CLC number: Q291
On-line Access: 2019-08-05
Received: 2019-04-03
Revision Accepted: 2019-05-26
Crosschecked: 2019-07-09
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Xiu-Zhi Li, Xiang-Hua Yan. Sensors for the mTORC1 pathway regulated by amino acids[J]. Journal of Zhejiang University Science B,in press.Frontiers of Information Technology & Electronic Engineering,in press.https://doi.org/10.1631/jzus.B1900181 @article{title="Sensors for the mTORC1 pathway regulated by amino acids", %0 Journal Article TY - JOUR
参与受氨基酸调控的哺乳动物雷帕霉素靶蛋白复合物1信号通路的感受体的研究进展关键词组: Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article
Reference[1]Abu-Remaileh M, Wyant GA, Kim C, et al., 2017. Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes. Science, 358(6364):807-813. [2]Aylett CHS, Sauer E, Imseng S, et al., 2016. Architecture of human mTOR complex 1. Science, 351(6268):48-52. [3]Baba M, Hong SB, Sharma N, et al., 2006. Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling. Proc Natl Acad Sci USA, 103(42):15552-15557. [4]Bar-Peled L, Schweitzer LD, Zoncu R, et al., 2012. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell, 150(6):1196-1208. [5]Bar-Peled L, Chantranupong L, Cherniack AD, et al., 2013. A tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1. Science, 340(6136):1100-1106. [6]Bonfils G, Jaquenoud M, Bontron S, et al., 2012. Leucyl-tRNA synthetase controls TORC1 via the EGO complex. Mol Cell, 46(1):105-110. [7]Brown EJ, Albers MW, Shin TB, et al., 1994. A mammalian protein targeted by G1-arresting rapamycin-receptor complex. Nature, 369(6483):756-758. [8]Buckbinder L, Talbott R, Seizinger BR, et al., 1994. Gene regulation by temperature-sensitive p53 mutants: identification of p53 response genes. Proc Natl Acad Sci USA, 91(22):10640-10644. [9]Budanov AV, Karin M, 2008. p53 target genes Sestrin1 and Sestrin2 connect genotoxic stress and mTOR signaling. Cell, 134(3):451-460. [10]Budanov AV, Shoshani T, Faerman A, et al., 2002. Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability. Oncogene, 21(39):6017-6031. [11]Buerger C, DeVries B, Stambolic V, 2006. Localization of Rheb to the endomembrane is critical for its signaling function. Biochem Biophys Res Commun, 344(3):869-880. [12]Burnett PE, Barrow RK, Cohen NA, et al., 1998. RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1. Proc Natl Acad Sci USA, 95(4):1432-1437. [13]Carroll B, Maetzel D, Maddocks OD, et al., 2016. Control of TSC2-Rheb signaling axis by arginine regulates mTORC1 activity. eLife, 5:e11058. [14]Castellano BM, Thelen AM, Moldavski O, et al., 2017. Lysosomal cholesterol activates mTORC1 via an SLC38A9-Niemann-Pick C1 signaling complex. Science, 355(6331):1306-1311. [15]Chantranupong L, Wolfson RL, Orozco JM, et al., 2014. The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1. Cell Rep, 9(1):1-8. [16]Chantranupong L, Wolfson RL, Sabatini DM, 2015. Nutrient-sensing mechanisms across evolution. Cell, 161(1):67-83. [17]Chantranupong L, Scaria SM, Saxton RA, et al., 2016. The CASTOR proteins are arginine sensors for the mTORC1 pathway. Cell, 165(1):153-164. [18]Chen J, Ou YH, Yang YY, et al., 2018. KLHL22 activates amino-acid-dependent mTORC1 signalling to promote tumorigenesis and ageing. Nature, 557(7706):585-589. [19]Chen X, Ma JJ, Tan M, et al., 2011. Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase. Nucleic Acids Res, 39(1):235-247. [20]Chiu MI, Katz H, Berlin V, 1994. RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex. Proc Natl Acad Sci USA, 91(26):12574-12578. [21]de Araujo MEG, Naschberger A, Fürnrohr BG, et al., 2017. Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling. Science, 358(6361):377-381. [22]Demetriades C, Doumpas N, Teleman AA, 2014. Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell, 156(4):786-799. [23]Deng L, Jiang C, Chen L, et al., 2015. The ubiquitination of RagA GTPase by RNF152 negatively regulates mTORC1 activation. Mol Cell, 58(5):804-818. [24]Dibble CC, Elis W, Menon S, et al., 2012. TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1. Mol Cell, 47(4):535-546. [25]Durán RV, Oppliger W, Robitaille AM, et al., 2012. Glutaminolysis activates Rag-mTORC1 signaling. Mol Cell, 47(3):349-358. [26]Efeyan A, Zoncu R, Chang S, et al., 2013. Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival. Nature, 493(7434):679-683. [27]Fan SJ, Snell C, Turley H, et al., 2016. PAT4 levels control amino-acid sensitivity of rapamycin-resistant mTORC1 from the Golgi and affect clinical outcome in colorectal cancer. Oncogene, 35(23):3004-3015. [28]Gai ZC, Wang Q, Yang C, et al., 2016. Structural mechanism for the arginine sensing and regulation of CASTOR1 in the mTORC1 signaling pathway. Cell Discov, 2:16051. [29]Gao HN, Hu H, Zheng N, et al., 2015. Leucine and histidine independently regulate milk protein synthesis in bovine mammary epithelial cells via mTOR signaling pathway. J Zhejiang Univ-Sci B (Biomed & Biotechnol), 16(6):560-572. [30]Grant GA, 2006. The ACT domain: a small molecule binding domain and its role as a common regulatory element. J Biol Chem, 281(45):33825-33829. [31]Grinde B, Seglen PO, 1981. Leucine inhibition of autophagic vacuole formation in isolated rat hepatocytes. Exp Cell Res, 134(1):33-39. [32]Gu X, Orozco JM, Saxton RA, et al., 2017. SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway. Science, 358(6364):813-818. [33]Han JM, Jeong SJ, Park MC, et al., 2012. Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell, 149(2):410-424. [34]Hara K, Yonezawa K, Weng QP, et al., 1998. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J Biol Chem, 273(23):14484-14494. [35]Hara K, Maruki Y, Long XM, et al., 2002. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell, 110(2):177-189. [36]Hasumi H, Baba M, Hong SB, et al., 2008. Identification and characterization of a novel folliculin-interacting protein FNIP2. Gene, 415(1-2):60-67. [37]He XD, Gong W, Zhang JN, et al., 2018. Sensing and transmitting intracellular amino acid signals through reversible lysine aminoacylations. Cell Metab, 27(1):151-166.e6. [38]Heitman J, Movva NR, Hall MN, 1991. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science, 253(5022):905-909. [39]Hirose E, Nakashima N, Sekiguchi T, et al., 1998. RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway. J Cell Sci, 111(Pt 1):11-21. [40]Ho A, Cho CS, Namkoong S, et al., 2016. Biochemical basis of Sestrin physiological activities. Trends Biochem Sci, 41(7):621-632. [41]Huttlin EL, Ting L, Bruckner RJ, et al., 2015. The BioPlex network: a systematic exploration of the human interactome. Cell, 162(2):425-440. [42]Inoki K, Li Y, Zhu TQ, et al., 2002. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat Cell Biol, 4(9):648-657. [43]Inoki K, Zhu TQ, Guan KL, 2003. TSC2 mediates cellular energy response to control cell growth and survival. Cell, 115(5):577-590. [44]Jewell JL, Russell RC, Guan KL, 2013. Amino acid signalling upstream of mTOR. Nat Rev Mol Cell Biol, 14(3):133-139. [45]Jewell JL, Kim YC, Russell RC, et al., 2015. Differential regulation of mTORC1 by leucine and glutamine. Science, 347(6218):194-198. [46]Jin GX, Lee SW, Zhang X, et al., 2015. Skp2-mediated RagA ubiquitination elicits a negative feedback to prevent amino-acid-dependent mTORC1 hyperactivation by recruiting GATOR1. Mol Cell, 58(6):989-1000. [47]Jung J, Genau HM, Behrends C, 2015. Amino acid-dependent mTORC1 regulation by the lysosomal membrane protein SLC38A9. Mol Cell Biol, 35(14):2479-2494. [48]Jung JW, Macalino SJY, Cui MH, et al., 2019. Transmembrane 4 L six family member 5 senses arginine for mTORC1 signaling. Cell Metab, 29(6):1306-1319.e7. [49]Kim DH, Sarbassov DD, Ali SM, et al., 2002. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell, 110(2):163-175. [50]Kim DH, Sarbassov DD, Ali SM, et al., 2003. GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell, 11(4):895-904. [51]Kim E, Goraksha-Hicks P, Li L, et al., 2008. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol, 10(8):935-945. [52]Kim H, An S, Ro SH, et al., 2015. Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. Nat Commun, 6:10025. [53]Koltin Y, Faucette L, Bergsma DJ, et al., 1991. Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein. Mol Cell Biol, 11(3):1718-1723. [54]Lawrence RE, Cho KF, Rappold R, et al., 2018. A nutrient-induced affinity switch controls mTORC1 activation by its Rag GTPase-Ragulator lysosomal scaffold. Nat Cell Biol, 20(9):1052-1063. [55]Layman DK, Anthony TG, Rasmussen BB, et al., 2015. Defining meal requirements for protein to optimize metabolic roles of amino acids. Am J Clin Nutr, 101(6):1330S-1338S. [56]Lee JH, Budanov AV, Park EJ, et al., 2010. Sestrin as a feedback inhibitor of TOR that prevents age-related pathologies. Science, 327(5970):1223-1228. [57]Lee JH, Cho US, Karin M, 2016. Sestrin regulation of TORC1: is Sestrin a leucine sensor? Sci Signal, 9(431):re5. [58]Lee M, Kim JH, Yoon I, et al., 2018. Coordination of the leucine-sensing Rag GTPase cycle by leucyl-tRNA synthetase in the mTORC1 signaling pathway. Proc Natl Acad Sci USA, 115(23):E5279-E5288. [59]Liu B, Du HW, Rutkowski R, et al., 2012. LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis. Science, 337(6092):351-354. [60]Long XM, Lin Y, Ortiz-Vega S, et al., 2005. Rheb binds and regulates the mTOR kinase. Curr Biol, 15(8):702-713. [61]Manning BD, Tee AR, Logsdon MN, et al., 2002. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway. Mol Cell, 10(1):151-162. [62]Menon S, Dibble CC, Talbott G, et al., 2014. Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome. Cell, 156(4):771-785. [63]Nada S, Hondo A, Kasai A, et al., 2009. The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes. EMBO J, 28(5):477-489. [64]Nakashima N, Noguchi E, Nishimoto T, 1999. Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p. Genetics, 152(3):853-867. [65]Nguyen TP, Frank AR, Jewell JL, 2017. Amino acid and small GTPase regulation of mTORC1. Cell Logist, 7(4):e1378794. [66]Nicklin P, Bergman P, Zhang BL, et al., 2009. Bidirectional transport of amino acids regulates mTOR and autophagy. Cell, 136(3):521-534. [67]Oshiro N, Takahashi R, Yoshino KI, et al., 2007. The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1. J Biol Chem, 282(28):20329-20339. [68]Pal R, Palmieri M, Chaudhury A, et al., 2018. Src regulates amino acid-mediated mTORC1 activation by disrupting GATOR1-Rag GTPase interaction. Nat Commun, 9(1):4351. [69]Park SG, Ewalt KL, Kim S, 2005. Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem Sci, 30(10):569-574. [70]Parmigiani A, Nourbakhsh A, Ding BX, et al., 2014. Sestrins inhibit mTORC1 kinase activation through the GATOR complex. Cell Rep, 9(4):1281-1291. [71]Peng M, Yin N, Li MO, 2014. Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling. Cell, 159(1):122-133. [72]Peng M, Yin N, Li MO, 2017. SZT2 dictates GATOR control of mTORC1 signalling. Nature, 543(7645):433-437. [73]Perera RM, Zoncu R, 2016. The lysosome as a regulatory hub. Annu Rev Cell Dev Biol, 32:223-253. [74]Peterson TR, Laplante M, Thoreen CC, et al., 2009. DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell, 137(5):873-886. [75]Petit CS, Roczniak-Ferguson A, Ferguson SM, 2013. Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases. J Cell Biol, 202(7):1107-1122. [76]Potter CJ, Pedraza LG, Xu T, 2002. Akt regulates growth by directly phosphorylating Tsc2. Nat Cell Biol, 4(9):658-665. [77]Quinlan CL, Kaiser SE, Bolaños B, et al., 2017. Targeting S-adenosylmethionine biosynthesis with a novel allosteric inhibitor of Mat2A. Nat Chem Biol, 13(7):785-792. [78]Rebsamen M, Pochini L, Stasyk T, et al., 2015. SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1. Nature, 519(7544):477-481. [79]Sabatini DM, Erdjument-Bromage H, Lui M, et al., 1994. RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell, 78(1):35-43. [80]Sabers CJ, Martin MM, Brunn GJ, et al., 1995. Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells. J Biol Chem, 270(2):815-822. [81]Saier MH Jr, Reddy VS, Tsu BV, et al., 2016. The Transporter Classification Database (TCDB):recent advances. Nucleic Acids Res, 44(D1):D372-D379. [82]Saito K, Araki Y, Kontani K, et al., 2005. Novel role of the small GTPase Rheb: its implication in endocytic pathway independent of the activation of mammalian target of rapamycin. J Biochem, 137(3):423-430. [83]Sancak Y, Thoreen CC, Peterson TR, et al., 2007. PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase. Mol Cell, 25(6):903-915. [84]Sancak Y, Peterson TR, Shaul YD, et al., 2008. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science, 320(5882):1496-1501. [85]Sancak Y, Bar-Peled L, Zoncu R, et al., 2010. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell, 141(2):290-303. [86]Saxton RA, Sabatini DM, 2017. mTOR signaling in growth, metabolism, and disease. Cell, 168(6):960-976. [87]Saxton RA, Knockenhauer KE, Schwartz TU, et al., 2016a. The apo-structure of the leucine sensor Sestrin2 is still elusive. Sci Signal, 9(446):ra92. [88]Saxton RA, Chantranupong L, Knockenhauer KE, et al., 2016b. Mechanism of arginine sensing by CASTOR1 upstream of mTORC1. Nature, 536(7615):229-233. [89]Saxton RA, Knockenhauer KE, Wolfson RL, et al., 2016c. Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science, 351(6268):53-58. [90]Schürmann A, Brauers A, Maßmann S, et al., 1995. Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem, 270(48):28982-28988. [91]Sekiguchi T, Hirose E, Nakashima N, et al., 2001. Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem, 276(10):7246-7257. [92]Shen K, Sabatini DM, 2018. Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms. Proc Natl Acad Sci USA, 115(38):9545-9550. [93]Shen K, Choe A, Sabatini DM, 2017. Intersubunit crosstalk in the Rag GTPase heterodimer enables mTORC1 to respond rapidly to amino acid availability. Mol Cell, 68(3):552-565.e8. [94]Shen K, Huang RK, Brignole EJ, et al., 2018. Architecture of the human GATOR1 and GATOR1-Rag GTPases complexes. Nature, 556(7699):64-69. [95]Shimobayashi M, Hall MN, 2016. Multiple amino acid sensing inputs to mTORC1. Cell Res, 26(1):7-20. [96]Son SM, Park SJ, Lee H, et al., 2019. Leucine signals to mTORC1 via its metabolite acetyl-coenzyme A. Cell Metab, 29(1):192-201.e7. [97]Stracka D, Jozefczuk S, Rudroff F, et al., 2014. Nitrogen source activates TOR (target of