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Volumn 6, Issue , 2016, Pages

Leptospiral outer membrane protein LipL32 induces inflammation and kidney injury in zebrafish larvae

Author keywords

[No Author keywords available]

Indexed keywords

LIPL32 PROTEIN, LEPTOSPIRA; LIPOPROTEIN; OUTER MEMBRANE PROTEIN;

EID: 84973861057     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27838     Document Type: Article
Times cited : (31)

References (60)
  • 1
    • 77957582069 scopus 로고    scopus 로고
    • Leptospira as an emerging pathogen: A review of its biology, pathogenesis and host immune responses
    • Evangelista, K. V. & Coburn, J. Leptospira as an emerging pathogen: a review of its biology, pathogenesis and host immune responses. Future Microbiol 5, 1413-1425 (2010).
    • (2010) Future Microbiol , vol.5 , pp. 1413-1425
    • Evangelista, K.V.1    Coburn, J.2
  • 2
    • 84868192681 scopus 로고    scopus 로고
    • Sequence of Leptospira santarosai serovar Shermani genome and prediction of virulence-associated genes
    • Chou, L. F. et al. Sequence of Leptospira santarosai serovar Shermani genome and prediction of virulence-associated genes. Gene 511, 364-370 (2012).
    • (2012) Gene , vol.511 , pp. 364-370
    • Chou, L.F.1
  • 3
    • 0030734509 scopus 로고    scopus 로고
    • Leptospirosis: An ignored cause of acute renal failure in Taiwan
    • Yang, C. W. et al. Leptospirosis: an ignored cause of acute renal failure in Taiwan. Am J Kidney Dis 30, 840-845 (1997).
    • (1997) Am J Kidney Dis , vol.30 , pp. 840-845
    • Yang, C.W.1
  • 4
    • 80655142462 scopus 로고    scopus 로고
    • Deciphering morphological determinants of the helix-shaped Leptospira
    • Slamti, L., de Pedro, M. A., Guichet, E. & Picardeau, M. Deciphering morphological determinants of the helix-shaped Leptospira. J Bacteriol 193, 6266-6275 (2011).
    • (2011) J Bacteriol , vol.193 , pp. 6266-6275
    • Slamti, L.1    De Pedro, M.A.2    Guichet, E.3    Picardeau, M.4
  • 5
    • 84901355321 scopus 로고    scopus 로고
    • Leptospira infections in freshwater fish in Morogoro Tanzania: A hidden public health threat
    • Mgode, G. F., Mhamphi, G. G., Katkweba, A. S. & Thomas, M. Leptospira infections in freshwater fish in Morogoro Tanzania: a hidden public health threat. Tanzan J Health Res 16, 112-117 (2014).
    • (2014) Tanzan J Health Res , vol.16 , pp. 112-117
    • Mgode, G.F.1    Mhamphi, G.G.2    Katkweba, A.S.3    Thomas, M.4
  • 6
    • 0036063382 scopus 로고    scopus 로고
    • The Leptospira outer membrane protein LipL32 induces tubulointerstitial nephritis-mediated gene expression in mouse proximal tubule cells
    • Yang, C. W. et al. The Leptospira outer membrane protein LipL32 induces tubulointerstitial nephritis-mediated gene expression in mouse proximal tubule cells. J Am Soc Nephrol 13, 2037-2045 (2002).
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2037-2045
    • Yang, C.W.1
  • 9
    • 5944225473 scopus 로고    scopus 로고
    • Leptospiral lipopolysaccharide activates cells through a TLR2-dependent mechanism
    • Werts, C. et al. Leptospiral lipopolysaccharide activates cells through a TLR2-dependent mechanism. Nat Immunol 2, 346-352 (2001).
    • (2001) Nat Immunol , vol.2 , pp. 346-352
    • Werts, C.1
  • 10
    • 84862004168 scopus 로고    scopus 로고
    • Renal involvement in leptospirosis: The effect of glycolipoprotein on renal water absorption
    • Cesar, K. R. et al. Renal involvement in leptospirosis: the effect of glycolipoprotein on renal water absorption. PLoS One 7, e37625 (2012).
    • (2012) PLoS One , vol.7
    • Cesar, K.R.1
  • 11
    • 84908219020 scopus 로고    scopus 로고
    • Murine lung injury caused by Leptospira interrogans glycolipoprotein, a specific Na/KATPase inhibitor
    • Goncalves-de-Albuquerque, C. F. et al. Murine lung injury caused by Leptospira interrogans glycolipoprotein, a specific Na/KATPase inhibitor. Respir Res 15, 93 (2014).
