Author: "Shen, Han-Ming" - Searchworks@Jio Institute Digital Library Search Results

881 results on '"Shen, Han-Ming"'

101. Tailorable Membrane‐Penetrating Nanoplatform for Highly Efficient Organelle‐Specific Localization

Author: Zhang, Xin, Wang, Chunfei, Feng, Gang, Jiang, Jianxia, Hu, Jiwen, du Rietz, Anna, Brommesson, Caroline, Zhang, Xuanjun, Ma, Yuguang, Roberg, Karin, Zhang, Fengling, Shen, Han-Ming, Uvdal, Kajsa, Hu, Zhang-Jun, Zhang, Xin, Wang, Chunfei, Feng, Gang, Jiang, Jianxia, Hu, Jiwen, du Rietz, Anna, Brommesson, Caroline, Zhang, Xuanjun, Ma, Yuguang, Roberg, Karin, Zhang, Fengling, Shen, Han-Ming, Uvdal, Kajsa, and Hu, Zhang-Jun
Abstract: Given the breadth of currently arising opportunities and concerns associated with nanoparticles for biomedical imaging, various types of nanoparticles have been widely exploited, especially for cellular/subcellular level probing. However, most currently reported nanoparticles either have inefficient delivery into cells or lack speciﬁcity for intracellular destinations. The absence of well-deﬁnednanoplatforms remains a critical challenge hindering practical nano-based imaging. Herein, the authors elaborate on a tailorable membrane-penetrating nanoplatform as a carrier with encapsulated actives and decorated surfaces to tackle the above-mentioned issues. The tunable contents in such a versatile nanoplatform oer huge ﬂexibility to reach the expected properties and functions. Aggregation-induced emission luminogen (AIEgen) is applied to achieve sought-after photophysical properties, speciﬁc targeting moieties are installed to give high affinity towards different desired organelles, and critical grafting of cell-penetrating cyclic disulﬁdes (CPCDs) to promote cellular uptake efficiency without sacriﬁcing the speciﬁcity. Hereafter, to validate its practicability, the tailored nano products are successfully applied to track the dynamic correlation between mitochondria and lysosomes during autophagy. The authors believe that the strategy and described materials can facilitate the development of functional nanomaterials for various life science applications
Published: 2021
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102. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Author: Klionsky, D, Abdel-Aziz, A, Abdelfatah, S, Abdellatif, M, Abdoli, A, Abel, S, Abeliovich, H, Abildgaard, M, Abudu, Y, Acevedo-Arozena, A, Adamopoulos, I, Adeli, K, Adolph, T, Adornetto, A, Aflaki, E, Agam, G, Agarwal, A, Aggarwal, B, Agnello, M, Agostinis, P, Agrewala, J, Agrotis, A, Aguilar, P, Ahmad, S, Ahmed, Z, Ahumada-Castro, U, Aits, S, Aizawa, S, Akkoc, Y, Akoumianaki, T, Akpinar, H, Al-Abd, A, Al-Akra, L, Al-Gharaibeh, A, Alaoui-Jamali, M, Alberti, S, Alcocer-Gómez, E, Alessandri, C, Ali, M, Alim Al-Bari, M, Aliwaini, S, Alizadeh, J, Almacellas, E, Almasan, A, Alonso, A, Alonso, G, Altan-Bonnet, N, Altieri, D, Álvarez, É, Alves, S, Alves da Costa, C, Alzaharna, M, Amadio, M, Amantini, C, Amaral, C, Ambrosio, S, Amer, A, Ammanathan, V, An, Z, Andersen, S, Andrabi, S, Andrade-Silva, M, Andres, A, Angelini, S, Ann, D, Anozie, U, Ansari, M, Antas, P, Antebi, A, Antón, Z, Anwar, T, Apetoh, L, Apostolova, N, Araki, T, Araki, Y, Arasaki, K, Araújo, W, Araya, J, Arden, C, Arévalo, M, Arguelles, S, Arias, E, Arikkath, J, Arimoto, H, Ariosa, A, Armstrong-James, D, Arnauné-Pelloquin, L, Aroca, A, Arroyo, D, Arsov, I, Artero, R, Asaro, D, Aschner, M, Ashrafizadeh, M, Ashur-Fabian, O, Atanasov, A, Au, A, Auberger, P, Auner, H, Aurelian, L, Autelli, R, Avagliano, L, Ávalos, Y, Aveic, S, Aveleira, C, Avin-Wittenberg, T, Aydin, Y, Ayton, S, Ayyadevara, S, Azzopardi, M, Baba, M, Backer, J, Backues, S, Bae, D, Bae, O, Bae, S, Baehrecke, E, Baek, A, Baek, S, Bagetta, G, Bagniewska-Zadworna, A, Bai, H, Bai, J, Bai, X, Bai, Y, Bairagi, N, Baksi, S, Balbi, T, Baldari, C, Balduini, W, Ballabio, A, Ballester, M, Balazadeh, S, Balzan, R, Bandopadhyay, R, Banerjee, S, Bánréti, Á, Bao, Y, Baptista, M, Baracca, A, Barbati, C, Bargiela, A, Barilà, D, Barlow, P, Barmada, S, Barreiro, E, Barreto, G, Bartek, J, Bartel, B, Bartolome, A, Barve, G, Basagoudanavar, S, Bassham, D, Bast, R, Basu, A, Batoko, H, Batten, I, Baulieu, E, Baumgarner, B, Bayry, J, Beale, R, Beau, I, Beaumatin, F, Bechara, L, Beck, G, Beers, M, Begun, J, Behrends, C, Behrens, G, Bei, R, Bejarano, E, Bel, S, Behl, C, Belaid, A, Belgareh-Touzé, N, Bellarosa, C, Belleudi, F, Belló Pérez, M, Bello-Morales, R, Beltran, J, Beltran, S, Benbrook, D, Bendorius, M, Benitez, B, Benito-Cuesta, I, Bensalem, J, Berchtold, M, Berezowska, S, Bergamaschi, D, Bergami, M, Bergmann, A, Berliocchi, L, Berlioz-Torrent, C, Bernard, A, Berthoux, L, Besirli, C, Besteiro, S, Betin, V, Beyaert, R, Bezbradica, J, Bhaskar, K, Bhatia-Kissova, I, Bhattacharya, R, Bhattacharya, S, Bhattacharyya, S, Bhuiyan, M, Bhutia, S, Bi, L, Bi, X, Biden, T, Bijian, K, Billes, V, Binart, N, Bincoletto, C, Birgisdottir, A, Bjorkoy, G, Blanco, G, Blas-Garcia, A, Blasiak, J, Blomgran, R, Blomgren, K, Blum, J, Boada-Romero, E, Boban, M, Boesze-Battaglia, K, Boeuf, P, Boland, B, Bomont, P, Bonaldo, P, Bonam, S, Bonfili, L, Bonifacino, J, Boone, B, Bootman, M, Bordi, M, Borner, C, Bornhauser, B, Borthakur, G, Bosch, J, Bose, S, Botana, L, Botas, J, Boulanger, C, Boulton, M, Bourdenx, M, Bourgeois, B, Bourke, N, Bousquet, G, Boya, P, Bozhkov, P, Bozi, L, Bozkurt, T, Brackney, D, Brandts, C, Braun, R, Braus, G, Bravo-Sagua, R, Bravo-San