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2. Author Correction: Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein

Author

Mao, Xiaobo, Gu, Hao, Kim, Donghoon, Kimura, Yasuyoshi, Wang, Ning, Xu, Enquan, Kumbhar, Ramhari, Ming, Xiaotian, Wang, Haibo, Chen, Chan, Zhang, Shengnan, Jia, Chunyu, Liu, Yuqing, Bian, Hetao, Karuppagounder, Senthilkumar S., Akkentli, Fatih, Chen, Qi, Jia, Longgang, Hwang, Heehong, Lee, Su Hyun, Ke, Xiyu, Chang, Michael, Li, Amanda, Yang, Jun, Rastegar, Cyrus, Sriparna, Manjari, Ge, Preston, Brahmachari, Saurav, Kim, Sangjune, Zhang, Shu, Shimoda, Yasushi, Saar, Martina, Liu, Haiqing, Kweon, Sin Ho, Ying, Mingyao, Workman, Creg J., Vignali, Dario A. A., Muller, Ulrike C., Liu, Cong, Ko, Han Seok, Dawson, Valina L., and Dawson, Ted M.

Published
2024
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4. Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein

Author

Mao, Xiaobo, Gu, Hao, Kim, Donghoon, Kimura, Yasuyoshi, Wang, Ning, Xu, Enquan, Kumbhar, Ramhari, Ming, Xiaotian, Wang, Haibo, Chen, Chan, Zhang, Shengnan, Jia, Chunyu, Liu, Yuqing, Bian, Hetao, Karuppagounder, Senthilkumar S., Akkentli, Fatih, Chen, Qi, Jia, Longgang, Hwang, Heehong, Lee, Su Hyun, Ke, Xiyu, Chang, Michael, Li, Amanda, Yang, Jun, Rastegar, Cyrus, Sriparna, Manjari, Ge, Preston, Brahmachari, Saurav, Kim, Sangjune, Zhang, Shu, Shimoda, Yasushi, Saar, Martina, Liu, Haiqing, Kweon, Sin Ho, Ying, Mingyao, Workman, Creg J., Vignali, Dario A. A., Muller, Ulrike C., Liu, Cong, Ko, Han Seok, Dawson, Valina L., and Dawson, Ted M.

Published
2024
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5. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author

Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Aqeilan, Rami I, Arama, Eli, Baehrecke, Eric H, Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A, Bartek, Jiri, Bazan, Nicolas G, Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Marco E, Blagosklonny, Mikhail V, Blander, J Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D, Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A, Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chen, Guo-Qiang, Chen, Quan, Chen, Youhai H, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M, Dawson, Valina L, De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus-Michael, Deberardinis, Ralph J, Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J Marie, Haupt, Ygal, He, Sudan, Heery, David M, Hengartner, Michael O, Hetz, Claudio, Hildeman, David A, Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J, and Kanneganti, Thirumala-Devi

Subjects
Biochemistry and Cell Biology, Biological Sciences, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Good Health and Well Being, Animals, Humans, Apoptosis, Cell Death, Caspases, Carcinogenesis, Mammals, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Apoptosis is a form of regulated cell death (RCD) that involves proteases of the caspase family. Pharmacological and genetic strategies that experimentally inhibit or delay apoptosis in mammalian systems have elucidated the key contribution of this process not only to (post-)embryonic development and adult tissue homeostasis, but also to the etiology of multiple human disorders. Consistent with this notion, while defects in the molecular machinery for apoptotic cell death impair organismal development and promote oncogenesis, the unwarranted activation of apoptosis promotes cell loss and tissue damage in the context of various neurological, cardiovascular, renal, hepatic, infectious, neoplastic and inflammatory conditions. Here, the Nomenclature Committee on Cell Death (NCCD) gathered to critically summarize an abundant pre-clinical literature mechanistically linking the core apoptotic apparatus to organismal homeostasis in the context of disease.

