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Your search keyword '"Ting, J.P.-Y."' showing total 19 results
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19 results on '"Ting, J.P.-Y."'

1. Sting agonist mitigates experimental autoimmune encephalomyelitis by stimulating type i ifn-dependent and -independent immune-regulatory pathways

Author

Markovic-Plese, S., Gallovic, M.D., Williams, J., Johnson, B.M., Uchimura, T., Bachelder, E.M., Ainslie, K.M., Gibson, S.A., Thamilarasan, M., Deng, M., Ting, J.P.-Y., Batty, C.J., Tam, J.W., Matsushima, G.K., and Chou, W.-C.

Abstract

The cGAS-cyclic GMP-AMP (cGAMP)-stimulator of IFN genes (STING) pathway induces a powerful type I IFN (IFN-I) response and is a prime candidate for augmenting immunity in cancer immunotherapy and vaccines. IFN-I also has immuneregulatory functions manifested in several autoimmune diseases and is a first-line therapy for relapsing-remitting multiple sclerosis. However, it is only moderately effective and can induce adverse effects and neutralizing Abs in recipients. Targeting cGAMP in autoimmunity is unexplored and represents a challenge because of the intracellular location of its receptor, STING. We used microparticle (MP)-encapsulated cGAMP to increase cellular delivery, achieve dose sparing, and reduce potential toxicity. In the C57BL/6 experimental allergic encephalomyelitis (EAE) model, cGAMP encapsulated in MPs (cGAMP MPs) administered therapeutically protected mice from EAE in a STING-dependent fashion, whereas soluble cGAMP was ineffective. Protection was also observed in a relapsing-remitting model. Importantly, cGAMP MPs protected against EAE at the peak of disease and were more effective than rIFN-b. Mechanistically, cGAMP MPs showed both IFN-I-dependent and -independent immunosuppressive effects. Furthermore, it induced the immunosuppressive cytokine IL-27 without requiring IFN-I. This augmented IL-10 expression through activated ERK and CREB. IL-27 and subsequent IL-10 were the most important cytokines to mitigate autoreactivity. Critically, cGAMP MPs promoted IFN-I as well as the immunoregulatory cytokines IL-27 and IL-10 in PBMCs from relapsing-remitting multiple sclerosis patients. Collectively, this study reveals a previously unappreciated immune-regulatory effect of cGAMP that can be harnessed to restrain T cell autoreactivity.

Published
2021
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2. Pulmonary Delivery of Nanoparticle-Bound Toll-like Receptor 9 Agonist for the Treatment of Metastatic Lung Cancer

Author

Harrison, E.B., Perry, J.L., Cheng, N., Ting, J.P.-Y., Tian, S., Luft, J.C., Kapadia, C.H., Sengottuvel, N., Desimone, J.M., Gorentla, B.K., and Pecot, C.V.

Abstract

CpG oligodeoxynucleotides are potent toll-like receptor (TLR) 9 agonists and have shown promise as anticancer agents in preclinical studies and clinical trials. Binding of CpG to TLR9 initiates a cascade of innate and adaptive immune responses, beginning with activation of dendritic cells and resulting in a range of secondary effects that include the secretion of pro-inflammatory cytokines, activation of natural killer cells, and expansion of T cell populations. Recent literature suggests that local delivery of CpG in tumors results in superior antitumor effects as compared to systemic delivery. In this study, we utilized PRINT (particle replication in nonwetting templates) nanoparticles as a vehicle to deliver CpG into murine lungs through orotracheal instillations. In two murine orthotopic metastasis models of non-small-cell lung cancer-344SQ (lung adenocarcinoma) and KAL-LN2E1 (lung squamous carcinoma), local delivery of PRINT-CpG into the lungs effectively promoted substantial tumor regression and also limited systemic toxicities associated with soluble CpG. Furthermore, cured mice were completely resistant to tumor rechallenge. Additionally, nanodelivery showed extended retention of CpG within the lungs as well as prolonged elevation of antitumor cytokines in the lungs, but no elevated levels of proinflammatory cytokines in the serum. These results demonstrate that PRINT-CpG is a potent nanoplatform for local treatment of lung cancer that has collateral therapeutic effects on systemic disease and an encouraging toxicity profile and may have the potential to treat lung metastasis of other cancer types.

Published
2020
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3. Mitochondrial GSDMD Pores DAMPen Pyroptosis

Author

Ting, J.P.-Y. and Barnett, K.C.