    • (2014) Respir Res , vol.15 , pp. 93
    • Goncalves-De-Albuquerque, C.F.1
  • 12
    • 84864760198 scopus 로고    scopus 로고
    • Leptospiral hemolysins induce proinflammatory cytokines through Toll-like receptor 2-and 4-mediated JNK and NF-kappaB signaling pathways
    • Wang, H. et al. Leptospiral hemolysins induce proinflammatory cytokines through Toll-like receptor 2-and 4-mediated JNK and NF-kappaB signaling pathways. PLoS One 7, e42266 (2012).
    • (2012) PLoS One , vol.7
    • Wang, H.1
  • 13
    • 84920527866 scopus 로고    scopus 로고
    • Identification of cell-binding adhesins of Leptospira interrogans
    • Evangelista, K. V. et al. Identification of cell-binding adhesins of Leptospira interrogans. PLoS Negl Trop Dis 8, e3215 (2014).
    • (2014) PLoS Negl Trop Dis , vol.8
    • Evangelista, K.V.1
  • 14
    • 0036121913 scopus 로고    scopus 로고
    • Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai
    • Cullen, P. A., Cordwell, S. J., Bulach, D. M., Haake, D. A. & Adler, B. Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai. Infect Immun 70, 2311-2318 (2002).
    • (2002) Infect Immun , vol.70 , pp. 2311-2318
    • Cullen, P.A.1    Cordwell, S.J.2    Bulach, D.M.3    Haake, D.A.4    Adler, B.5
  • 16
    • 0034104388 scopus 로고    scopus 로고
    • The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection
    • Haake, D. A. et al. The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection. Infect Immun 68, 2276-2285 (2000).
    • (2000) Infect Immun , vol.68 , pp. 2276-2285
    • Haake, D.A.1
  • 17
    • 0034912192 scopus 로고    scopus 로고
    • Leptospiral proteins recognized during the humoral immune response to leptospirosis in humans
    • Guerreiro, H. et al. Leptospiral proteins recognized during the humoral immune response to leptospirosis in humans. Infect Immun 69, 4958-4968 (2001).
    • (2001) Infect Immun , vol.69 , pp. 4958-4968
    • Guerreiro, H.1
  • 18
    • 33749264811 scopus 로고    scopus 로고
    • Leptospiral outer membrane protein induces extracellular matrix accumulation through a TGF-beta1/Smaddependent pathway
    • Tian, Y. C. et al. Leptospiral outer membrane protein induces extracellular matrix accumulation through a TGF-beta1/Smaddependent pathway. J Am Soc Nephrol 17, 2792-2798 (2006).
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2792-2798
    • Tian, Y.C.1
  • 19
    • 33644520001 scopus 로고    scopus 로고
    • Toll-like receptor 2 mediates early inflammation by leptospiral outer membrane proteins in proximal tubule cells
    • Yang, C. W. et al. Toll-like receptor 2 mediates early inflammation by leptospiral outer membrane proteins in proximal tubule cells. Kidney Int 69, 815-822 (2006).
    • (2006) Kidney Int , vol.69 , pp. 815-822
    • Yang, C.W.1
  • 20
    • 84876891567 scopus 로고    scopus 로고
    • Essential calcium-binding cluster of Leptospira LipL32 protein for inflammatory responses through the Toll-like receptor 2 pathway
    • Lo, Y. Y. et al. Essential calcium-binding cluster of Leptospira LipL32 protein for inflammatory responses through the Toll-like receptor 2 pathway. J Biol Chem 288, 12335-12344 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 12335-12344
    • Lo, Y.Y.1
  • 21
    • 63449094406 scopus 로고    scopus 로고
    • Crystal structure of LipL32, the most abundant surface protein of pathogenic Leptospira spp
    • Vivian, J. P. et al. Crystal structure of LipL32, the most abundant surface protein of pathogenic Leptospira spp. J Mol Biol 387, 1229-1238 (2009).
