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21 results on '"Nurnberger, Thorsten"'

3. A common toxin fold mediates microbial attack and plant defense

Author

Ottmann, Christian, Luberacki, Borries, Kufner, Isabell, Koch, Wolfgang, Brunner, Frederic, Weyand, Michael, Mattinen, Laura, Pirhonen, Minna, Anderluh, Gregor, Seitz, Hanns Ulrich, Nurnberger, Thorsten, and Oecking, Claudia

Subjects
Gene expression -- Research, Plant immunology -- Genetic aspects, Plant-pathogen relationships -- Genetic aspects, Crystals -- Structure, Crystals -- Evaluation, Science and technology
Abstract

Many plant pathogens secrete toxins that enhance microbial virulence by killing host cells. Usually, these toxins are produced by particular microbial taxa, such as bacteria or fungi. In contrast, many bacterial, fungal and oomycete species produce necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs) that trigger leaf necrosis and immunity-associated responses in various plants. We have determined the crystal structure of an NLP from the phytopathogenic oomycete Pythium aphaniderrnatum to 1.35[Angstrom] resolution. The protein fold exhibits structural similarities to cytolytic toxins produced by marine organisms (actinoporins). Computational modeling of the 3-dimensional structure of NLPs from another oomycete, Phytophthora parasitica, and from the phytopathogenic bacterium, Pectobacterium carotovorum, revealed a high extent of fold conservation. Expression of the 2 oomycete NLPs in an nlp-deficient P. carotovorum strain restored bacterial virulence, suggesting that NLPs of prokaryotic and eukaryotic origins are orthologous proteins. NLP mutant protein analyses revealed that identical structural properties were required to cause plasma membrane permeabilization and cytolysis in plant cells, as well as to restore bacterial virulence. In sum, NLPs are conserved virulence factors whose taxonomic distribution is exceptional for microbial phytotoxins, and that contribute to host infection by plasma membrane destruction and cytolysis. We further show that NLP-mediated phytotoxicity and plant defense gene expression share identical fold requirements, suggesting that toxin-mediated interference with host integrity triggers plant immunity-associated responses. Phytotoxin-induced cellular damage-associated activation of plant defenses is reminiscent of microbial toxin-induced inflammasome activation in vertebrates and may thus constitute another conserved element in animal and plant innate immunity. crystal structure | immunity | pathogen | plant immunity | phytotoxin

Published
2009

4. Phytotoxicity and innate immune responses induced by Nep1-like proteins ([W])

Author

Qutob, Dinah, Kemmerling, Birgit, Brunner, Frederic, Kufner, Isabell, Engelhardt, Stefan, Gust, Andrea A., Luberacki, Borries, Seitz, Hanns Ulrich, Stahl, Dietmar, Rauhut, Thomas, Glawischnig, Erich, Schween, Gabriele, Lacombe, Benoit, Watanabe, Naohide, Lam, Eric, Schlichting, Rita, Scheel, Dierk, Nau, Katja, Dodt, Gabriele, Hubert, David, Gijzen, Mark, and Nurnberger, Thorsten

Subjects
Immune response -- Research, Arabidopsis thaliana -- Research, Peptides -- Research, Necrosis -- Risk factors, Necrosis -- Research, Biological sciences, Science and technology
Published
2006

5. Specific Bacterial Suppressors of MAMP Signaling Upstream of MAPKKK in Arabidopsis Innate Immunity

Author

He, Ping, Shan, Libo, Lin, Nai-Chun, Martin, Gregory B., Kemmerling, Birgit, Nurnberger, Thorsten, and Sheen, Jen