Abstract

Noncanoncial inflammasome activation by cytosolic lipopolysaccharide (LPS) causes pyroptotic cell death facilitated by gasdermin D (GSDMD) pore formation. In this issue of Immunity, Huang et al. describe how cytosolic LPS in endothelial cells does not cause cell death but restrains endothelial cell proliferation. �� 2020 Elsevier Inc.Noncanoncial inflammasome activation by cytosolic lipopolysaccharide (LPS) causes pyroptotic cell death facilitated by gasdermin D (GSDMD) pore formation. In this issue of Immunity, Huang et al. describe how cytosolic LPS in endothelial cells does not cause cell death but restrains endothelial cell proliferation.

Published
2020
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4. TRAF3IP3 negatively regulates cytosolic RNA induced anti-viral signaling by promoting TBK1 K48 ubiquitination

Author

Davis, B.K., Tam, J.W., Conti, B.J., Liang, K., Wang, L., Zhang, Y., Ting, J.P.-Y., Sun, S., Li, S., Deng, M., Luo, X., Brickey, W.J., Guo, H., Ko, C.-C., Lei, Y.L., Zhang, L., and Petrucelli, A.

Abstract

Innate immunity to nucleic acids forms the backbone for anti-viral immunity and several inflammatory diseases. Upon sensing cytosolic viral RNA, retinoic acid-inducible gene-I-like receptors (RLRs) interact with the mitochondrial antiviral signaling protein (MAVS) and activate TANK-binding kinase 1 (TBK1) to induce type I interferon (IFN-I). TRAF3-interacting protein 3 (TRAF3IP3, T3JAM) is essential for T and B cell development. It is also well-expressed by myeloid cells, where its role is unknown. Here we report that TRAF3IP3 suppresses cytosolic poly(I:C), 5���ppp-dsRNA, and vesicular stomatitis virus (VSV) triggers IFN-I expression in overexpression systems and Traf3ip3���/��� primary myeloid cells. The mechanism of action is through the interaction of TRAF3IP3 with endogenous TRAF3 and TBK1. This leads to the degradative K48 ubiquitination of TBK1 via its K372 residue in a DTX4-dependent fashion. Mice with myeloid-specific gene deletion of Traf3ip3 have increased RNA virus-triggered IFN-I production and reduced susceptibility to virus. These results identify a function of TRAF3IP3 in the regulation of the host response to cytosolic viral RNA in myeloid cells.

Published
2020
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5. Platelet-activating factor (PAF) mediates NLRP3-NEK7 inflammasome induction independently of PAFR

Author

Deng, M., Golenbock, D.T., Beutler, B., Tam, J.W., Brickey, W.J., Johnson, B.M., New, J.S., Koller, B.H., McKinnon, K.P., Shi, H., Ting, J.P.-Y., Guo, H., and Lenox, A.

Subjects
lipids (amino acids, peptides, and proteins), respiratory system
Abstract

The role of lipids in inflammasome activation remains underappreciated. The phospholipid, platelet-activating factor (PAF), exerts multiple physiological functions by binding to a G protein-coupled seven-transmembrane receptor (PAFR). PAF is associated with a number of inflammatory disorders, yet the molecular mechanism underlying its proinflammatory function remains to be fully elucidated. We show that multiple PAF isoforms and PAF-like lipids can activate the inflammasome, resulting in IL-1�� and IL-18 maturation. This is dependent on NLRP3, ASC, caspase-1, and NEK7, but not on NLRC4, NLRP1, NLRP6, AIM2, caspase-11, or GSDMD. Inflammasome activation by PAF also requires potassium efflux and calcium influx but not lysosomal cathepsin or mitochondrial reactive oxygen species. PAF exacerbates peritonitis partly through inflammasome activation, but PAFR is dispensable for PAF-induced inflammasome activation in vivo or in vitro. These findings reveal that PAF represents a damage-associated signal that activates the canonical inflammasome independently of PAFR and provides an explanation for the ineffectiveness of PAFR antagonist in blocking PAF-mediated inflammation in the clinic.

Published
2019
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6. Viral DNA Binding to NLRC3, an Inhibitory Nucleic Acid Sensor, Unleashes STING, a Cyclic Dinucleotide Receptor that Activates Type I Interferon

Author

Zhang, L., Ting, J.P.-Y., Dokholyan, N.V., Petrucelli, A.S., Li, X., Zhang, S., Zhu, C., Li, P., Ariel, P., Tam, J.W., Zhao, B., Mo, J., Ke, H., Duncan, J.A., and Deng, M.

Abstract

Immune suppression is a crucial component of immunoregulation and a subgroup of nucleotide-binding domain (NBD), leucine-rich repeat (LRR)-containing proteins (NLRs) attenuate innate immunity. How this inhibitory function is controlled is unknown. A key question is whether microbial ligands can regulate this inhibition. NLRC3 is a negative regulator that attenuates type I interferon (IFN-I) response by sequestering and attenuating stimulator of interferon genes (STING) activation. Here, we report that NLRC3 binds viral DNA and other nucleic acids through its LRR domain. DNA binding to NLRC3 increases its ATPase activity, and ATP-binding by NLRC3 diminishes its interaction with STING, thus licensing an IFN-I response. This work uncovers a mechanism wherein viral nucleic acid binding releases an inhibitory innate receptor from its target.

