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  1. Article ; Online: The Cvt pathway as a model for selective autophagy.

    Lynch-Day, Melinda A / Klionsky, Daniel J

    FEBS letters

    2010  Volume 584, Issue 7, Page(s) 1359–1366

    Abstract: Autophagy is a highly conserved, ubiquitous process that is responsible for the degradation of cytosolic components in response to starvation. Autophagy is generally considered to be non-selective; however, there are selective types of autophagy that use ...

    Abstract Autophagy is a highly conserved, ubiquitous process that is responsible for the degradation of cytosolic components in response to starvation. Autophagy is generally considered to be non-selective; however, there are selective types of autophagy that use receptor and adaptor proteins to specifically isolate a cargo. One type of selective autophagy in yeast is the cytoplasm to vacuole targeting (Cvt) pathway. The Cvt pathway is responsible for the delivery of the hydrolase aminopeptidase I to the vacuole; as such, it is the only known biosynthetic pathway that utilizes the core machinery of autophagy. Nonetheless, it serves as a model for the study of selective autophagy in other organisms.
    MeSH term(s) Autophagy ; Models, Biological ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
    Chemical Substances Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2010-02-08
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2010.02.013
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  2. Article ; Online: The Ume6-Sin3-Rpd3 complex regulates ATG8 transcription to control autophagosome size.

    Backues, Steven K / Lynch-Day, Melinda A / Klionsky, Daniel J

    Autophagy

    2012  Volume 8, Issue 12, Page(s) 1835–1836

    Abstract: The vast majority of studies addressing the induction of autophagy have focused upon cytoplasmic aspects of its regulation. Recently, we have started to expand our knowledge regarding the nuclear events of autophagic induction. Many autophagy-related ... ...

    Abstract The vast majority of studies addressing the induction of autophagy have focused upon cytoplasmic aspects of its regulation. Recently, we have started to expand our knowledge regarding the nuclear events of autophagic induction. Many autophagy-related genes are transcriptionally upregulated upon induction of autophagy, but only in a limited number of cases do we know the pathways leading to this upregulation. Few transcription factors have been implicated in controlling autophagy genes in yeast. However, many of the ATG genes show some level of transcriptional induction upon starvation. Now, we show that transcription of ATG8 is repressed under growing conditions by the Ume6-Sin3-Rpd3 complex.
    MeSH term(s) Autophagy ; Autophagy-Related Protein 8 Family ; Microtubule-Associated Proteins/genetics ; Models, Biological ; Multiprotein Complexes/metabolism ; Phagosomes/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription, Genetic
    Chemical Substances ATG8 protein, S cerevisiae ; Autophagy-Related Protein 8 Family ; Microtubule-Associated Proteins ; Multiprotein Complexes ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2012-09-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.21845
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  3. Article ; Online: Corrigendum: The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy.

    Füllgrabe, Jens / Lynch-Day, Melinda A / Heldring, Nina / Li, Wenbo / Struijk, Robert B / Ma, Qi / Hermanson, Ola / Rosenfeld, Michael G / Klionsky, Daniel J / Joseph, Bertrand

    Nature

    2017  Volume 543, Issue 7647, Page(s) 742

    Language English
    Publishing date 2017--30
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature22027
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  4. Article ; Online: The role of autophagy in Parkinson's disease.

    Lynch-Day, Melinda A / Mao, Kai / Wang, Ke / Zhao, Mantong / Klionsky, Daniel J

    Cold Spring Harbor perspectives in medicine

    2012  Volume 2, Issue 4, Page(s) a009357

    Abstract: Great progress has been made toward understanding the pathogenesis of Parkinson's disease (PD) during the past two decades, mainly as a consequence of the discovery of specific gene mutations contributing to the onset of PD. Recently, dysregulation of ... ...

    Abstract Great progress has been made toward understanding the pathogenesis of Parkinson's disease (PD) during the past two decades, mainly as a consequence of the discovery of specific gene mutations contributing to the onset of PD. Recently, dysregulation of the autophagy pathway has been observed in the brains of PD patients and in animal models of PD, indicating the emerging role of autophagy in this disease. Indeed, autophagy is increasingly implicated in a number of pathophysiologies, including various neurodegenerative diseases. This article will lead you through the connection between autophagy and PD by introducing the concept and physiological function of autophagy, and the proteins related to autosomal dominant and autosomal recessive PD, particularly α-synuclein and PINK1-PARKIN, as they pertain to autophagy.
    MeSH term(s) Animals ; Autophagy/genetics ; Autophagy/physiology ; Humans ; Mitochondria/metabolism ; Mitochondria/physiology ; Mitophagy ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/physiopathology ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
    Chemical Substances alpha-Synuclein ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27) ; Protein Kinases (EC 2.7.-) ; PTEN-induced putative kinase (EC 2.7.11.1)
    Language English
    Publishing date 2012-03-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 2157-1422
    ISSN (online) 2157-1422
    DOI 10.1101/cshperspect.a009357
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler.

    Echtenkamp, Frank J / Gvozdenov, Zlata / Adkins, Nicholas L / Zhang, Yang / Lynch-Day, Melinda / Watanabe, Shinya / Peterson, Craig L / Freeman, Brian C

    Molecular cell

    2016  Volume 64, Issue 5, Page(s) 888–899

    Abstract: Molecular chaperones govern protein homeostasis, being allied to the beginning (folding) and ending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with native factors, including fully assembled complexes. The ... ...

