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1. Chloroplastic Protein NRIP1 Mediates Innate Immune Receptor Recognition of a Viral Effector

Author: Caplan, Jeffrey L., Mamillapalli, Padmavathi, Burch-Smith, Tessa M., Czymmek, Kirk, and Dinesh-Kumar, S.P.
Subjects: Developmental biology, Virus diseases, Biological sciences
Abstract: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2007.12.031 Byline: Jeffrey L. Caplan (1), Padmavathi Mamillapalli (1), Tessa M. Burch-Smith (1), Kirk Czymmek (2), S.P. Dinesh-Kumar (1) Keywords: CELLIMMUNO; MOLIMMUNO Abstract: Plant innate immunity relies on the recognition of pathogen effector molecules by nucleotide-binding-leucine-rich repeat (NB-LRR) immune receptor families. Previously we have shown the N immune receptor, a member of TIR-NB-LRR family, indirectly recognizes the 50 kDa helicase (p50) domain of Tobacco mosaic virus (TMV) through its TIR domain. We have identified an N receptor-interacting protein, NRIP1, that directly interacts with both N's TIR domain and p50. NRIP1 is a functional rhodanese sulfurtransferase and is required for N to provide complete resistance to TMV. Interestingly, NRIP1 that normally localizes to the chloroplasts is recruited to the cytoplasm and nucleus by the p50 effector. As a consequence, NRIP1 interacts with N only in the presence of the p50 effector. Our findings show that a chloroplastic protein is intimately involved in pathogen recognition. We propose that N's activation requires a prerecognition complex containing the p50 effector and NRIP1. Author Affiliation: (1) Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA (2) Department of Biological Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, USA Article History: Received 17 April 2007; Revised 18 October 2007; Accepted 12 December 2007 Article Note: (miscellaneous) Published: February 7, 2008
Published: 2008

2. Differential binding of calmodulin-related proteins to their targets revealed through high-density Arabidopsis protein microarrays

Author: Popescu, Sorina C., Popescu, George V., Bachan, Shawn, Zhang, Zimei, Seay, Montrell, Gerstein, Mark, Snyder, Michael, and Dinesh-Kumar, S.P.
Subjects: Calmodulin -- Research, Protein-protein interactions -- Research, Arabidopsis thaliana -- Genetic aspects, Arabidopsis thaliana -- Research, Eukaryotes -- Genetic aspects, Eukaryotes -- Research, Protein microarrays -- Research, Science and technology
Abstract: Calmodulins (CaMs) are the most ubiquitous calcium sensors in eukaryotes. A number of CaM-binding proteins have been identified through classical methods, and many proteins have been predicted to bind CaMs based on their structural homology with known targets. However, multicellular organisms typically contain many CaM-like (CML) proteins, and a global identification of their targets and specificity of interaction is lacking. In an effort to develop a platform for large-scale analysis of proteins in plants we have developed a protein microarray and used it to study the global analysis of CaM/CML interactions. An Arabidopsis thaliana expression collection containing 1,133 ORFs was generated and used to produce proteins with an optimized medium-throughput plant-based expression system. Protein microarrays were prepared and screened with several CaMs/CMLs. A large number of previously known and novel CaM/CML targets were identified, including transcription factors, receptor and intracellular protein kinases, F-box proteins, RNA-binding proteins, and proteins of unknown function. Multiple CaM/CML proteins bound many binding partners, but the majority of targets were specific to one or a few CaMs/CMLs indicating that different CaM family members function through different targets. Based on our analyses, the emergent CaM/CML interactome is more extensive than previously predicted. Our results suggest that calcium functions through distinct CaM/ CML proteins to regulate a wide range of targets and cellular activities. calmodulin-interacting proteins | protein interaction network
Published: 2007

3. Efficient virus-induced gene silencing in Arabidopsis (1)

Author: Burch-Smith, Tessa M., Schiff, Michael, Liu, Yule, and Dinesh-Kumar, S.P.
Subjects: Arabidopsis thaliana -- Genetic aspects, Arabidopsis thaliana -- Research, Gene silencing -- Analysis, Genomes -- Research, Biological sciences, Science and technology
Published: 2006

4. Virus Induced Gene Silencing of a DEFICIENS Ortholog in Nicotiana Benthamiana

Author: Liu, Yule, Nakayama, Naomi, Schiff, Michael, Litt, Amy, Irish, Vivian F., and Dinesh-Kumar, S.P.
Published: 2004
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5. Autophagy Regulates Programmed Cell Death during the Plant Innate Immune Response

Author: Liu, Yule, Schiff, Michael, Czymmek, Kirk, Talloczy, Zsolt, Levine, Beth, and Dinesh-Kumar, S.P.
Subjects: Biochemistry, Apoptosis, Developmental biology, Biological sciences
Abstract: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2005.03.007 Byline: Yule Liu (1), Michael Schiff (1), Kirk Czymmek (2), Zsolt Talloczy (3), Beth Levine (3)(4), S.P. Dinesh-Kumar (1) Abstract: The plant innate immune response includes the hypersensitive response (HR), a form of programmed cell death (PCD). PCD must be restricted to infection sites to prevent the HR from playing a pathologic rather than protective role. Here we show that plant BECLIN 1, an ortholog of the yeast and mammalian autophagy gene ATG6/VPS30/beclin 1, functions to restrict HR PCD to infection sites. Initiation of HR PCD is normal in BECLIN 1-deficient plants, but remarkably, healthy uninfected tissue adjacent to HR lesions and leaves distal to the inoculated leaf undergo unrestricted PCD. In the HR PCD response, autophagy is induced in both pathogen-infected cells and distal uninfected cells; this is reduced in BECLIN 1-deficient plants. The restriction of HR PCD also requires orthologs of other autophagy-related genes including PI3K/VPS34, ATG3, and ATG7. Thus, the evolutionarily conserved autophagy pathway plays an essential role in plant innate immunity and negatively regulates PCD. Author Affiliation: (1) Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520 (2) Department of Biological Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, Delaware 19711 (3) Department of Medicine, Columbia University College of Physicians and Surgeons, New York, New York 10032 (4) Department of Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390 Article Note: (miscellaneous) Published: May 19, 2005
Published: 2005

6. The COP9 signalosome interacts physically with [SCF.sup.COI1] and modulates jasmonate responses

Author: Feng, Suhua, Ma, Ligeng, Wang, Xiping, Xie, Daoxin, Dinesh-Kumar, S.P., Wei, Ning, and Deng, Xing Wang
Subjects: Jasmine -- Genetic aspects, Jasmine -- Physiological aspects, Gene expression -- Research, Plants -- Photomorphogenesis, Plants -- Research, Biological sciences, Science and technology
Published: 2003

7. Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene--mediated resistance response to Tobacco mosaic virus

Author: Liu, Yule, Schiff, Michael, Serino, Giovanna, Deng, Xing-Wang, and Dinesh-Kumar, S.P.
Subjects: Tobacco mosaic virus -- Research, Plant-pathogen relationships -- Research, Plant immunology -- Genetic aspects, Biological sciences, Science and technology
Published: 2002

8. Virus-Induced Gene Silencing (VIGS)

Author: Padmanabhan, M.S., primary and Dinesh-Kumar, S.P., additional
Published: 2008
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9. Virus-Induced Gene Silencing Offers a Functional Genomics Platform for Studying Plant Cell Wall Formation

Author: Zhu, Xiaohong, Pattathil, Sivakumar, Mazumder, Koushik, Brehm, Amanda, Hahn, Michael G., Dinesh-Kumar, S.P., and Joshi, Chandrashekhar P.
Published: 2010
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10. Signaling in plant-microbe interactions

Author: Baker, Barbara, Zambryski, Patricia, Staskewicz, Brian, and Dinesh-Kumar, S.P.
Subjects: Bacteria, Pathogenic -- Research, Bacterial diseases of plants -- Research, Plant viruses -- Research, Virus diseases of plants -- Research, Science and technology, Research
Abstract: Analysis of viral and bacterial pathogenesis has revealed common themes in the ways in which plants and animals respond to pathogenic agents. Pathogenic bacteria use macromolecule delivery systems (types Ill and IV) to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells. The molecular events that constitute critical steps of plant-pathogen interactions seem to involve ligand-receptor mechanisms for pathogen recognition and the induction of signal transduction pathways in the plant that lead to defense responses. Unraveling the molecular bask of. resistance pathways has laid a foundation for the rational design of crop protection strategies., Since the onset of civilization, plant diseases have had catastrophic effects on crops and the well-being of human populations. For example, the fungus Phytophthora infestans caused the epidemic that triggered [...]
Published: 1997