    • (2009) J Mol Biol , vol.387 , pp. 1229-1238
    • Vivian, J.P.1
  • 22
    • 77449117998 scopus 로고    scopus 로고
    • Calcium binds to LipL32, a lipoprotein from pathogenic Leptospira, and modulates fibronectin binding
    • Tung, J. Y., Yang, C. W., Chou, S. W., Lin, C. C. & Sun, Y. J. Calcium binds to LipL32, a lipoprotein from pathogenic Leptospira, and modulates fibronectin binding. J Biol Chem 285, 3245-3252 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 3245-3252
    • Tung, J.Y.1    Yang, C.W.2    Chou, S.W.3    Lin, C.C.4    Sun, Y.J.5
  • 23
    • 42949159838 scopus 로고    scopus 로고
    • LipL32 is an extracellular matrix-interacting protein of Leptospira spp. And Pseudoalteromonas tunicate
    • Hoke, D. E., Egan, S., Cullen, P. A. & Adler, B. LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata. Infect Immun 76, 2063-2069 (2008).
    • (2008) Infect Immun , vol.76 , pp. 2063-2069
    • Hoke, D.E.1    Egan, S.2    Cullen, P.A.3    Adler, B.4
  • 24
    • 80052542448 scopus 로고    scopus 로고
    • Identification of candidate host proteins that interact with LipL32, the major outer membrane protein of pathogenic Leptospira, by random phage display peptide library
    • Chaemchuen, S., Rungpragayphan, S., Poovorawan, Y. & Patarakul, K. Identification of candidate host proteins that interact with LipL32, the major outer membrane protein of pathogenic Leptospira, by random phage display peptide library. Vet Microbiol 153, 178-185 (2011).
    • (2011) Vet Microbiol , vol.153 , pp. 178-185
    • Chaemchuen, S.1    Rungpragayphan, S.2    Poovorawan, Y.3    Patarakul, K.4
  • 25
    • 66949159845 scopus 로고    scopus 로고
    • Transcriptome profiling and functional analyses of the zebrafish embryonic innate immune response to Salmonella infection
    • Stockhammer, O. W., Zakrzewska, A., Hegedus, Z., Spaink, H. P. & Meijer, A. H. Transcriptome profiling and functional analyses of the zebrafish embryonic innate immune response to Salmonella infection. J Immunol 182, 5641-5653 (2009).
    • (2009) J Immunol , vol.182 , pp. 5641-5653
    • Stockhammer, O.W.1    Zakrzewska, A.2    Hegedus, Z.3    Spaink, H.P.4    Meijer, A.H.5
  • 26
    • 77952698205 scopus 로고    scopus 로고
    • Zebrafish as a model host for Candida albicans infection
    • Chao, C. C. et al. Zebrafish as a model host for Candida albicans infection. Infect Immun 78, 2512-2521 (2010).
    • (2010) Infect Immun , vol.78 , pp. 2512-2521
    • Chao, C.C.1
  • 27
    • 0036081383 scopus 로고    scopus 로고
    • Streptococcus-zebrafish model of bacterial pathogenesis
    • Neely, M. N., Pfeifer, J. D. & Caparon, M. Streptococcus-zebrafish model of bacterial pathogenesis. Infect Immun 70, 3904-3914 (2002).
    • (2002) Infect Immun , vol.70 , pp. 3904-3914
    • Neely, M.N.1    Pfeifer, J.D.2    Caparon, M.3
  • 28
    • 84879330799 scopus 로고    scopus 로고
    • Innate immune recognition of the microbiota promotes host-microbial symbiosis
    • Chu, H. & Mazmanian, S. K. Innate immune recognition of the microbiota promotes host-microbial symbiosis. Nat Immunol 14, 668-675 (2013).
    • (2013) Nat Immunol , vol.14 , pp. 668-675
    • Chu, H.1    Mazmanian, S.K.2
  • 29
    • 42949130073 scopus 로고    scopus 로고
    • The zebrafish pronephros: A model to study nephron segmentation
    • Wingert, R. A. & Davidson, A. J. The zebrafish pronephros: a model to study nephron segmentation. Kidney Int 73, 1120-1127 (2008).
    • (2008) Kidney Int , vol.73 , pp. 1120-1127
    • Wingert, R.A.1    Davidson, A.J.2
  • 30
    • 68349115091 scopus 로고    scopus 로고
    • Leptospira interrogans stably infects zebrafish embryos, altering phagocyte behavior and homing to specific tissues
    • Davis, J. M., Haake, D. A. & Ramakrishnan, L. Leptospira interrogans stably infects zebrafish embryos, altering phagocyte behavior and homing to specific tissues. PLoS Negl Trop Dis 3, e463 (2009).
