메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Surface Glycosylation Profiles of Urine Extracellular Vesicles

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN 2; CARBOHYDRATE DERIVATIVE; CD24 ANTIGEN; LECTIN; N ACETYLGLUCOSAMINE; N ACETYLLACTOSAMINE; N ACETYLNEURAMINIC ACID; TAMM HORSFALL GLYCOPROTEIN; UNCLASSIFIED DRUG; VESICULAR TRANSPORT PROTEIN;

EID: 84884376120     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074801     Document Type: Article
Times cited : (92)

References (61)
  • 1
    • 35848968871 scopus 로고    scopus 로고
    • Prevalence of chronic kidney disease in the United States
    • Coresh J, Selvin E, Stevens LA, Manzi J, Kusek JW, et al. (2007) Prevalence of chronic kidney disease in the United States. Jama 298: 2038-2047.
    • (2007) Jama , vol.298 , pp. 2038-2047
    • Coresh, J.1    Selvin, E.2    Stevens, L.A.3    Manzi, J.4    Kusek, J.W.5
  • 2
    • 34547461117 scopus 로고    scopus 로고
    • Chronic kidney disease as a global public health problem: approaches and initiatives - a position statement from Kidney Disease Improving Global Outcomes
    • Levey AS, Atkins R, Coresh J, Cohen EP, Collins AJ, et al. (2007) Chronic kidney disease as a global public health problem: approaches and initiatives- a position statement from Kidney Disease Improving Global Outcomes. Kidney Int 72: 247-259.
    • (2007) Kidney Int , vol.72 , pp. 247-259
    • Levey, A.S.1    Atkins, R.2    Coresh, J.3    Cohen, E.P.4    Collins, A.J.5
  • 3
    • 43549090868 scopus 로고    scopus 로고
    • Prevalence of chronic kidney disease in population-based studies: systematic review
    • Zhang QL, Rothenbacher D, (2008) Prevalence of chronic kidney disease in population-based studies: systematic review. BMC Public Health 8: 117.
    • (2008) BMC Public Health , vol.8 , pp. 117
    • Zhang, Q.L.1    Rothenbacher, D.2
  • 4
    • 36348987649 scopus 로고    scopus 로고
    • Risk management of renal biopsy: 1387 cases over 30 years in a single centre
    • Stratta P, Canavese C, Marengo M, Mesiano P, Besso L, et al. (2007) Risk management of renal biopsy: 1387 cases over 30 years in a single centre. Eur J Clin Invest 37: 954-963.
    • (2007) Eur J Clin Invest , vol.37 , pp. 954-963
    • Stratta, P.1    Canavese, C.2    Marengo, M.3    Mesiano, P.4    Besso, L.5
  • 5
    • 0346103696 scopus 로고    scopus 로고
    • Timing of complications in percutaneous renal biopsy
    • Whittier WL, Korbet SM, (2004) Timing of complications in percutaneous renal biopsy. J Am Soc Nephrol 15: 142-147.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 142-147
    • Whittier, W.L.1    Korbet, S.M.2
  • 8
    • 21344441046 scopus 로고    scopus 로고
    • Prospects for urinary proteomics: exosomes as a source of urinary biomarkers
    • Hoorn EJ, Pisitkun T, Zietse R, Gross P, Frokiaer J, et al. (2005) Prospects for urinary proteomics: exosomes as a source of urinary biomarkers. Nephrology (Carlton) 10: 283-290.
    • (2005) Nephrology (Carlton) , vol.10 , pp. 283-290
    • Hoorn, E.J.1    Pisitkun, T.2    Zietse, R.3    Gross, P.4    Frokiaer, J.5
  • 9
    • 77954244728 scopus 로고    scopus 로고
    • Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease
    • Miranda KC, Bond DT, McKee M, Skog J, Paunescu TG, et al. (2010) Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease. Kidney Int 78: 191-199.