Published
2023

6. ADP‐ribosyltransferases, an update on function and nomenclature

Author

Lüscher, Bernhard, Ahel, Ivan, Altmeyer, Matthias, Ashworth, Alan, Bai, Peter, Chang, Paul, Cohen, Michael, Corda, Daniela, Dantzer, Françoise, Daugherty, Matthew D, Dawson, Ted M, Dawson, Valina L, Deindl, Sebastian, Fehr, Anthony R, Feijs, Karla LH, Filippov, Dmitri V, Gagné, Jean‐Philippe, Grimaldi, Giovanna, Guettler, Sebastian, Hoch, Nicolas C, Hottiger, Michael O, Korn, Patricia, Kraus, W Lee, Ladurner, Andreas, Lehtiö, Lari, Leung, Anthony KL, Lord, Christopher J, Mangerich, Aswin, Matic, Ivan, Matthews, Jason, Moldovan, George‐Lucian, Moss, Joel, Natoli, Gioacchino, Nielsen, Michael L, Niepel, Mario, Nolte, Friedrich, Pascal, John, Paschal, Bryce M, Pawłowski, Krzysztof, Poirier, Guy G, Smith, Susan, Timinszky, Gyula, Wang, Zhao‐Qi, Yélamos, José, Yu, Xiaochun, Zaja, Roko, and Ziegler, Mathias

Subjects
Biochemistry and Cell Biology, Biological Sciences, Infectious Diseases, Emerging Infectious Diseases, Genetics, Underpinning research, 5.1 Pharmaceuticals, Development of treatments and therapeutic interventions, 1.1 Normal biological development and functioning, Generic health relevance, ADP Ribose Transferases, Protein Biosynthesis, Adenosine Diphosphate Ribose, Adenosine Diphosphate, ADP-ribosylation, MARylation, PARP, PARylation, posttranslational modification, Medicinal and Biomolecular Chemistry, Medical Biochemistry and Metabolomics, Biochemistry & Molecular Biology, Biochemistry and cell biology, Medical biochemistry and metabolomics, Medicinal and biomolecular chemistry
Abstract

ADP-ribosylation, a modification of proteins, nucleic acids, and metabolites, confers broad functions, including roles in stress responses elicited, for example, by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis, and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases (ARTs), which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ARTs are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as antiviral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ARTs and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ARTs that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ARTs to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.

Published
2022

12. Bi-allelic TTI1 variants cause an autosomal-recessive neurodevelopmental disorder with microcephaly

Author

Serey-Gaut, Margaux, Cortes, Marisol, Makrythanasis, Periklis, Suri, Mohnish, Taylor, Alexander M.R., Sullivan, Jennifer A., Asleh, Ayat N., Mitra, Jaba, Dar, Mohamad A., McNamara, Amy, Shashi, Vandana, Dugan, Sarah, Song, Xiaofei, Rosenfeld, Jill A., Cabrol, Christelle, Iwaszkiewicz, Justyna, Zoete, Vincent, Pehlivan, Davut, Akdemir, Zeynep Coban, Roeder, Elizabeth R., Littlejohn, Rebecca Okashah, Dibra, Harpreet K., Byrd, Philip J., Stewart, Grant S., Geckinli, Bilgen B., Posey, Jennifer, Westman, Rachel, Jungbluth, Chelsy, Eason, Jacqueline, Sachdev, Rani, Evans, Carey-Anne, Lemire, Gabrielle, VanNoy, Grace E., O’Donnell-Luria, Anne, Mau-Them, Frédéric Tran, Juven, Aurélien, Piard, Juliette, Nixon, Cheng Yee, Zhu, Ying, Ha, Taekjip, Buckley, Michael F., Thauvin, Christel, Essien Umanah, George K., Van Maldergem, Lionel, Lupski, James R., Roscioli, Tony, Dawson, Valina L., Dawson, Ted M., and Antonarakis, Stylianos E.