Subjects
Arabidopsis thaliana, Biological sciences
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2006.02.047 Byline: Ping He (1), Libo Shan (1), Nai-Chun Lin (2), Gregory B. Martin (2), Birgit Kemmerling (3), Thorsten Nurnberger (3), Jen Sheen (1) Abstract: Plants and animals possess innate immune systems to prevent infections and are effectively 'nonhosts' for most potential pathogens. The molecular mechanisms underlying nonhost immunity in plants remain obscure. In Arabidopsis, nonhost/nonpathogenic Pseudomonas syringae sustains but pathogenic P. syringae suppresses early MAMP (microbe-associated molecular pattern) marker-gene activation. We performed a cell-based genetic screen of virulence factors and identified AvrPto and AvrPtoB as potent and unique suppressors of early-defense gene transcription and MAP kinase (MAPK) signaling. Unlike effectors of mammalian pathogens, AvrPto and AvrPtoB intercept multiple MAMP-mediated signaling upstream of MAPKKK at the plasma membrane linked to the receptor. In transgenic Arabidopsis, AvrPto blocks early MAMP signaling and enables nonhost P. syringae growth. Deletions of avrPto and avrPtoB from pathogenic P. syringae reduce its virulence. The studies reveal a fundamental role of MAMP signaling in nonhost immunity, and a novel action of type III effectors from pathogenic bacteria. Author Affiliation: (1) Department of Molecular Biology, Massachusetts General Hospital, and Department of Genetics, Harvard Medical School, Boston, MA 02114, USA (2) Boyce Thompson Institute for Plant Research and Department of Plant Pathology, Cornell University, Ithaca, NY 14853, USA (3) Eberhard-Karls-Universitat Tubingen, Zentrum fur Molekularbiologie der Pflanzen (ZMBP), Auf der Morgenstelle 5, D-72076 Tubingen, Germany Article History: Received 29 July 2005; Revised 8 November 2005; Accepted 8 February 2006 Article Note: (miscellaneous) Published: May 4, 2006

Published
2006

6. Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in Arabidopsis innate immunity

Author

Ping He, Nurnberger, Thorsten, Nai-Chun Lin, Libo Shan; Jen Sheen, Martin, Gregory B., and Kemmerling, Birgit

Subjects
Arabidopsis -- Genetic aspects, Phosphotransferases -- Research, Genetic research, Biological sciences
Abstract

A cell-based genetic screen of virulence factors helped to identify AvrPto and AvrPtoB as potent and unique suppressors of early defense screen gene transcription and MAP kinase signaling. The studies revealed a fundamental role of microbe-associated molecular pattern (MAMP) signaling in nonhost immunity, and a novel action of type III effectors from pathogenic bacteria.

Published
2006

7. Non-self recognition, transcriptional reprogramming, and secondary metabolite accumulation during plant/pathogen interactions

Author

Hahlbrock, Klaus, Bednarek, Pawel, Ciolkowski, Ingo, Hamberger, Bjorn, Heise, Andreas, Liedgens, Hiltrud, Logemann, Elke, Nurnberger, Thorsten, Schmelzer, Elmon, Somssich, Imre E., and Tan, Jianwen

Subjects
Plants -- Research, Science and technology
Abstract

Disease resistance of plants involves two distinct forms of chemical communication with the pathogen: recognition and defense. Both are essential components of a highly complex, multifaceted defense response, which begins with non-self recognition through the perception of pathogen-derived signal molecules and results in the production, inter alia, of antibiotically active compounds (phytoalexins) and cell wall-reinforcing material around the infection site. To elucidate the molecular details and the genomic basis of the underlying chains of events, we used two different experimental systems: suspension-cultured cells of Petroselinum crispum (parsley) and wild-type as well as mutant plants of Arabidopsis thaliana. Particular emphasis was placed on the structural and functional identification of signal and defense molecules, and on the mechanisms of signal perception, intracellular signal transduction and transcriptional reprogramming, including the structural and functional characterization of the responsible cis-acting gene promoter elements and transacting regulatory proteins. Comparing P. crispum and A. thaliana allows us to distinguish species-specific defense mechanisms from more universal responses, and furthermore provides general insights into the nature of the interactions. Despite the complexity of the pathogen defense response, it is experimentally tractable, and knowledge gained so far has opened up a new realm of gene technology-assisted strategies for resistance breeding of crop plants.