    • (2010) Kidney Int , vol.78 , pp. 191-199
    • Miranda, K.C.1    Bond, D.T.2    McKee, M.3    Skog, J.4    Paunescu, T.G.5
  • 11
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun T, Shen RF, Knepper MA, (2004) Identification and proteomic profiling of exosomes in human urine. Proc Natl Acad Sci 101: 13368-13373.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 12
    • 84861678077 scopus 로고    scopus 로고
    • A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes
    • Raj DAA, Fiume I, Capasso G, Pocsfalvi G, (2012) A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes. Kidney Int 81: 1263-1272.
    • (2012) Kidney Int , vol.81 , pp. 1263-1272
    • Raj, D.A.A.1    Fiume, I.2    Capasso, G.3    Pocsfalvi, G.4
  • 14
    • 49749121101 scopus 로고    scopus 로고
    • Urinary exosomal transcription factors, a new class of biomarkers for renal disease
    • Zhou H, Cheruvanky A, Hu X, Matsumoto T, Hiramatsu N, et al. (2008) Urinary exosomal transcription factors, a new class of biomarkers for renal disease. Kidney Int 74: 613-621.
    • (2008) Kidney Int , vol.74 , pp. 613-621
    • Zhou, H.1    Cheruvanky, A.2    Hu, X.3    Matsumoto, T.4    Hiramatsu, N.5
  • 15
    • 81155152351 scopus 로고    scopus 로고
    • Exosomes and the kidney: prospects for diagnosis and therapy of renal diseases
    • van Balkom BW, Pisitkun T, Verhaar MC, Knepper MA, (2011) Exosomes and the kidney: prospects for diagnosis and therapy of renal diseases. Kidney Int 80: 1138-1145.
    • (2011) Kidney Int , vol.80 , pp. 1138-1145
    • van Balkom, B.W.1    Pisitkun, T.2    Verhaar, M.C.3    Knepper, M.A.4
  • 16
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • Adachi J, Kumar C, Zhang Y, Olsen JV, Mann M, (2006) The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol 7: R80.
    • (2006) Genome Biol , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 20
    • 79953081976 scopus 로고    scopus 로고
    • Interaction and uptake of exosomes by ovarian cancer cells
    • Escrevente C, Keller S, Altevogt P, Costa J, (2011) Interaction and uptake of exosomes by ovarian cancer cells. BMC Cancer 11: 108.
    • (2011) BMC Cancer , vol.11 , pp. 108
    • Escrevente, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 21
    • 84884401766 scopus 로고    scopus 로고
    • A Tight-Knit Group: Protein Glycosylation, Endoplasmic Reticulum Stress and the Unfolded Protein Response
    • In: Agostinis P, Samali A editors, Springer Netherlands
    • Gerlach JQ, Sharma S, Leister KJ, Joshi L (2012) A Tight-Knit Group: Protein Glycosylation, Endoplasmic Reticulum Stress and the Unfolded Protein Response. In: Agostinis P, Samali A editors. Endoplasmic Reticulum Stress in Health and Disease. Springer Netherlands. 23-39.
    • (2012) Endoplasmic Reticulum Stress in Health and Disease , pp. 23-39
    • Gerlach, J.Q.1    Sharma, S.2    Leister, K.J.3    Joshi, L.4
  • 22
    • 79955752164 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response and diabetic kidney disease
    • Cunard R, Sharma K, (2011) The endoplasmic reticulum stress response and diabetic kidney disease. Am J Physiol Renal Physiol 300: F1054-1061.
    • (2011) Am J Physiol Renal Physiol , vol.300
    • Cunard, R.1    Sharma, K.2
  • 23
    • 74449085963 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in proteinuric kidney disease
    • Cybulsky AV, (2010) Endoplasmic reticulum stress in proteinuric kidney disease. Kidney Int 77: 187-193.