Pedro, J, Brest, P, Bringer, M, Briones-Herrera, A, Broaddus, V, Brodersen, P, Brodsky, J, Brody, S, Bronson, P, Bronstein, J, Brown, C, Brown, R, Brum, P, Brumell, J, Brunetti-Pierri, N, Bruno, D, Bryson-Richardson, R, Bucci, C, Buchrieser, C, Bueno, M, Buitrago-Molina, L, Buraschi, S, Buch, S, Buchan, J, Buckingham, E, Budak, H, Budini, M, Bultynck, G, Burada, F, Burgoyne, J, Burón, M, Bustos, V, Büttner, S, Butturini, E, Byrd, A, Cabas, I, Cabrera-Benitez, S, Cadwell, K, Cai, J, Cai, L, Cai, Q, Cairó, M, Calbet, J, Caldwell, G, Caldwell, K, Call, J, Calvani, R, Calvo, A, Calvo-Rubio Barrera, M, Camara, N, Camonis, J, Camougrand, N, Campanella, M, Campbell, E, Campbell-Valois, F, Campello, S, Campesi, I, Campos, J, Camuzard, O, Cancino, J, Candido de Almeida, D, Canesi, L, Caniggia, I, Canonico, B, Cantí, C, Cao, B, Caraglia, M, Caramés, B, Carchman, E, Cardenal-Muñoz, E, Cardenas, C, Cardenas, L, Cardoso, S, Carew, J, Carle, G, Carleton, G, Carloni, S, Carmona-Gutierrez, D, Carneiro, L, Carnevali, O, Carosi, J, Carra, S, Carrier, A, Carrier, L, Carroll, B, Carter, A, Carvalho, A, Casanova, M, Casas, C, Casas, J, Cassioli, C, Castillo, E, Castillo, K, Castillo-Lluva, S, Castoldi, F, Castori, M, Castro, A, Castro-Caldas, M, Castro-Hernandez, J, Castro-Obregon, S, Catz, S, Cavadas, C, Cavaliere, F, Cavallini, G, Cavinato, M, Cayuela, M, Cebollada Rica, P, Cecarini, V, Cecconi, F, Cechowska-Pasko, M, Cenci, S, Ceperuelo-Mallafré, V, Cerqueira, J, Cerutti, J, Cervia, D, Cetintas, V, Cetrullo, S, Chae, H, Chagin, A, Chai, C, Chakrabarti, G, Chakrabarti, O, Chakraborty, T, Chami, M, Chamilos, G, Chan, D, Chan, E, Chan, H, Chan, M, Chan, Y, Chandra, P, Chang, C, Chang, H, Chang, K, Chao, J, Chapman, T, Charlet-Berguerand, N, Chatterjee, S, Chaube, S, 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N, Cortese, K, Costa, M, Costantino, S, Costelli, P, Coto-Montes, A, Crack, P, Crespo, J, Criollo, A, Crippa, V, Cristofani, R, Csizmadia, T, Cuadrado, A, Cui, B, Cui, J, Cui, Y, Culetto, E, Cumino, A, Cybulsky, A, Czaja, M, Czuczwar, S, D'Adamo, S, D'Amelio, M, D'Arcangelo, D, D'Lugos, A, D'Orazi, G, da Silva, J, Dafsari, H, Dagda, R, Dagdas, Y, Daglia, M, Dai, X, Dai, Y, Dal Col, J, Dalhaimer, P, Dalla Valle, L, Dallenga, T, Dalmasso, G, Damme, M, Dando, I, Dantuma, N, Darling, A, Das, H, Dasarathy, S, Dasari, S, Dash, S, Daumke, O, Dauphinee, A, Davies, J, Dávila, V, Davis, R, Davis, T, Dayalan Naidu, S, De Amicis, F, De Bosscher, K, De Felice, F, De Franceschi, L, De Leonibus, C, de Mattos Barbosa, M, De Meyer, G, De Milito, A, De Nunzio, C, De Palma, C, De Santi, M, De Virgilio, C, De Zio, D, Debnath, J, Debosch, B, Decuypere, J, Deehan, M, Deflorian, G, Degregori, J, Dehay, B, Del Rio, G, Delaney, J, Delbridge, L, Delorme-Axford, E, Delpino, M, Demarchi, F, Dembitz, V, Demers, N, Deng, H, Deng, Z, Dengjel, J, Dent, P, Denton, D, Depamphilis, M, Der, C, Deretic, V, Descoteaux, A, Devis, L, Devkota, S, Devuyst, O, Dewson, G, Dharmasivam, M, Dhiman, R, di Bernardo, D, Di Cristina, M, Di Domenico, F, Di Fazio, P, Di Fonzo, A, Di Guardo, G, Di Guglielmo, G, Di Leo, L, Di Malta, C, Di Nardo, A, Di Rienzo, M, Di Sano, F, Diallinas, G, Diao, J, Diaz-Araya, G, Díaz-Laviada, I, Dickinson, J, Diederich, M, Dieudé, M, Dikic, I, Ding, S, Ding, W, Dini, L, Dinić, J, Dinic, M, Dinkova-Kostova, A, Dionne, M, Distler, J, Diwan, A, Dixon, I, Djavaheri-Mergny, M, Dobrinski, I, Dobrovinskaya, O, Dobrowolski, R, Dobson, R, Đokić, J, Dokmeci Emre, S, Donadelli, M, Dong, B, Dong, X, Dong, Z, Dorn Ii, G, Dotsch, V, Dou, H, Dou, J, Dowaidar, M, Dridi, S, Drucker, L, Du, A, Du, C, Du, G, Du, H, Du, L, du Toit, A, Duan, S, Duan, X, Duarte, S, Dubrovska, A, Dunlop, E, Dupont, N, Durán, R, Dwarakanath, B, Dyshlovoy, S, Ebrahimi-Fakhari, D, Eckhart, L, Edelstein, C, Efferth, T, Eftekharpour, E, Eichinger, L, Eid, N, Eisenberg, T, Eissa, N, Eissa, S, Ejarque, M, El Andaloussi, A, El-Hage, N, El-Naggar, S, Eleuteri, A, El-Shafey, E, Elgendy, M, Eliopoulos, A, Elizalde, M, Elks, P, Elsasser, H, Elsherbiny, E, Emerling, B, Emre, N, Eng, C, Engedal, N, Engelbrecht, A, Engelsen, A, Enserink, J, Escalante, R, Esclatine, A, Escobar-Henriques, M, Eskelinen, E, Espert, L, Eusebio, M, Fabrias, G, Fabrizi, C, Facchiano, A, Facchiano, F, Fadeel, B, Fader, C, Faesen, A, Fairlie, W, Falcó, A, Falkenburger, B, Fan, D, Fan, J, Fan, Y, Fang, E, Fang, Y, Fanto, M, Farfel-Becker, T, Faure, M, Fazeli, G, Fedele, A, Feldman, A, Feng, D, Feng, J, Feng, L, Feng, Y, Feng, W, Fenz