Published
2019
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7. The NLRP3 inflammasome: molecular activation and regulation to therapeutics

Author

Swanson, K.V., Ting, J.P.-Y., and Deng, M.

Subjects
integumentary system
Abstract

NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) is an intracellular sensor that detects a broad range of microbial motifs, endogenous danger signals and environmental irritants, resulting in the formation and activation of the NLRP3 inflammasome. Assembly of the NLRP3 inflammasome leads to caspase 1-dependent release of the pro-inflammatory cytokines IL-1�� and IL-18, as well as to gasdermin D-mediated pyroptotic cell death. Recent studies have revealed new regulators of the NLRP3 inflammasome, including new interacting or regulatory proteins, metabolic pathways and a regulatory mitochondrial hub. In this Review, we present the molecular, cell biological and biochemical bases of NLRP3 activation and regulation and describe how this mechanistic understanding is leading to potential therapeutics that target the NLRP3 inflammasome.

Published
2019
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8. A nanoparticle-incorporated STING activator enhances antitumor immunity in PD-L1-insensitive models of triple-negative breast cancer

Author

Cheng, N., Ainslie, K.M., Bachelder, E.M., Miao, L., Watkins-Schulz, R., Huang, L., Darr, D.B., Liu, Q., Ting, J.P.-Y., McKinnon, K.P., David, C.N., Johnson, B.M., Peine, K.J., Yuan, H., Montgomery, S.A., and Junkins, R.D.

Abstract

Triple-negative breast cancer (TNBC) has few therapeutic options, and alternative approaches are urgently needed. Stimulator of IFN genes (STING) is becoming an exciting target for therapeutic adjuvants. However, STING resides inside the cell, and the intracellular delivery of CDNs, such as cGAMP, is required for the optimal activation of STING. We show that liposomal nanoparticle-delivered cGAMP (cGAMP-NP) activates STING more effectively than soluble cGAMP. These particles induce innate and adaptive host immune responses to preexisting tumors in both orthotopic and genetically engineered models of basal-like TNBC. cGAMP-NPs also reduce melanoma tumor load, with limited responsivity to anti-PD-L1. Within the tumor microenvironment, cGAMP-NPs direct both mouse and human macrophages (M), reprograming from protumorigenic M2-like phenotype toward M1-like phenotype; enhance MHC and costimulatory molecule expression; reduce M2 biomarkers; increase IFN-��-producing T cells; augment tumor apoptosis; and increase CD4+ and CD8+ T cell infiltration. Activated T cells are required for tumor suppression, as their depletion reduces antitumor activity. Importantly, cGAMP-NPs prevent the formation of secondary tumors, and a single dose is sufficient to inhibit TNBC. These data suggest that a minimal system comprised of cGAMP-NP alone is sufficient to modulate the tumor microenvironment to effectively control PD-L1-insensitive TNBC.

Published
2018
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9. A robust microparticle platform for a STING-targeted adjuvant that enhances both humoral and cellular immunity during vaccination

Author

Sempowski, G.D., Collier, M.A., Cheng, N., Gallovic, M.D., Shterev, I., Junkins, R.D., Ainslie, K.M., Johnson, B.M., Ting, J.P.-Y., McGee, C.E., Bachelder, E.M., David, C.N., Watkins-Schulz, R., and McKinnon, K.

Abstract

Most FDA-approved adjuvants for infectious agents boost humoral but not cellular immunity, and have poorly-understood mechanisms. Stimulator of interferon genes (STING, also known as MITA, MPYS, or ERIS) is an exciting adjuvant target due to its role in cyclic dinucleotide (CDN)-driven anti-viral immunity; however, a major hindrance is STING's cytosolic localization which requires intracellular delivery of its agonists. As a result, STING agonists administered in a soluble form have elicited suboptimal immune responses. Delivery of STING agonists via particle platforms has proven a more successful strategy, but the opportunity for improved formulations and bioactivity remains. In this study we evaluated the adjuvant activity of the potent STING agonist, CDN 3���3���-cGAMP (cGAMP), encapsulated in acid-sensitive acetalated dextran (Ace-DEX) polymeric microparticles (MPs) which passively target antigen-presenting cells for intracellular release. This formulation was superior to all particle delivery systems evaluated and maintained its bioactivity following a sterilizing dose of gamma irradiation. Compared to soluble cGAMP, the Ace-DEX cGAMP MPs enhanced type-I interferon responses nearly 1000-fold in vitro and 50-fold in vivo, caused up to a 104-fold boost in antibody titers, increased Th1-associated responses, and expanded germinal center B cells and memory T cells. Furthermore, the encapsulated cGAMP elicited no observable toxicity in animals and achieved protective immunity against a lethal influenza challenge seven months post-immunization when using CDN adjuvant doses up to 100-fold lower than previous reports. For these reasons, Ace-DEX MP-encapsulated cGAMP represents a potent vaccine adjuvant of humoral and cellular immunity.