    • (2010) Kidney Int , vol.77 , pp. 187-193
    • Cybulsky, A.V.1
  • 24
    • 68949209952 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and renal disease
    • Dickhout JG, Krepinsky JC, (2009) Endoplasmic reticulum stress and renal disease. Antioxid Redox Signal 11: 2341-2352.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2341-2352
    • Dickhout, J.G.1    Krepinsky, J.C.2
  • 25
    • 77949730282 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a progression factor for kidney injury
    • Inagi R, (2010) Endoplasmic reticulum stress as a progression factor for kidney injury. Curr Opin Pharmacol 10: 156-165.
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 156-165
    • Inagi, R.1
  • 26
    • 83655163805 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Stress in UMOD-Related Kidney Disease: A Human Pathologic Study
    • Adam J, Bollee G, Fougeray S, Noel LH, Antignac C, et al. (2011) Endoplasmic Reticulum Stress in UMOD-Related Kidney Disease: A Human Pathologic Study. Am J Kidney Dis 59: 117-121.
    • (2011) Am J Kidney Dis , vol.59 , pp. 117-121
    • Adam, J.1    Bollee, G.2    Fougeray, S.3    Noel, L.H.4    Antignac, C.5
  • 27
    • 59449086729 scopus 로고    scopus 로고
    • Alteration of N-glycosylation in the kidney in a mouse model of systemic lupus erythematosus: relative quantification of N-glycans using an isotope-tagging method
    • Hashii N, Kawasaki N, Itoh S, Nakajima Y, Kawanishi T, et al. (2009) Alteration of N-glycosylation in the kidney in a mouse model of systemic lupus erythematosus: relative quantification of N-glycans using an isotope-tagging method. Immunology 126: 336-345.
    • (2009) Immunology , vol.126 , pp. 336-345
    • Hashii, N.1    Kawasaki, N.2    Itoh, S.3    Nakajima, Y.4    Kawanishi, T.5
  • 28
    • 84856637730 scopus 로고    scopus 로고
    • Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts towards complex-type N-glycosylation in classical galactosemia
    • Staubach S, Schadewaldt P, Wendel U, Nohroudi K, Hanisch FG, (2011) Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts towards complex-type N-glycosylation in classical galactosemia. J Proteome Res 11: 906-916.
    • (2011) J Proteome Res , vol.11 , pp. 906-916
    • Staubach, S.1    Schadewaldt, P.2    Wendel, U.3    Nohroudi, K.4    Hanisch, F.G.5
  • 31
    • 84860241278 scopus 로고    scopus 로고
    • Harnessing glycomics technologies: integrating structure with function for glycan characterization
    • Robinson LN, Artpradit C, Raman R, Shriver ZH, Ruchirawat M, et al. (2012) Harnessing glycomics technologies: integrating structure with function for glycan characterization. Electrophoresis 33: 797-814.
    • (2012) Electrophoresis , vol.33 , pp. 797-814
    • Robinson, L.N.1    Artpradit, C.2    Raman, R.3    Shriver, Z.H.4    Ruchirawat, M.5
  • 33
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: carbohydrate-specific reagents and biological recognition molecules
    • Sharon N, (2007) Lectins: carbohydrate-specific reagents and biological recognition molecules. J Biol Chem 282: 2753-2764.
    • (2007) J Biol Chem , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 34
    • 44749092185 scopus 로고    scopus 로고
    • Identification of N-glycan of alpha-fetoprotein by lectin affinity microarray
    • Chen P, Liu Y, Kang X, Sun L, Yang P, et al. (2008) Identification of N-glycan of alpha-fetoprotein by lectin affinity microarray. J Cancer Res Clin Oncol 134: 851-860.
    • (2008) J Cancer Res Clin Oncol , vol.134 , pp. 851-860
    • Chen, P.1    Liu, Y.2    Kang, X.3    Sun, L.4    Yang, P.5
  • 35
    • 33646380883 scopus 로고    scopus 로고
    • Application of lectin microarray to crude samples: differential glycan profiling of lec mutants
    • Ebe Y, Kuno A, Uchiyama N, Koseki-Kuno S, Yamada M, et al. (2006) Application of lectin microarray to crude samples: differential glycan profiling of lec mutants. J Biochem 139: 323-327.