Published
2023
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13. Gut-Initiated Alpha Synuclein Fibrils Drive Parkinson's Disease Phenotypes: Temporal Mapping of non-Motor Symptoms and REM Sleep Behavior Disorder

Author

Dautan, Daniel, primary, Paslawski, Wojciech, additional, Montejo, Sergio, additional, Doyon, Daniel, additional, Marangiu, Roberta, additional, Kaplitt, Michael G, additional, Chen, Rong, additional, Dawson, Valina L., additional, Zhang, Xiaoqun, additional, Dawson, Ted M., additional, and Svenningsson, Per, additional

Published
2024
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14. CYFIP1 Dosages Exhibit Divergent Behavioral Impact via Diametric Regulation of NMDA Receptor Complex Translation in Mouse Models of Psychiatric Disorders

Author

Kim, Nam-Shik, Ringeling, Francisca Rojas, Zhou, Ying, Nguyen, Ha Nam, Temme, Stephanie J., Lin, Yu-Ting, Eacker, Stephen, Dawson, Valina L., Dawson, Ted M., Xiao, Bo, Hsu, Kuei-sen, Canzar, Stefan, Li, Weidong, Worley, Paul, Christian, Kimberly M., Yoon, Ki-Jun, Song, Hongjun, and Ming, Guo-li

Published
2022
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17. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018

Author

Galluzzi, Lorenzo, Vitale, Ilio, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Annicchiarico-Petruzzelli, Margherita, Antonov, Alexey V, Arama, Eli, Baehrecke, Eric H, Barlev, Nickolai A, Bazan, Nicolas G, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Katiuscia, Blagosklonny, Mikhail V, Blomgren, Klas, Borner, Christoph, Boya, Patricia, Brenner, Catherine, Campanella, Michelangelo, Candi, Eleonora, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chandel, Navdeep S, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Cohen, Gerald M, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Dawson, Ted M, Dawson, Valina L, De Laurenzi, Vincenzo, De Maria, Ruggero, Debatin, Klaus-Michael, DeBerardinis, Ralph J, Deshmukh, Mohanish, Di Daniele, Nicola, Di Virgilio, Francesco, Dixit, Vishva M, Dixon, Scott J, Duckett, Colin S, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Fimia, Gian Maria, Fulda, Simone, García-Sáez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Golstein, Pierre, Gottlieb, Eyal, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Gross, Atan, Hajnoczky, Gyorgy, Hardwick, J Marie, Harris, Isaac S, Hengartner, Michael O, Hetz, Claudio, Ichijo, Hidenori, Jäättelä, Marja, Joseph, Bertrand, Jost, Philipp J, Juin, Philippe P, Kaiser, William J, Karin, Michael, Kaufmann, Thomas, Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N, Klionsky, Daniel J, Knight, Richard A, Kumar, Sharad, Lee, Sam W, Lemasters, John J, Levine, Beth, Linkermann, Andreas, Lipton, Stuart A, Lockshin, Richard A, López-Otín, Carlos, Lowe, Scott W, Luedde, Tom, Lugli, Enrico, MacFarlane, Marion, Madeo, Frank, Malewicz, Michal, Malorni, Walter, and Manic, Gwenola

Subjects
Biochemistry and Cell Biology, Biological Sciences, Animals, Cell Death, Humans, Lysosomes, Mitochondrial Membrane Transport Proteins, Mitochondrial Permeability Transition Pore, Necrosis, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Over the past decade, the Nomenclature Committee on Cell Death (NCCD) has formulated guidelines for the definition and interpretation of cell death from morphological, biochemical, and functional perspectives. Since the field continues to expand and novel mechanisms that orchestrate multiple cell death pathways are unveiled, we propose an updated classification of cell death subroutines focusing on mechanistic and essential (as opposed to correlative and dispensable) aspects of the process. As we provide molecularly oriented definitions of terms including intrinsic apoptosis, extrinsic apoptosis, mitochondrial permeability transition (MPT)-driven necrosis, necroptosis, ferroptosis, pyroptosis, parthanatos, entotic cell death, NETotic cell death, lysosome-dependent cell death, autophagy-dependent cell death, immunogenic cell death, cellular senescence, and mitotic catastrophe, we discuss the utility of neologisms that refer to highly specialized instances of these processes. The mission of the NCCD is to provide a widely accepted nomenclature on cell death in support of the continued development of the field.