Published
2018
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10. NLRX1 Facilitates Histoplasma capsulatum-Induced LC3-Associated Phagocytosis for Cytokine Production in Macrophages

Author

Liu, C.-Y., Huang, J.-H., Wu-Hsieh, B.A., Ting, J.P.-Y., Hsieh, S.-T., Chang, T.-H., Chen, W.-Y., Kan, H.-W., and Wu, S.-Y.

Subjects
digestive, oral, and skin physiology, equipment and supplies, human activities
Abstract

LC3-associated phagocytosis (LAP) is an emerging non-canonical autophagy process that bridges signaling from pattern-recognition receptors (PRRs) to autophagic machinery. LAP formation results in incorporation of lipidated LC3 into phagosomal membrane (termed LAPosome). Increasing evidence reveals that LAP functions as an innate defense mechanism against fungal pathogens. However, the molecular mechanism involved and the consequence of LAP in regulating anti-fungal immune response remain largely unexplored. Here we show that Histoplasma capsulatum is taken into LAPosome upon phagocytosis by macrophages. Interaction of H. capsulatum with Dectin-1 activates Syk and triggers subsequent NADPH oxidase-mediated reactive oxygen species (ROS) response that is involved in LAP induction. Inhibiting LAP induction by silencing LC3��/�� or treatment with ROS inhibitor impairs the activation of MAPKs-AP-1 pathway, thereby reduces macrophage proinflammatory cytokine response to H. capsulatum. Additionally, we unravel the importance of NLRX1 in fungus-induced LAP. NLRX1 facilitates LAP by interacting with TUFM which associates with autophagic proteins ATG5-ATG12 for LAPosome formation. Macrophages from Nlrx1-/- mice or TUFM-silenced cells exhibit reduced LAP induction and LAP-mediated MAPKs-AP-1 activation for cytokine response to H. capsulatum. Furthermore, inhibiting ROS production in Nlrx1-/- macrophages almost completely abolishes H. capsulatum-induced LC3 conversion, indicating that both Dectin-1/Syk/ROS-dependent pathway and NLRX1-TUFM complex-dependent pathway collaboratively contribute to LAP induction. Our findings reveal new pathways underlying LAP induction by H. capsulatum for macrophage cytokine response.

Published
2018
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11. Investigation of tunable acetalated dextran microparticle platform to optimize M2e-based influenza vaccine efficacy

Author

Chen, N., Gallovic, M.D., Ting, J.P.-Y., Ainslie, K.M., Bachelder, E.M., and Tiet, P.

Abstract

Influenza places a significant health and economic burden on society. Efficacy of seasonal influenza vaccines can be suboptimal due to poor matching between vaccine and circulating viral strains. An influenza vaccine that is broadly protective against multiple virus strains would significantly improve vaccine efficacy. The highly conserved ectodomain of matrix protein 2 (M2e) and 3���3��� cyclic GMP-AMP (cGAMP) were selected as the antigen and adjuvant, respectively, to develop the basis for a potential universal influenza vaccine. The magnitude and kinetics of adaptive immune responses can have great impact on vaccine efficacy. M2e and cGAMP were therefore formulated within acetalated dextran (Ace-DEX) microparticles (MPs) of varying degradation profiles to examine the effect of differential vaccine delivery on humoral, cellular, and protective immunity. All Ace-DEX MP vaccines containing M2e and cGAMP elicited potent humoral and cellular responses in vivo and offered substantial protection against a lethal influenza challenge, suggesting significant vaccine efficacy. Serum antibodies from Ace-DEX MP vaccinated mice also demonstrated cross reactivity against M2e sequences of various viral strains, which indicates the potential for broadly protective immunity. Of all the formulations tested, the slowest-degrading M2e or cGAMP MPs elicited the greatest antibody production, cellular response, and protection against a viral challenge. This indicated the importance of flexible control over antigen and adjuvant delivery. Overall, robust immune responses, cross reactivity against multiple viral strains, and tunable delivery profiles make the Ace-DEX MP platform a powerful subunit vaccine delivery system.