11. Transposon tagging of tobacco mosaic virus resistance gene N: its possible role in the TMV-N-mediated signal transduction pathway

Author: Dinesh-Kumar, S.P., Whitham, Steve, Choi, Doil, Hehl, Reinhard, Corr, Catherine, and Baker, Barbara
Subjects: Plants -- Diseases and pests, Cellular signal transduction -- Research, Tobacco mosaic virus -- Research, Science and technology
Abstract: The hypersensitive response, product of an interaction between resistance genes and a pathogen avirulence gene product, is a defense mechanism in plants to combat pathogen invasions. In tobacco plants afflicted by the mosaic virus, the resistance gene (N) functions in a signal transduction pathway by stimulating rapid defense responses. A sequence analysis of the N gene reveals that it encodes a protein with an amino-terminal domain.
Published: 1995

12. Permanent fixation of a transposable element insert in the A2 gene of maize (Zea mays L.)

Author: Thatiparthi, V.R., Dinesh-Kumar, S.P., and Peterson, P.A.
Subjects: Transposons -- Research, Genetic transformation -- Research, Insertion elements, DNA -- Research, Gene expression -- Research, Corn -- Genetic aspects, Biological sciences
Abstract: Some genetic variations help organisms adapt to their environments. The presence of transposable elements can catalyze genetic change and is reflected in the case of footprint creation at positions where element excisions are made. The I element has been tested with the En/Spm to determine its stability in generating genetic change. It was shown that the element exhibited stability in both insertion and composition.
Published: 1995

13. The product of the tobacco mosaic virus resistance gene N: similarity to Toll and the interleukin-1 receptor

Author: Whitham, Steve, Dinesh-Kumar, S.P., Choi, Doil, Hehl, Reinhard, Corr, Catherine, and Baker, Barbara
Subjects: Tobacco mosaic virus -- Genetic aspects, Interleukin-1 -- Research, Biological sciences
Abstract: The resistance gene N of tobacco, which mediates the resistance to the tobacco mosaic virus (TMV), is isolated by transposon tagging. The tagging uses the maize activator transposon, which confers the genomic DNA fragment with an N gene to TMV susceptible tobacco. The plant disease resistance genes identify and combat the invading pathogens by triggering host defense responses. This is performed by the resistance gene N, which encodes the 131.4 kDa protein with an amino acid terminal domain.
Published: 1994

14. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Author: Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. Bhutia, S.K. Biagosch, C. Bianchi, M.W. Biard-Piechaczyk, M. Billes, V. Bincoletto, C. Bingol, B. Bird, S.W. Bitoun, M. Bjedov, I. Blackstone, C. Blanc, L. Blanco, G.A. Blomhoff, H.K. Boada-Romero, E. Böckler, S. Boes, M. Boesze-Battaglia, K. Boise, L.H. Bolino, A. Boman, A. Bonaldo, P. Bordi, M. Bosch, J. Botana, L.M. Botti, J. Bou, G. Bouché, M. Bouchecareilh, M. Boucher, M.-J. Boulton, M.E. Bouret, S.G. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N. Braga, V.M.M. Brancolini, C. Braus, G.H. Bravo-San-Pedro, J.M. Brennan, L.A. Bresnick, E.H. Brest, P. Bridges, D. Bringer, M.-A. Brini, M. Brito, G.C. Brodin, B. Brookes, P.S. Brown, E.J. Brown, K. Broxmeyer, H.E. Bruhat, A. Brum, P.C. Brumell, J.H. Brunetti-Pierri, N. Bryson-Richardson, R.J. Buch, S. Buchan, A.M. Budak, H. Bulavin, D.V. Bultman, S.J. Bultynck, G. Bumbasirevic, V. Burelle, Y. Burke, R.E. Burmeister, M. Bütikofer, P. Caberlotto, L. Cadwell, K. Cahova, M. Cai, D. Cai, J. Cai, Q. Calatayud, S. Camougrand, N. Campanella, M. Campbell, G.R. Campbell, M. Campello, S. Candau, R. Caniggia, I. Cantoni, L. Cao, L. Caplan, A.B. Caraglia, M. Cardinali, C. Cardoso, S.M. Carew, J.S. Carleton, L.A. Carlin, C.R. Carloni, S. Carlsson, S.R. Carmona-Gutierrez, D. Carneiro, L.A.M. Carnevali, O. Carra, S. Carrier, A. Carroll, B. Casas, C. Casas, J. Cassinelli, G. Castets, P. Castro-Obregon, S. Cavallini, G. Ceccherini, I. Cecconi, F. Cederbaum, A.I. Ceña, V. Cenci, S. Cerella, C. Cervia, D. Cetrullo, S. Chaachouay, H. Chae, H.-J. Chagin, A.S. Chai, C.-Y. Chakrabarti, G. Chamilos, G. Chan, E.Y.W. Chan, M.T.V. Chandra, D. Chandra, P. Chang, C.-P. Chang, R.C.-C. Chang, T.Y. Chatham, J.C. Chatterjee, S. Chauhan, S. Che, Y. Cheetham, M.E. Cheluvappa, R. Chen, C.-J. Chen, G. Chen, G.-C. Chen, G. Chen, H. Chen, J.W. Chen, J.-K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S.-D. Chen, S. Chen, S.S.-L. Chen, W. Chen, W.-J. Chen, W.Q. Chen, W. Chen, X. Chen, Y.-H. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Y.-Q. Chen, Y. Chen, Z. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, H. Cheong, H. Cherry, S. Chesney, J. Cheung, C.H.A. Chevet, E. Chi, H.C. Chi, S.-G. Chiacchiera, F. Chiang, H.-L. Chiarelli, R. Chiariello, M. Chieppa, M. Chin, L.-S. Chiong, M. Chiu, G.N.C. Cho, D.-H. Cho, S.-G. Cho, W.C. Cho, Y.-Y. Cho, Y.-S. Choi, A.M.K. Choi, E.-J. Choi, E.-K. Choi, J. Choi, M.E. Choi, S.-I. Chou, T.-F. Chouaib, S. Choubey, D. Choubey, V. Chow, K.-C. Chowdhury, K. Chu, C.T. Chuang, T.-H. Chun, T. Chung, H. Chung, T. Chung, Y.-L. Chwae, Y.-J. Cianfanelli, V. Ciarcia, R. Ciechomska, I.A. Ciriolo, M.R. Cirone, M. Claerhout, S. Clague, M.J. Cl� ria, J. Clarke, P.G.H. Clarke, R. Clementi, E. Cleyrat, C. Cnop, M. Coccia, E.M. Cocco, T. Codogno, P. Coers, J. Cohen, E.E.W. Colecchia, D. Coletto, L. Coll, N.S. Colucci-Guyon, E. Comincini, S. Condello, M. Cook, K.L. Coombs, G.H. Cooper, C.D. Cooper, J.M. Coppens, I. Corasaniti, M.T. Corazzari, M. Corbalan, R. Corcelle-Termeau, E. Cordero, M.D. Corral-Ramos, C. Corti, O. Cossarizza, A. Costelli, P. Costes, S. Cotman, S.L. Coto-Montes, A. Cottet, S. Couve, E. Covey, L.R. Cowart, L.A. Cox, J.S. Coxon, F.P. Coyne, C.B. Cragg, M.S. Craven, R.J. Crepaldi, T. Crespo, J.L. Criollo, A. Crippa, V. Cruz, M.T. Cuervo, A.M. Cuezva, J.M. Cui, T. Cutillas, P.R. Czaja, M.J. Czyzyk-Krzeska, M.F. Dagda, R.K. Dahmen, U. Dai, C. Dai, W. Dai, Y. Dalby, K.N. Valle, L.D. Dalmasso, G. D'amelio, M. Damme, M. Darfeuille-Michaud, A. Dargemont, C. Darley-Usmar, V.M. Dasarathy, S. Dasgupta, B. Dash, S. Dass, C.R. Davey, H.M. Davids, L.M. Dávila, D. Davis, R.J. Dawson, T.M. Dawson, V.L. Daza, P. de Belleroche, J. de Figueiredo, P. de Figueiredo, R.C.B.Q. de la Fuente, J. De Martino, L. De Matteis, A. De Meyer, G.R.Y. De Milito, A. De Santi, M. de Souza, W. De Tata, V. De Zio, D. Debnath, J. Dechant, R. Decuypere, J.-P. Deegan, S. Dehay, B. Del Bello, B. Del Re, D.P. Delage-Mourroux, R. Delbridge, L.M.D. Deldicque, L. Delorme-Axford, E. Deng, Y. Dengjel, J. Denizot, M. Dent, P. Der, C.J. Deretic, V. Derrien, B. Deutsch, E. Devarenne, T.P. Devenish, R.J. Di Bartolomeo, S. Di Daniele, N. Di Domenico, F. Di Nardo, A. Di Paola, S. Di Pietro, A. Di Renzo, L. Di Antonio, A. Díaz-Araya, G. Díaz-Laviada, I. Diaz-Meco, M.T. Diaz-Nido, J. Dickey, C.A. Dickson, R.C. Diederich, M. Digard, P. Dikic, I. Dinesh-Kumar, S.P. Ding, C. Ding, W.-X. Ding, Z. Dini, L. Distler, J.H.W. Diwan, A. Djavaheri-Mergny, M. Dmytruk, K. Dobson, R.C.J. Doetsch, V. Dokladny, K. Dokudovskaya, S. Donadelli, M. Dong, X.C. Dong, X. Dong, Z. Donohue, T.M., Jr. Donohue-Jr, T.M. Doran, K.S. D'orazi, G. Dorn, G.W., II Dosenko, V. Dridi, S. Drucker, L. Du, J. Du, L.-L. Du, L. du Toit, A. Dua, P. Duan, L. Duann, P. Dubey, V.K. Duchen, M.R. Duchosal, M.A. Duez, H. Dugail, I. Dumit, V.I. Duncan, M.C. Dunlop, E.A. Dunn, W.A., Jr. Dupont, N. Dupuis, L. Durán, R.V. Durcan, T.M. Duvezin-Caubet, S. Duvvuri, U. Eapen, V. Ebrahimi-Fakhari, D. Echard, A. Eckhart, L. Edelstein, C.L. Edinger, A.L. Eichinger, L. Eisenberg, T. Eisenberg-Lerner, A. Eissa, N.T. El-Deiry, W.S. El-Khoury, V. Elazar, Z. Eldar-Finkelman, H. Elliott, C.J.H. Emanuele, E. Emmenegger, U. Engedal, N. Engelbrecht, A.-M. Engelender, S. Enserink, J.M. Erdmann, R. Erenpreisa, J. Eri, R. Eriksen, J.L. Erman, A. Escalante, R. Eskelinen, E.-L. Espert, L. Esteban-Martínez, L. Evans, T.J. Fabri, M. Fabrias, G. Fabrizi, C. Facchiano, A. Færgeman, N.J. Faggioni, A. Fairlie, W.D. Fan, C. Fan, D. Fan, J. Fang, S. Fanto, M. Fanzani, A. Farkas, T. Faure, M. Favier, F.B. Fearnhead, H. Federici, M. Fei, E. Felizardo, T.C. Feng, H. Feng, Y. Feng, Y. Ferguson, T.A. Fernández, Á.F. Fernandez-Barrena, M.G. Fernandez-Checa, J.C. Fernández-López, A. Fernandez-Zapico, M.E. Feron, O. Ferraro, E. Ferreira-Halder, C.V. Fesus, L. Feuer, R. Fiesel, F.C. Filippi-Chiela, E.C. Filomeni, G. Fimia, G.M. Fingert, J.H. Finkbeiner, S. Finkel, T. Fiorito, F. Fisher, P.B. Flajolet, M. Flamigni, F. Florey, O. Florio, S. Floto, R.A. Folini, M. Follo, C. Fon, E.A. Fornai, F. Fortunato, F. Fraldi, A. Franco, R. Francois, A. François, A. Frankel, L.B. Fraser, I.D.C. Frey, N. Freyssenet, D.G. Frezza, C. Friedman, S.L. Frigo, D.E. Fu, D. Fuentes, J.M. Fueyo, J. Fujitani, Y. Fujiwara, Y. Fujiya, M. Fukuda, M. Fulda, S. Fusco, C. Gabryel, B. Gaestel, M. Gailly, P. Gajewska, M. Galadari, S. Galili, G. Galindo, I. Galindo, M.F. Galliciotti, G. Galluzzi, L. Galluzzi, L. Galy, V. Gammoh, N. Gandy, S. Ganesan, A.K. Ganesan, S. Ganley, I.G. Gannagé, M. Gao, F.-B. Gao, F. Gao, J.-X. Nannig, L.G. Véscovi, E.G. Garcia-Macía, M. Garcia-Ruiz, C. Garg, A.D. Garg, P.K. Gargini, R. Gassen, N.C. Gatica, D. Gatti, E. Gavard, J. Gavathiotis, E. Ge, L. Ge, P. Ge, S. Gean, P.-W. Gelmetti, V. Genazzani, A.A. Geng, J. Genschik, P. Gerner, L. Gestwicki, J.E. Gewirtz, D.A. Ghavami, S. Ghigo, E. Ghosh, D. Giammarioli, A.M. Giampieri, F. Giampietri, C. Giatromanolaki, A. Gibbings, D.J. Gibellini, L. Gibson, S.B. Ginet, V. Giordano, A. Giorgini, F. Giovannetti, E. Girardin, S.E. Gispert, S. Giuliano, S. Gladson, C.L. Glavic, A. Gleave, M. Godefroy, N. Gogal, R.M., Jr. Gokulan, K. Goldman, G.H. Goletti, D. Goligorsky, M.S. Gomes, A.V. Gomes, L.C. Gomez, H. Gomez-Manzano, C. Gómez-Sánchez, R. Gonçalves, D.A.P. Goncu, E. Gong, Q. Gongora, C. Gonzalez, C.B. Gonzalez-Alegre, P. Gonzalez-Cabo, P. González-Polo, R.A. Goping, I.S. Gorbea, C. Gorbunov, N.V. Goring, D.R. Gorman, A.M. Gorski, S.M. Goruppi, S. Goto-Yamada, S. Gotor, C. Gottlieb, R.A. Gozes, I. Gozuacik, D. Graba, Y. Graef, M. Granato, G.E. Grant, G.D. Grant, S. Gravina, G.L. Green, D.R. Greenhough, A. Greenwood, M.T. Grimaldi, B. Gros, F. Grose, C. Groulx, J.-F. Gruber, F. Grumati, P. Grune, T. Guan, J.-L. Guan, K.-L. Guerra, B. Guillen, C. Gulshan, K. Gunst, J. Guo, C. Guo, L. Guo, M. Guo, W. Guo, X.-G. Gust, A.A. Gustafsson, Å.B. Gutierrez, E. Gutierrez, M.G. Gwak, H.-S. Haas, A. Haber, J.E. Hadano, S. 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Steegborn, C. Steele, J.W. Stefanis, L. Steffan, J. Stellrecht, C.M. Stenmark, H. Stepkowski, T.M. Stern, S.T. Stevens, C. Stockwell, B.R. Stoka, V. Storchova, Z. Stork, B. Stratoulias, V. Stravopodis, D.J. Strnad, P. Strohecker, A.M. Ström, A.-L. Stromhaug, P. Stulik, J. Su, Y.-X. Su, Z. Subauste, C.S. Subramaniam, S. Sue, C.M. Suh, S.W. Sui, X. Sukseree, S. Sulzer, D. Sun, F.-L. Sun, J. Sun, J. Sun, S.-Y. Sun, Y. Sun, Y. Sun, Y. Sundaramoorthy, V. Sung, J. Suzuki, H. Suzuki, K. Suzuki, N. Suzuki, T. Suzuki, Y.J. Swanson, M.S. Swanton, C. Swärd, K. Swarup, G. Sweeney, S.T. Sylvester, P.W. Szatmari, Z. Szegezdi, E. Szlosarek, P.W. Taegtmeyer, H. Tafani, M. Taillebourg, E. Tait, S.W.G. Takacs-Vellai, K. Takahashi, Y. Takáts, S. Takemura, G. Takigawa, N. Talbot, N.J. Tamagno, E. Tamburini, J. Tan, C.-P. Tan, L. Tan, M.L. Tan, M. Tan, Y.-J. Tanaka, K. Tanaka, M. Tang, D. Tang, D. Tang, G. Tanida, I. Tanji, K. Tannous, B.A. Tapia, J.A. Tasset-Cuevas, I. Tatar, M. Tavassoly, I. 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Vaccaro, M.I. Váchová, L. Vakifahmetoglu-Norberg, H. Valdor, R. Valente, E.M. Vallette, F. Valverde, A.M. Van den Berghe, G. Van Den Bosch, L. van den Brink, G.R. van der Goot, F.G. van der Klei, I.J. van der Laan, L.J.W. van Doorn, W.G. van Egmond, M. van Golen, K.L. Van Kaer, L. Campagne, M.L. Vandenabeele, P. Vandenberghe, W. Vanhorebeek, I. Varela-Nieto, I. Vasconcelos, M.H. Vasko, R. Vavvas, D.G. Vega-Naredo, I. Velasco, G. Velentzas, A.D. Velentzas, P.D. Vellai, T. Vellenga, E. Vendelbo, M.H. Venkatachalam, K. Ventura, N. Ventura, S. Veras, P.S.T. Verdier, M. Vertessy, B.G. Viale, A. Vidal, M. Vieira, H.L.A. Vierstra, R.D. Vigneswaran, N. Vij, N. Vila, M. Villar, M. Villar, V.H. Villarroya, J. Vindis, C. Viola, G. Viscomi, M.T. Vitale, G. Vogl, D.T. Voitsekhovskaja, O.V. von Haefen, C. von Schwarzenberg, K. Voth, D.E. Vouret-Craviari, V. Vuori, K. Vyas, J.M. Waeber, C. Walker, C.L. Walker, M.J. Walter, J. Wan, L. Wan, X. Wang, B. Wang, C. Wang, C.-Y. Wang, C. Wang, C. Wang, C. 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Zhang, J. Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.
Published: 2016

15. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author: Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. Bhutia, S.K. Biagosch, C. Bianchi, M.W. Biard-Piechaczyk, M. Billes, V. Bincoletto, C. Bingol, B. Bird, S.W. Bitoun, M. Bjedov, I. Blackstone, C. Blanc, L. Blanco, G.A. Blomhoff, H.K. Boada-Romero, E. Böckler, S. Boes, M. Boesze-Battaglia, K. Boise, L.H. Bolino, A. Boman, A. Bonaldo, P. Bordi, M. Bosch, J. Botana, L.M. Botti, J. Bou, G. Bouché, M. Bouchecareilh, M. Boucher, M.-J. Boulton, M.E. Bouret, S.G. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N. Braga, V.M.M. Brancolini, C. Braus, G.H. Bravo-San-Pedro, J.M. Brennan, L.A. Bresnick, E.H. Brest, P. Bridges, D. Bringer, M.-A. Brini, M. Brito, G.C. Brodin, B. Brookes, P.S. Brown, E.J. Brown, K. Broxmeyer, H.E. Bruhat, A. Brum, P.C. Brumell, J.H. Brunetti-Pierri, N. Bryson-Richardson, R.J. Buch, S. Buchan, A.M. Budak, H. Bulavin, D.V. Bultman, S.J. Bultynck, G. Bumbasirevic, V. Burelle, Y. Burke, R.E. Burmeister, M. Bütikofer, P. Caberlotto, L. Cadwell, K. Cahova, M. Cai, D. Cai, J. Cai, Q. Calatayud, S. Camougrand, N. Campanella, M. Campbell, G.R. Campbell, M. Campello, S. Candau, R. Caniggia, I. Cantoni, L. Cao, L. Caplan, A.B. Caraglia, M. Cardinali, C. Cardoso, S.M. Carew, J.S. Carleton, L.A. Carlin, C.R. Carloni, S. Carlsson, S.R. Carmona-Gutierrez, D. Carneiro, L.A.M. Carnevali, O. Carra, S. Carrier, A. Carroll, B. Casas, C. Casas, J. Cassinelli, G. Castets, P. Castro-Obregon, S. Cavallini, G. Ceccherini, I. Cecconi, F. Cederbaum, A.I. Ceña, V. Cenci, S. Cerella, C. Cervia, D. Cetrullo, S. Chaachouay, H. Chae, H.-J. Chagin, A.S. Chai, C.-Y. Chakrabarti, G. Chamilos, G. Chan, E.Y.W. Chan, M.T.V. Chandra, D. Chandra, P. Chang, C.-P. Chang, R.C.-C. Chang, T.Y. Chatham, J.C. Chatterjee, S. Chauhan, S. Che, Y. Cheetham, M.E. Cheluvappa, R. Chen, C.-J. Chen, G. Chen, G.-C. Chen, G. Chen, H. Chen, J.W. Chen, J.-K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S.-D. Chen, S. Chen, S.S.-L. Chen, W. Chen, W.-J. Chen, W.Q. Chen, W. Chen, X. Chen, Y.-H. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Y.-Q. Chen, Y. Chen, Z. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, H. Cheong, H. Cherry, S. Chesney, J. Cheung, C.H.A. Chevet, E. Chi, H.C. Chi, S.-G. Chiacchiera, F. Chiang, H.-L. Chiarelli, R. Chiariello, M. Chieppa, M. Chin, L.-S. Chiong, M. Chiu, G.N.C. Cho, D.-H. Cho, S.-G. Cho, W.C. Cho, Y.-Y. Cho, Y.-S. Choi, A.M.K. Choi, E.-J. Choi, E.-K. Choi, J. Choi, M.E. Choi, S.-I. Chou, T.-F. Chouaib, S. Choubey, D. Choubey, V. Chow, K.-C. Chowdhury, K. Chu, C.T. Chuang, T.-H. Chun, T. Chung, H. Chung, T. Chung, Y.-L. Chwae, Y.-J. Cianfanelli, V. Ciarcia, R. Ciechomska, I.A. Ciriolo, M.R. Cirone, M. Claerhout, S. Clague, M.J. Clària, J. Clarke, P.G.H. Clarke, R. Clementi, E. Cleyrat, C. Cnop, M. Coccia, E.M. Cocco, T. Codogno, P. Coers, J. Cohen, E.E.W. Colecchia, D. Coletto, L. Coll, N.S. Colucci-Guyon, E. Comincini, S. Condello, M. Cook, K.L. Coombs, G.H. Cooper, C.D. Cooper, J.M. Coppens, I. Corasaniti, M.T. Corazzari, M. Corbalan, R. 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Papini, A. Parajuli, N. Pardo, J. Parekh, V.V. Parenti, G. Park, J.-I. Park, J. Park, O.K. Parker, R. Parlato, R. Parys, J.B. Parzych, K.R. Pasquet, J.-M. Pasquier, B. Pasumarthi, K.B.S. Patterson, C. Pattingre, S. Pattison, S. Pause, A. Pavenstädt, H. Pavone, F. Pedrozo, Z. Peña, F.J. Peñalva, M.A. Pende, M. Peng, J. Penna, F. Penninger, J.M. Pensalfini, A. Pepe, S. Pereira, G.J.S. Pereira, P.C. de la Cruz, V.P. Pérez-Pérez, M.E. Pérez-Rodríguez, D. Pérez-Sala, D. Perier, C. Perl, A. Perlmutter, D.H. Perrotta, I. Pervaiz, S. Pesonen, M. Pessin, J.E. Peters, G.J. Petersen, M. Petrache, I. Petrof, B.J. Petrovski, G. Phang, J.M. Piacentini, M. Pierdominici, M. Pierre, P. Pierrefite-Carle, V. Pietrocola, F. Pimentel-Muiños, F.X. Pinar, M. Pineda, B. Pinkas-Kramarski, R. Pinti, M. Pinton, P. Piperdi, B. Piret, J.M. Platanias, L.C. Platta, H.W. Plowey, E.D. Pöggeler, S. Poirot, M. Polčic, P. Poletti, A. Poon, A.H. Popelka, H. Popova, B. Poprawa, I. Poulose, S.M. Poulton, J. Powers, S.K. Powers, T. Pozuelo-Rubio, M. Prak, K. Prange, R. Prescott, M. Priault, M. Prince, S. Proia, R.L. Proikas-Cezanne, T. Prokisch, H. Promponas, V.J. Przyklenk, K. Puertollano, R. Pugazhenthi, S. Puglielli, L. Pujol, A. Puyal, J. Pyeon, D. Qi, X. Qian, W.-B. Qin, Z.-H. Qiu, Y. Qu, Z. Quadrilatero, J. Quinn, F. Raben, N. Rabinowich, H. Radogna, F. Ragusa, M.J. Rahmani, M. Raina, K. Ramanadham, S. Ramesh, R. Rami, A. Randall-Demllo, S. Randow, F. Rao, H. Rao, V.A. Rasmussen, B.B. Rasse, T.M. Ratovitski, E.A. Rautou, P.-E. Ray, S.K. Razani, B. Reed, B.H. Reggiori, F. Rehm, M. Reichert, A.S. Rein, T. Reiner, D.J. Reits, E. Ren, J. Ren, X. Renna, M. Reusch, J.E.B. Revuelta, J.L. Reyes, L. Rezaie, A.R. Richards, R.I. Richardson, R. Richetta, C. Riehle, M.A. Rihn, B.H. Rikihisa, Y. Riley, B.E. Rimbach, G. Rippo, M.R. Ritis, K. Rizzi, F. Rizzo, E. Roach, P.J. Robbins, J. Roberge, M. Roca, G. Roccheri, M.C. Rocha, S. Rodrigues, C.M.P. Rodríguez, C.I. de Cordoba, S.R. Rodriguez-Muela, N. Roelofs, J. Rogov, V.V. Rohn, T.T. Rohrer, B. Romanelli, D. Romani, L. Romano, P.S. Roncero, M.I.G. Rosa, J.L. Rosello, A. Rosen, K.V. Rosenstiel, P. Rost-Roszkowska, M. Roth, K.A. Roué, G. Rouis, M. Rouschop, K.M. Ruan, D.T. Ruano, D. Rubinsztein, D.C. Rucker, E.B., III Rudich, A. Rudolf, E. Rudolf, R. Ruegg, M.A. Ruiz-Roldan, C. Ruparelia, A.A. Rusmini, P. Russ, D.W. Russo, G.L. Russo, G. Russo, R. Rusten, T.E. Ryabovol, V. Ryan, K.M. Ryter, S.W. Sabatini, D.M. Sacher, M. Sachse, C. Sack, M.N. Sadoshima, J. Saftig, P. Sagi-Eisenberg, R. Sahni, S. Saikumar, P. Saito, T. Saitoh, T. Sakakura, K. Sakoh-Nakatogawa, M. Sakuraba, Y. Salazar-Roa, M. Salomoni, P. Saluja, A.K. Salvaterra, P.M. Salvioli, R. Samali, A. Sanchez, A.M.J. Sánchez-Alcázar, J.A. Sanchez-Prieto, R. Sandri, M. Sanjuan, M.A. Santaguida, S. Santambrogio, L. Santoni, G. Dos Santos, C.N. Saran, S. Sardiello, M. Sargent, G. Sarkar, P. Sarkar, S. Sarrias, M.R. Sarwal, M.M. Sasakawa, C. Sasaki, M. Sass, M. Sato, K. Sato, M. Satriano, J. Savaraj, N. Saveljeva, S. Schaefer, L. Schaible, U.E. Scharl, M. Schatzl, H.M. Schekman, R. Scheper, W. Schiavi, A. Schipper, H.M. Schmeisser, H. Schmidt, J. Schmitz, I. Schneider, B.E. Schneider, E.M. Schneider, J.L. Schon, E.A. Schönenberger, M.J. Schönthal, A.H. Schorderet, D.F. Schröder, B. Schuck, S. Schulze, R.J. Schwarten, M. Schwarz, T.L. Sciarretta, S. Scotto, K. Scovassi, A.I. Screaton, R.A. Screen, M. Seca, H. Sedej, S. Segatori, L. Segev, N. Seglen, P.O. Seguí-Simarro, J.M. Segura-Aguilar, J. Seiliez, I. Seki, E. Sell, C. Semenkovich, C.F. Semenza, G.L. Sen, U. Serra, A.L. Serrano-Puebla, A. Sesaki, H. Setoguchi, T. Settembre, C. Shacka, J.J. Shajahan-Haq, A.N. Shapiro, I.M. Sharma, S. She, H. Shen, C.