Published
2018

18. Guidelines on experimental methods to assess mitochondrial dysfunction in cellular models of neurodegenerative diseases

Author

Connolly, Niamh MC, Theurey, Pierre, Adam-Vizi, Vera, Bazan, Nicolas G, Bernardi, Paolo, Bolaños, Juan P, Culmsee, Carsten, Dawson, Valina L, Deshmukh, Mohanish, Duchen, Michael R, Düssmann, Heiko, Fiskum, Gary, Galindo, Maria F, Hardingham, Giles E, Hardwick, J Marie, Jekabsons, Mika B, Jonas, Elizabeth A, Jordán, Joaquin, Lipton, Stuart A, Manfredi, Giovanni, Mattson, Mark P, McLaughlin, BethAnn, Methner, Axel, Murphy, Anne N, Murphy, Michael P, Nicholls, David G, Polster, Brian M, Pozzan, Tullio, Rizzuto, Rosario, Satrústegui, Jorgina, Slack, Ruth S, Swanson, Raymond A, Swerdlow, Russell H, Will, Yvonne, Ying, Zheng, Joselin, Alvin, Gioran, Anna, Moreira Pinho, Catarina, Watters, Orla, Salvucci, Manuela, Llorente-Folch, Irene, Park, David S, Bano, Daniele, Ankarcrona, Maria, Pizzo, Paola, and Prehn, Jochen HM

Subjects
Biochemistry and Cell Biology, Biological Sciences, Neurodegenerative, Aging, Acquired Cognitive Impairment, Brain Disorders, Neurosciences, 2.1 Biological and endogenous factors, Aetiology, Neurological, Animals, Humans, Mitochondria, Models, Biological, Neurodegenerative Diseases, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Neurodegenerative diseases are a spectrum of chronic, debilitating disorders characterised by the progressive degeneration and death of neurons. Mitochondrial dysfunction has been implicated in most neurodegenerative diseases, but in many instances it is unclear whether such dysfunction is a cause or an effect of the underlying pathology, and whether it represents a viable therapeutic target. It is therefore imperative to utilise and optimise cellular models and experimental techniques appropriate to determine the contribution of mitochondrial dysfunction to neurodegenerative disease phenotypes. In this consensus article, we collate details on and discuss pitfalls of existing experimental approaches to assess mitochondrial function in in vitro cellular models of neurodegenerative diseases, including specific protocols for the measurement of oxygen consumption rate in primary neuron cultures, and single-neuron, time-lapse fluorescence imaging of the mitochondrial membrane potential and mitochondrial NAD(P)H. As part of the Cellular Bioenergetics of Neurodegenerative Diseases (CeBioND) consortium ( www.cebiond.org ), we are performing cross-disease analyses to identify common and distinct molecular mechanisms involved in mitochondrial bioenergetic dysfunction in cellular models of Alzheimer's, Parkinson's, and Huntington's diseases. Here we provide detailed guidelines and protocols as standardised across the five collaborating laboratories of the CeBioND consortium, with additional contributions from other experts in the field.

Published
2018

19. Opportunities for the repurposing of PARP inhibitors for the therapy of non‐oncological diseases

Author

Berger, Nathan A, Besson, Valerie C, Boulares, A Hamid, Bürkle, Alexander, Chiarugi, Alberto, Clark, Robert S, Curtin, Nicola J, Cuzzocrea, Salvatore, Dawson, Ted M, Dawson, Valina L, Haskó, György, Liaudet, Lucas, Moroni, Flavio, Pacher, Pál, Radermacher, Peter, Salzman, Andrew L, Snyder, Solomon H, Soriano, Francisco Garcia, Strosznajder, Robert P, Sümegi, Balázs, Swanson, Raymond A, and Szabo, Csaba

Subjects
Orphan Drug, Brain Disorders, Neurosciences, Rare Diseases, Lung, Evaluation of treatments and therapeutic interventions, 6.1 Pharmaceuticals, 5.1 Pharmaceuticals, Development of treatments and therapeutic interventions, Good Health and Well Being, Acute Disease, Animals, Chronic Disease, Drug Repositioning, Humans, Poly(ADP-ribose) Polymerase Inhibitors, Pharmacology and Pharmaceutical Sciences, Pharmacology & Pharmacy
Abstract