    Abstract Molecular chaperones govern protein homeostasis, being allied to the beginning (folding) and ending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with native factors, including fully assembled complexes. The significance of these connections is poorly understood. To delineate why Hsp90 and its cochaperone p23 interact with a mature structure, we focused on the RSC chromatin remodeler. Both Hsp90 and p23 triggered the release of RSC from DNA or a nucleosome. Although Hsp90 only freed bound RSC, p23 enhanced nucleosome remodeling prior to discharging the complex. In vivo, RSC mobility and remodeling function were chaperone dependent. Our results suggest Hsp90 and p23 contribute to proteostasis by chaperoning mature factors through energetically unfavorable events, thereby maintaining the cellular pool of active native proteins. In the case of RSC, p23 and Hsp90 promote a dynamic action, allowing a limited number of remodelers to effectively maintain chromatin in a pliable state.
    MeSH term(s) Animals ; Chromatin Assembly and Disassembly ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Deletion ; HSP90 Heat-Shock Proteins/genetics ; HSP90 Heat-Shock Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Nucleosomes/metabolism ; Protein Conformation ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances DNA-Binding Proteins ; HSP90 Heat-Shock Proteins ; Molecular Chaperones ; Nucleosomes ; RSC complex, S cerevisiae ; SBA1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Transcription Factors
    Language English
    Publishing date 2016-11-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2016.09.040
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  6. Article ; Online: The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy.

    Füllgrabe, Jens / Lynch-Day, Melinda A / Heldring, Nina / Li, Wenbo / Struijk, Robert B / Ma, Qi / Hermanson, Ola / Rosenfeld, Michael G / Klionsky, Daniel J / Joseph, Bertrand

    Nature

    2013  Volume 500, Issue 7463, Page(s) 468–471

    Abstract: Autophagy is an evolutionarily conserved catabolic process involved in several physiological and pathological processes. Although primarily cytoprotective, autophagy can also contribute to cell death; it is thus important to understand what distinguishes ...

    Abstract Autophagy is an evolutionarily conserved catabolic process involved in several physiological and pathological processes. Although primarily cytoprotective, autophagy can also contribute to cell death; it is thus important to understand what distinguishes the life or death decision in autophagic cells. Here we report that induction of autophagy is coupled to reduction of histone H4 lysine 16 acetylation (H4K16ac) through downregulation of the histone acetyltransferase hMOF (also called KAT8 or MYST1), and demonstrate that this histone modification regulates the outcome of autophagy. At a genome-wide level, we find that H4K16 deacetylation is associated predominantly with the downregulation of autophagy-related genes. Antagonizing H4K16ac downregulation upon autophagy induction results in the promotion of cell death. Our findings establish that alteration in a specific histone post-translational modification during autophagy affects the transcriptional regulation of autophagy-related genes and initiates a regulatory feedback loop, which serves as a key determinant of survival versus death responses upon autophagy induction.
    MeSH term(s) Acetylation/drug effects ; Autophagy/drug effects ; Autophagy/genetics ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Down-Regulation/drug effects ; Epistasis, Genetic/drug effects ; Feedback, Physiological ; Histone Acetyltransferases/metabolism ; Histones/metabolism ; Humans ; Lysine/chemistry ; Lysine/metabolism ; Sirolimus/pharmacology ; Transcription, Genetic/drug effects ; Transcription, Genetic/genetics
    Chemical Substances Histones ; Histone Acetyltransferases (EC 2.3.1.48) ; KAT8 protein, human (EC 2.3.1.48) ; Lysine (K3Z4F929H6) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2013-07-17
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature12313
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    Zs.A 26: Show issues Location:
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  7. Article ; Online: Ume6 transcription factor is part of a signaling cascade that regulates autophagy.

    Bartholomew, Clinton R / Suzuki, Tsukasa / Du, Zhou / Backues, Steven K / Jin, Meiyan / Lynch-Day, Melinda A / Umekawa, Midori / Kamath, Avani / Zhao, Mantong / Xie, Zhiping / Inoki, Ken / Klionsky, Daniel J

    Proceedings of the National Academy of Sciences of the United States of America

    2012  Volume 109, Issue 28, Page(s) 11206–11210

    Abstract: Autophagy has been implicated in a number of physiological processes important for human heath and disease. Autophagy involves the formation of a double-membrane cytosolic vesicle, an autophagosome. Central to the formation of the autophagosome is the ... ...

    Abstract Autophagy has been implicated in a number of physiological processes important for human heath and disease. Autophagy involves the formation of a double-membrane cytosolic vesicle, an autophagosome. Central to the formation of the autophagosome is the ubiquitin-like protein autophagy-related (Atg)8 (microtubule-associated protein 1 light chain 3/LC3 in mammalian cells). Following autophagy induction, Atg8 shows the greatest change in expression of any of the proteins required for autophagy. The magnitude of autophagy is, in part, controlled by the amount of Atg8; thus, controlling Atg8 protein levels is one potential mechanism for modulating autophagy activity. We have identified a negative regulator of ATG8 transcription, Ume6, which acts along with a histone deacetylase complex including Sin3 and Rpd3 to regulate Atg8 levels; deletion of any of these components leads to an increase in Atg8 and a concomitant increase in autophagic activity. A similar regulatory mechanism is present in mammalian cells, indicating that this process is highly conserved.
    MeSH term(s) Autophagy ; Autophagy-Related Protein 8 Family ; Gene Deletion ; HeLa Cells ; Histone Deacetylases/metabolism ; Humans ; Lysosomes/metabolism ; Microtubule-Associated Proteins/metabolism ; Models, Biological ; Models, Genetic ; Promoter Regions, Genetic ; Protein Kinases/metabolism ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Sin3 Histone Deacetylase and Corepressor Complex/metabolism ; Transcription, Genetic ; Vacuoles/metabolism
    Chemical Substances ATG8 protein, S cerevisiae ; Autophagy-Related Protein 8 Family ; Microtubule-Associated Proteins ; Repressor Proteins ; SIN3 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; UME6 protein, S cerevisiae ; Protein Kinases (EC 2.7.-) ; Rim15 protein, S cerevisiae (EC 2.7.1.-) ; RPD3 protein, S cerevisiae (EC 3.5.1.-) ; Histone Deacetylases (EC 3.5.1.98) ; Sin3 Histone Deacetylase and Corepressor Complex (EC 3.5.1.98)
    Language English
    Publishing date 2012-06-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1200313109
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  8. Article ; Online: A genomic screen for yeast mutants defective in selective mitochondria autophagy.