-K.J. Shen, C.-C. Shen, H.-M. Shen, S. Shen, W. Sheng, R. Sheng, X. Sheng, Z.-H. Shepherd, T.G. Shi, J. Shi, Q. Shi, Q. Shi, Y. Shibutani, S. Shibuya, K. Shidoji, Y. Shieh, J.-J. Shih, C.-M. Shimada, Y. Shimizu, S. Shin, D.W. Shinohara, M.L. Shintani, M. Shintani, T. Shioi, T. Shirabe, K. Shiri-Sverdlov, R. Shirihai, O. Shore, G.C. Shu, C.-W. Shukla, D. Sibirny, A.A. Sica, V. Sigurdson, C.J. Sigurdsson, E.M. Sijwali, P.S. Sikorska, B. Silveira, W.A. Silvente-Poirot, S. Silverman, G.A. Simak, J. Simmet, T. Simon, A.K. Simon, H.-U. Simone, C. Simons, M. Simonsen, A. Singh, R. Singh, S.V. Singh, S.K. Sinha, D. Sinha, S. Sinicrope, F.A. Sirko, A. Sirohi, K. Sishi, B.J.N. Sittler, A. Siu, P.M. Sivridis, E. Skwarska, A. Slack, R. Slaninová, I. Slavov, N. Smaili, S.S. Smalley, K.S.M. Smith, D.R. Soenen, S.J. Soleimanpour, S.A. Solhaug, A. Somasundaram, K. Son, J.H. Sonawane, A. Song, C. Song, F. Song, H.K. Song, J.-X. Song, W. Soo, K.Y. Sood, A.K. Soong, T.W. Soontornniyomkij, V. Sorice, M. Sotgia, F. Soto-Pantoja, D.R. Sotthibundhu, A. Sousa, M.J. Spaink, H.P. Span, P.N. Spang, A. Sparks, J.D. Speck, P.G. Spector, S.A. Spies, C.D. Springer, W. Clair, D.S. Stacchiotti, A. Staels, B. Stang, M.T. Starczynowski, D.T. Starokadomskyy, P. Steegborn, C. Steele, J.W. Stefanis, L. Steffan, J. Stellrecht, C.M. Stenmark, H. Stepkowski, T.M. Stern, S.T. Stevens, C. Stockwell, B.R. Stoka, V. Storchova, Z. Stork, B. Stratoulias, V. Stravopodis, D.J. Strnad, P. Strohecker, A.M. Ström, A.-L. Stromhaug, P. Stulik, J. Su, Y.-X. Su, Z. Subauste, C.S. Subramaniam, S. Sue, C.M. Suh, S.W. Sui, X. Sukseree, S. Sulzer, D. Sun, F.-L. Sun, J. Sun, J. Sun, S.-Y. Sun, Y. Sun, Y. Sun, Y. Sundaramoorthy, V. Sung, J. Suzuki, H. Suzuki, K. Suzuki, N. Suzuki, T. Suzuki, Y.J. Swanson, M.S. Swanton, C. Swärd, K. Swarup, G. Sweeney, S.T. Sylvester, P.W. Szatmari, Z. Szegezdi, E. Szlosarek, P.W. Taegtmeyer, H. Tafani, M. Taillebourg, E. Tait, S.W.G. Takacs-Vellai, K. Takahashi, Y. Takáts, S. Takemura, G. Takigawa, N. Talbot, N.J. Tamagno, E. Tamburini, J. Tan, C.-P. Tan, L. Tan, M.L. Tan, M. Tan, Y.-J. Tanaka, K. Tanaka, M. Tang, D. Tang, D. Tang, G. Tanida, I. Tanji, K. Tannous, B.A. Tapia, J.A. Tasset-Cuevas, I. Tatar, M. Tavassoly, I. Tavernarakis, N. Taylor, A. Taylor, G.S. Taylor, G.A. Taylor, J.P. Taylor, M.J. Tchetina, E.V. Tee, A.R. Teixeira-Clerc, F. Telang, S. Tencomnao, T. Teng, B.-B. Teng, R.-J. Terro, F. Tettamanti, G. Theiss, A.L. Theron, A.E. Thomas, K.J. Thomé, M.P. Thomes, P.G. Thorburn, A. Thorner, J. Thum, T. Thumm, M. Thurston, T.L.M. Tian, L. Till, A. Ting, J.P.-Y. Ting, J.P.Y. Titorenko, V.I. Toker, L. Toldo, S. Tooze, S.A. Topisirovic, I. Torgersen, M.L. Torosantucci, L. Torriglia, A. Torrisi, M.R. Tournier, C. Towns, R. Trajkovic, V. Travassos, L.H. Triola, G. Tripathi, D.N. Trisciuoglio, D. Troncoso, R. Trougakos, I.P. Truttmann, A.C. Tsai, K.-J. Tschan, M.P. Tseng, Y.-H. Tsukuba, T. Tsung, A. Tsvetkov, A.S. Tu, S. Tuan, H.-Y. Tucci, M. Tumbarello, D.A. Turk, B. Turk, V. Turner, R.F.B. Tveita, A.A. Tyagi, S.C. Ubukata, M. Uchiyama, Y. Udelnow, A. Ueno, T. Umekawa, M. Umemiya-Shirafuji, R. Underwood, B.R. Ungermann, C. Ureshino, R.P. Ushioda, R. Uversky, V.N. Uzcátegui, N.L. Vaccari, T. Vaccaro, M.I. Váchová, L. Vakifahmetoglu-Norberg, H. Valdor, R. Valente, E.M. Vallette, F. Valverde, A.M. Van den Berghe, G. Van Den Bosch, L. van den Brink, G.R. van der Goot, F.G. van der Klei, I.J. van der Laan, L.J.W. van Doorn, W.G. van Egmond, M. van Golen, K.L. Van Kaer, L. Campagne, M.L. Vandenabeele, P. Vandenberghe, W. Vanhorebeek, I. Varela-Nieto, I. Vasconcelos, M.H. Vasko, R. Vavvas, D.G. Vega-Naredo, I. Velasco, G. Velentzas, A.D. Velentzas, P.D. Vellai, T. Vellenga, E. Vendelbo, M.H. Venkatachalam, K. Ventura, N. Ventura, S. Veras, P.S.T. Verdier, M. Vertessy, B.G. Viale, A. Vidal, M. Vieira, H.L.A. Vierstra, R.D. Vigneswaran, N. Vij, N. Vila, M. Villar, M. Villar, V.H. Villarroya, J. Vindis, C. Viola, G. Viscomi, M.T. Vitale, G. Vogl, D.T. Voitsekhovskaja, O.V. von Haefen, C. von Schwarzenberg, K. Voth, D.E. Vouret-Craviari, V. Vuori, K. Vyas, J.M. Waeber, C. Walker, C.L. Walker, M.J. Walter, J. Wan, L. Wan, X. Wang, B. Wang, C. Wang, C.-Y. Wang, C. Wang, C. Wang, C. Wang, D. Wang, F. Wang, F. Wang, G. Wang, H.-J. Wang, H. Wang, H.-G. Wang, H. Wang, H.-D. Wang, J. Wang, J. Wang, M. Wang, M.-Q. Wang, P.-Y. Wang, P. Wang, R.C. Wang, S. Wang, T.-F. Wang, X. Wang, X.-J. Wang, X.-W. Wang, X. Wang, X. Wang, Y. Wang, Y. Wang, Y. Wang, Y.-J. Wang, Y. Wang, Y. Wang, Y.T. Wang, Y. Wang, Z.-N. Wappner, P. Ward, C. Ward, D.M.V. Warnes, G. Watada, H. Watanabe, Y. Watase, K. Weaver, T.E. Weekes, C.D. Wei, J. Weide, T. Weihl, C.C. Weindl, G. Weis, S.N. Wen, L. Wen, X. Wen, Y. Westermann, B. Weyand, C.M. White, A.R. White, E. Whitton, J.L. Whitworth, A.J. Wiels, J. Wild, F. Wildenberg, M.E. Wileman, T. Wilkinson, D.S. Wilkinson, S. Willbold, D. Williams, C. Williams, K. Williamson, P.R. Winklhofer, K.F. Witkin, S.S. Wohlgemuth, S.E. Wollert, T. Wolvetang, E.J. Wong, E. Wong, G.W. Wong, R.W. Wong, V.K.W. Woodcock, E.A. Wright, K.L. Wu, C. Wu, D. Wu, G.S. Wu, J. Wu, J. Wu, M. Wu, M. Wu, S. Wu, W.K.K. Wu, Y. Wu, Z. Xavier, C.P.R. Xavier, R.J. Xia, G.-X. Xia, T. 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Zhang, J. Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.
Published: 2016