Published
2018
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12. Acetalated Dextran Microparticles for Codelivery of STING and TLR7/8 Agonists

Author

Johnson, B.M., Johnson, M.M., Ting, J.P.-Y., Gallovic, M.D., Collier, M.A., MacIntyre, A.N., Bachelder, E.M., Ainslie, K.M., Sempowski, G.D., and Junkins, R.D.

Abstract

Vaccines are the most effective tool for preventing infectious diseases; however, subunit vaccines, considered the safest type, suffer from poor immunogenicity and require adjuvants to create a strong and sustained immune response. As adjuvants, pathogen-associated molecular patterns (PAMPs) offer potent immunostimulatory properties and defined mechanisms of action through their cognate pattern recognition receptors (PRRs). Their activity can be further enhanced through combining two or more PAMPs, particularly those that activate multiple immune signaling pathways. However, the cytosolic localization of many PRRs requires intracellular delivery of PAMPs for optimal biological activity, which is particularly true of the stimulator of interferon genes (STING) PRR. Using acetalated dextran (Ace-DEX) microparticles (MPs) encapsulating STING agonist 3���3���-cyclic GMP-AMP (cGAMP) combined with soluble PAMPS, we screened the effect of codelivery of adjuvants using primary mouse bone marrow derived dendritic cells (BMDCs). We identified that codelivery of cGAMP MPs and soluble Toll-like receptor 7/8 (TLR7/8) agonist resiquimod (R848) elicited the broadest cytokine response. cGAMP and R848 were then coencapsulated within Ace-DEX MPs via electrospray. Using the model antigen ovalbumin, we observed that Ace-DEX MPs coencapsulating cGAMP and R848 (cGAMP/R848 Ace-DEX MPs) induced antigen-specific cellular immunity, and a balanced Th1/Th2 humoral response that was greater than cGAMP Ace-DEX MPs alone and PAMPs delivered in separate MPs. These data indicate that polymeric Ace-DEX MPs loaded with STING and TLR7/8 agonists represent a potent cellular and humoral vaccine adjuvant.

Published
2018
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13. A spike in inflammation

Author

Johnson, B.M., Junkins, R.D., and Ting, J.P.-Y.

Subjects
animal diseases
Abstract

The innate immune system is the first line of defence against invading microorganisms. Specialized immune cells, primarily myeloid cells, sense conserved pathogen-associated molecular patterns (PAMPs) through pattern recognition receptors (PRRs) to coordinate an immune response. One important class of PRRs is the nucleotide-binding domain and leucine-rich-repeat (NLR) proteins. In the presence of pathogens, NLR proteins trigger the formation of the inflammasome. This large macromolecular complex has caspase-1 activity, which stimulates production of the inflammatory cytokines interleukin (IL)-1�� and IL-18, leading to inflammation and inflammatory cell death (pyroptosis). Extensive work has characterized the biochemical cues that activate immunity through PRRs such as NLRs. However, in addition to conserved molecular patterns, pathogens also adopt conserved shapes and surface structures. For example, some bacteria have complex surface topographies created through nanofeatures such as flagella, pili and fimbriae. It has long been hypothesized that these physical cues are also sensed by the immune system through PRRs, but definitive experimental proof has remained elusive, partly because of the difficulties in separating the physical and biochemical immunological inputs produced by these natural structures.

Published
2018
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14. Inflammasomes in myeloid cells: Warriors within

Author

Brickey, W.J., Ting, J.P.-Y., and Jha, S.

Abstract

The inflammasome is a large multimeric protein complex comprising an effector protein that demonstrates specificity for a variety of activators or ligands; an adaptor molecule; and procaspase-1, which is converted to caspase-1 upon inflammasome activation. Inflammasomes are expressed primarily by myeloid cells and are located within the cell. The macromolecular inflammasome structure can be visualized by cryo-electron microscopy. This complex has been found to play a role in a variety of disease models in mice, and several have been genetically linked to human diseases. In most cases, the effector protein is a member of the NLR (nucleotide-binding domain leucine-rich repeat-containing) or NOD (nucleotide oligomerization domain)-like receptor protein family. However, other effectors have also been described, with the most notable being AIM-2 (absent in melanoma 2), which recognizes DNA to elicit inflammasome function. This review will focus on the role of the inflammasome in myeloid cells and its role in health and disease.