Araujo, T, Ferguson, T, Fernández, Á, Fernandez-Checa, J, Fernández-Veledo, S, Fernie, A, Ferrante, A, Ferraresi, A, Ferrari, M, Ferreira, J, Ferro-Novick, S, Figueras, A, Filadi, R, Filigheddu, N, Filippi-Chiela, E, Filomeni, G, Fimia, G, Fineschi, V, Finetti, F, Finkbeiner, S, Fisher, E, Fisher, P, Flamigni, F, Fliesler, S, Flo, T, Florance, I, Florey, O, Florio, T, Fodor, E, Follo, C, Fon, E, Forlino, A, Fornai, F, Fortini, P, Fracassi, A, Fraldi, A, Franco, B, Franco, R, Franconi, F, Frankel, L, Friedman, S, Fröhlich, L, Frühbeck, G, Fuentes, J, Fujiki, Y, Fujita, N, Fujiwara, Y, Fukuda, M, Fulda, S, Furic, L, Furuya, N, Fusco, C, Gack, M, Gaffke, L, Galadari, S, Galasso, A, Galindo, M, Gallolu Kankanamalage, S, Galluzzi, L, Galy, V, Gammoh, N, Gan, B, Ganley, I, Gao, F, Gao, H, Gao, M, Gao, P, Gao, S, Gao, W, Gao, X, Garcera, A, Garcia, M, Garcia, V, García-Del Portillo, F, Garcia-Escudero, V, Garcia-Garcia, A, Garcia-Macia, M, García-Moreno, D, Garcia-Ruiz, C, García-Sanz, P, Garg, A, Gargini, R, Garofalo, T, Garry, R, Gassen, N, Gatica, D, Ge, L, Ge, W, Geiss-Friedlander, R, Gelfi, C, Genschik, P, Gentle, I, Gerbino, V, Gerhardt, C, Germain, K, Germain, M, Gewirtz, D, Ghasemipour Afshar, E, Ghavami, S, Ghigo, A, Ghosh, M, Giamas, G, Giampietri, C, Giatromanolaki, A, Gibson, G, Gibson, S, Ginet, V, Giniger, E, Giorgi, C, Girao, H, Girardin, S, Giridharan, M, Giuliano, S, Giulivi, C, Giuriato, S, Giustiniani, J, Gluschko, A, Goder, V, Goginashvili, A, Golab, J, Goldstone, D, Golebiewska, A, Gomes, L, Gomez, R, Gómez-Sánchez, R, Gomez-Puerto, M, Gomez-Sintes, R, Gong, Q, Goni, F, González-Gallego, J, Gonzalez-Hernandez, T, Gonzalez-Polo, R, Gonzalez-Reyes, J, González-Rodríguez, P, Goping, I, Gorbatyuk, M, Gorbunov, N, Görgülü, K, Gorojod, R, Gorski, S, Goruppi, S, Gotor, C, Gottlieb, R, Gozes, I, Gozuacik, D, Graef, M, Gräler, M, Granatiero, V, Grasso, D, Gray, J, Green, D, Greenhough, A, Gregory, S, Griffin, E, Grinstaff, M, Gros, F, Grose, C, Gross, A, Gruber, F, Grumati, P, Grune, T, Gu, X, Guan, J, Guardia, C, Guda, K, Guerra, F, Guerri, C, Guha, P, Guillén, C, Gujar, S, Gukovskaya, A, Gukovsky, I, Gunst, J, Günther, A, Guntur, A, Guo, C, Guo, H, Guo, L, Guo, M, Gupta, P, Gupta, S, Gupta, V, Gustafsson, A, Gutterman, D, H B, R, Haapasalo, A, Haber, J, Hać, A, Hadano, S, Hafrén, A, Haidar, M, Hall, B, Halldén, G, Hamacher-Brady, A, Hamann, A, Hamasaki, M, Han, W, Hansen, M, Hanson, P, Hao, Z, Harada, M, Harhaji-Trajkovic, L, Hariharan, N, Haroon, N, Harris, J, Hasegawa, T, Hasima Nagoor, N, Haspel, J, Haucke, V, Hawkins, W, Hay, B, Haynes, C, Hayrabedyan, S, Hays, T, He, C, He, Q, He, R, He, Y, Heakal, Y, Heberle, A, Hejtmancik, J, Helgason, G, Henkel, V, Herb, M, Hergovich, A, Herman-Antosiewicz, A, Hernández, A, Hernandez, C, Hernandez-Diaz, S, Hernandez-Gea, V, Herpin, A, Herreros, J, Hervás, J, Hesselson, D, Hetz, C, Heussler, V, Higuchi, Y, Hilfiker, S, Hill, J, Hlavacek, W, Ho, E, Ho, I, Ho, P, Ho, S, Ho, W, Hobbs, G, Hochstrasser, M, Hoet, P, Hofius, D, Hofman, P, Höhn, A, Holmberg, C, Hombrebueno, J, Yi-Ren Hong, C, Hooper, L, Hoppe, T, Horos, R, Hoshida, Y, Hsin, I, Hsu, H, Hu, B, Hu, D, Hu, L, Hu, M, Hu, R, Hu, W, Hu, Y, Hu, Z, Hua, F, Hua, J, Hua, Y, Huan, C, Huang, C, Huang, H, Huang, K, Huang, M, Huang, R, Huang, S, Huang, T, Huang, X, Huang, Y, Huber, T, Hubert, V, Hubner, C, Hughes, S, Hughes, W, Humbert, M, Hummer, G, Hurley, J, Hussain, S, Hussey, P, Hutabarat, M, Hwang, H, Hwang, S, Ieni, A, Ikeda, F, Imagawa, Y, Imai, Y, Imbriano, C, Imoto, M, Inman, D, Inoki, K, Iovanna, J, Iozzo, R, Ippolito, G, Irazoqui, J, Iribarren, P, Ishaq, M, Ishikawa, M, Ishimwe, N, Isidoro, C, Ismail, N, Issazadeh-Navikas, S, Itakura, E, Ito, D, Ivankovic, D, Ivanova, S, Iyer, A, Izquierdo, J, Izumi, M, Jäättelä, M, Jabir, M, Jackson, W, Jacobo-Herrera, N, Jacomin, A, Jacquin, E, Jadiya, P, Jaeschke, H, Jagannath, C, Jakobi, A, Jakobsson, J, Janji, B, Jansen-Dürr, P, Jansson, P, Jantsch, J, Januszewski, S, Jassey, A, Jean, S, Jeltsch-David, H, Jendelova, P, Jenny, A, Jensen, T, Jessen, N, Jewell, J, Ji, J, Jia, L, Jia, R, Jiang, L, Jiang, Q, Jiang, R, Jiang, T, Jiang, X, Jiang, Y, Jimenez-Sanchez, M, Jin, E, Jin, F, Jin, H, Jin, L, Jin, M, Jin, S, Jo, E, Joffre, C, Johansen, T, Johnson, G, Johnston, S, Jokitalo, E, Jolly, M, Joosten, L, Jordan, J, Joseph, B, Ju, D, Ju, J, Juárez, E, Judith, D, Juhász, G, Jun, Y, Jung, C, Jung, S, Jung, Y, Jungbluth, H, Jungverdorben, J, Just, S, Kaarniranta, K, Kaasik, A, Kabuta, T, Kaganovich, D, Kahana, A, Kain, R, Kajimura, S, Kalamvoki, M, Kalia, M, Kalinowski, D, Kaludercic, N, Kalvari, I, Kaminska, J, Kaminskyy, V, Kanamori, H, Kanasaki, K, Kang, C, Kang, R, Kang, S, Kaniyappan, S, Kanki, T, Kanneganti, T, Kanthasamy, A, Kantorow, M, Kapuy, O, Karamouzis, M, Karim, M, Karmakar, P, Katare, R, Kato, M, Kaufmann, S, Kauppinen, A, Kaushal, G, Kaushik, S, Kawasaki, K, Kazan, K, Ke, P, Keating, D, Keber, U, Kehrl, J, Keller, K, Keller, C, Kemper, J, Kenific, C, Kepp, O, Kermorgant, S, Kern, A, Ketteler, R, Keulers, T, Khalfin, B, Khalil, H, Khambu, B, Khan, S, Khandelwal, V, Khandia, R, Kho, W, Khobrekar, N, Khuansuwan, S, Khundadze, M, Killackey, S, Kim, D, Kim, E, Kim, H, Hyung-Ryong Kim, N, Kim, J, Kim, K, Kim, P, Kim, 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Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