    • (2009) PLoS Negl Trop Dis , vol.3 , pp. e463
    • Davis, J.M.1    Haake, D.A.2    Ramakrishnan, L.3
  • 31
    • 77949679554 scopus 로고    scopus 로고
    • FlaB PCR-based identification of pathogenic leptospiral isolates
    • Natarajaseenivasan, K. et al. FlaB PCR-based identification of pathogenic leptospiral isolates. J Microbiol Immunol Infect 43, 62-69 (2010).
    • (2010) J Microbiol Immunol Infect , vol.43 , pp. 62-69
    • Natarajaseenivasan, K.1
  • 32
    • 77954206504 scopus 로고    scopus 로고
    • Leptospiral outer membrane lipoprotein LipL32 binding on toll-like receptor 2 of renal cells as determined with an atomic force microscope
    • Hsu, S. H. et al. Leptospiral outer membrane lipoprotein LipL32 binding on toll-like receptor 2 of renal cells as determined with an atomic force microscope. Biochemistry 49, 5408-5417 (2010).
    • (2010) Biochemistry , vol.49 , pp. 5408-5417
    • Hsu, S.H.1
  • 34
    • 42149124615 scopus 로고    scopus 로고
    • Conservation and divergence of gene families encoding components of innate immune response systems in zebrafish
    • Stein, C., Caccamo, M., Laird, G. & Leptin, M. Conservation and divergence of gene families encoding components of innate immune response systems in zebrafish. Genome Biol 8, R251 (2007).
    • (2007) Genome Biol , vol.8 , pp. R251
    • Stein, C.1    Caccamo, M.2    Laird, G.3    Leptin, M.4
  • 35
    • 84929493843 scopus 로고    scopus 로고
    • Evaluation of cell binding activities of Leptospira ECM adhesins
    • Robbins, G. T. et al. Evaluation of cell binding activities of Leptospira ECM adhesins. PLoS Negl Trop Dis 9, e0003712 (2015).
    • (2015) PLoS Negl Trop Dis , vol.9
    • Robbins, G.T.1
  • 36
    • 84897953140 scopus 로고    scopus 로고
    • Vaccination with leptospiral outer membrane lipoprotein LipL32 reduces kidney invasion of Leptospira interrogans serovar canicola in hamsters
    • Humphryes, P. C. et al. Vaccination with leptospiral outer membrane lipoprotein LipL32 reduces kidney invasion of Leptospira interrogans serovar canicola in hamsters. Clin Vaccine Immunol 21, 546-551 (2014).
    • (2014) Clin Vaccine Immunol , vol.21 , pp. 546-551
    • Humphryes, P.C.1
  • 37
    • 84924406142 scopus 로고    scopus 로고
    • Current immunological and molecular tools for leptospirosis: Diagnostics, vaccine design, and biomarkers for predicting severity
    • Rajapakse, S., Rodrigo, C., Handunnetti, S. M. & Fernando, S. D. Current immunological and molecular tools for leptospirosis: diagnostics, vaccine design, and biomarkers for predicting severity. Ann Clin Microbiol Antimicrob 14, 2 (2015).
    • (2015) Ann Clin Microbiol Antimicrob , vol.14 , pp. 2
    • Rajapakse, S.1    Rodrigo, C.2    Handunnetti, S.M.3    Fernando, S.D.4
  • 38
    • 0030962512 scopus 로고    scopus 로고
    • Purification and characterization of a Na+, K+ ATPase inhibitor found in an endotoxin of Leptospira interrogans
    • Burth, P., YounesIbrahim, M., Goncalez, F. H. F. S., Costa, E. R. & Faria, M. V. C. Purification and characterization of a Na+, K+ ATPase inhibitor found in an endotoxin of Leptospira interrogans. Infect Immun 65, 1557-1560 (1997).
    • (1997) Infect Immun , vol.65 , pp. 1557-1560
    • Burth, P.1    YounesIbrahim, M.2    Goncalez, F.H.F.S.3    Costa, E.R.4    Faria, M.V.C.5
  • 39
    • 0028999119 scopus 로고
    • Inhibition of Na,K-ATPase by an endotoxin extracted from Leptospira interrogans: A possible mechanism for the physiopathology of leptospirosis
    • Younes-Ibrahim, M. et al. Inhibition of Na,K-ATPase by an endotoxin extracted from Leptospira interrogans: a possible mechanism for the physiopathology of leptospirosis. C R Acad Sci III 318, 619-625 (1995).