Published
2003

8. A novel protein elicitor (PaNie) from Pythium aphanidermatum induces multiple defense responses in carrot, Arabidopsis, and tobacco (1)

Author

Veit, Stefan, Worle, Jorg Manfred, Nurnberger, Thorsten, Koch, Wolfgang, and Seitz, Hanns Ulrich

Subjects
Amino acids -- Research, Arabidopsis -- Research, Arabidopsis -- Physiological aspects, Carrots -- Research, Carrots -- Physiological aspects, Tobacco (Plant) -- Research, Tobacco (Plant) -- Physiological aspects, Biological sciences, Science and technology
Published
2001

13. Oligopeptide elicitor-mediated defense gene activation in cultured parsley cells

Author

Hahlbrock, Klaus, Scheel, Dierk, Logemann, Elke, Nurnberger, Thorsten, Parniske, Martin, Reinold, Susanne, Sacks, Wendy R., and Schmelzer, Elmon

Subjects
Plants -- Diseases and pests, Cellular signal transduction -- Research, Oligopeptides -- Analysis, Science and technology
Abstract

The elicitor/suspension-cultured parsley cell system is a good model for studying elicitor recognition, signal transduction and defense gene activation. Elicitor binding by a receptor in the plasma membrane causes H2O2 cell responses, which are followed by transient changes in phosphorylation of proteins and activation of defense genes. With some limitations, each individual defense response was seen to be closely mimicked in elicitor/culture parsley cells, thus upholding the validity of the system.

Published
1995

14. High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses

Author

Nurnberger, Thorsten, Nennstiel, Dirk, Jabs, Thorsten, Sacks, Wendy R., Hahlbrock, Klaus, and Scheel, Dierk

Subjects
Oligopeptides -- Research, Amino acids -- Research, Plasma membranes -- Analysis, Cellular signal transduction -- Analysis, Biological sciences
Abstract

The induction of a 13 amino acid oligopeptide, derived from a fungal 42 kDa glycoprotein elicitor, into parsley cells elicits the response of a crude cell wall preparation and triggers elicitor-specific signal transduction pathways in the plant. The changes include plasma membrane permeability to ions, defense-related gene activation and increased ethylene bio-synthesis. The parsley system provides a good model to study elicitor-specific polypeptide reception and the related gene in the plants.

Published
1994

15. A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence

Author

Chinchilla, Delphine, Zipfel, Cyril, Robatzek, Silke, Kemmerling, Birgit, Nurnberger, Thorsten, Jones, Jonathan D. G., Felix, Georg, and Boller, Thomas

Subjects
Plant defenses -- Research -- Genetic aspects, Plant diseases -- Genetic aspects -- Properties -- Research, Pathology, Molecular -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation, Research, Genetic aspects, Properties
Abstract

Author(s): Delphine Chinchilla (corresponding author) [1]; Cyril Zipfel [1, 2]; Silke Robatzek [1, 3]; Birgit Kemmerling [4]; Thorsten Nürnberger [4]; Jonathan D. G. Jones [2]; Georg Felix [1, 4]; Thomas [...]

Published
2007
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16. Hrp[Z.sub.Psph] from the plant pathogen Pseudomonas syringae pv. phaseolicola binds to lipid bilayers and forms an ion-conducting pore in vitro

Author

Lee, Justin, Klusener, Birgit, Tsiamis, George, Stevens, Conrad, Neyt, Cecile, Tampakaki, Anastasia P., Panopoulos, Nickolas J., Noller, Joachim, Weiler, Elmar W., Cornelis, Guy R., Mansfield, John W., and Nurnberger, Thorsten

Subjects
Bacteria, Pathogenic -- Genetic aspects, Bacterial genetics -- Research, Science and technology
Abstract

