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KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds.

American journal of botany

Helm M, Schmid M, Hierl G, Terneus K, Tan L, Lottspeich F, Kieliszewski MJ, Gietl C.
PMID: 21632425
Am J Bot. 2008 Sep;95(9):1049-62. doi: 10.3732/ajb.2007404.

KDEL-tailed cysteine endopeptidases are a group of papain-type peptidases found in senescing tissue undergoing programmed cell death (PCD). Their genes have so far been cloned and analyzed in 12 angiosperms. They are synthesized as proenzymes with a C-terminal KDEL...

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Helm M, Schmid M, Hierl G, et al. KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds. Am J Bot. 2008;95(9):1049-62doi: 10.3732/ajb.2007404.
Helm, M., Schmid, M., Hierl, G., Terneus, K., Tan, L., Lottspeich, F., Kieliszewski, M. J., & Gietl, C. (2008). KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds. American journal of botany, 95(9), 1049-62. https://doi.org/10.3732/ajb.2007404
Helm, Michael, et al. "KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds." American journal of botany vol. 95,9 (2008): 1049-62. doi: https://doi.org/10.3732/ajb.2007404
Helm M, Schmid M, Hierl G, Terneus K, Tan L, Lottspeich F, Kieliszewski MJ, Gietl C. KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds. Am J Bot. 2008 Sep;95(9):1049-62. doi: 10.3732/ajb.2007404. PMID: 21632425.
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Molecular Cloning and Expression Analysis of Triticale Phytocystatins During Development and Germination of Seeds.

Plant molecular biology reporter

Szewińska J, Zdunek-Zastocka E, Pojmaj M, Bielawski W.
PMID: 24415837
Plant Mol Biol Report. 2012;30:867-877. doi: 10.1007/s11105-011-0384-4.

Three triticale cDNAs encoding inhibitors of cysteine endopeptidases, belonging to phytocystatins, have been identified and designated as

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Szewińska J, Zdunek-Zastocka E, Pojmaj M, et al. Molecular Cloning and Expression Analysis of Triticale Phytocystatins During Development and Germination of Seeds. Plant Mol Biol Report. 2012;30:867-877doi: 10.1007/s11105-011-0384-4.
Szewińska, J., Zdunek-Zastocka, E., Pojmaj, M., & Bielawski, W. (2012). Molecular Cloning and Expression Analysis of Triticale Phytocystatins During Development and Germination of Seeds. Plant molecular biology reporter, 30867-877. https://doi.org/10.1007/s11105-011-0384-4
Szewińska, Joanna, et al. "Molecular Cloning and Expression Analysis of Triticale Phytocystatins During Development and Germination of Seeds." Plant molecular biology reporter vol. 30 (2012): 867-877. doi: https://doi.org/10.1007/s11105-011-0384-4
Szewińska J, Zdunek-Zastocka E, Pojmaj M, Bielawski W. Molecular Cloning and Expression Analysis of Triticale Phytocystatins During Development and Germination of Seeds. Plant Mol Biol Report. 2012;30:867-877. doi: 10.1007/s11105-011-0384-4. PMID: 24415837; PMCID: PMC3881564.
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Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes.

Meat science

Prates JA, Ribeiro AM, Correia AA.
PMID: 22061503
Meat Sci. 2001 Mar;57(3):283-90. doi: 10.1016/s0309-1740(00)00103-0.

The role of endogenous cysteine endopeptidases (EC 3.4.22; calpains and cathepsins B, L and H) in rabbit (Oryctolagus cuniculus L.) meat tenderisation and some related changes (formation of the 30 kDa fragment and myofibrillar structure weakening), during ageing (9...

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Prates JA, Ribeiro AM, Correia AA. Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes. Meat Sci. 2001;57(3):283-90doi: 10.1016/s0309-1740(00)00103-0.
Prates, J. A., Ribeiro, A. M., & Correia, A. A. (2001). Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes. Meat science, 57(3), 283-90. https://doi.org/10.1016/s0309-1740(00)00103-0
Prates, J A, et al. "Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes." Meat science vol. 57,3 (2001): 283-90. doi: https://doi.org/10.1016/s0309-1740(00)00103-0
Prates JA, Ribeiro AM, Correia AA. Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes. Meat Sci. 2001 Mar;57(3):283-90. doi: 10.1016/s0309-1740(00)00103-0. PMID: 22061503.
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Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing.

Meat science

Mestre Prates JA, Garcia E Costa FJ, Ribeiro AM, Dias Correia AA.
PMID: 22063919
Meat Sci. 2002 May;61(1):103-13. doi: 10.1016/s0309-1740(01)00175-9.

The contribution of major structural (myofibrillar fragmentation upon mechanical treatment) and ultra-structural (Z-line degradation, loss of electron density of M-line, transversal disruption of sarcomeres at N(2)-line level, longitudinal fissure of myofibrils, and loss of transversal alignments of Z- and...

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Mestre Prates JA, Garcia E Costa FJ, Ribeiro AM, et al. Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing. Meat Sci. 2002;61(1):103-13doi: 10.1016/s0309-1740(01)00175-9.
Mestre Prates, J. A., Garcia E Costa, F. J., Ribeiro, A. M., & Dias Correia, A. A. (2002). Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing. Meat science, 61(1), 103-13. https://doi.org/10.1016/s0309-1740(01)00175-9
Mestre Prates, José A, et al. "Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing." Meat science vol. 61,1 (2002): 103-13. doi: https://doi.org/10.1016/s0309-1740(01)00175-9
Mestre Prates JA, Garcia E Costa FJ, Ribeiro AM, Dias Correia AA. Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing. Meat Sci. 2002 May;61(1):103-13. doi: 10.1016/s0309-1740(01)00175-9. PMID: 22063919.
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Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense.

Frontiers in plant science

Höwing T, Huesmann C, Hoefle C, Nagel MK, Isono E, Hückelhoven R, Gietl C.
PMID: 24605116
Front Plant Sci. 2014 Feb 24;5:58. doi: 10.3389/fpls.2014.00058. eCollection 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 (KDEL CysEP). KDEL CysEPs...

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Höwing T, Huesmann C, Hoefle C, et al. Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense. Front Plant Sci. 2014;5:58doi: 10.3389/fpls.2014.00058.
Höwing, T., Huesmann, C., Hoefle, C., Nagel, M. K., Isono, E., Hückelhoven, R., & Gietl, C. (2014). Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense. Frontiers in plant science, 558. https://doi.org/10.3389/fpls.2014.00058
Höwing, Timo, et al. "Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense." Frontiers in plant science vol. 5 (2014): 58. doi: https://doi.org/10.3389/fpls.2014.00058
Höwing T, Huesmann C, Hoefle C, Nagel MK, Isono E, Hückelhoven R, Gietl C. Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense. Front Plant Sci. 2014 Feb 24;5:58. doi: 10.3389/fpls.2014.00058. eCollection 2014. PMID: 24605116; PMCID: PMC3932416.
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Showing 1 to 5 of 5 entries