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

Author: Klionsky, D.J. Abdalla, F.C. Abeliovich, H. Abraham, R.T. Acevedo-Arozena, A. Adeli, K. Agholme, L. Agnello, M. Agostinis, P. Aguirre-Ghiso, J.A. Ahn, H.J. Ait-Mohamed, O. Ait-Si-Ali, S. Akematsu, T. Akira, S. Al-Younes, H.M. Al-Zeer, M.A. Albert, M.L. Albin, R.L. Alegre-Abarrategui, J. Aleo, M.F. Alirezaei, M. Almasan, A. Almonte-Becerril, M. Amano, A. Amaravadi, R. Amarnath, S. Amer, A.O. Andrieu-Abadie, N. Anantharam, V. Ann, D.K. Anoopkumar-Dukie, S. Aoki, H. Apostolova, N. Arancia, G. Aris, J.P. Asanuma, K. Asare, N.Y.O. Ashida, H. Askanas, V. Askew, D.S. Auberger, P. Baba, M. Backues, S.K. Baehrecke, E.H. Bahr, B.A. Bai, X.-Y. Bailly, Y. Baiocchi, R. Baldini, G. Balduini, W. Ballabio, A. Bamber, B.A. Bampton, E.T.W. Bánhegyi, G. Bartholomew, C.R. Bassham, D.C. Bast Jr., R.C. Batoko, H. Bay, B.-H. Beau, I. Béchet, D.M. Begley, T.J. Behl, C. Behrends, C. Bekri, S. Bellaire, B. Bendall, L.J. Benetti, L. Berliocchi, L. Bernardi, H. Bernassola, F. Besteiro, S. Bhatia-Kissova, I. Bi, X. Biard-Piechaczyk, M. Blum, J.S. Boise, L.H. Bonaldo, P. Boone, D.L. Bornhauser, B.C. Bortoluci, K.R. Bossis, I. Bost, F. Bourquin, J.-P. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N.R. Brancolini, C. Brech, A. Brenman, J.E. Brennand, A. Bresnick, E.H. Brest, P. Bridges, D. Bristol, M.L. Brookes, P.S. Brown, E.J. Brumell, J.H. Brunetti-Pierri, N. Brunk, U.T. Bulman, D.E. Bultman, S.J. Bultynck, G. Burbulla, L.F. Bursch, W. Butchar, J.P. Buzgariu, W. Bydlowski, S.P. Cadwell, K. Cahová, M. Cai, D. Cai, J. Cai, Q. Calabretta, B. Calvo-Garrido, J. Camougrand, N. Campanella, M. Campos-Salinas, J. Candi, E. Cao, L. Caplan, A.B. Carding, S.R. Cardoso, S.M. Carew, J.S. Carlin, C.R. Carmignac, V. Carneiro, L.A.M. Carra, S. Caruso, R.A. Casari, G. Casas, C. Castino, R. Cebollero, E. Cecconi, F. Celli, J. Chaachouay, H. Chae, H.-J. Chai, C.-Y. Chan, D.C. Chan, E.Y. Chang, R.C.-C. Che, C.-M. Chen, C.-C. Chen, G.-C. Chen, G.-Q. Chen, M. Chen, Q. Chen, S.S.-L. Chen, W. Chen, X. Chen, X. Chen, X. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, Y. Cheong, H. Cheong, J.-H. Cherry, S. Chess-Williams, R. Cheung, Z.H. Chevet, E. Chiang, H.-L. Chiarelli, R. Chiba, T. Chin, L.-S. Chiou, S.-H. Chisari, F.V. Cho, C.H. Cho, D.-H. Choi, A.M.K. Choi, D. Choi, K.S. Choi, M.E. Chouaib, S. Choubey, D. Choubey, V. Chu, C.T. Chuang, T.-H. Chueh, S.-H. Chun, T. Chwae, Y.-J. Chye, M.-L. Ciarcia, R. Ciriolo, M.R. Clague, M.J. Clark, R.S.B. Clarke, P.G.H. Clarke, R. Codogno, P. Coller, H.A. Colombo, M.I. Comincini, S. Condello, M. Condorelli, F. Cookson, M.R. Coombs, G.H. Coppens, I. Corbalan, R. Cossart, P. Costelli, P. Costes, S. Coto-Montes, A. Couve, E. Coxon, F.P. Cregg, J.M. Crespo, J.L. Cronjé, M.J. Cuervo, A.M. Cullen, J.J. Czaja, M.J. D'Amelio, M. Darfeuille-Michaud, A. Davids, L.M. Davies, F.E. De Felici, M. De Groot, J.F. De Haan, C.A.M. De Martino, L. De Milito, A. De Tata, V. Debnath, J. Degterev, A. Dehay, B. 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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 on these processes. These guidelines are not meant to be a formulaic set of rules, because the appropriate assays depend in part on the question being asked and the system being used. In addition, we emphasize that no individual assay is guaranteed to be the most appropriate one in every situation, and we strongly recommend the use of multiple assays to monitor autophagy. In these guidelines, we consider these various methods of assessing autophagy and what information can, or cannot, be obtained from them. Finally, by discussing the merits and limits of particular autophagy assays, we hope to encourage technical innovation in the field. © 2012 Landes Bioscience.
Published: 2012