The hrp gene clusters of plant pathogenic bacteria control pathogenicity on their host plants and ability to elicit the hypersensitive reaction in resistant plants. Some hrp gene products constitute elements of the type III secretion system, by which effector proteins are exported and delivered into plant cells. Here, we show that the hrpZ gene product from the bean halo-blight pathogen, Pseudomonas syringae pv. phaseolicola (Hrp[Z.sub.Psph]), is secreted in an hrp-dependent manner in P. syringae pv. phaseolicola and exported by the type III secretion system in the mammalian pathogen Yersinia enterocolitica. Hrp[Z.sub.Psph] was found to associate stably with liposomes and synthetic bilayer membranes. Under symmetric ionic conditions, addition of 2 nM of purified recombinant Hrp[Z.sub.Psph] to the cis compartment of planar lipid bilayers provoked an ion current with a large unitary conductivity of 207 pS. Hrp[Z.sub.Psph]-related proteins from P. syringae pv. tomato or syringae triggered ion currents similar to those stimulated by Hrp[Z.sub.Psph]. The Hrp[Z.sub.Psph]-mediated ion-conducting pore was permeable for cations but did not mediate fluxes of [Cl.sup.-]. Such pore-forming activity may allow nutrient release and/or delivery of virulence factors during bacterial colonization of host plants.

Published
2001

17. A life or death switch

Author

Gust, Andrea A. and Nurnberger, Thorsten

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The identification of two receptors for salicylic acid reveals how the hormone controls cell death and survival during plant immune responses, in tissues close to and distant from the site [...]