    • (1995) C R Acad Sci III , vol.318 , pp. 619-625
    • Younes-Ibrahim, M.1
  • 40
    • 0031063989 scopus 로고    scopus 로고
    • Na, K-ATPase: A molecular target for Leptospira interrogans endotoxin
    • Younes-Ibrahim, M. et al. Na, K-ATPase: a molecular target for Leptospira interrogans endotoxin. Braz J Med Biol Res 30, 213-223 (1997).
    • (1997) Braz J Med Biol Res , vol.30 , pp. 213-223
    • Younes-Ibrahim, M.1
  • 41
    • 84857819545 scopus 로고    scopus 로고
    • Downregulation of the Na/K-ATPase pump by leptospiral glycolipoprotein activates the NLRP3 inflammasome
    • Lacroix-Lamande, S. et al. Downregulation of the Na/K-ATPase pump by leptospiral glycolipoprotein activates the NLRP3 inflammasome. J Immunol 188, 2805-2814 (2012).
    • (2012) J Immunol , vol.188 , pp. 2805-2814
    • Lacroix-Lamande, S.1
  • 42
    • 70349269503 scopus 로고    scopus 로고
    • Leptospira: The dawn of the molecular genetics era for an emerging zoonotic pathogen
    • Ko, A. I., Goarant, C. & Picardeau, M. Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen. Nat Rev Microbiol 7, 736-747 (2009).
    • (2009) Nat Rev Microbiol , vol.7 , pp. 736-747
    • Ko, A.I.1    Goarant, C.2    Picardeau, M.3
  • 43
    • 0033765375 scopus 로고    scopus 로고
    • Leptospira outer membrane protein activates NF-kappaB and downstream genes expressed in medullary thick ascending limb cells
    • Yang, C. W. et al. Leptospira outer membrane protein activates NF-kappaB and downstream genes expressed in medullary thick ascending limb cells. J Am Soc Nephrol 11, 2017-2026 (2000).
    • (2000) J Am Soc Nephrol , vol.11 , pp. 2017-2026
    • Yang, C.W.1
  • 44
    • 78651234446 scopus 로고    scopus 로고
    • Leptospirosis: A Toll road from B lymphocytes
    • Werts, C. Leptospirosis: a Toll road from B lymphocytes. Chang Gung Med J 33, 591-601 (2010).
    • (2010) Chang Gung Med J , vol.33 , pp. 591-601
    • Werts, C.1
  • 45
    • 84893784254 scopus 로고    scopus 로고
    • Leptospira Interrogans induces fibrosis in the mouse kidney through Inos-dependent, TLR-and NLRindependent signaling pathways
    • Fanton d'Andon, M. et al. Leptospira Interrogans induces fibrosis in the mouse kidney through Inos-dependent, TLR-and NLRindependent signaling pathways. PLoS Negl Trop Dis 8, e2664 (2014).
    • (2014) PLoS Negl Trop Dis , vol.8 , pp. e2664
    • Fanton D'Andon, M.1
  • 46
    • 62449313550 scopus 로고    scopus 로고
    • Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans
    • Murray, G. L. et al. Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans. Infect Immun 77, 952-958 (2009).
    • (2009) Infect Immun , vol.77 , pp. 952-958
    • Murray, G.L.1
  • 48
    • 78951479838 scopus 로고    scopus 로고
    • Characterization of conserved combined T and B cell epitopes in Leptospira interrogans major outer membrane proteins OmpL1 and LipL41
    • Lin, X., Sun, A., Ruan, P., Zhang, Z. & Yan, J. Characterization of conserved combined T and B cell epitopes in Leptospira interrogans major outer membrane proteins OmpL1 and LipL41. BMC Microbiol 11, 21 (2011).
    • (2011) BMC Microbiol , vol.11 , pp. 21
    • Lin, X.1    Sun, A.2    Ruan, P.3    Zhang, Z.4    Yan, J.5
  • 50
    • 34548127051 scopus 로고    scopus 로고
    • The Wilms tumor genes wt1a and wt1b control different steps during formation of the zebrafish pronephros
    • Perner, B., Englert, C. & Bollig, F. The Wilms tumor genes wt1a and wt1b control different steps during formation of the zebrafish pronephros. Dev Biol 309, 87-96 (2007).