103. Hepatitis B virus infection contributes to oxidative stress in a population exposed to aflatoxin B1 and high-risk for hepatocellular carcinoma

Author: Liu, Zhi-Ming, Li, Le-Qun, Peng, Min-Hao, Liu, Tang-Wei, Qin, Zhong, Guo, Ya, Xiao, Kai-Yin, Ye, Xin-Ping, Mo, Xin-Shao, Qin, Xue, Li, Shan, Yan, Lu-Nan, Shen, Han-Ming, Wang, LianWen, Wang, Qiao, Wang, Kai-bo, Liang, Ren-xiang, Wei, Zong-liang, Ong, Choon Nam, Santella, Regina M., and Peng, Tao
Published: 2008
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104. NFκB signaling in carcinogenesis and as a potential molecular target for cancer therapy

Author: Shen, Han-Ming and Tergaonkar, Vinay
Published: 2009
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105. Modulation of Atggenes expression in aged rat liver, brain, and kidney by caloric restriction analyzed via single-nucleus/cell RNA sequencing

Author: Yang, Chuanbin, Xia, Siyu, Zhang, Wei, Shen, Han-Ming, and Wang, Jigang
Abstract: ABSTRACTDysregulation of macroautophagy/autophagy has been closely implicated in aging. Caloric restriction (CR) is an effective intervention of aging partially via activation of autophagy. Recently, a high-throughput single-cell RNA-seq technique has been employed to detect the comprehensive transcriptomes of individual cells. However, the transcriptional networks of ATG(autophagy related) genes in the aging process and the modulation of ATGgenes expression by CR at the single-cell level have not been elucidated. Here, by performing data analysis of single nucleus/cells RNA sequencing in rats undergoing aging and the modulation by CR, we demonstrate that the transcription patterns of Atggenes in different cell types of rat liver, brain, and kidney are highly heterogeneous. Importantly, CR reversed aging-induced changes of multiple Atggenes across different cell types in the brain, liver, and kidney. In summary, our results, for the first time, provide comprehensive information on Atggene expression in specific cell types of different organs in a mammal during aging and give novel insight into the protective role of autophagy and CR in aging at the single-cell resolution.Abbreviations:ATGgenes: autophagy-related genes; Atg5: autophagy related 5; Atg7: autophagy related 7; CR: caloric restriction; DEATG: differentially expressed autophagy-related; NAFLD: nonalcoholic fatty liver disease; ScRNA-seq: single-cell RNA sequencing
Published: 2023
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106. Full-coverage regulations of autophagy by ROS: from induction to maturation.

