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.
Timo Höwing +7 more
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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 +6 more
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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 +4 more
doaj +3 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
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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.
Hideki Kato, Takao Mtnamikawa
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Purification and Characterization of a Cysteine Endopeptidase in Cotyledons of Germinated Mung Bean Seeds [PDF]
Plant Physiology, 1990 A cysteine endopeptidase (EC 3.4.22.-) present in cotyledons of mung bean (Vigna radiata) seedlings was purified to homogeneity, as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). This proteinase has an apparent molecular mass of 33 kilodaltons as estimated by SDS-PAGE and belongs to the class of cysteine proteinases as ...
Yoshiko Yamaoka +2 more
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A Boophilus microplus vitellin-degrading cysteine endopeptidase [PDF]
Parasitology, 2003 Here we describe the purification and characterization of a vitellin (VT) degrading cysteine endopeptidase (VTDCE) from eggs of the hard tick Boophilus microplus. A homogeneous enzyme preparation was obtained by chromatographic fractionation on ion-exchange and gel filtration columns and an autolysis step.
Adriana Seixas +6 more
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Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG [PDF]
Proceedings of the National Academy of Sciences, 2004 Pathogenic bacteria have developed complex and diverse virulence mechanisms that weaken or disable the host immune defense system. IdeS (IgG-degrading e nzyme of Streptococcus pyogenes ) is a secreted cysteine endopeptidase from the human pathogen S.
Katja Wenig +5 more
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Immobilization of Procerain B, a Cysteine Endopeptidase, on Amberlite MB-150 Beads
PLoS ONE, 2013 Proteases are involved in several crucial biological processes and reported to have important physiological functions. They also have multifarious applications in different industries. The immobilized form of the enzyme further improves its industrial applicability. Here, we report covalent immobilization of a novel cysteine endopeptidase (procerain B)
Abhay Narayan Singh +2 more
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Hormonal Regulation of Expression of Two Cysteine Endopeptidase Genes in Rice Seedlings [PDF]
Plant and Cell Physiology, 1997 Two cDNA probes (pRP60 and pRP80) were used to examine the hormonal regulation of expression of two cysteine endopeptidase genes in germinated whole seeds and de-embryonated seeds of rice. The pRP60 protein is a major rice cysteine endopeptidase named REP-1 that digests rice glutelin, the main seed storage protein.
Ai Shintani +2 more
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