Published
2012

18. Guidelines for the use and interpretation of assays for monitoring autophagy.

Author

Luxembourg Centre for Systems Biomedicine (LCSB): Clinical & Experimental Neuroscience (Krüger Group) [research center], Klionsky, Daniel J., Abdalla, Fabio C., Abeliovich, Hagai, Abraham, Robert T., Acevedo-Arozena, Abraham, Adeli, Khosrow, Agholme, Lotta, Agnello, Maria, Agostinis, Patrizia, Aguirre-Ghiso, Julio A., Ahn, Hyung Jun, Ait-Mohamed, Ouardia, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akira, Shizuo, Al-Younes, Hesham M., Al-Zeer, Munir A., Albert, Matthew L., Albin, Roger L., Alegre-Abarrategui, Javier, Aleo, Maria Francesca, Alirezaei, Mehrdad, Almasan, Alexandru, Almonte-Becerril, Maylin, Amano, Atsuo, Amaravadi, Ravi, Amarnath, Shoba, Amer, Amal O., Andrieu-Abadie, Nathalie, Anantharam, Vellareddy, Ann, David K., Anoopkumar-Dukie, Shailendra, Aoki, Hiroshi, Apostolova, Nadezda, Arancia, Giuseppe, Aris, John P., Asanuma, Katsuhiko, Asare, Nana Y. O., Ashida, Hisashi, Askanas, Valerie, Askew, David S., Auberger, Patrick, Baba, Misuzu, Backues, Steven K., Baehrecke, Eric H., Bahr, Ben A., Bai, Xue-Yuan, Bailly, Yannick, Baiocchi, Robert, Baldini, Giulia, Balduini, Walter, Ballabio, Andrea, Bamber, Bruce A., Bampton, Edward T. W., Banhegyi, Gabor, Bartholomew, Clinton R., Bassham, Diane C., Bast, Robert C. Jr, Batoko, Henri, Bay, Boon-Huat, Beau, Isabelle, Bechet, Daniel M., Begley, Thomas J., Behl, Christian, Behrends, Christian, Bekri, Soumeya, Bellaire, Bryan, Bendall, Linda J., Benetti, Luca, Berliocchi, Laura, Bernardi, Henri, Bernassola, Francesca, Besteiro, Sebastien, Bhatia-Kissova, Ingrid, Bi, Xiaoning, Biard-Piechaczyk, Martine, Blum, Janice S., Boise, Lawrence H., Bonaldo, Paolo, Boone, David L., Bornhauser, Beat C., Bortoluci, Karina R., Bossis, Ioannis, Bost, Frederic, Bourquin, Jean-Pierre, Boya, Patricia, Boyer-Guittaut, Michael, Bozhkov, Peter V., Brady, Nathan R., Brancolini, Claudio, Brech, Andreas, Brenman, Jay E., Brennand, Ana, Bresnick, Emery H., Brest, Patrick, Bridges, Dave, Bristol, Molly L., Brookes, Paul S., Brown, Eric J., Brumell, John H., Brunetti-Pierri, Nicola, Brunk, Ulf T., Bulman, Dennis E., Bultman, Scott J., Bultynck, Geert, Burbulla, Lena F., Bursch, Wilfried, Butchar, Jonathan P., Buzgariu, Wanda, Bydlowski, Sergio P., Cadwell, Ken, Cahova, Monika, Cai, Dongsheng, Cai, Jiyang, Cai, Qian, Calabretta, Bruno, Calvo-Garrido, Javier, Camougrand, Nadine, Campanella, Michelangelo, Campos-Salinas, Jenny, Candi, Eleonora, Cao, Lizhi, Caplan, Allan B., Carding, Simon R., Cardoso, Sandra M., Carew, Jennifer S., Carlin, Cathleen R., Carmignac, Virginie, Carneiro, Leticia A. M., Carra, Serena, Caruso, Rosario A., Casari, Giorgio, Casas, Caty, Castino, Roberta, Cebollero, Eduardo, Cecconi, Francesco, Celli, Jean, Chaachouay, Hassan, Chae, Han-Jung, Chai, Chee-Yin, Chan, David C., Chan, Edmond Y., Chang, Raymond Chuen-Chung, Che, Chi-Ming, Chen, Ching-Chow, Chen, Guang-Chao, Chen, Guo-Qiang, Chen, Min, Chen, Quan, Chen, Steve S.