17. What Can Plant Autophagy Do for an Innate Immune Response?

Author: Hayward, Andrew P., primary and Dinesh-Kumar, S.P., additional
Published: 2011
Full Text: View/download PDF

18. Special Delivery for MHC II via Autophagy

Author: Hayward, Andrew P., primary and Dinesh-Kumar, S.P., additional
Published: 2010
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19. Autophagy and plant innate immunity: Defense through degradation

Author: Hayward, Andrew P., primary, Tsao, Jeffrey, additional, and Dinesh-Kumar, S.P., additional
Published: 2009
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20. Induced ER Chaperones Regulate a Receptor-like Kinase to Mediate Antiviral Innate Immune Response in Plants

Author: Caplan, Jeffrey L., primary, Zhu, Xiaohong, additional, Mamillapalli, Padmavathi, additional, Marathe, Rajendra, additional, Anandalakshmi, Radhamani, additional, and Dinesh-Kumar, S.P., additional
Published: 2009
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21. The Development of Protein Microarrays and Their Applications in DNA–Protein and Protein–Protein Interaction Analyses of Arabidopsis Transcription Factors

Author: Gong, Wei, primary, He, Kun, additional, Covington, Mike, additional, Dinesh-Kumar, S.P., additional, Snyder, Michael, additional, Harmer, Stacey L., additional, Zhu, Yu-Xian, additional, and Deng, Xing Wang, additional
Published: 2008
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22. Autophagy Takes Its TOLL on Innate Immunity

Author: Seay, Montrell D., primary and Dinesh-Kumar, S.P., additional
Published: 2007
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23. Using Viral Vectors to Silence Endogenous Genes

Author: Caplan, Jeffrey, primary and Dinesh‐Kumar, S.P., additional
Published: 2006
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24. Life After Death: Are Autophagy Genes Involved in Cell Death and Survival During Plant Innate Immune Responses?

Author: Seay, Montrell, primary and Dinesh-Kumar, S.P., additional
Published: 2005
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25. Genome-Wide ORFeome Cloning and Analysis of Arabidopsis Transcription Factor Genes

Author: Gong, Wei, primary, Shen, Yun-Ping, additional, Ma, Li-Geng, additional, Pan, Yi, additional, Du, Yun-Long, additional, Wang, Dong-Hui, additional, Yang, Jian-Yu, additional, Hu, Li-De, additional, Liu, Xin-Fang, additional, Dong, Chun-Xia, additional, Ma, Li, additional, Chen, Yan-Hui, additional, Yang, Xiao-Yuan, additional, Gao, Ying, additional, Zhu, Danmeng, additional, Tan, Xiaoli, additional, Mu, Jin-Ye, additional, Zhang, Da-Bing, additional, Liu, Yu-Le, additional, Dinesh-Kumar, S.P., additional, Li, Yi, additional, Wang, Xi-Ping, additional, Gu, Hong-Ya, additional, Qu, Li-Jia, additional, Bai, Shu-Nong, additional, Lu, Ying-Tang, additional, Li, Jia-Yang, additional, Zhao, Jin-Dong, additional, Zuo, Jianru, additional, Huang, Hai, additional, Deng, Xing Wang, additional, and Zhu, Yu-Xian, additional
Published: 2004
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26. P58IPK, a Plant Ortholog of Double-Stranded RNA-Dependent Protein Kinase PKR Inhibitor, Functions in Viral Pathogenesis

Author: Bilgin, Damla D, primary, Liu, Yule, additional, Schiff, Michael, additional, and Dinesh-Kumar, S.P, additional
Published: 2003
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27. Plant Defense

Author: Marathe, Rajendra, primary and Dinesh-Kumar, S.P, additional
Published: 2003
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28. A sequence required for −1 ribosomal frameshifting located four kilobases downstream of the frameshift site 1 1Edited by D. E. Draper

Author: Paul, Cynthia P, primary, Barry, Jennifer K, additional, Dinesh-Kumar, S.P, additional, Brault, Véronique, additional, and Miller, W.Allen, additional
Published: 2001
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29. Aphid Transmission and Systemic Plant Infection Determinants of Barley Yellow Dwarf Luteovirus-PAV are Contained in the Coat Protein Readthrough Domain and 17-kDa Protein, Respectively

Author: CHAY, C.A., primary, GUNASINGE, U.B., additional, DINESH-KUMAR, S.P., additional, MILLER, W.A., additional, and GRAY, STEWART M., additional
Published: 1996
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30. Genes and cis-Acting Sequences Involved in Replication of Barley Yellow Dwarf Virus-PAV RNA

Author: Mohan, B.R., primary, Dinesh-Kumar, S.P., additional, and Miller, W.Allen, additional
Published: 1995
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31. Replication of Barley Yellow Dwarf Virus Satellite RNA Transcripts in Oat Protoplasts

Author: Silver, Stanley L., primary, Rasochova, Lada, additional, Dinesh-Kumar, S.P., additional, and Miller, W.Allen, additional
Published: 1994
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32. Precise mapping and in vitro translation of a trifunctional subgenomic RNA of barley yellow dwarf virus

Author: Dinesh-Kumar, S.P., primary, Brault, Veronique, additional, and Allen^Miller, W., additional
Published: 1992
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33. Virus-Induced Gene Silencing Offers a Functional Genomics Platform for Studying Plant Cell Wall Formation.

Author: Xiaohong Zhu, Pattathil, Sivakumar, Mazumder, Koushik, Brehm, Amanda, Hahn, Michael G., Dinesh-Kumar, S.P ., and Joshi, Chandrashekhar P .
Subjects: PLANT cell walls, CELLULOSE, XYLANS, LIGNINS, NICOTIANA, PLANT genetics
Abstract: Virus-induced gene silencing (VIGS) is a powerful genetic tool for rapid assessment of plant gene functions in the post-genomic era. Here, we successfully implemented a Tobacco Rattle Virus (TRV)-based VIGS system to study functions of genes involved in either primary or secondary cell wall formation in Nicotiana benthamiana plants. A 3-week post-VIGS time frame is sufficient to observe phenotypic alterations in the anatomical structure of stems and chemical composition of the primary and secondary cell walls. We used cell wall glycan-directed monoclonal antibodies to demonstrate that alteration of cell wall polymer synthesis during the secondary growth phase of VIGS plants has profound effects on the extractability of components from woody stem cell walls. Therefore, TRV-based VIGS together with cell wall component profiling methods provide a high-throughput gene discovery platform for studying plant cell wall formation from a bioenergy perspective. [ABSTRACT FROM PUBLISHER]
Published: 2010
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34. Genome-Wide ORFeome Cloning and Analysis of Arabidopsis Transcription Factor Genes.

Author: Wei Gong, Yun-Ping Shen, Li-Geng Ma, Yi Pan, Yun-Long Du, Dong-Hui Wang, Jian-Yu Yang, Li-De Hu, Xin-Fang Liu, Chun-Xia Dong, Li Ma, Yan-Hui Chen, Xiao-Yuan Yang, Ying Gao, Danmeng Zhu, Xiaoli Tan, Jin-Ye Mu, Da-Bing Zhang, Yu-Le Liu, and Dinesh-Kumar, S.P.
Subjects: ARABIDOPSIS, PLANT genomes, GENOMES, CLONING, TRANSCRIPTION factors, PROTEINS
Abstract: Here, we report our effort in generating an ORFeome collection for the Arabidopsis transcription factor (TF) genes. In total, ORFeome clones representing 1,282 Arabidopsis TF genes have been obtained in the Gateway high throughput cloning pENTR vector, including 411 genes whose annotation lack cDNA support. All the ORFeome inserts have also been mobilized into a yeast expression destination vector, with an estimated 85% rate of expressing the respective proteins. Sequence analysis of these clones revealed that 34 of them did not match with either the reported cDNAs or current predicted open-reading-frame sequences. Among those, novel alternative splicing of TF gene transcripts is responsible for the observed differences in at least five genes. However, those alternative splicing events do not appear to be differentially regulated among distinct Arabidopsis tissues examined. Lastly, expression of those TF genes in 17 distinct Arabidopsis organ types and the cultured cells was profiled using a 70-mer oligo microarray. [ABSTRACT FROM AUTHOR]
Published: 2004
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35. Two MAPK cascades, NPR1, and TGA transcription factors play a role in Pto-mediated disease resistance in tomato.