The recent clinical availability of the PARP inhibitor olaparib (Lynparza) opens the door for potential therapeutic repurposing for non-oncological indications. Considering (a) the preclinical efficacy data with PARP inhibitors in non-oncological diseases and (b) the risk-benefit ratio of treating patients with a compound that inhibits an enzyme that has physiological roles in the regulation of DNA repair, we have selected indications, where (a) the severity of the disease is high, (b) the available therapeutic options are limited, and (c) the duration of PARP inhibitor administration could be short, to provide first-line options for therapeutic repurposing. These indications are as follows: acute ischaemic stroke; traumatic brain injury; septic shock; acute pancreatitis; and severe asthma and severe acute lung injury. In addition, chronic, devastating diseases, where alternative therapeutic options cannot halt disease development (e.g. Parkinson's disease, progressive multiple sclerosis or severe fibrotic diseases), should also be considered. We present a preclinical and clinical action plan for the repurposing of PARP inhibitors.Linked articlesThis article is part of a themed section on Inventing New Therapies Without Reinventing the Wheel: The Power of Drug Repurposing. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v175.2/issuetoc.

Published
2018

20. Intracellular Signaling

Author

Thompson, John W., primary, Xu, Jinchong, additional, Dawson, Valina L., additional, Perez-Pinzon, Miguel A., additional, and Dawson, Ted M., additional

Published
2022
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21. Contributors