-L., Chen, Wenli, Chen, Xihui, Chen, Xiangmei, Chen, Xiequn, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Zhixiang, Cheng, Alan, Cheng, Christopher H. K., Cheng, Yan, Cheong, Heesun, Cheong, Jae-Ho, Cherry, Sara, Chess-Williams, Russ, Cheung, Zelda H., Chevet, Eric, Chiang, Hui-Ling, Chiarelli, Roberto, Chiba, Tomoki, Chin, Lih-Shen, Chiou, Shih-Hwa, Chisari, Francis V., Cho, Chi Hin, Cho, Dong-Hyung, Choi, Augustine M. K., Choi, Dooseok, Choi, Kyeong Sook, Choi, Mary E., Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chu, Charleen T., Chuang, Tsung-Hsien, Chueh, Sheau-Huei, Chun, Taehoon, Chwae, Yong-Joon, Chye, Mee-Len, Ciarcia, Roberto, Ciriolo, Maria R., Clague, Michael J., Clark, Robert S. B., Clarke, Peter G. H., Clarke, Robert, Codogno, Patrice, Coller, Hilary A., Colombo, Maria I., Comincini, Sergio, Condello, Maria, Condorelli, Fabrizio, Cookson, Mark R., Coombs, Graham H., Coppens, Isabelle, Corbalan, Ramon, Cossart, Pascale, Costelli, Paola, Costes, Safia, Coto-Montes, Ana, Couve, Eduardo, Coxon, Fraser P., Cregg, James M., Crespo, Jose L., Cronje, Marianne J., Cuervo, Ana Maria, Cullen, Joseph J., Czaja, Mark J., D'Amelio, Marcello, Darfeuille-Michaud, Arlette, Davids, Lester M., Davies, Faith E., De Felici, Massimo, de Groot, John F., de Haan, Cornelis A. M., De Martino, Luisa, De Milito, Angelo, De Tata, Vincenzo, Debnath, Jayanta, Degterev, Alexei, Dehay, Benjamin, Delbridge, Lea M. D., Demarchi, Francesca, Deng, Yi Zhen, Dengjel, Jorn, Dent, Paul, Denton, Donna, Deretic, Vojo, Desai, Shyamal D., Devenish, Rodney J., Di Gioacchino, Mario, Di Paolo, Gilbert, Di Pietro, Chiara, Diaz-Araya, Guillermo, Diaz-Laviada, Ines, Diaz-Meco, Maria T., Diaz-Nido, Javier, Dikic, Ivan, Dinesh-Kumar, Savithramma P., Ding, Wen-Xing, Distelhorst, Clark W., Diwan, Abhinav, Djavaheri-Mergny, Mojgan, Dokudovskaya, Svetlana, Dong, Zheng, Dorsey, Frank C., Dosenko, Victor, Dowling, James J., Doxsey, Stephen, Dreux, Marlene, Drew, Mark E., Duan, Qiuhong, Duchosal, Michel A., Duff, Karen, Dugail, Isabelle, Durbeej, Madeleine, Duszenko, Michael, Edelstein, Charles L., Edinger, Aimee L., Egea, Gustavo, Eichinger, Ludwig, Eissa, N. Tony, Ekmekcioglu, Suhendan, El-Deiry, Wafik S., Elazar, Zvulun, Elgendy, Mohamed, Ellerby, Lisa M., Eng, Kai Er, Engelbrecht, Anna-Mart, Engelender, Simone, Erenpreisa, Jekaterina, Escalante, Ricardo, Esclatine, Audrey, Eskelinen, Eeva-Liisa, Espert, Lucile, Espina, Virginia, Fan, Huizhou, Fan, Jia, Fan, Qi-Wen, Fan, Zhen, Fang, Shengyun, Fang, Yongqi, Fanto, Manolis, Fanzani, Alessandro, Farkas, Thomas, Farre, Jean-Claude, Faure, Mathias, Fechheimer, Marcus, Feng, Carl G., Feng, Jian, Feng, Qili, Feng, Youji, Fesus, Laszlo, Feuer, Ralph, Figueiredo-Pereira, Maria E., Fimia, Gian Maria, Fingar, Diane C., Finkbeiner, Steven, Finkel, Toren, Finley, Kim D., Fiorito, Filomena, Fisher, Edward A., Fisher, Paul B., Flajolet, Marc, Florez-McClure, Maria L., Florio, Salvatore, Fon, Edward A., Fornai, Francesco, Fortunato, Franco, Fotedar, Rati, Fowler, Daniel H., Fox, Howard S., Franco, Rodrigo, Frankel, Lisa B., Fransen, Marc, Fuentes, Jose M., Fueyo, Juan, Fujii, Jun, Fujisaki, Kozo, Fujita, Eriko, Fukuda, Mitsunori, Furukawa, Ruth H., Gaestel, Matthias, Gailly, Philippe, Gajewska, Malgorzata, Galliot, Brigitte, Galy, Vincent, Ganesh, Subramaniam, Ganetzky, Barry, Ganley, Ian G., Gao, Fen-Biao, Gao, George F., Gao, Jinming, Garcia, Lorena, Garcia-Manero, Guillermo, Garcia-Marcos, Mikel, Garmyn, Marjan, Gartel, Andrei L., Gatti, Evelina, Gautel, Mathias, Gawriluk, Thomas R., Gegg, Matthew E., Geng, Jiefei, Germain, Marc, Gestwicki, Jason E., Gewirtz, David A., Ghavami, Saeid, Ghosh, Pradipta, Giammarioli, Anna M., Giatromanolaki, Alexandra N., Gibson, Spencer B., Gilkerson, Robert W., Ginger, Michael L., Ginsberg, Henry N., Golab, Jakub, Goligorsky, Michael