonicus

Fish & Shellfish Immunology
Cathepsin C is a cysteine protease widely found in invertebrates and vertebrates, and has the important physiological role participating in proteolysis in vivo and activating various functional proteases in immune/inflammatory cells in the animals. In order to study the role of cathepsin C in the disease resistance of shrimp, we cloned cathepsin C gene
Zuhao, Tu, Jian, Zhong, Hongquan, Li, Liangjuan, Sun, Yucong, Huang, Shiping, Yang, Yishan, Lu, Shuanghu, Cai   +7 more
openaire   +2 more sources