Author

Adams, Harold P., primary, Adeoye, Opeolu, additional, Albers, Gregory W., additional, Alexandrov, Andrei V., additional, Amin-Hanjani, Sepideh, additional, An, Hongyu, additional, Anderson, Craig S., additional, Anrather, Josef, additional, Aparicio, Hugo J., additional, Arai, Ken, additional, Aronowski, Jaroslaw, additional, Atchaneeyasakul, Kunakorn, additional, Audebert, Heinrich, additional, Auer, Roland N., additional, Awad, Issam A., additional, Ay, Hakan, additional, Baltan, Selva, additional, Balu, Ramani, additional, Behbahani, Mandana, additional, Benavente, Oscar R., additional, Bershad, Eric M., additional, Berthaud, Jimmy V., additional, Blackburn, Spiros L., additional, Bonati, Leo H., additional, Bösel, Julian, additional, Bousser, Marie Germaine, additional, Broderick, Joseph P., additional, Brown, Martin M., additional, Brown, Wendy, additional, Brust, John C.M., additional, Bushnell, Cheryl, additional, Canhão, Patrícia, additional, Caplan, Louis R., additional, Carrión-Penagos, Julián, additional, Castellanos, Mar, additional, Caunca, Michelle R., additional, Chabriat, Hugues, additional, Chamorro, Angel, additional, Chen, Jieli, additional, Chen, Jun, additional, Chopp, Michael, additional, Christorforids, Greg, additional, Connolly, E. Sander, additional, Cramer, Steven C., additional, Cucchiara, Brett L., additional, Czap, Alexandra L., additional, Dannenbaum, Mark J., additional, Davis, Patricia H., additional, Dawson, Ted M., additional, Dawson, Valina L., additional, Day, Arthur L., additional, De Silva, T. Michael, additional, de Sousa, Diana Aguiar, additional, Del Brutto, Victor J., additional, del Zoppo, Gregory J., additional, Derdeyn, Colin P., additional, Di Tullio, Marco R., additional, Diener, Hans Christoph, additional, Diringer, Michael N., additional, Dobkin, Bruce H., additional, Dzialowski, Imanuel, additional, Elkind, Mitchell S.V., additional, Elm, Jordan, additional, Feigin, Valery L., additional, Ferro, José Manuel, additional, Field, Thalia S., additional, Fischer, Marlene, additional, Fornage, Myriam, additional, Furie, Karen L., additional, Garcia-Bonilla, Lidia, additional, Giannotta, Steven L., additional, Gobin, Y. Pierre, additional, Goldberg, Mark P., additional, Goldstein, Larry B., additional, Gonzales, Nicole R., additional, Greer, David M., additional, Grotta, James C., additional, Guo, Ruiming, additional, Gutierrez, Jose, additional, Harmel, Peter, additional, Howard, George, additional, Howard, Virginia J., additional, Hwang, Jee-Yeon, additional, Iadecola, Costantino, additional, Jahan, Reza, additional, Jickling, Glen C., additional, Joutel, Anne, additional, Kasner, Scott E., additional, Katan, Mira, additional, Kellner, Christopher P., additional, Khan, Muhib, additional, Kidwell, Chelsea S., additional, Kim, Helen, additional, Kim, Jong S., additional, Kircher, Charles E., additional, Krings, Timo, additional, Krishnamurthi, Rita V., additional, Kurth, Tobias, additional, Lansberg, Maarten G., additional, Levy, Elad I., additional, Liebeskind, David S., additional, Liew, Sook-Lei, additional, Lin, David J., additional, Lisle, Benjamin, additional, Lo, Eng H., additional, Lyden, Patrick D., additional, Maki, Takakuni, additional, Maragkos, Georgios A., additional, Marosfoi, Miklos, additional, McCullough, Louise D., additional, Meckler, Jason M., additional, Meschia, James Frederick, additional, Messé, Steven R., additional, Mocco, J, additional, Mokin, Maxim, additional, Mooney, Michael A., additional, Morgenstern, Lewis B., additional, Moskowitz, Michael A., additional, Mullen, Michael T., additional, Nägel, Steffen, additional, Nedergaard, Maiken, additional, Neira, Justin A., additional, Newman, Sarah, additional, Nicholson, Patrick J., additional, Norrving, Bo, additional, O’Donnell, Martin, additional, Ofengeim, Dimitry, additional, Ogata, Jun, additional, Ogilvy, Christopher S., additional, Orrù, Emanuele, additional, Ortega-Gutiérrez, Santiago, additional, Padrick, Matthew Maximillian, additional, Parsha, Kaushik, additional, Parsons, Mark, additional, Patel, Neil V., additional, Patel, Virendra I., additional, Pawlikowska, Ludmila, additional, Pérez, Adriana, additional, Perez-Pinzon, Miguel A., additional, Picard, John M., additional, Polster, Sean P., additional, Powers, William J., additional, Puetz, Volker, additional, Putaala, Jukka, additional, Rabinovich, Margarita, additional, Ransom, Bruce R., additional, Roa, Jorge A., additional, Rosenberg, Gary A., additional, Rossitto, Christina P., additional, Rundek, Tatjana, additional, Russin, Jonathan J., additional, Sacco, Ralph L., additional, Safouris, Apostolos, additional, Samaniego, Edgar A., additional, Sansing, Lauren H., additional, Satani, Nikunj, additional, Sattenberg, Ronald J., additional, Saver, Jeffrey L., additional, Savitz, Sean I., additional, Schmidt, Christian, additional, Seshadri, Sudha, additional, Sharma, Vijay K., additional, Sharp, Frank R., additional, Sheth, Kevin N., additional, Siddiqi, Omar K., additional, Singhal, Aneesh B., additional, Sobey, Christopher G., additional, Sommer, Clemens J., additional, Spetzler, Robert F., additional, Stapleton, Christopher J., additional, Strickland, Ben A., additional, Su, Hua, additional, Suarez, José I., additional, Takayama, Hiroo, additional, Tarsia, Joseph, additional, Tatlisumak, Turgut, additional, Thomas, Ajith J., additional, Thompson, John W., additional, Tsivgoulis, Georgios, additional, Tournier-Lasserve, Elizabeth, additional, Vidal, Gabriel, additional, Wakhloo, Ajay K., additional, Weksler, Babette B., additional, Willey, Joshua Z., additional, Wintermark, Max, additional, Wong, Lawrence K.S., additional, Xi, Guohua, additional, Xu, Jinchong, additional, Yaghi, Shadi, additional, Yamaguchi, Takenori, additional, Yang, Tuo, additional, Yasaka, Masahiro, additional, Zahuranec, Darin B., additional, Zhang, Feng, additional, Zhang, John H., additional, Zheng, Zhitong, additional, Zukin, R. Suzanne, additional, and Zweifler, Richard M., additional

Published
2022
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25. Blocking the Self-Destruct Program of Dopamine Neurons through Macrophage Migration Inhibitory Factor Nuclease Inhibition.