Published
2017
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15. 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. 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Published
2016

16. 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. 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. Hagedorn, M. Hahn, D.R. Halayko, A.J. Hamacher-Brady, A. Hamada, K. Hamai, A. Hamann, A. Hamasaki, M. Hamer, I. Hamid, Q. Hammond, E.M. Han, F. Han, W. Handa, J.T. Hanover, J.A. Hansen, M. Harada, M. Harhaji-Trajkovic, L. Harper, J.W. Harrath, A.H. Harris, A.L. Harris, J. Hasler, U. Hasselblatt, P. Hasui, K. Hawley, R.G. Hawley, T.S. He, C. He, C.Y. He, F. He, G. He, R.-R. He, X.-H. He, Y.-W. He, Y.-Y. Heath, J.K. Hébert, M.-J. Heinzen, R.A. Helgason, G.V. Hensel, M. Henske, E.P. Her, C. Herman, P.K. Hernández, A. Hernandez, C. Hernández-Tiedra, S. Hetz, C. Hiesinger, P.R. Higaki, K. Hilfiker, S. Hill, B.G. Hill, J.A. Hill, W.D. Hino, K. Hofius, D. Hofman, P. Höglinger, G.U. Höhfeld, J. Holz, M.K. Hong, Y. Hood, D.A. Hoozemans, J.J.M. Hoppe, T. Hsu, C. Hsu, C.-Y. Hsu, L.-C. Hu, D. Hu, G. Hu, H.-M. Hu, H. Hu, M.C. Hu, Y.-C. Hu, Z.-W. Hua, F. Hua, Y. Huang, C. Huang, H.-L. Huang, K.-H. Huang, K.-Y. Huang, S. Huang, S. Huang, W.-P. Huang, Y.-R. Huang, Y. Huang, Y. Huber, T.B. Huebbe, P. Huh, W.-K. Hulmi, J.J. Hur, G.M. Hurley, J.H. Husak, Z. Hussain, S.N.A. Hussain, S. Hwang, J.J. Hwang, S. Hwang, T.I.S. Ichihara, A. Imai, Y. Imbriano, C. Inomata, M. Into, T. Iovane, V. Iovanna, J.L. Iozzo, R.V. Ip, N.Y. Irazoqui, J.E. Iribarren, P. Isaka, Y. Isakovic, A.J. Ischiropoulos, H. Isenberg, J.S. Ishaq, M. Ishida, H. Ishii, I. Ishmael, J.E. Isidoro, C. Isobe, K.-I. Isono, E. Issazadeh-Navikas, S. Itahana, K. Itakura, E. Ivanov, A.I. Iyer, A.K.V. Izquierdo, J.M. Izumi, Y. Izzo, V. Jäättelä, M. Jaber, N. Jackson, D.J. Jackson, W.T. Jacob, T.G. Jacques, T.S. Jagannath, C. Jain, A. Jana, N.R. Jang, B.K. Jani, A. Janji, B. Jannig, P.R. Jansson, P.J. Jean, S. Jendrach, M. Jeon, J.-H. Jessen, N. Jeung, E.-B. Jia, K. Jia, L. Jiang, H. Jiang, H. Jiang, L. Jiang, T. Jiang, X. Jiang, X. Jiang, Y. Jiang, Y. Jiménez, A. Jin, C. Jin, H. Jin, L. Jin, M. Jin, S. Jinwal, U.K. Jo, E.-K. Johansen, T. Johnson, D.E. Johnson, G.V.W. Johnson, J.D. Jonasch, E. Jones, C. Joosten, L.A.B. Jordan, J. Joseph, A.-M. Joseph, B. Joubert, A.M. Ju, D. Ju, J. Juan, H.-F. Juenemann, K. Juhász, G. Jung, H.S. Jung, J.U. Jung, Y.-K. Jungbluth, H. Justice, M.J. Jutten, B. Kaakoush, N.O. Kaarniranta, K. Kaasik, A. Kabuta, T. Kaeffer, B. Kågedal, K. Kahana, A. Kajimura, S. Kakhlon, O. Kalia, M. Kalvakolanu, D.V. Kamada, Y. Kambas, K. Kaminskyy, V.O. Kampinga, H.H. Kandouz, M. Kang, C. Kang, R. Kang, T.-C. Kanki, T. Kanneganti, T.-D. Kanno, H. Kanthasamy, A.G. Kantorow, M. Kaparakis-Liaskos, M. Kapuy, O. Karantza, V. Karim, M.R. Karmakar, P. Kaser, A. Kaushik, S. Kawula, T. Kaynar, A.M. Ke, P.-Y. Ke, Z.-J. Kehrl, J.H. Keller, K.E. Kemper, J.K. Kenworthy, A.K. Kepp, O. Kern, A. Kesari, S. Kessel, D. Ketteler, R. Kettelhut, I.C. Khambu, B. Khan, M.M. Khandelwal, V.K.M. Khare, S. Kiang, J.G. Kiger, A.A. Kihara, A. Kim, A.L. Kim, C.H. Kim, D.R. Kim, D.-H. Kim, E.K. Kim, H.Y. Kim, H.-R. Kim, J.