    Kanki, Tomotake / Wang, Ke / Baba, Misuzu / Bartholomew, Clinton R / Lynch-Day, Melinda A / Du, Zhou / Geng, Jiefei / Mao, Kai / Yang, Zhifen / Yen, Wei-Lien / Klionsky, Daniel J

    Molecular biology of the cell

    2009  Volume 20, Issue 22, Page(s) 4730–4738

    Abstract: Mitophagy is the process of selective mitochondrial degradation via autophagy, which has an important role in mitochondrial quality control. Very little is known, however, about the molecular mechanism of mitophagy. A genome-wide yeast mutant screen for ... ...

    Abstract Mitophagy is the process of selective mitochondrial degradation via autophagy, which has an important role in mitochondrial quality control. Very little is known, however, about the molecular mechanism of mitophagy. A genome-wide yeast mutant screen for mitophagy-defective strains identified 32 mutants with a block in mitophagy, in addition to the known autophagy-related (ATG) gene mutants. We further characterized one of these mutants, ylr356wDelta that corresponds to a gene whose function has not been identified. YLR356W is a mitophagy-specific gene that was not required for other types of selective autophagy or macroautophagy. The deletion of YLR356W partially inhibited mitophagy during starvation, whereas there was an almost complete inhibition at post-log phase. Accordingly, we have named this gene ATG33. The new mutants identified in this analysis will provide a useful foundation for researchers interested in the study of mitochondrial homeostasis and quality control.
    MeSH term(s) Autophagy/physiology ; Biological Assay/methods ; Cell Cycle/physiology ; Gene Knockout Techniques ; Mitochondria/physiology ; Mutation ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Starvation
    Chemical Substances Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2009-09-30
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E09-03-0225
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  9. Article: Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler

    Echtenkamp, Frank J / Brian C. Freeman / Craig L. Peterson / Melinda Lynch-Day / Nicholas L. Adkins / Shinya Watanabe / Yang Zhang / Zlata Gvozdenov

    Molecular cell. 2016 Dec. 01, v. 64, no. 5

    2016  

    Abstract: Molecular chaperones govern protein homeostasis, being allied to the beginning (folding) and ending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with native factors, including fully assembled complexes. The ... ...

    Abstract Molecular chaperones govern protein homeostasis, being allied to the beginning (folding) and ending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with native factors, including fully assembled complexes. The significance of these connections is poorly understood. To delineate why Hsp90 and its cochaperone p23 interact with a mature structure, we focused on the RSC chromatin remodeler. Both Hsp90 and p23 triggered the release of RSC from DNA or a nucleosome. Although Hsp90 only freed bound RSC, p23 enhanced nucleosome remodeling prior to discharging the complex. In vivo, RSC mobility and remodeling function were chaperone dependent. Our results suggest Hsp90 and p23 contribute to proteostasis by chaperoning mature factors through energetically unfavorable events, thereby maintaining the cellular pool of active native proteins. In the case of RSC, p23 and Hsp90 promote a dynamic action, allowing a limited number of remodelers to effectively maintain chromatin in a pliable state.
    Keywords DNA ; homeostasis ; molecular chaperones ; nucleosomes
    Language English
    Dates of publication 2016-1201
    Size p. 888-899.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2016.09.040
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  10. Article ; Online: Guidelines for the use and interpretation of assays for monitoring autophagy.