Author: Zhou, Jing, Li, Xin-Yu, Liu, Yu-Jia, Feng, Ji, Wu, Yong, Shen, Han-Ming, and Lu, Guo-Dong
Subjects: RIBONUCLEOSIDE diphosphate reductase, MITOGEN-activated protein kinase phosphatases, DEATH receptors, TUBULINS, CATHEPSIN B, THIOREDOXIN-interacting protein, NF-kappa B, MITOGEN-activated protein kinases
Abstract: Macroautophagy/autophagy is an evolutionarily well-conserved recycling process in response to stress conditions, including a burst of reactive oxygen species (ROS) production. High level of ROS attack key cellular macromolecules. Protein cysteinyl thiols or non-protein thiols as the major redox-sensitive targets thus constitute the first-line defense. Autophagy is unique, because it removes not only oxidized/damaged proteins but also bulky ROS-generating organelles (such as mitochondria and peroxisome) to restrict further ROS production. The oxidative regulations of autophagy occur in all processes of autophagy, from induction, phagophore nucleation, phagophore expansion, autophagosome maturation, cargo delivery to the lysosome, and finally to degradation of the cargo and recycling of the products, as well as autophagy gene transcription. Mechanically, these regulations are achieved through direct or indirect manners. Direct thiol oxidation of key proteins such as ATG4, ATM and TFEB are responsible for specific regulations in phagophore expansion, cargo recognition and autophagy gene transcription, respectively. Meanwhile, oxidation of certain redox-sensitive chaperone-like proteins (e.g. PRDX family members and PARK7) may impair a nonspecifically local reducing environment in the phagophore membrane, and influence BECN1-involved phagophore nucleation and mitophagy recognition. However, ROS do exhibit some inhibitory effects on autophagy through direct oxidation of key autophagy regulators such as ATG3, ATG7 and SENP3 proteins. SQSTM1 provides an alternative antioxidant mechanism when autophagy is unavailable or impaired. However, it is yet to be unraveled how cells evolve to equip proteins with different redox susceptibility and in their correct subcellular positions, and how cells fine-tune autophagy machinery in response to different levels of ROS. Abbreviations: AKT1/PKB: AKT serine/threonine kinase 1; AMPK: AMP-activated protein kinase; ATG: autophagy related; ATM: ATM serine/threonine kinase; BAX: BCL2 associated X, apoptosis regulator; BECN1: beclin 1; BH3: BCL2-homology-3; CAV1: caveolin 1; CCCP: carbonyl cyanide m-chlorophenylhydrazone; CTSB: cathepsin B; CTSL: cathepsin L; DAPK: death associated protein kinase; ER: endoplasmic reticulum; ETC: electron transport chain; GSH: glutathione; GSTP1: glutathione S-transferase pi 1; H2O2: hydrogen peroxide; HK2: hexokinase 2; KEAP1: kelch like ECH associated protein 1; MAMs: mitochondria-associated ER membranes; MAP1LC3B/LC3: microtubule associated protein 1 light chain 3 beta; MAPK8/JNK1: mitogen-activated protein kinase 8; MAP3K5/ASK1: mitogen-activated protein kinase kinase kinase 5; MCOLN1: mucolipin 1; MMP: mitochondrial membrane potential; MTOR: mechanistic target of rapamycin kinase; NFE2L2/NRF2: nuclear factor, erythroid 2 like 2; NFKB1: nuclear factor kappa B subunit 1; NOX: NADPH oxidase; O2-: superoxide radical anion; p-Ub: phosphorylated Ub; PARK7/DJ-1: Parkinsonism associated deglycase; PE: phosphatidylethanolamine; PEX5: peroxisomal biogenesis factor 5; PINK1: PTEN induced kinase 1; PPP3CA/calcineurin: protein phosphatase 3 catalytic subunit beta; PRDX: peroxiredoxin; PRKAA1: protein kinase AMP-activated catalytic subunit alpha 1; PRKD/PKD: protein kinase D; PRKN/parkin: parkin RBR E3 ubiquitin protein ligase; PtdIns3K: class III phosphatidylinositol 3-kinase; PtdIns3P: phosphatidylinositol-3-phosphate; PTEN: phosphatase and tensin homolog; ROS: reactive oxygen species; SENP3: SUMO specific peptidase 3; SIRT1: sirtuin 1; SOD1: superoxide dismutase 1; SQSTM1/p62: sequestosome 1; SUMO: small ubiquitin like modifier; TFEB: transcription factor EB; TRAF6: TNF receptor associated factor 6; TSC2: TSC complex subunit 2; TXN: thioredoxin; TXNRD1: thioredoxin reductase 1; TXNIP: thioredoxin interacting protein; Ub: ubiquitin; ULK1: unc-51 like autophagy activating kinase 1. [ABSTRACT FROM AUTHOR]
Published: 2022
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107. Targeting mitophagy to promote apoptosis is a potential therapeutic strategy for cancer.