S., Golstein, Pierre, Gomez-Manzano, Candelaria, Goncu, Ebru, Gongora, Celine, Gonzalez, Claudio D., Gonzalez, Ramon, Gonzalez-Estevez, Cristina, Gonzalez-Polo, Rosa Ana, Gonzalez-Rey, Elena, Gorbunov, Nikolai V., Gorski, Sharon, Goruppi, Sandro, Gottlieb, Roberta A., Gozuacik, Devrim, Granato, Giovanna Elvira, Grant, Gary D., Green, Kim N., Gregorc, Ales, Gros, Frederic, Grose, Charles, Grunt, Thomas W., Gual, Philippe, Guan, Jun-Lin, Guan, Kun-Liang, Guichard, Sylvie M., Gukovskaya, Anna S., Gukovsky, Ilya, Gunst, Jan, Gustafsson, Asa B., Halayko, Andrew J., Hale, Amber N., Halonen, Sandra K., Hamasaki, Maho, Han, Feng, Han, Ting, Hancock, Michael K., Hansen, Malene, Harada, Hisashi, Harada, Masaru, Hardt, Stefan E., Harper, J. Wade, Harris, Adrian L., Harris, James, Harris, Steven D., Hashimoto, Makoto, Haspel, Jeffrey A., Hayashi, Shin-Ichiro, Hazelhurst, Lori A., He, Congcong, He, You-Wen, Hebert, Marie-Josee, Heidenreich, Kim A., Helfrich, Miep H., Helgason, Gudmundur V., Henske, Elizabeth P., Herman, Brian, Herman, Paul K., Hetz, Claudio, Hilfiker, Sabine, Hill, Joseph A., Hocking, Lynne J., Hofman, Paul, Hofmann, Thomas G., Hohfeld, Jorg, Holyoake, Tessa L., Hong, Ming-Huang, Hood, David A., Hotamisligil, Gokhan S., Houwerzijl, Ewout J., Hoyer-Hansen, Maria, Hu, Bingren, Hu, Chien-An A., Hu, Hong-Ming, Hua, Ya, Huang, Canhua, Huang, Ju, Huang, Shengbing, Huang, Wei-Pang, Huber, Tobias B., Huh, Won-Ki, Hung, Tai-Ho, Hupp, Ted R., Hur, Gang Min, Hurley, James B., Hussain, Sabah N. A., Hussey, Patrick J., Hwang, Jung Jin, Hwang, Seungmin, Ichihara, Atsuhiro, Ilkhanizadeh, Shirin, Inoki, Ken, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L., Ip, Nancy Y., Isaka, Yoshitaka, Ishida, Hiroyuki, Isidoro, Ciro, Isobe, Ken-Ichi, Iwasaki, Akiko, Izquierdo, Marta, Izumi, Yotaro, Jaakkola, Panu M., Jaattela, Marja, Jackson, George R., Jackson, William T., Janji, Bassam, Jendrach, Marina, Jeon, Ju-Hong, Jeung, Eui-Bae, Jiang, Hong, Jiang, Hongchi, Jiang, Jean X., Jiang, Ming, Jiang, Qing, Jiang, Xuejun, Jimenez, Alberto, Jin, Meiyan, Jin, Shengkan, Joe, Cheol O., Johansen, Terje, Johnson, Daniel E., Johnson, Gail V. W., Jones, Nicola L., Joseph, Bertrand, Joseph, Suresh K., Joubert, Annie M., Juhasz, Gabor, Juillerat-Jeanneret, Lucienne, Jung, Chang Hwa, Jung, Yong-Keun, Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kadowaki, Motoni, Kagedal, Katarina, Kamada, Yoshiaki, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kanamori, Hiromitsu, Kang, Chanhee, Kang, Khong Bee, Kang, Kwang Il, Kang, Rui, Kang, Yoon-A., Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kanthasamy, Arthi, Karantza, Vassiliki, Kaushal, Gur P., Kaushik, Susmita, Kawazoe, Yoshinori, Ke, Po-Yuan, Kehrl, John H., Kelekar, Ameeta, Kerkhoff, Claus, Kessel, David H., Khalil, Hany, Kiel, Jan A. K. W., Kiger, Amy A., Kihara, Akio, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Dong-Hou, Kim, Eun-Kyoung, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, John K., Kim, Peter K., Kim, Seong Who, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., King, Jason S., Kinsella, Timothy J., Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kitamoto, Katsuhiko, Kitazato, Kaio, Klein, Ludger, Klimecki, Walter T., Klucken, Jochen, Knecht, Erwin, Ko, Ben C. B., Koch, Jan C., Koga, Hiroshi, Koh, Jae-Young, Koh, Young Ho, Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Hee Jeong, Kong, Wei-Jia, Korolchuk, Viktor