    • (2007) Dev Biol , vol.309 , pp. 87-96
    • Perner, B.1    Englert, C.2    Bollig, F.3
  • 52
    • 80055113387 scopus 로고    scopus 로고
    • Microinjection of mRNA and morpholino antisense oligonucleotides in zebrafish embryos
    • Yuan, S. & Sun, Z. Microinjection of mRNA and morpholino antisense oligonucleotides in zebrafish embryos. J Vis Exp 27, e1113 (2009).
    • (2009) J Vis Exp , vol.27 , pp. e1113
    • Yuan, S.1    Sun, Z.2
  • 53
    • 84937910940 scopus 로고    scopus 로고
    • Common and specific downstream signaling targets controlled by Tlr2 and Tlr5 innate immune signaling in zebrafish
    • Yang, S., Marin-Juez, R., Meijer, A. H. & Spaink, H. P. Common and specific downstream signaling targets controlled by Tlr2 and Tlr5 innate immune signaling in zebrafish. BMC Genomics 16, 547 (2015).
    • (2015) BMC Genomics , vol.16 , pp. 547
    • Yang, S.1    Marin-Juez, R.2    Meijer, A.H.3    Spaink, H.P.4
  • 54
    • 61449231622 scopus 로고    scopus 로고
    • Evolution of lipopolysaccharide (LPS) recognition and signaling: Fish TLR4 does not recognize LPS and negatively regulates NF-kappaB activation
    • Sepulcre, M. P. et al. Evolution of lipopolysaccharide (LPS) recognition and signaling: fish TLR4 does not recognize LPS and negatively regulates NF-kappaB activation. J Immunol 182, 1836-1845 (2009).
    • (2009) J Immunol , vol.182 , pp. 1836-1845
    • Sepulcre, M.P.1
  • 55
    • 80052341827 scopus 로고    scopus 로고
    • Inhibition of the P2X7 receptor reduces cystogenesis in PKD
    • Chang, M. Y. et al. Inhibition of the P2X7 receptor reduces cystogenesis in PKD. J Am Soc Nephrol 22, 1696-1706 (2011).
    • (2011) J Am Soc Nephrol , vol.22 , pp. 1696-1706
    • Chang, M.Y.1
  • 56
    • 77949300126 scopus 로고    scopus 로고
    • Nephrotoxicity assessments of acetaminophen during zebrafish embryogenesis
    • Peng, H. C. et al. Nephrotoxicity assessments of acetaminophen during zebrafish embryogenesis. Comp Biochem Physiol C Toxicol Pharmacol 151, 480-486 (2010).
    • (2010) Comp Biochem Physiol C Toxicol Pharmacol , vol.151 , pp. 480-486
    • Peng, H.C.1
  • 57
    • 84891781815 scopus 로고    scopus 로고
    • Development of an automated imaging pipeline for the analysis of the zebrafish larval kidney
    • Westhoff, J. H. et al. Development of an automated imaging pipeline for the analysis of the zebrafish larval kidney. PLoS One 8, e82137 (2013).
    • (2013) PLoS One , vol.8
    • Westhoff, J.H.1
  • 58
    • 46349109999 scopus 로고    scopus 로고
    • Distinct functions for ERK1 and ERK2 in cell migration processes during zebrafish gastrulation
    • Krens, S. F. et al. Distinct functions for ERK1 and ERK2 in cell migration processes during zebrafish gastrulation. Dev Biol 319, 370-383 (2008).
    • (2008) Dev Biol , vol.319 , pp. 370-383
    • Krens, S.F.1
  • 59
    • 17644368516 scopus 로고    scopus 로고
    • Acute renal failure in zebrafish: A novel system to study a complex disease
    • Hentschel, D. M. et al. Acute renal failure in zebrafish: a novel system to study a complex disease. Am J Physiol Renal Physiol 288, F923-929 (2005).
    • (2005) Am J Physiol Renal Physiol , vol.288 , pp. F923-929
    • Hentschel, D.M.1
  • 60
    • 12744273128 scopus 로고    scopus 로고
    • Detection of pathogenic leptospires by real-time quantitative PCR
    • Levett, P. N. et al. Detection of pathogenic leptospires by real-time quantitative PCR. J Med Microbiol 54, 45-49 (2005).
    • (2005) J Med Microbiol , vol.54 , pp. 45-49
    • Levett, P.N.1


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