Results 1 to 10 of about 183,470 (243)

The role of KDEL-tailed cysteine endopeptidases of Arabidopsis (AtCEP2 and AtCEP1) in root development. [PDF]

PLoS One, 2018
Plants encode a unique group of papain-type cysteine endopeptidases (CysEP) characterized by a C-terminal KDEL endoplasmic reticulum retention signal (KDEL-CysEP) and an unusually broad substrate specificity.
Höwing T, Dann M, Müller B, Helm M, Scholz S, Schneitz K, Hammes UZ, Gietl C.   +7 more
europepmc   +5 more sources

Involvement of Arabidopsis thaliana endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 (AtCEP1) in powdery mildew-induced and AtCPR5-controlled cell death. [PDF]

PLoS ONE, 2017
Programmed cell death (PCD) is a prerequisite for successful development and it limits the spread of biotrophic pathogens in a rapid hypersensitive response at the site of infection.
Timo Höwing, Marcel Dann, Caroline Hoefle, Ralph Hückelhoven, Christine Gietl   +4 more
doaj   +4 more sources

Lysosomal cysteine endopeptidases mediate interleukin 1-stimulated cartilage proteoglycan degradation. [PDF]

Biochemical Journal, 1992
The peptidyl diazomethane inactivator of cysteine endopeptidases, benzyloxycarbonyl-Tyr-Ala-CHN2, was tested as an inhibitor of interleukin 1 alpha-stimulated release of proteoglycan from bovine nasal septum cartilage explants. Like the previously tested epoxidyl peptide proinhibitor trans-epoxysuccinyl-leucylamido-(3-methyl)butane ethyl ester, it ...
D. Buttle, J. Saklatvala
semanticscholar   +5 more sources

Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense [PDF]

Frontiers in Plant Science, 2014
Programmed cell death (PCD) is a genetically determined process in all multicellular organisms. Plant PCD is effected by a unique group of papain-type cysteine endopeptidases (CysEP) with a C-terminal KDEL endoplasmic reticulum (ER) retention signal ...
Timo eHöwing, Christina eHuesmann, Caroline eHoefle, Marie-Kristin eNagel, Erika eIsono, Ralph eHuckelhoven, Christine eGietl   +6 more
doaj   +3 more sources

Safety evaluation of the food enzyme papain from the latex of <i>Carica papaya</i> L. [PDF]

EFSA J
The food enzyme papain (EC 3.4.22.2) is extracted from the latex of unripe Carica papaya L. by Nagase (Europe) GmbH. It is intended to be used in six food manufacturing processes.
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano M, Van Loveren H, Vernis L, Criado A, Fraguas Cristina CF, Cavanna D, Liu Y.   +16 more
europepmc   +3 more sources

Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)

Biological chemistry, 2001
The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata.
S. V. Cavalli, A. Cortadi, M. Arribére, P. Conforti, N. Caffini, N. Priolo   +5 more
semanticscholar   +5 more sources

Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases. [PDF]

, 2010
Dipeptidyl-peptidase VI from Bacillus sphaericus and YkfC from Bacillus subtilis have both previously been characterized as highly specific γ-D-glutamyl-L-diamino acid endopeptidases. The crystal structure of a YkfC ortholog from Bacillus cereus (BcYkfC)
Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L, Bakolitsa, Constantina, Cai, Xiaohui, Carlton, Dennis, Chen, Connie, Chiu, Hsiu Ju, Chiu, Michelle, Clayton, Thomas, Das, Debanu, Deacon, Ashley M, Deller, Marc C, Duan, Lian, Ellrott, Kyle, Elsliger, Marc André, Farr, Carol L, Feuerhelm, Julie, Godzik, Adam, Grant, Joanna C, Grzechnik, Anna, Han, Gye Won, Hodgson, Keith O, Jaroszewski, Lukasz, Jin, Kevin K, Klock, Heath E, Knuth, Mark W, Kozbial, Piotr, Krishna, S Sri, Kumar, Abhinav, Lam, Winnie W, Lesley, Scott A, Marciano, David, Miller, Mitchell D, Morse, Andrew T, Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Puckett, Christina, Reyes, Ron, Tien, Henry J, Trame, Christine B, van den Bedem, Henry, Weekes, Dana, Wilson, Ian A, Wooley, John, Wooten, Tiffany, Xu, Qingping, Yeh, Andrew   +48 more
core   +5 more sources

Cysteine endopeptidase activity in sprouting potato tubers. [PDF]

Agricultural and Biological Chemistry, 1985
The crude fraction extracted at pH 6.0 from sprouting potato tubers (pH 6.0 fraction) hydrolyzed casein and BAN A at pH 6.0. This pH 6.0 fraction contained not only caseinase activity but also gelatinase activity, detected by active staining of PAGE-gel with gelatin, as endopeptidases, and both activities increased during sprouting of tubers.
Nobuo Kitamura, Yoshiharu Maruyama
openaire   +3 more sources

Identification and Characterization of a Rice Cysteine Endopeptidase that Digests Glutelin [PDF]

European Journal of Biochemistry, 1996
Little or no endopeptidase activity was detected in extracts from storage organs of dark‐grown rice seeds until day 6 or post‐imbibition, and the activity expressed per seed increased notably after day 9, reached a maximum on day 18, then decreased.
H, Kato, T, Minamikawa
openaire   +4 more sources

Two New Cysteine Endopeptidases Obtained from the Latex of Araujia hortorum Fruits

Journal of Protein Chemistry, 2001
Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively.
W. Obregón, M. Arribére, Susana Morcelle del Valle, C. Liggieri, N. Caffini, N. Priolo   +5 more
semanticscholar   +4 more sources