Author

Patel, Jaimin, Dawson, Valina L., and Dawson, Ted M.

Abstract

Parkinson’s disease (PD) is a progressive neurodegenerative condition that pathognomonically involves the death of dopaminergic neurons in the substantia nigra pars compacta, resulting in a myriad of motor and nonmotor symptoms. Given the insurmountable burden of this disease on the population and healthcare system, significant efforts have been put forth toward generating disease modifying therapies. This class of treatments characteristically alters disease course, as opposed to current strategies that focus on managing symptoms. Previous literature has implicated the cell death pathway known as parthanatos in PD progression. Inhibition of this pathway by targeting poly (ADP)-ribose polymerase 1 (PARP1) prevents neurodegeneration in a model of idiopathic PD. However, PARP1 has a vast repertoire of functions within the body, increasing the probability of side effects with the long-term treatment likely necessary for clinically significant neuroprotection. Recent work culminated in the development of a novel agent targeting the macrophage migration inhibitory factor (MIF) nuclease domain, also named parthanatos-associated apoptosis-inducing factor nuclease (PAAN). This nuclease activity specifically executes the terminal step in parthanatos. Parthanatos-associated apoptosis-inducing factor nuclease inhibitor-1 was neuroprotective in multiple preclinical mouse models of PD. This piece will focus on contextualizing this discovery, emphasizing its significance, and discussing its potential implications for parthanatos-directed treatment. © 2024 International Parkinson and Movement Disorder Society. [ABSTRACT FROM AUTHOR]

Published
2024
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26. α-Synuclein pathology disrupts mitochondrial function in dopaminergic and cholinergic neurons at-risk in Parkinson’s disease

Author

Geibl, Fanni F., primary, Henrich, Martin T., additional, Xie, Zhong, additional, Zampese, Enrico, additional, Tkatch, Tatiana, additional, Wokosin, David L., additional, Nasiri, Elena, additional, Grotmann, Constantin A., additional, Dawson, Valina L., additional, Dawson, Ted M., additional, Chandel, Navdeep S., additional, Oertel, Wolfgang H., additional, and Surmeier, D. James, additional

Published
2023
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28. Enhanced mTORC1 signaling and protein synthesis in pathologic α-synuclein cellular and animal models of Parkinson’s disease

Author

Khan, Mohammed Repon, primary, Yin, Xiling, additional, Kang, Sung-Ung, additional, Mitra, Jaba, additional, Wang, Hu, additional, Ryu, Taekyung, additional, Brahmachari, Saurav, additional, Karuppagounder, Senthilkumar S., additional, Kimura, Yasuyoshi, additional, Jhaldiyal, Aanishaa, additional, Kim, Hyun Hee, additional, Gu, Hao, additional, Chen, Rong, additional, Redding-Ochoa, Javier, additional, Troncoso, Juan, additional, Na, Chan Hyun, additional, Ha, Taekjip, additional, Dawson, Valina L., additional, and Dawson, Ted M., additional

Published
2023
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30. Poly(ADP-ribose) drives pathologic α-synuclein neurodegeneration in Parkinson’s disease

Author

Kam, Tae-In, Mao, Xiaobo, Park, Hyejin, Chou, Shih-Ching, Karuppagounder, Senthilkumar S., Umanah, George Essien, Yun, Seung Pil, Brahmachari, Saurav, Panicker, Nikhil, Chen, Rong, Andrabi, Shaida A., Qi, Chen, Poirier, Guy G., Pletnikova, Olga, Troncoso, Juan C., Bekris, Lynn M., Leverenz, James B., Pantelyat, Alexander, Ko, Han Seok, Rosenthal, Liana S., Dawson, Ted M., and Dawson, Valina L.