I., Kotake, Yaichiro, Koukourakis, Michael I., Kouri Flores, Juan B., Kovacs, Attila L., Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kretz-Remy, Carole, Krichevsky, Anna M., Kroemer, Guido, Krüger, Rejko, Krut, Oleg, Ktistakis, Nicholas T., Kuan, Chia-Yi, Kucharczyk, Roza, Kumar, Ashok, Kumar, Raj, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kurz, Tino, Kwon, Ho Jeong, La Spada, Albert R., Lafont, Frank, Lamark, Trond, Landry, Jacques, Lane, Jon D., Lapaquette, Pierre, Laporte, Jocelyn F., Laszlo, Lajos, Lavandero, Sergio, Lavoie, Josee N., Layfield, Robert, Lazo, Pedro A., Le, Weidong, Le Cam, Laurent, Ledbetter, Daniel J., Lee, Alvin J. 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Javier, Olsen, Laura J., Olsson, Stefan, Opota, Onya, Osborne, Timothy F., Ostrander, Gary K., Otsu, Kinya, Ou, Jing-Hsiung James, Ouimet, Mireille, Overholtzer, Michael, Ozpolat, Bulent, Paganetti, Paolo, Pagnini, Ugo, Pallet, Nicolas, Palmer, Glen E., Palumbo, Camilla, Pan, Tianhong, Panaretakis, Theocharis, Pandey, Udai Bhan, Papackova, Zuzana, Papassideri, Issidora, Paris, Irmgard, Park, Junsoo, Park, Ohkmae K., Parys, Jan B., Parzych, Katherine R., Patschan, Susann, Patterson, Cam, Pattingre, Sophie, Pawelek, John M., Peng, Jianxin, Perlmutter, David H., Perrotta, Ida, Perry, George, Pervaiz, Shazib, Peter, Matthias, Peters, Godefridus J., Petersen, Morten, Petrovski, Goran, Phang, James M., Piacentini, Mauro, Pierre, Philippe, Pierrefite-Carle, Valerie, Pierron, Gerard, Pinkas-Kramarski, Ronit, Piras, Antonio, Piri, Natik, Platanias, Leonidas C., Poggeler, Stefanie, Poirot, Marc, Poletti, Angelo, Pous, Christian, Pozuelo-Rubio, Mercedes, Praetorius-Ibba, Mette, Prasad, Anil, Prescott, Mark, Priault, Muriel, Produit-Zengaffinen, Nathalie, Progulske-Fox, Ann, Proikas-Cezanne, Tassula, Przedborski, Serge, Przyklenk, Karin, Puertollano, Rosa, Puyal, Julien, Qian, Shu-Bing, Qin, Liang, Qin, Zheng-Hong, Quaggin, Susan E., Raben, Nina, Rabinowich, Hannah, Rabkin, Simon W., Rahman, Irfan, Rami, Abdelhaq, Ramm, Georg, Randall, Glenn, Randow, Felix, Rao, V. 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Abstract

In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes. A key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process vs. those that measure flux through the autophagy pathway (i.e., the complete process); thus, a block in macroautophagy that results in autophagosome accumulation needs to be differentiated from stimuli that result in increased autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused o

Published
2012
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21. Mitogen-activated Protein Kinases Play on Essential Role in Oxidative Burst-independent Expression of Pathogenesis-related Genes in Parsley.

Author

Kroj, Thomas, Rudd, Jason J., Nurnberger, Thorsten, Gäbler, Yvonne, Lee, Justin, and Scheel, Dierk

Subjects
*PARSLEY, *PLANT genetics, *GENE expression in plants, *PLANT defenses, *PROTEIN kinases
Abstract

Discusses the existence of parallel pathways that operate to induce the transcriptional activation of particular sets of defense-related genes in parsley. Indication that one pathway is triggered downstream of the oxidative burst and controls genes implicated in phytoalexin biosynthesis; Second pathway's independence from the oxidative burst and dependence on mitogen-activated protein kinase.

Published
2003
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