Author: Ekengren, Sophia K., Yule Liu, Schiff, Michael, Dinesh-Kumar, S.P., and Martin, Gregory B.
Subjects: TOMATO disease & pest resistance, PROTEIN kinases, TRANSCRIPTION factors
Abstract: The tomato Pto kinase confers resistance to the causative agent of bacterial speck disease, Pseudomonas syringae pv. tomato, by recognizing the pathogen effector proteins AvrPto or AvrPtoB. Pto-mediated resistance requires multiple signal transduction pathways and has been shown to activate many defense responses including an oxidative burst, rapid changes in the expression of over 400 genes, and localized cell death. We have tested the role in Pto-mediated resistance in tomato of a set of 21 genes from other species known to be involved in defense-related signaling. Expression of each gene was suppressed by virus-induced gene silencing (VIGS) and the effect on disease symptoms and bacterial growth during the tomato– Pseudomonas incompatible interaction was determined. We found that Pto-mediated resistance was compromised by silencing of genes encoding two mitogen-activated protein (MAP) kinase kinases, MEK1 and MEK2, two MAP kinases, NTF6 and wound-induced protein kinase (WIPK), a key regulator of systemic acquired resistance (SAR), NPR1, and two transcription factors, TGA1a and TGA2.2. A lesser impact on Pto-mediated resistance was observed in plants silenced for RAR1 and COI1. The identification of nine genes that play a role in resistance to bacterial speck disease both advances our knowledge of Pto signal transduction and demonstrates the conservation of many defense signaling components among diverse plant species. [ABSTRACT FROM AUTHOR]
Published: 2003
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36. The COP9 Signalosome Interacts Physically with SCF[supCOI1] and Modulates Jasmonate Responses.

Author: Suhua Feng, Ligeng Ma, Xiping Wang, Daoxin Xie, Dinesh-Kumar, S.P., Ning Wei, and Xing Wang Deng
Subjects: GEL permeation chromatography, CHROMATOGRAPHIC analysis, PLANT cells & tissues, PLANT anatomy, CYTOLOGY
Abstract: Demonstrates that endogenous as well as epitope-tagged COI1, forms SCF[supCOI1] and associates directly with the COP9 signalosome (CSN) in vivo, using coimmunoprecipitation and gel-filtration analyses. Description of CSN; Areas where CSN plays a role; Factors associated with CSN.
Published: 2003
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37. Structure-function analysis of the tobacco mosaic virus resistance gene N.

Author: Dinesh-Kumar, S.P. and Wai-Hong Tham
Subjects: *TOBACCO mosaic virus, *DISEASE resistance of plants
Abstract: Presents a structure-function analysis of the tobacco mosaic virus (TMV) resistance gene N. Examination of various N deletion and point mutations that introduce single amino acid substitution mutants in vivo; Factors lead to the introduction of TMV resistance.
Published: 2000
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38. Permanent fixation of a transportable element insert in the A2 gene of maize (Zea mays L.).

Author: Thatiparti, V.R. and Dinesh-Kumar, S.P.
Subjects: CORN genetics
Abstract: Presents a genetic study to test the excisability of the I element from the transposase A (TNPA) product of the En/Spm element in allele of maize. Interaction of I element with TNPA; Findings that I element is highly stable at a2-m1 allele of maize.
Published: 1995

39. Virus Induced Gene Silencing of a DEFICIENSOrtholog in Nicotiana Benthamiana

Author: Liu, Yule, Nakayama, Naomi, Schiff, Michael, Litt, Amy, Irish, Vivian, and Dinesh-Kumar, S.P.
Abstract: Traditionally, developmental studies in plant biology have suffered from the lack of a convenient means to study gene function in non-model plant species. Here we show that virus-induced gene silencing (VIGS) is an effective new tool to study the function of orthologs of floral homeotic genes such as DEFICIENS(DEF) in non-model systems. We used a tobacco rattle virus (TRV)-based VIGS approach to study the function of the Nicotiana benthamiana DEFortholog (NbDEF). Silencing of NbDEFin N. benthamianausing TRV-VIGS was similar to that of Antirrhinum defand Arabidopsis ap3mutants and caused transformation of petals into sepals and stamens into carpels. Molecular analysis of the NbDEF-silenced plants revealed a dramatic reduction of the levels of NbDEFmRNA and protein in flowers. NbDEFsilencing was specific and has no effect on the mRNA levels of NbTM6, the closest paralog of NbDEF. A dramatic reduction of the levels of N. benthamiana GLOBOSA(NbGLO) mRNA and protein was also observed in flowers of NbDEF-silenced plants, suggesting that cross-regulation of this GLO-like gene by NbDEF. Taken together, our results suggest that NbDEFis a functional homolog of Antirrhinum DEF. Our results are significant in that they show that TRV efficiently induces gene silencing in young and differentiating flowers and that VIGS is a promising new tool for analyses of developmental gene function in non-model organisms.
Published: 2004
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40. A sequence required for −1 ribosomal frameshifting located four kilobases downstream of the frameshift site11Edited by D. E. Draper

Author: Paul, Cynthia P, Barry, Jennifer K, Dinesh-Kumar, S.P, Brault, Véronique, and Miller, W.Allen
Abstract: Programmed ribosomal frameshifting allows one mRNA to encode regulate expression of, multiple open reading frames (ORFs). The polymerase encoded by ORF 2 of Barley yellow dwarf virus(BYDV) is expressed viaminus one (−1) frameshifting from the overlapping ORF 1. Previously, this appeared to be mediated by a 116 nt RNA sequence that contains canonical −1 frameshift signals including a shifty heptanucleotide followed by a highly structured region. However, unlike known −1 frameshift signals, the reporter system required the zero frame stop codon and did not require a consensus shifty site for expression of the −1 ORF. In contrast, full-length viral RNA required a functional shifty site for frameshifting in wheat germ extract, while the stop codon was not required. Increasing translation initiation efficiency by addition of a 5′ cap on the naturally uncapped viral RNA, decreased the frameshift rate. Unlike any other known RNA, a region four kilobases downstream of the frameshift site was required for frameshifting. This included an essential 55 base tract followed by a 179 base tract that contributed to full frameshifting. The effects of most mutations on frameshifting correlated with the ability of viral RNA to replicate in oat protoplasts, indicating that the wheat germ extract accurately reflected control of BYDV RNA translation in the infected cell. However, the overall frameshift rate appeared to be higher in infected cells, based on immunodetection of viral proteins. These findings show that use of short recoding sequences out of context in reporter constructs may overlook distant signals. Most importantly, the remarkably long-distance interaction reported here suggests the presence of a novel structure that can facilitate ribosomal frameshifting.
Published: 2001
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41. Plant Defense: One Post, Multiple Guards?!

Author: Marathe, Rajendra and Dinesh-Kumar, S.P.
Subjects: *ARABIDOPSIS, *MICROBIAL virulence
Abstract: Arabidopsis RIN4 is a key bacterial virulence target that is guarded by the resistance (R) protein RPM1. Two recent studies suggest that another R protein, RPS2, also guards RIN4. Bacterial avirulence (Avr) effectors AvrB, AvrRpm1, and AvrRpt2 alter this key protein. R proteins RPM1 and RPS2 recognize the altered status and initiate a defense-signaling response. The guard hypothesis is in! [Copyright &y& Elsevier]
Published: 2003
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42. P58IPK, a Plant Ortholog of Double-Stranded RNA-Dependent Protein Kinase PKR Inhibitor, Functions in Viral Pathogenesis

Author: Bilgin, Damla D., Liu, Yule, Schiff, Michael, and Dinesh-Kumar, S.P.
Subjects: *PROTEIN kinases, *INTERFERON inducers, *NICOTIANA, *ARABIDOPSIS, *PLANT diseases
Abstract: P58IPK is a cellular inhibitor of the mammalian double-stranded RNA-activated protein kinase (PKR). Here we provide evidence for the existence of its homolog in plants and its role in viral infection at the organism level. Viral infection of P58IPK-silenced Nicotiana benthamiana and Arabidopsis knockouts leads to host death. This host cell death is associated with phosphorylation of the α subunit of eukaryotic translation initiation factor (eIF-2α). Loss of P58IPK leads to reduced virus titer, suggesting that wild-type P58IPK protein plays an important role in viral pathogenesis. Although our complementation results using mammalian P58IPK suggest conservation of the P58IPK pathway in plants and animals, its biological significance seems to be different in these two systems. In animals, P58IPK is recruited by the influenza virus to limit PKR-mediated innate antiviral response. In plants, P58IPK is required by viruses for virulence and therefore functions as a susceptibility factor. [Copyright &y& Elsevier]
Published: 2003
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