Author: Tang, Yancheng, Wang, Liming, Qin, Jiangjiang, Lu, Yingying, Shen, Han-Ming, and Chen, Hu-Biao
Subjects: ANTINEOPLASTIC agents, DRUG resistance in cancer cells, CELL death, DRUG resistance, NEURODEGENERATION, NATURAL products, QUALITY control, APOPTOSIS
Abstract: Many anticancer agents exert cytotoxicity and trigger apoptosis through the induction of mitochondrial dysfunction. Mitophagy, as a key mitochondrial quality control mechanism, can remove damaged mitochondria in an effective and timely manner, which may result in drug resistance. Although the implication of mitophagy in neurodegenerative diseases has been extensively studied, the role and mechanism of mitophagy in tumorigenesis and cancer therapy are largely unknown. In a recent study, we found that the inhibition of PINK1-PRKN-mediated mitophagy can significantly enhance the anticancer efficacy of magnolol, a natural product with potential anticancer properties. On the one hand, magnolol can induce severe mitochondrial dysfunction, including mitochondrial depolarization, excessive mitochondrial fragmentation and the generation of mitochondrial ROS, leading to apoptosis. On the other hand, magnolol induces PINK1-PRKN-dependent mitophagy via activation of two rounds of feedforward amplification loops. The blockage of mitophagy through genetic or pharmacological approaches promotes rather than attenuates magnolol-induced cell death. Furthermore, inhibition of mitophagy by using distinct inhibitors targeting different mitophagic stages effectively enhances magnolol's anticancer efficacy in vivo. Taken together, our findings strongly indicate that manipulation of mitophagy in cancer treatment will be a promising therapeutic strategy for overcoming cancer drug resistance and improving the therapeutic efficacy of anticancer agents. [ABSTRACT FROM AUTHOR]
Published: 2023
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108. Identification and characterization of major flavonoids and caffeoylquinic acids in three Compositae plants by LC/DAD-APCI/MS

Author: Lai, Jia-Ping, Lim, Yew Heng, Su, Jin, Shen, Han-Ming, and Ong, Choon Nam
Published: 2007
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109. IKK[beta] programs to turn on the GADD45[alpha]-MKK4-JNK apoptotic cascade specifically via p50 NF-[kappa]B in arsenite response

Author: Song, Lun, Li, Jingxia, Zhang, Dongyun, Liu, Zheng-gang, Ye, Jianping, Zhan, Qimin, Shen, Han-Ming, Whiteman, Matt, and Huang, Chuanshu
Subjects: Apoptosis -- Research, Cancer cells -- Research, Protein research, Biological sciences
Abstract: Cross talk between NF-[kappa]B and c-Jun N-terminal kinases (JNKs) has been implicated in the cell life and death decision under various stresses. Functional suppression of JNK activation by NF-[kappa]B has recently been proposed as a key cellular survival mechanism and contributes to cancer cells escaping from apoptosis. We provide a novel scenario of the proapoptotic role of I[kappa]B kinase [beta] (IKK[beta])-NF-[kappa]B, which can act as the activator of the JNK pathway through the induction of GADD45[alpha] for triggering MKK4/JNK activation, in response to the stimulation of arsenite, a cancer therapeutic reagent. This effect of IKK[beta]NF-[kappa]B is dependent on p50 but not the p65/relA NF-[kappa]B subunit, which can increase the stability of GADD45[alpha] protein through suppressing its ubiquitination and proteasome-dependent degradation. IKK[beta]-NF-[kappa]B can therefore either activate or suppress the JNK cascade and consequently mediate pro- or antiapoptotic effects, depending on the manner of its induction. Furthermore, the NF-[kappa]B p50 subunit can exert a novel regulatory function on protein modification independent of the classical NF-[kappa]B transcriptional activity.
Published: 2006

110. Quercetin induces p53‐independent cancer cell death through lysosome activation by the transcription factor EB and Reactive Oxygen Species‐dependent ferroptosis

Author: Wang, Zi‐Xuan, primary, Ma, Jing, additional, Li, Xin‐Yu, additional, Wu, Yong, additional, Shi, Huan, additional, Chen, Yao, additional, Lu, Guang, additional, Shen, Han‐Ming, additional, Lu, Guo‐Dong, additional, and Zhou, Jing, additional
Published: 2021
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111. Hydroxychloroquine/Chloroquine as Therapeutics for COVID-19: Truth under the Mystery

Author: Chen, Yao, primary, Li, Mei-Xiu, additional, Lu, Guo-Dong, additional, Shen, Han-Ming, additional, and Zhou, Jing, additional
Published: 2021
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112. Photodynamic therapy accelerates skin wound healing through promoting re-epithelialization

Author: Yang, Zengjun, primary, Hu, Xiaohong, additional, Zhou, Lina, additional, He, Yaxiong, additional, Zhang, Xiaorong, additional, Yang, Jiacai, additional, Ju, Zhenyu, additional, Liou, Yih-Cherng, additional, Shen, Han-Ming, additional, Luo, Gaoxing, additional, Hamblin, Michael R, additional, He, Weifeng, additional, and Yin, Rui, additional
Published: 2021
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113. Mono-2-ethylhexyl phthalate drives progression of PINK1-parkin-mediated mitophagy via increasing mitochondrial ROS to exacerbate cytotoxicity

Author: Xu, Jian, primary, Wang, Liming, additional, Zhang, Lihuan, additional, Zheng, Fang, additional, Wang, Fang, additional, Leng, Jianhang, additional, Wang, Keyi, additional, Héroux, Paul, additional, Shen, Han-Ming, additional, Wu, Yihua, additional, and Xia, Dajing, additional
Published: 2021
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114. Luteolin sensitizes tumor necrosis factor-α-induced apoptosis in human tumor cells

Author: Shi, Ran-Xin, Ong, Choon-Nam, and Shen, Han-Ming
Published: 2004
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115. Autophagy Is a Cell Self-Protective Mechanism Against Arsenic-Induced Cell Transformation

Author: Zhang, Tao, Qi, Yuanlin, Liao, Mingjun, Xu, Mei, Bower, Kimberley A., Frank, Jacqueline A., Shen, Han-Ming, Luo, Jia, Shi, Xianglin, and Chen, Gang
Published: 2012
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116. JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species

Author: Shen, Han-Ming and Liu, Zheng-gang
Published: 2006
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117. Autophagy is a survival force via suppression of necrotic cell death

Author: Shen, Han-Ming and Codogno, Patrice
Published: 2012
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118. The Role of Autophagy in Liver Cancer: Crosstalk in Signaling Pathways and Potential Therapeutic Targets

Author: Cui, Jianzhou, primary, Shen, Han-Ming, additional, and Lim, Lina Hsiu Kim, additional
Published: 2020
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119. mTOR S-nitrosylation inhibits autophagy and lysosomal proteolysis