Published
2018

31. AIF3 splicing switch triggers neurodegeneration

Author

Liu, Shuiqiao, Zhou, Mi, Ruan, Zhi, Wang, Yanan, Chang, Calvin, Sasaki, Masayuki, Rajaram, Veena, Lemoff, Andrew, Nambiar, Kalyani, Wang, Jennifer E., Hatanpaa, Kimmo J., Luo, Weibo, Dawson, Ted M., Dawson, Valina L., and Wang, Yingfei

Published
2021
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35. Protein Translation in the Pathogenesis of Parkinson's Disease.

Author

Ashraf, Daniyal, Khan, Mohammed Repon, Dawson, Ted M., and Dawson, Valina L.

Subjects
PARKINSON'S disease, PROTEINS, PATHOGENESIS, AMYOTROPHIC lateral sclerosis
Abstract

In recent years, research into Parkinson's disease and similar neurodegenerative disorders has increasingly suggested that these conditions are synonymous with failures in proteostasis. However, the spotlight of this research has remained firmly focused on the tail end of proteostasis, primarily aggregation, misfolding, and degradation, with protein translation being comparatively overlooked. Now, there is an increasing body of evidence supporting a potential role for translation in the pathogenesis of PD, and its dysregulation is already established in other similar neurodegenerative conditions. In this paper, we consider how altered protein translation fits into the broader picture of PD pathogenesis, working hand in hand to compound the stress placed on neurons, until this becomes irrecoverable. We will also consider molecular players of interest, recent evidence that suggests that aggregates may directly influence translation in PD progression, and the implications for the role of protein translation in our development of clinically useful diagnostics and therapeutics. [ABSTRACT FROM AUTHOR]

Published
2024
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36. Farnesol prevents aging-related muscle weakness in mice through enhanced farnesylation of Parkin-interacting substrate

Author

Bae, Ju-Hyeon, primary, Jo, Areum, additional, Cho, Sung Chun, additional, Lee, Yun-Il, additional, Kam, Tae-In, additional, You, Chang-Lim, additional, Jeong, Hyeon-Ju, additional, Kim, Hyebeen, additional, Jeong, Myong-Ho, additional, Jeong, Yideul, additional, Ha, Young Wan, additional, Kim, Yu Seon, additional, Kim, Jiwoon, additional, Woo, Seung-Hwa, additional, Kim, Minseok S., additional, Shin, Eui Seok, additional, Song, Sang Ok, additional, Kang, Hojin, additional, Khang, Rin, additional, Park, Soojeong, additional, Park, Joobae, additional, Dawson, Valina L., additional, Dawson, Ted M., additional, Park, Sang Chul, additional, Shin, Joo-Ho, additional, and Kang, Jong-Sun, additional

Published
2023
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45. Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease

Author

Lee, Byoung Dae, Shin, Joo-Ho, VanKampen, Jackalina, Petrucelli, Leonard, West, Andrew B, Ko, Han Seok, Lee, Yun-Il, Maguire-Zeiss, Kathleen A, Bowers, William J, Federoff, Howard J, Dawson, Valina L, and Dawson, Ted M

Subjects
Aging, Brain Disorders, Parkinson's Disease, Neurosciences, Neurodegenerative, Aetiology, 2.1 Biological and endogenous factors, Neurological, Humans, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Mutation, Neurons, Parkinson Disease, Phosphorylation, Protein Kinase Inhibitors, Protein Serine-Threonine Kinases, Protein-Serine-Threonine Kinases, Medical and Health Sciences, Immunology
Abstract

Leucine-rich repeat kinase-2 (LRRK2) mutations are a common cause of Parkinson's disease. Here we identify inhibitors of LRRK2 kinase that are protective in in vitro and in vivo models of LRRK2-induced neurodegeneration. These results establish that LRRK2-induced degeneration of neurons in vivo is kinase dependent and that LRRK2 kinase inhibition provides a potential new neuroprotective paradigm for the treatment of Parkinson's disease.

Published
2010

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