    Klionsky, Daniel J / Abdalla, Fabio C / Abeliovich, Hagai / Abraham, Robert T / Acevedo-Arozena, Abraham / Adeli, Khosrow / Agholme, Lotta / Agnello, Maria / Agostinis, Patrizia / Aguirre-Ghiso, Julio A / Ahn, Hyung Jun / Ait-Mohamed, Ouardia / Ait-Si-Ali, Slimane / Akematsu, Takahiko / Akira, Shizuo / Al-Younes, Hesham M / Al-Zeer, Munir A / Albert, Matthew L / Albin, Roger L /
    Alegre-Abarrategui, Javier / Aleo, Maria Francesca / Alirezaei, Mehrdad / Almasan, Alexandru / Almonte-Becerril, Maylin / Amano, Atsuo / Amaravadi, Ravi / Amarnath, Shoba / Amer, Amal O / Andrieu-Abadie, Nathalie / Anantharam, Vellareddy / Ann, David K / Anoopkumar-Dukie, Shailendra / Aoki, Hiroshi / Apostolova, Nadezda / Arancia, Giuseppe / Aris, John P / Asanuma, Katsuhiko / Asare, Nana Y O / Ashida, Hisashi / Askanas, Valerie / Askew, David S / Auberger, Patrick / Baba, Misuzu / Backues, Steven K / Baehrecke, Eric H / Bahr, Ben A / Bai, Xue-Yuan / Bailly, Yannick / Baiocchi, Robert / Baldini, Giulia / Balduini, Walter / Ballabio, Andrea / Bamber, Bruce A / Bampton, Edward T W / Bánhegyi, Gábor / Bartholomew, Clinton R / Bassham, Diane C / Bast, Robert C / Batoko, Henri / Bay, Boon-Huat / Beau, Isabelle / Béchet, Daniel M / Begley, Thomas J / Behl, Christian / Behrends, Christian / Bekri, Soumeya / Bellaire, Bryan / Bendall, Linda J / Benetti, Luca / Berliocchi, Laura / Bernardi, Henri / Bernassola, Francesca / Besteiro, Sébastien / Bhatia-Kissova, Ingrid / Bi, Xiaoning / Biard-Piechaczyk, Martine / Blum, Janice S / Boise, Lawrence H / Bonaldo, Paolo / Boone, David L / Bornhauser, Beat C / Bortoluci, Karina R / Bossis, Ioannis / Bost, Frédéric / Bourquin, Jean-Pierre / Boya, Patricia / Boyer-Guittaut, Michaël / Bozhkov, Peter V / Brady, Nathan R / Brancolini, Claudio / Brech, Andreas / Brenman, Jay E / Brennand, Ana / Bresnick, Emery H / Brest, Patrick / Bridges, Dave / Bristol, Molly L / Brookes, Paul S / Brown, Eric J / Brumell, John H / Brunetti-Pierri, Nicola / Brunk, Ulf T / Bulman, Dennis E / Bultman, Scott J / Bultynck, Geert / Burbulla, Lena F / Bursch, Wilfried / Butchar, Jonathan P / Buzgariu, Wanda / Bydlowski, Sergio P / Cadwell, Ken / Cahová, Monika / Cai, Dongsheng / Cai, Jiyang / Cai, Qian / Calabretta, Bruno / Calvo-Garrido, Javier / Camougrand, Nadine / Campanella, Michelangelo / Campos-Salinas, Jenny / Candi, Eleonora / Cao, Lizhi / Caplan, Allan B / Carding, Simon R / Cardoso, Sandra M / Carew, Jennifer S / Carlin, Cathleen R / Carmignac, Virginie / Carneiro, Leticia A M / Carra, Serena / Caruso, Rosario A / Casari, Giorgio / Casas, Caty / Castino, Roberta / Cebollero, Eduardo / Cecconi, Francesco / Celli, Jean / Chaachouay, Hassan / Chae, Han-Jung / Chai, Chee-Yin / Chan, David C / Chan, Edmond Y / Chang, Raymond Chuen-Chung / Che, Chi-Ming / Chen, Ching-Chow / Chen, Guang-Chao / Chen, Guo-Qiang / Chen, Min / Chen, Quan / Chen, Steve S-L / Chen, WenLi / Chen, Xi / Chen, Xiangmei / Chen, Xiequn / Chen, Ye-Guang / Chen, Yingyu / Chen, Yongqiang / Chen, Yu-Jen / Chen, Zhixiang / Cheng, Alan / Cheng, Christopher H K / Cheng, Yan / Cheong, Heesun / Cheong, Jae-Ho / Cherry, Sara / Chess-Williams, Russ / Cheung, Zelda H / Chevet, Eric / Chiang, Hui-Ling / Chiarelli, Roberto / Chiba, Tomoki / Chin, Lih-Shen / Chiou, Shih-Hwa / Chisari, Francis V / Cho, Chi Hin / Cho, Dong-Hyung / Choi, Augustine M K / Choi, DooSeok / Choi, Kyeong Sook / Choi, Mary E / Chouaib, Salem / Choubey, Divaker / Choubey, Vinay / Chu, Charleen T / Chuang, Tsung-Hsien / Chueh, Sheau-Huei / Chun, Taehoon / Chwae, Yong-Joon / Chye, Mee-Len / Ciarcia, Roberto / Ciriolo, Maria R / Clague, Michael J / Clark, Robert S B / Clarke, Peter G H / Clarke, Robert / Codogno, Patrice / Coller, Hilary A / Colombo, María I / Comincini, Sergio / Condello, Maria / Condorelli, Fabrizio / Cookson, Mark R / Coombs, Graham H / Coppens, Isabelle / Corbalan, Ramon / Cossart, Pascale / Costelli, Paola / Costes, Safia / Coto-Montes, Ana / Couve, Eduardo / Coxon, Fraser P / Cregg, James M / Crespo, José L / Cronjé, Marianne J / Cuervo, Ana Maria / Cullen, Joseph J / Czaja, Mark J / D'Amelio, Marcello / Darfeuille-Michaud, Arlette / Davids, Lester M / Davies, Faith E / De Felici, Massimo / de Groot, John F / de Haan, Cornelis A M / De Martino, Luisa / De Milito, Angelo / De Tata, Vincenzo / Debnath, Jayanta / Degterev, Alexei / Dehay, Benjamin / Delbridge, Lea M D / Demarchi, Francesca / Deng, Yi Zhen / Dengjel, Jörn / Dent, Paul / Denton, Donna / Deretic, Vojo / Desai, Shyamal D / Devenish, Rodney J / Di Gioacchino, Mario / Di Paolo, Gilbert / Di Pietro, Chiara / Díaz-Araya, Guillermo / Díaz-Laviada, Inés / Diaz-Meco, Maria T / Diaz-Nido, Javier / Dikic, Ivan / Dinesh-Kumar, Savithramma P / Ding, Wen-Xing / Distelhorst, Clark W / Diwan, Abhinav / Djavaheri-Mergny, Mojgan / Dokudovskaya, Svetlana / Dong, Zheng / Dorsey, Frank C / Dosenko, Victor / Dowling, James J / Doxsey, Stephen / Dreux, Marlène / Drew, Mark E / Duan, Qiuhong / Duchosal, Michel A / Duff, Karen / Dugail, Isabelle / Durbeej, Madeleine / Duszenko, Michael / Edelstein, Charles L / Edinger, Aimee L / Egea, Gustavo / Eichinger, Ludwig / Eissa, N Tony / Ekmekcioglu, Suhendan / El-Deiry, Wafik S / Elazar, Zvulun / Elgendy, Mohamed / Ellerby, Lisa M / Eng, Kai Er / Engelbrecht, Anna-Mart / Engelender, Simone / Erenpreisa, Jekaterina / Escalante, Ricardo / Esclatine, Audrey / Eskelinen, Eeva-Liisa / Espert, Lucile / Espina, Virginia / Fan, Huizhou / Fan, Jia / Fan, Qi-Wen / Fan, Zhen / Fang, Shengyun / Fang, Yongqi / Fanto, Manolis / Fanzani, Alessandro / Farkas, Thomas / Farré, Jean-Claude / Faure, Mathias / Fechheimer, Marcus / Feng, Carl G / Feng, Jian / Feng, Qili / Feng, Youji / Fésüs, László / Feuer, Ralph / Figueiredo-Pereira, Maria E / Fimia, Gian Maria / Fingar, Diane C / Finkbeiner, Steven / Finkel, Toren / Finley, Kim D / Fiorito, Filomena / Fisher, Edward A / Fisher, Paul B / Flajolet, Marc / Florez-McClure, Maria L / Florio, Salvatore / Fon, Edward A / Fornai, Francesco / Fortunato, Franco / Fotedar, Rati / Fowler, Daniel H / Fox, Howard S / Franco, Rodrigo / Frankel, Lisa B / Fransen, Marc / Fuentes, José M / Fueyo, Juan / Fujii, Jun / Fujisaki, Kozo / Fujita, Eriko / Fukuda, Mitsunori / Furukawa, Ruth H / Gaestel, Matthias / Gailly, Philippe / Gajewska, Malgorzata / Galliot, Brigitte / Galy, Vincent / Ganesh, Subramaniam / Ganetzky, Barry / Ganley, Ian G / Gao, Fen-Biao / Gao, George F / Gao, Jinming / Garcia, Lorena / Garcia-Manero, Guillermo / Garcia-Marcos, Mikel / Garmyn, Marjan / Gartel, Andrei L / Gatti, Evelina / Gautel, Mathias / Gawriluk, Thomas R / Gegg, Matthew E / Geng, Jiefei / Germain, Marc / Gestwicki, Jason E / Gewirtz, David A / Ghavami, Saeid / Ghosh, Pradipta / Giammarioli, Anna M / Giatromanolaki, Alexandra N / Gibson, Spencer B / Gilkerson, Robert W / Ginger, Michael L / Ginsberg, Henry N / Golab, Jakub / Goligorsky, Michael S / Golstein, Pierre / Gomez-Manzano, Candelaria / Goncu, Ebru / Gongora, Céline / Gonzalez, Claudio D / Gonzalez, Ramon / González-Estévez, Cristina / González-Polo, Rosa Ana / Gonzalez-Rey, Elena / Gorbunov, Nikolai V / Gorski, Sharon / Goruppi, Sandro / Gottlieb, Roberta A / Gozuacik, Devrim / Granato, Giovanna Elvira / Grant, Gary D / Green, Kim N / Gregorc, Aleš / Gros, Frédéric / Grose, Charles / Grunt, Thomas W / Gual, Philippe / Guan, Jun-Lin / Guan, Kun-Liang / Guichard, Sylvie M / Gukovskaya, Anna S / Gukovsky, Ilya / Gunst, Jan / Gustafsson, Asa B / Halayko, Andrew J / Hale, Amber N / Halonen, Sandra K / Hamasaki, Maho / Han, Feng / Han, Ting / Hancock, Michael K / Hansen, Malene / Harada, Hisashi / Harada, Masaru / Hardt, Stefan E / Harper, J Wade / Harris, Adrian L / Harris, James / Harris, Steven D / Hashimoto, Makoto / Haspel, Jeffrey A / Hayashi, Shin-ichiro / Hazelhurst, Lori A / He, Congcong / He, You-Wen / Hébert, Marie-Joseé / Heidenreich, Kim A / Helfrich, Miep H / Helgason, Gudmundur V / Henske, Elizabeth P / Herman, Brian / Herman, Paul K / Hetz, Claudio / Hilfiker, Sabine / Hill, Joseph A / Hocking, Lynne J / Hofman, Paul / Hofmann, Thomas G / Höhfeld, Jörg / Holyoake, Tessa L / Hong, Ming-Huang / Hood, David A / Hotamisligil, Gökhan S / Houwerzijl, Ewout J / Høyer-Hansen, Maria / Hu, Bingren / Hu, Chien-An A / Hu, Hong-Ming / Hua, Ya / Huang, Canhua / Huang, Ju / Huang, Shengbing / Huang, Wei-Pang / Huber, Tobias B / Huh, Won-Ki / Hung, Tai-Ho / Hupp, Ted R / Hur, Gang Min / Hurley, James B / Hussain, Sabah N A / Hussey, Patrick J / Hwang, Jung Jin / Hwang, Seungmin / Ichihara, Atsuhiro / Ilkhanizadeh, Shirin / Inoki, Ken / Into, Takeshi / Iovane, Valentina / Iovanna, Juan L / Ip, Nancy Y / Isaka, Yoshitaka / Ishida, Hiroyuki / Isidoro, Ciro / Isobe, Ken-ichi / Iwasaki, Akiko / Izquierdo, Marta / Izumi, Yotaro / Jaakkola, Panu M / Jäättelä, Marja / Jackson, George R / Jackson, William T / Janji, Bassam / Jendrach, Marina / Jeon, Ju-Hong / Jeung, Eui-Bae / Jiang, Hong / Jiang, Hongchi / Jiang, Jean X / Jiang, Ming / Jiang, Qing / Jiang, Xuejun / Jiménez, Alberto / Jin, Meiyan / Jin, Shengkan / Joe, Cheol O / Johansen, Terje / Johnson, Daniel E / Johnson, Gail V W / Jones, Nicola L / Joseph, Bertrand / Joseph, Suresh K / Joubert, Annie M / Juhász, Gábor / Juillerat-Jeanneret, Lucienne / Jung, Chang Hwa / Jung, Yong-Keun / Kaarniranta, Kai / Kaasik, Allen / Kabuta, Tomohiro / Kadowaki, Motoni / Kagedal, Katarina / Kamada, Yoshiaki / Kaminskyy, Vitaliy O / Kampinga, Harm H / Kanamori, Hiromitsu / Kang, Chanhee / Kang, Khong Bee / Kang, Kwang Il / Kang, Rui / Kang, Yoon-A / Kanki, Tomotake / Kanneganti, Thirumala-Devi / Kanno, Haruo / Kanthasamy, Anumantha G / Kanthasamy, Arthi / Karantza, Vassiliki / Kaushal, Gur P / Kaushik, Susmita / Kawazoe, Yoshinori / Ke, Po-Yuan / Kehrl, John H / Kelekar, Ameeta / Kerkhoff, Claus / Kessel, David H / Khalil, Hany / Kiel, Jan A K W / Kiger, Amy A / Kihara, Akio / Kim, Deok Ryong / Kim, Do-Hyung / Kim, Dong-Hou / Kim, Eun-Kyoung / Kim, Hyung-Ryong / Kim, Jae-Sung / Kim, Jeong Hun / Kim, Jin Cheon / Kim, John K / Kim, Peter K / Kim, Seong Who / Kim, Yong-Sun / Kim, Yonghyun / Kimchi, Adi / Kimmelman, Alec C / King, Jason S / Kinsella, Timothy J / Kirkin, Vladimir / Kirshenbaum, Lorrie A / Kitamoto, Katsuhiko / Kitazato, Kaio / Klein, Ludger / Klimecki, Walter T / Klucken, Jochen / Knecht, Erwin / Ko, Ben C B / Koch, Jan C / Koga, Hiroshi / Koh, Jae-Young / Koh, Young Ho / Koike, Masato / Komatsu, Masaaki / Kominami, Eiki / Kong, Hee Jeong / Kong, Wei-Jia / Korolchuk, Viktor I / Kotake, Yaichiro / Koukourakis, Michael I / Kouri Flores, Juan B / Kovács, Attila L / Kraft, Claudine / Krainc, Dimitri / Krämer, Helmut / Kretz-Remy, Carole / Krichevsky, Anna M / Kroemer, Guido / Krüger, Rejko / Krut, Oleg / Ktistakis, Nicholas T / Kuan, Chia-Yi / Kucharczyk, Roza / Kumar, Ashok / Kumar, Raj / Kumar, Sharad / Kundu, Mondira / Kung, Hsing-Jien / Kurz, Tino / Kwon, Ho Jeong / La Spada, Albert R / Lafont, Frank / Lamark, Trond / Landry, Jacques / Lane, Jon D / Lapaquette, Pierre / Laporte, Jocelyn F / László, Lajos / Lavandero, Sergio / Lavoie, Josée N / Layfield, Robert / Lazo, Pedro A / Le, Weidong / Le Cam, Laurent / Ledbetter, Daniel J / Lee, Alvin J X / Lee, Byung-Wan / Lee, Gyun Min / Lee, Jongdae / Lee, Ju-Hyun / Lee, Michael / Lee, Myung-Shik / Lee, Sug Hyung / Leeuwenburgh, Christiaan / Legembre, Patrick / Legouis, Renaud / Lehmann, Michael / Lei, Huan-Yao / Lei, Qun-Ying / Leib, David A / Leiro, José / Lemasters, John J / Lemoine, Antoinette / Lesniak, Maciej S / Lev, Dina / Levenson, Victor V / Levine, Beth / Levy, Efrat / Li, Faqiang / Li, Jun-Lin / Li, Lian / Li, Sheng / Li, Weijie / Li, Xue-Jun / Li, Yan-bo / Li, Yi-Ping / Liang, Chengyu / Liang, Qiangrong / Liao, Yung-Feng / Liberski, Pawel P / Lieberman, Andrew / Lim, Hyunjung J / Lim, Kah-Leong / Lim, Kyu / Lin, Chiou-Feng / Lin, Fu-Cheng / Lin, Jian / Lin, Jiandie D / Lin, Kui / Lin, Wan-Wan / Lin, Weei-Chin / Lin, Yi-Ling / Linden, Rafael / Lingor, Paul / Lippincott-Schwartz, Jennifer / Lisanti, Michael P / Liton, Paloma B / Liu, Bo / Liu, Chun-Feng / Liu, Kaiyu / Liu, Leyuan / Liu, Qiong A / Liu, Wei / Liu, Young-Chau / Liu, Yule / Lockshin, Richard A / Lok, Chun-Nam / Lonial, Sagar / Loos, Benjamin / Lopez-Berestein, Gabriel / López-Otín, Carlos / Lossi, Laura / Lotze, Michael T / Lőw, Peter / Lu, Binfeng / Lu, Bingwei / Lu, Bo / Lu, Zhen / Luciano, Frédéric / Lukacs, Nicholas W / Lund, Anders H / Lynch-Day, Melinda A / Ma, Yong / Macian, Fernando / MacKeigan, Jeff P / Macleod, Kay F / Madeo, Frank / Maiuri, Luigi / Maiuri, Maria Chiara / Malagoli, Davide / Malicdan, May Christine V / Malorni, Walter / Man, Na / Mandelkow, Eva-Maria / Manon, Stéphen / Manov, Irena / Mao, Kai / Mao, Xiang / Mao, Zixu / Marambaud, Philippe / Marazziti, Daniela / Marcel, Yves L / Marchbank, Katie / Marchetti, Piero / Marciniak, Stefan J / Marcondes, Mateus / Mardi, Mohsen / Marfe, Gabriella / Mariño, Guillermo / Markaki, Maria / Marten, Mark R / Martin, Seamus J / Martinand-Mari, Camille / Martinet, Wim / Martinez-Vicente, Marta / Masini, Matilde / Matarrese, Paola / Matsuo, Saburo / Matteoni, Raffaele / Mayer, Andreas / Mazure, Nathalie M / McConkey, David J / McConnell, Melanie J / McDermott, Catherine / McDonald, Christine / McInerney, Gerald M / McKenna, Sharon L / McLaughlin, BethAnn / McLean, Pamela J / McMaster, Christopher R / McQuibban, G Angus / Meijer, Alfred J / Meisler, Miriam H / Meléndez, Alicia / Melia, Thomas J / Melino, Gerry / Mena, Maria A / Menendez, Javier A / Menna-Barreto, Rubem F S / Menon, Manoj B / Menzies, Fiona M / Mercer, Carol A / Merighi, Adalberto / Merry, Diane E / Meschini, Stefania / Meyer, Christian G / Meyer, Thomas F / Miao, Chao-Yu / Miao, Jun-Ying / Michels, Paul A M / Michiels, Carine / Mijaljica, Dalibor / Milojkovic, Ana / Minucci, Saverio / Miracco, Clelia / Miranti, Cindy K / Mitroulis, Ioannis / Miyazawa, Keisuke / Mizushima, Noboru / Mograbi, Baharia / Mohseni, Simin / Molero, Xavier / Mollereau, Bertrand / Mollinedo, Faustino / Momoi, Takashi / Monastyrska, Iryna / Monick, Martha M / Monteiro, Mervyn J / Moore, Michael N / Mora, Rodrigo / Moreau, Kevin / Moreira, Paula I / Moriyasu, Yuji / Moscat, Jorge / Mostowy, Serge / Mottram, Jeremy C / Motyl, Tomasz / Moussa, Charbel E-H / Müller, Sylke / Muller, Sylviane / Münger, Karl / Münz, Christian / Murphy, Leon O / Murphy, Maureen E / Musarò, Antonio / Mysorekar, Indira / Nagata, Eiichiro / Nagata, Kazuhiro / Nahimana, Aimable / Nair, Usha / Nakagawa, Toshiyuki / Nakahira, Kiichi / Nakano, Hiroyasu / Nakatogawa, Hitoshi / Nanjundan, Meera / Naqvi, Naweed I / Narendra, Derek P / Narita, Masashi / Navarro, Miguel / Nawrocki, Steffan T / Nazarko, Taras Y / Nemchenko, Andriy / Netea, Mihai G / Neufeld, Thomas P / Ney, Paul A / Nezis, Ioannis P / Nguyen, Huu Phuc / Nie, Daotai / Nishino, Ichizo / Nislow, Corey / Nixon, Ralph A / Noda, Takeshi / Noegel, Angelika A / Nogalska, Anna / Noguchi, Satoru / Notterpek, Lucia / Novak, Ivana / Nozaki, Tomoyoshi / Nukina, Nobuyuki / Nürnberger, Thorsten / Nyfeler, Beat / Obara, Keisuke / Oberley, Terry D / Oddo, Salvatore / Ogawa, Michinaga / Ohashi, Toya / Okamoto, Koji / Oleinick, Nancy L / Oliver, F Javier / Olsen, Laura J / Olsson, Stefan / Opota, Onya / Osborne, Timothy F / Ostrander, Gary K / Otsu, Kinya / Ou, Jing-hsiung James / Ouimet, Mireille / Overholtzer, Michael / Ozpolat, Bulent / Paganetti, Paolo / Pagnini, Ugo / Pallet, Nicolas / Palmer, Glen E / Palumbo, Camilla / Pan, Tianhong / Panaretakis, Theocharis / Pandey, Udai Bhan / Papackova, Zuzana / Papassideri, Issidora / Paris, Irmgard / Park, Junsoo / Park, Ohkmae K / Parys, Jan B / Parzych, Katherine R / Patschan, Susann / Patterson, Cam / Pattingre, Sophie / Pawelek, John M / Peng, Jianxin / Perlmutter, David H / Perrotta, Ida / Perry, George / Pervaiz, Shazib / Peter, Matthias / Peters, Godefridus J / Petersen, Morten / Petrovski, Goran / Phang, James M / Piacentini, Mauro / Pierre, Philippe / Pierrefite-Carle, Valérie / Pierron, Gérard / Pinkas-Kramarski, Ronit / Piras, Antonio / Piri, Natik / Platanias, Leonidas C / Pöggeler, Stefanie / Poirot, Marc / Poletti, Angelo / Poüs, Christian / Pozuelo-Rubio, Mercedes / Prætorius-Ibba, Mette / Prasad, Anil / Prescott, Mark / Priault, Muriel / Produit-Zengaffinen, Nathalie / Progulske-Fox, Ann / Proikas-Cezanne, Tassula / Przedborski, Serge / Przyklenk, Karin / Puertollano, Rosa / Puyal, Julien / Qian, Shu-Bing / Qin, Liang / Qin, Zheng-Hong / Quaggin, Susan E / Raben, Nina / Rabinowich, Hannah / Rabkin, Simon W / Rahman, Irfan / Rami, Abdelhaq / Ramm, Georg / Randall, Glenn / Randow, Felix / Rao, V Ashutosh / Rathmell, Jeffrey C / Ravikumar, Brinda / Ray, Swapan K / Reed, Bruce H / Reed, John C / Reggiori, Fulvio / Régnier-Vigouroux, Anne / Reichert, Andreas S / Reiners, John J / Reiter, Russel J / Ren, Jun / Revuelta, José L / Rhodes, Christopher J / Ritis, Konstantinos / Rizzo, Elizete / Robbins, Jeffrey / Roberge, Michel / Roca, Hernan / Roccheri, Maria C / Rocchi, Stephane / Rodemann, H Peter / Rodríguez de Córdoba, Santiago / Rohrer, Bärbel / Roninson, Igor B / Rosen, Kirill / Rost-Roszkowska, Magdalena M / Rouis, Mustapha / Rouschop, Kasper M A / Rovetta, Francesca / Rubin, Brian P / Rubinsztein, David C / Ruckdeschel, Klaus / Rucker, Edmund B / Rudich, Assaf / Rudolf, Emil / Ruiz-Opazo, Nelson / Russo, Rossella / Rusten, Tor Erik / Ryan, Kevin M / Ryter, Stefan W / Sabatini, David M / Sadoshima, Junichi / Saha, Tapas / Saitoh, Tatsuya / Sakagami, Hiroshi / Sakai, Yasuyoshi / Salekdeh, Ghasem Hoseini / Salomoni, Paolo / Salvaterra, Paul M / Salvesen, Guy / Salvioli, Rosa / Sanchez, Anthony M J / Sánchez-Alcázar, José A / Sánchez-Prieto, Ricardo / Sandri, Marco / Sankar, Uma / Sansanwal, Poonam / Santambrogio, Laura / Saran, Shweta / Sarkar, Sovan / Sarwal, Minnie / Sasakawa, Chihiro / Sasnauskiene, Ausra / Sass, Miklós / Sato, Ken / Sato, Miyuki / Schapira, Anthony H V / Scharl, Michael / Schätzl, Hermann M / Scheper, Wiep / Schiaffino, Stefano / Schneider, Claudio / Schneider, Marion E / Schneider-Stock, Regine / Schoenlein, Patricia V / Schorderet, Daniel F / Schüller, Christoph / Schwartz, Gary K / Scorrano, Luca / Sealy, Linda / Seglen, Per O / Segura-Aguilar, Juan / Seiliez, Iban / Seleverstov, Oleksandr / Sell, Christian / Seo, Jong Bok / Separovic, Duska / Setaluri, Vijayasaradhi / Setoguchi, Takao / Settembre, Carmine / Shacka, John