Author: Tan, Bryce W.Q., primary, Tan, Sijie, additional, Tan, Byorn W.L., additional, Navakkode, Sheeja, additional, Ng, Cheng Yang, additional, Yuan, Steven, additional, Liang, Mui Cheng, additional, Liu, Chao, additional, Yin, Shi, additional, Chai, Chou, additional, Chew, Katherine C.M., additional, Tai, Yee Kit, additional, Sajikumar, Sreedharan, additional, Lam, Yulin, additional, Liao, Ping, additional, Shen, Han-Ming, additional, Lim, Kah-Leong, additional, Wong, Esther, additional, and Soong, Tuck Wah, additional
Published: 2020
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120. Garciesculenxanthone B induces PINK1-Parkin-mediated mitophagy and prevents ischemia-reperfusion brain injury in mice

Author: Wu, Man, primary, Lu, Guang, additional, Lao, Yuan-zhi, additional, Zhang, Hong, additional, Zheng, Dan, additional, Zheng, Zhao-qing, additional, Yi, Juan, additional, Xiang, Qian, additional, Wang, Li-ming, additional, Tan, Hong-sheng, additional, Zhou, Hua, additional, Shen, Han-ming, additional, and Xu, Hong-xi, additional
Published: 2020
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121. Ticagrelor inhibits the NLRP3 inflammasome to protect against inflammatory disease independent of the P2Y12 signaling pathway

Author: Huang, Bo, primary, Qian, Yufeng, additional, Xie, Shujun, additional, Ye, Xianhua, additional, Chen, Hanwen, additional, Chen, Zhifeng, additional, Zhang, Lihuan, additional, Xu, Jinming, additional, Hu, Hu, additional, Ma, Shenglin, additional, Héroux, Paul, additional, Wang, Di, additional, Shen, Han-Ming, additional, Wu, Yihua, additional, and Xia, Dajing, additional
Published: 2020
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122. Dual role of oxidative stress-JNK activation in autophagy and apoptosis induced by nickel oxide nanoparticles in human cancer cells

Author: Cho, Yik-Lam, primary, Tan, Hayden Weng Siong, additional, Saquib, Quaiser, additional, Ren, Yi, additional, Ahmad, Javed, additional, Wahab, Rizwan, additional, He, Weifeng, additional, Bay, Boon-Huat, additional, and Shen, Han-Ming, additional
Published: 2020
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123. The Long and the Short of PTEN in the Regulation of Mitophagy

Author: Wang, Liming, primary, Lu, Guang, additional, and Shen, Han-Ming, additional
Published: 2020
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124. 3‐O‐acetylrubianol C (3AR‐C) induces RIPK1‐dependent programmed cell death by selective inhibition of IKKβ

Author: Kang, Kidong, primary, Quan, Khong Trong, additional, Byun, Hee Sun, additional, Lee, So‐Ra, additional, Piao, Xuezhe, additional, Ju, Eunjin, additional, Park, Kyeong Ah, additional, Sohn, Kyung‐Cheol, additional, Shen, Han‐Ming, additional, Na, MinKyun, additional, and Hur, Gang Min, additional
Published: 2020
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125. Bone marrow stromal cell‐derived growth inhibitor serves as a stress sensor to induce autophagy

Author: Zhang, Jianbin, primary, Wang, Liming, additional, Xu, Jian, additional, Tang, Yancheng, additional, Huang, Bo, additional, Chen, Zhifeng, additional, Zhang, Ting, additional, Shen, Han‐Ming, additional, Wu, Yihua, additional, and Xia, Dajing, additional
Published: 2020
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126. Post-translational Modifications of Key Machinery in the Control of Mitophagy

Author: Wang, Liming, primary, Qi, Hao, additional, Tang, Yancheng, additional, and Shen, Han-Ming, additional
Published: 2020
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127. Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19

Author: Yang, Naidi, primary and Shen, Han-Ming, additional
Published: 2020
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128. Autophagy and Tumor Database: ATdb, a novel database connecting autophagy and tumor

Author: Chen, Kelie, primary, Yang, Dexin, additional, Zhao, Fan, additional, Wang, Shengchao, additional, Ye, Yao, additional, Sun, Wenjie, additional, Lu, Haohua, additional, Ruan, Zhi, additional, Xu, Jinming, additional, Wang, Tianru, additional, Lu, Guang, additional, Wang, Liming, additional, Shi, Yu, additional, Zhang, Honghe, additional, Wu, Han, additional, Lu, Weiguo, additional, Shen, Han-Ming, additional, Xia, Dajing, additional, and Wu, Yihua, additional
Published: 2020
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129. Autophagic secretion of mitochondria (ASM): an alternative way for getting rid of damaged mitochondria.

Author: Tan, Hayden Weng Siong, Lu, Guang, and Shen, Han-Ming
Subjects: MITOCHONDRIA, SECRETION, QUALITY control, ISOPRENYLATION, EXTRACELLULAR vesicles
Abstract: PINK1-PRKN/Parkin-mediated mitophagy represents an important mitochondrial quality control (MQC) pathway that clears damaged/dysfunctional mitochondria. Although the conjugation of mammalian Atg8-family proteins (mATG8s) to phosphatidylethanolamine (PE) is a defining step in autophagy, its role in mitophagy remains unclear. In our recent study, we found that the mATG8 conjugation system is not required for PINK1-PRKN-mediated mitochondria clearance. Instead, mATG8 conjugation system-independent mitochondria clearance relies on secretory autophagy, a process we term as the autophagic secretion of mitochondria (ASM). As ASM results in the spurious activation of the CGAS-STING1 pathway, we propose that defects in mATG8 lipidation may promote inflammation through ASM. [ABSTRACT FROM AUTHOR]
Published: 2023
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130. A Novel Scoring System for Pivotal Autophagy-Related Genes Predicts Outcomes after Chemotherapy in Advanced Ovarian Cancer Patients

Author: Niu, Yuequn, primary, Sun, Wenjie, additional, Chen, Kelie, additional, Fu, Zhiqin, additional, Chen, Yaqing, additional, Zhu, Jianqing, additional, Chen, Hanwen, additional, Shi, Yu, additional, Zhang, Honghe, additional, Wang, Liming, additional, Shen, Han-Ming, additional, Xia, Dajing, additional, and Wu, Yihua, additional
Published: 2019
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131. Inhibition of the JAK-STAT3 pathway by andrographolide enhances chemosensitivity of cancer cells to doxorubicin