-S. Kim, J.H. Kim, J.C. Kim, J.H. Kim, K.W. Kim, M.D. Kim, M.-M. Kim, P.K. Kim, S.W. Kim, S.-Y. Kim, Y.-S. Kim, Y. Kimchi, A. Kimmelman, A.C. Kimura, T. King, J.S. Kirkegaard, K. Kirkin, V. Kirshenbaum, L.A. Kishi, S. Kitajima, Y. Kitamoto, K. Kitaoka, Y. Kitazato, K. Kley, R.A. Klimecki, W.T. Klinkenberg, M. Klucken, J. Knævelsrud, H. Knecht, E. Knuppertz, L. Ko, J.-L. Kobayashi, S. Koch, J.C. Koechlin-Ramonatxo, C. Koenig, U. Koh, Y.H. Köhler, K. Kohlwein, S.D. Koike, M. Komatsu, M. Kominami, E. Kong, D. Kong, H.J. Konstantakou, E.G. Kopp, B.T. Korcsmaros, T. Korhonen, L. Korolchuk, V.I. Koshkina, N.V. Kou, Y. Koukourakis, M.I. Koumenis, C. Kovács, A.L. Kovács, T. Kovacs, W.J. Koya, D. Kraft, C. Krainc, D. Kramer, H. Kravic-Stevovic, T. Krek, W. Kretz-Remy, C. Krick, R. Krishnamurthy, M. Kriston-Vizi, J. Kroemer, G. Kruer, M.C. Kruger, R. Ktistakis, N.T. Kuchitsu, K. Kuhn, C. Kumar, A.P. Kumar, A. Kumar, A. Kumar, D. Kumar, D. Kumar, R. Kumar, S. Kundu, M. Kung, H.-J. Kuno, A. Kuo, S.-H. Kuret, J. Kurz, T. Kwok, T. Kwon, T.K. Kwon, Y.T. Kyrmizi, I. La Spada, A.R. Lafont, F. Lahm, T. Lakkaraju, A. Lam, T. Lamark, T. Lancel, S. Landowski, T.H. Lane, D.J.R. Lane, J.D. Lanzi, C. Lapaquette, P. Lapierre, L.R. Laporte, J. Laukkarinen, J. Laurie, G.W. Lavandero, S. Lavie, L. Lavoie, M.J. Law, B.Y.K. Law, H.K.-W. Law, K.B. Layfield, R. Lazo, P.A. Le Cam, L. Le Roch, K.G. Le Stunff, H. Leardkamolkarn, V. Lecuit, M. Lee, B.-H. Lee, C.-H. Lee, E.F. Lee, G.M. Lee, H.-J. Lee, H. Lee, J.K. Lee, J. Lee, J.-H. Lee, J.H. Lee, M. Lee, M.-S. Lee, P.J. Lee, S.W. Lee, S.-J. Lee, S.-J. Lee, S.Y. Lee, S.H. Lee, S.S. Lee, S.-J. Lee, S. Lee, Y.-R. Lee, Y.J. Lee, Y.H. Leeuwenburgh, C. Lefort, S. Legouis, R. Lei, J. Lei, Q.-Y. Leib, D.A. Leibowitz, G. Lekli, I. Lemaire, S.D. Lemasters, J.J. Lemberg, M.K. Lemoine, A. Leng, S. Lenz, G. Lenzi, P. Lerman, L.O. Barbato, D.L. Leu, J.I.J. Leung, H.Y. Levine, B. Lewis, P.A. Lezoualch, F. Li, C. Li, F. Li, F.-J. Li, J. Li, K. Li, L. Li, M. Li, Q. Li, R. Li, S. Li, W. Li, X. Li, Y. Lian, J. Liang, C. Liang, Q. Liao, Y. Liberal, J. Liberski, P.P. Lie, P. Lieberman, A.P. Lim, H.J. Lim, K.-L. Lim, K. Lima, R.T. Lin, C.-S. Lin, C.-F. Lin, F. Lin, F. Lin, F.-C. Lin, K. Lin, K.-H. Lin, P.-H. Lin, T. Lin, W.-W. Lin, Y.-S. Lin, Y. Linden, R. Lindholm, D. Lindqvist, L.M. Lingor, P. Linkermann, A. Liotta, L.A. Lipinski, M.M. Lira, V.A. Lisanti, M.P. Liton, P.B. Liu, B. Liu, C. Liu, C.-F. Liu, F. Liu, H.-J. Liu, J. Liu, J.-J. Liu, J.-L. Liu, K. Liu, L. Liu, L. Liu, Q. Liu, R.-Y. Liu, S. Liu, S. Liu, W. Liu, X.-D. Liu, X. Liu, X.-H. Liu, X. Liu, X. Liu, X. Liu, Y. Liu, Y. Liu, Z. Liu, Z. Liuzzi, J.P. Lizard, G. Ljujic, M. Lodhi, I.J. Logue, S.E. Lokeshwar, B.L. Long, Y.C. Lonial, S. Loos, B. López-Otín, C. López-Vicario, C. Lorente, M. Lorenzi, P.L. Lõrincz, P. Los, M. Lotze, M.T. Lovat, P.E. Lu, B. Lu, B. Lu, J. Lu, Q. Lu, S.-M. Lu, S. Lu, Y. Luciano, F. Luckhart, S. Lucocq, J.M. Ludovico, P. Lugea, A. Lukacs, N.W. Lum, J.J. Lund, A.H. Luo, H. Luo, J. Luo, S. Luparello, C. Lyons, T. Ma, J. Ma, Y. Ma, Y. Ma, Z. Machado, J. Machado-Santelli, G.M. Macian, F. 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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