rapamycin) complex 1 via glutamine and independently of Gtr/Rag proteins. J Biol Chem, 289(36):25010-25020. [98]Su MY, Morris KL, Kim DJ, et al., 2017. Hybrid structure of the RagA/C-ragulator mTORC1 activation complex. Mol Cell, 68(5):835-846.e3. [99]Sutter BM, Wu X, Laxman S, et al., 2013. Methionine inhibits autophagy and promotes growth by inducing the SAM-responsive methylation of PP2A. Cell, 154(2):403-415. [100]Takagi Y, Kobayashi T, Shiono M, et al., 2008. Interaction of folliculin (Birt-Hogg-Dubé gene product) with a novel Fnip1-like (FnipL/Fnip2) protein. Oncogene, 27(40):5339-5347. [101]Taylor PM, 2014. Role of amino acid transporters in amino acid sensing. Am J Clin Nutr, 99(1):223S-230S. [102]Tee AR, Manning BD, Roux PP, et al., 2003. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol, 13(15):1259-1268. [103]Thomas JD, Zhang YJ, Wei YH, et al., 2014. Rab1A is an mTORC1 activator and a colorectal oncogene. Cancer Cell, 26(5):754-769. [104]Tsun ZY, Bar-Peled L, Chantranupong L, et al., 2013. The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1. Mol Cell, 52(4):495-505. [105]Vander Haar E, Lee SI, Bandhakavi S, et al., 2007. Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nat Cell Biol, 9(3):316-323. [106]Velasco-Miguel S, Buckbinder L, Jean P, et al., 1999. PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes. Oncogene, 18(1):127-137. [107]Wang LF, Harris TE, Roth RA, et al., 2007. PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding. J Biol Chem, 282(27):20036-20044. [108]Wang SY, Tsun ZY, Wolfson RL, et al., 2015. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1. Science, 347(6218):188-194. [109]Wolfson RL, Chantranupong L, Saxton RA, et al., 2016. Sestrin2 is a leucine sensor for the mTORC1 pathway. Science, 351(6268):43-48. [110]Wolfson RL, Chantranupong L, Wyant GA, et al., 2017. KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1. Nature, 543(7645):438-442. [111]Wright MD, Rudy GB, Ni J, 2000. The L6 membrane proteins—a new four-transmembrane superfamily. Protein Sci, 9(8):1594-1600. [112]Wu H, Wang FL, Hu SL, et al., 2012. MiR-20a and miR-106b negatively regulate autophagy induced by leucine deprivation via suppression of ULK1 expression in C2C12 myoblasts. Cell Signal, 24(11):2179-2186. [113]Wyant GA, Abu-Remaileh M, Wolfson RL, et al., 2017. mTORC1 activator SLC38A9 is required to efflux essential amino acids from lysosomes and use protein as a nutrient. Cell, 171(3):642-654.e12. [114]Xia J, Wang R, Zhang TL, et al., 2016. Structural insight into the arginine-binding specificity of CASTOR1 in amino acid-dependent mTORC1 signaling. Cell Discov, 2:16035. [115]Yan XH, Sun QM, Ji J, et al., 2012. Reconstitution of leucine-mediated autophagy via the mTORC1-Barkor pathway in vitro. Autophagy, 8(2):213-221. [116]Yang HJ, Jiang XL, Li BR, et al., 2017. Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. Nature, 552(7685):368-373. [117]Yang HR, Wang J, Liu MJ, et al., 2016. 4.4 Å resolution Cryo-EM structure of human mTOR complex 1. Protein Cell, 7(12):878-887. [118]Yonehara R, Nada S, Nakai T, et al., 2017. Structural basis for the assembly of the Ragulator-Rag GTPase complex. Nat Commun, 8(1):1625. [119]Zhang TL, Wang R, Wang ZJ, et al., 2017. Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1. Nat Commun, 8(1):1394. [120]Zoncu R, Bar-Peled L, Efeyan A, et al., 2011. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase. Science, 334(6056):678-683. Journal of Zhejiang University-SCIENCE, 38 Zheda Road, Hangzhou
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