Author: Zhou, Jing, Ong, Choon-Nam, Hur, Gang-Min, and Shen, Han-Ming
Published: 2010
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132. Pharmacological and Chemopreventive Studies of Chrysanthemum

Author: Shen, Han-Ming, primary and Shi, Ranxin, additional
Published: 2004
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133. Critical role of Bid and Bax in indirubin-3′-monoxime-induced apoptosis in human cancer cells

Author: Shi, Jie and Shen, Han-Ming
Published: 2008
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134. Evaluation of oxidative stress in a group of adolescents exposed to a high level of aflatoxin B1—a multi-center and multi-biomarker study

Author: Peng, Tao, Li, Le-Qun, Peng, Min-Hao, Liu, Zhi-Ming, Liu, Tang-Wei, Guo, Ya, Xiao, Kai-Yin, Qin, Zhong, Ye, Xin-Ping, Mo, Xin-Shao, Yan, Lu-Nan, Lee, Bee-Lam, Shen, Han-Ming, Tamae, Kazuyoshi, Wang, Lian Wen, Wang, Qiao, Khan, Khalid M., Wang, Kai-Bo, Liang, Ren-Xiang, Wei, Zong-Liang, Kasai, Hiroshi, Ong, Choon Nam, and Santella, Regina M.
Published: 2007

135. Critical role of oxidative stress and sustained JNK activation in aloe-emodin-mediated apoptotic cell death in human hepatoma cells

Author: Lu, Guo Dong, Shen, Han-Ming, Chung, Maxey C.M., and Ong, Choon Nam
Published: 2007

136. Is correction for protein concentration appropriate for protein adduct dosimetry? Hypothesis and clues from an aflatoxin B1-exposed population

Author: Peng, Tao, Li, Le-Qun, Peng, Min-Hao, Liu, Zhi-Ming, Liu, Tang-Wei, Yan, Lu-Nan, Shen, Han-Ming, Wang, LianWen, Wang, Qiao, Wang, Kai-bo, Liang, Ren-xiang, Wei, Zong-liang, Ong, Choon Nam, and Santella, Regina M.
Published: 2007

137. Critical role of pro-apoptotic Bcl-2 family members in andrographolide-induced apoptosis in human cancer cells

Author: Zhou, Jing, Zhang, Siyuan, Choon-Nam, Ong, and Shen, Han-Ming
Published: 2006
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138. DETECTION OF OXIDATIVE DNA DAMAGE IN HUMAN SPERM AND ITS ASSOCIATION WITH SPERM FUNCTION AND MALE INFERTILITY

Author: SHEN, HAN-MING, primary and ONG, CHOON-NAM, additional
Published: 2001
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139. Parthenolide sensitizes ultraviolet (UV)-B-induced apoptosis via protein kinase C-dependent pathways

Author: Won, Yen-Kim, Ong, Choon-Nam, and Shen, Han-Ming
Published: 2005

140. Suppressed NF-κB and sustained JNK activation contribute to the sensitization effect of parthenolide to TNF-α-induced apoptosis in human cancer cells

Author: Zhang, Siyuan, Lin, Zhong-Ning, Yang, Cheng-Feng, Shi, Xianglin, Ong, Choon-Nam, and Shen, Han-Ming
Published: 2004

141. Chemopreventive activity of parthenolide against UVB-induced skin cancer and its mechanisms

Author: Won, Yen-Kim, Ong, Choon-Nam, Shi, Xianglin, and Shen, Han-Ming
Published: 2004

142. Inhibitory effect of emodin on tumor invasion through suppression of activator protein-1 and nuclear factor-κB

Author: Huang, Qing, Shen, Han-Ming, and Ong, Choon-Nam
Published: 2004
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143. Detection of apoptotic alterations in sperm in subfertile patients and their correlations with sperm quality

Author: Shen, Han-Ming, Dai, Jun, Chia, Sin-Eng, Lim, Alvin, and Ong, Choon-Nam
Published: 2002

144. Exposure to acrylonitrile induced DNA strand breakage and sex chromosome aneuploidy in human spermatozoa

Author: Xu, De-Xiang, Zhu, Qi-Xing, Zheng, Lu-Kang, Wang, Qu-Nan, Shen, Han-Ming, Deng, Li-Xia, and Ong, Choon-Nam
Published: 2003
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145. The associations among semen quality, oxidative DNA damage in human spermatozoa and concentrations of cadmium, lead and selenium in seminal plasma

Author: Xu, De-Xiang, Shen, Han-Ming, Zhu, Qi-Xing, Chua, Laiha, Wang, Qu-Nan, Chia, Sin-Eng, and Ong, Choon-Nam
Published: 2003
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146. Protective Effect of Ebselen on Aflatoxin B1-Induced Cytotoxicity in Primary Rat Hepatocytes

Author: Yang, Cheng-Feng, Liu, Jin, Shen, Han-Ming, and Ong, Choon-Nam
Published: 2000

147. Targeted metabolomics reveals differential biological effects of nanoplastics and nanoZnO in human lung cells

Author: Lim, Swee Ling, primary, Ng, Cheng Teng, additional, Zou, Li, additional, Lu, Yonghai, additional, Chen, Jiaqing, additional, Bay, Boon Huat, additional, Shen, Han-Ming, additional, and Ong, Choon Nam, additional
Published: 2019
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148. Critical role of AMPK in redox regulation under glucose starvation

Author: Ren, Yi, primary and Shen, Han-Ming, additional
Published: 2019
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149. Dysregulated autophagy in COPD: A pathogenic process to be deciphered

Author: Tan, W.S. Daniel, primary, Shen, Han-Ming, additional, and Wong, W.S. Fred, additional
Published: 2019
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150. Synthetic lethality targeting LKB1 mutant and EGFR wild type human non-small cell lung cancer cells by glucose starvation and SGLT2 inhibition

Author: Ren, Yi, primary, Chen, Jiaqing, additional, Mo, Xiaofan, additional, Yang, Qiqi, additional, Chen, Peishi, additional, Lu, Guang, additional, Tan, Hayden Weng-Siong, additional, Yi, Juan, additional, Yu, Qiang, additional, Kim, You-Sun, additional, Mallilankaraman, Karthik, additional, and Shen, Han-Ming, additional
Published: 2019
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