J / Shanmugam, Mala / Shapiro, Irving M / Shaulian, Eitan / Shaw, Reuben J / Shelhamer, James H / Shen, Han-Ming / Shen, Wei-Chiang / Sheng, Zu-Hang / Shi, Yang / Shibuya, Kenichi / Shidoji, Yoshihiro / Shieh, Jeng-Jer / Shih, Chwen-Ming / Shimada, Yohta / Shimizu, Shigeomi / Shintani, Takahiro / Shirihai, Orian S / Shore, Gordon C / Sibirny, Andriy A / Sidhu, Stan B / Sikorska, Beata / Silva-Zacarin, Elaine C M / Simmons, Alison / Simon, Anna Katharina / Simon, Hans-Uwe / Simone, Cristiano / Simonsen, Anne / Sinclair, David A / Singh, Rajat / Sinha, Debasish / Sinicrope, Frank A / Sirko, Agnieszka / Siu, Parco M / Sivridis, Efthimios / Skop, Vojtech / Skulachev, Vladimir P / Slack, Ruth S / Smaili, Soraya S / Smith, Duncan R / Soengas, Maria S / Soldati, Thierry / Song, Xueqin / Sood, Anil K / Soong, Tuck Wah / Sotgia, Federica / Spector, Stephen A / Spies, Claudia D / Springer, Wolfdieter / Srinivasula, Srinivasa M / Stefanis, Leonidas / Steffan, Joan S / Stendel, Ruediger / Stenmark, Harald / Stephanou, Anastasis / Stern, Stephan T / Sternberg, Cinthya / Stork, Björn / Strålfors, Peter / Subauste, Carlos S / Sui, Xinbing / Sulzer, David / Sun, Jiaren / Sun, Shi-Yong / Sun, Zhi-Jun / Sung, Joseph J Y / Suzuki, Kuninori / Suzuki, Toshihiko / Swanson, Michele S / Swanton, Charles / Sweeney, Sean T / Sy, Lai-King / Szabadkai, Gyorgy / Tabas, Ira / Taegtmeyer, Heinrich / Tafani, Marco / Takács-Vellai, Krisztina / Takano, Yoshitaka / Takegawa, Kaoru / Takemura, Genzou / Takeshita, Fumihiko / Talbot, Nicholas J / Tan, Kevin S W / Tanaka, Keiji / Tanaka, Kozo / Tang, Daolin / Tang, Dingzhong / Tanida, Isei / Tannous, Bakhos A / Tavernarakis, Nektarios / Taylor, Graham S / Taylor, Gregory A / Taylor, J Paul / Terada, Lance S / Terman, Alexei / Tettamanti, Gianluca / Thevissen, Karin / Thompson, Craig B / Thorburn, Andrew / Thumm, Michael / Tian, FengFeng / Tian, Yuan / Tocchini-Valentini, Glauco / Tolkovsky, Aviva M / Tomino, Yasuhiko / Tönges, Lars / Tooze, Sharon A / Tournier, Cathy / Tower, John / Towns, Roberto / Trajkovic, Vladimir / Travassos, Leonardo H / Tsai, Ting-Fen / Tschan, Mario P / Tsubata, Takeshi / Tsung, Allan / Turk, Boris / Turner, Lorianne S / Tyagi, Suresh C / Uchiyama, Yasuo / Ueno, Takashi / Umekawa, Midori / Umemiya-Shirafuji, Rika / Unni, Vivek K / Vaccaro, Maria I / Valente, Enza Maria / Van den Berghe, Greet / van der Klei, Ida J / van Doorn, Wouter / van Dyk, Linda F / van Egmond, Marjolein / van Grunsven, Leo A / Vandenabeele, Peter / Vandenberghe, Wim P / Vanhorebeek, Ilse / Vaquero, Eva C / Velasco, Guillermo / Vellai, Tibor / Vicencio, Jose Miguel / Vierstra, Richard D / Vila, Miquel / Vindis, Cécile / Viola, Giampietro / Viscomi, Maria Teresa / Voitsekhovskaja, Olga V / von Haefen, Clarissa / Votruba, Marcela / Wada, Keiji / Wade-Martins, Richard / Walker, Cheryl L / Walsh, Craig M / Walter, Jochen / Wan, Xiang-Bo / Wang, Aimin / Wang, Chenguang / Wang, Dawei / Wang, Fan / Wang, Fen / Wang, Guanghui / Wang, Haichao / Wang, Hong-Gang / Wang, Horng-Dar / Wang, Jin / Wang, Ke / Wang, Mei / Wang, Richard C / Wang, Xinglong / Wang, Xuejun / Wang, Ying-Jan / Wang, Yipeng / Wang, Zhen / Wang, Zhigang Charles / Wang, Zhinong / Wansink, Derick G / Ward, Diane M / Watada, Hirotaka / Waters, Sarah L / Webster, Paul / Wei, Lixin / Weihl, Conrad C / Weiss, William A / Welford, Scott M / Wen, Long-Ping / Whitehouse, Caroline A / Whitton, J Lindsay / Whitworth, Alexander J / Wileman, Tom / Wiley, John W / Wilkinson, Simon / Willbold, Dieter / Williams, Roger L / Williamson, Peter R / Wouters, Bradly G / Wu, Chenghan / Wu, Dao-Cheng / Wu, William K K / Wyttenbach, Andreas / Xavier, Ramnik J / Xi, Zhijun / Xia, Pu / Xiao, Gengfu / Xie, Zhiping / Xie, Zhonglin / Xu, Da-zhi / Xu, Jianzhen / Xu, Liang / Xu, Xiaolei / Yamamoto, Ai / Yamamoto, Akitsugu / Yamashina, Shunhei / Yamashita, Michiaki / Yan, Xianghua / Yanagida, Mitsuhiro / Yang, Dun-Sheng / Yang, 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    Autophagy

    2012  Volume 8, Issue 4, Page(s) 445–544

    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 ... ...

    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.
    MeSH term(s) Animals ; Autophagy/genetics ; Biological Assay/methods ; Humans ; Models, Biological
    Keywords covid19
    Language English
    Publishing date 2012-09-19
    Publishing country United States
    Document type Guideline ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.19496
    Database MEDical Literature Analysis and Retrieval System OnLINE

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