17. The pathogenic role of the inflammasome in neurodegenerative diseases

Author

Ting, J.P.-Y. and Freeman, L.C.

Abstract

The inflammasome is a large macromolecular complex that contains multiple copies of a receptor or sensor of pathogen-derived or damage-derived molecular patterns, pro-caspase-1, and an adaptor called ASC (apoptotic speck containing protein with a CARD), which results in caspase-1 maturation. Caspase-1 then mediates the release of pro-inflammatory cytokines such as IL-1�� and IL-18. These cytokines play critical roles in mediating immune responses during inflammation and innate immunity. Broader studies of the inflammasome over the years have implicated their roles in the pathogenesis of a variety of inflammatory diseases. Recently, studies have shown that the inflammasome modulates neuroinflammatory cells and the initial stages of neuroinflammation. A secondary cascade of events associated with neuroinflammation (such as oxidative stress) has been shown to activate the inflammasome, making the inflammasome a promising therapeutic target in the modulation of neurodegenerative diseases. This review will focus on the pathogenic role that inflammasomes play in neurologic diseases such as Alzheimer's disease, traumatic brain injury, and multiple sclerosis.

Published
2016
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18. An NLRP3 Mutation Causes Arthropathy and Osteoporosis in Humanized Mice

Author

Bateman, T.A., Koller, B.H., Nguyen, M., Dye, R., Repenning, P.W., Livingston, E.W., Snouwaert, J.N., Kovarova, M., Brigman, B.E., Moy, S.S., and Ting, J.P.-Y.

Subjects
integumentary system
Abstract

The NLRP3 inflammasome plays a critical role in host defense by facilitating caspase I activation and maturation of IL-1�� and IL-18, whereas dysregulation of inflammasome activity results in autoinflammatory disease. Factors regulating human NLRP3 activity that contribute to the phenotypic heterogeneity of NLRP3-related diseases have largely been inferred from the study of Nlrp3 mutant mice. By generating a mouse line in which the NLRP3 locus is humanized by syntenic replacement, we show the functioning of the human NLRP3 proteins in vivo, demonstrating the ability of the human inflammasome to orchestrate immune reactions in response to innate stimuli. Humanized mice expressing disease-associated mutations develop normally but display acute sensitivity to endotoxin and develop progressive and debilitating arthritis characterized by granulocytic infiltrates, elevated cytokines, erosion of bones, and osteoporosis. This NLRP3-dependent arthritis model provides a platform for testing therapeutic reagents targeting the human inflammasome.

Published
2016
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19. Reining in uncontrolled inflammasome with PKA

Author

Ting, J.P.-Y. and Swanson, K.V.

Subjects
integumentary system
Abstract

During the course of infection, the detection of pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) by pattern-recognition receptors (PRRs) can lead to inflammasome formation, with subsequent activation of ccaspase-1, secretion of interleukin 1�� (IL-1��) and IL-18, and cell death via pyroptosis. However, this process must be tightly controlled, as uncontrolled inflammasome activation can lead to a plethora of disease outcomes. In this issue, Mortimer et al. describe how phosphorylation of the PRR NLRP3 by the kinase PKA, after inflammasome activation, attenuates the inflammasome to halt the inflammatory response3. Gain-of-function mutations in the gene encoding NLRP3 cause a family of related autoimmune disorders called ���CAPS��� (���cryopyrin-associated periodic syndrome���) that result in aberrant activation of the NLRP3 inflammasome with uncontrolled secretion of IL-1�� and IL-18. The authors also provide insight into why some of the NLRP3 mutations that induce CAPS drive unregulated activation of the inflammasome.

Published
2016
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