    • (2006) J Biochem , vol.139 , pp. 323-327
    • Ebe, Y.1    Kuno, A.2    Uchiyama, N.3    Koseki-Kuno, S.4    Yamada, M.5
  • 36
    • 48749083261 scopus 로고    scopus 로고
    • Concept, strategy and realization of lectin-based glycan profiling
    • Hirabayashi J, (2008) Concept, strategy and realization of lectin-based glycan profiling. J Biochem 144: 139-147.
    • (2008) J Biochem , vol.144 , pp. 139-147
    • Hirabayashi, J.1
  • 37
    • 28544452519 scopus 로고    scopus 로고
    • Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling
    • Kuno A, Uchiyama N, Koseki-Kuno S, Ebe Y, Takashima S, et al. (2005) Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling. Nat Methods 2: 851-856.
    • (2005) Nat Methods , vol.2 , pp. 851-856
    • Kuno, A.1    Uchiyama, N.2    Koseki-Kuno, S.3    Ebe, Y.4    Takashima, S.5
  • 38
    • 20444501805 scopus 로고    scopus 로고
    • Development of a lectin microarray for the rapid analysis of protein glycopatterns
    • Pilobello KT, Krishnamoorthy L, Slawek D, Mahal LK, (2005) Development of a lectin microarray for the rapid analysis of protein glycopatterns. Chembiochem 6: 985-989.
    • (2005) Chembiochem , vol.6 , pp. 985-989
    • Pilobello, K.T.1    Krishnamoorthy, L.2    Slawek, D.3    Mahal, L.K.4
  • 40
    • 35148845555 scopus 로고    scopus 로고
    • A novel strategy for mammalian cell surface glycome profiling using lectin microarray
    • Tateno H, Uchiyama N, Kuno A, Togayachi A, Sato T, et al. (2007) A novel strategy for mammalian cell surface glycome profiling using lectin microarray. Glycobiology 17: 1138-1146.
    • (2007) Glycobiology , vol.17 , pp. 1138-1146
    • Tateno, H.1    Uchiyama, N.2    Kuno, A.3    Togayachi, A.4    Sato, T.5
  • 43
    • 62449087144 scopus 로고    scopus 로고
    • Isolation of extracellular membranous vesicles for proteomic analysis
    • Mathias RA, Lim JW, Ji H, Simpson RJ, (2009) Isolation of extracellular membranous vesicles for proteomic analysis. Methods Mol Biol 528: 227-242.
    • (2009) Methods Mol Biol , vol.528 , pp. 227-242
    • Mathias, R.A.1    Lim, J.W.2    Ji, H.3    Simpson, R.J.4
  • 44
    • 42749085108 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Thery C, Amigorena S, Raposo G, Clayton A, (2006) Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr Protoc Cell Biol 30: 3.22.21-23.22.29.
    • (2006) Curr Protoc Cell Biol , vol.30 , pp. 21-29
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 45
    • 33646161950 scopus 로고    scopus 로고
    • Collection, storage, preservation, and normalization of human urinary exosomes for biomarker discovery
    • Zhou H, Yuen PS, Pisitkun T, Gonzales PA, Yasuda H, et al. (2006) Collection, storage, preservation, and normalization of human urinary exosomes for biomarker discovery. Kidney Int 69: 1471-1476.
    • (2006) Kidney Int , vol.69 , pp. 1471-1476
    • Zhou, H.1    Yuen, P.S.2    Pisitkun, T.3    Gonzales, P.A.4    Yasuda, H.5
  • 46
    • 35348979185 scopus 로고    scopus 로고
    • CD24 is a marker of exosomes secreted into urine and amniotic fluid
    • Keller S, Rupp C, Stoeck A, Runz S, Fogel M, et al. (2007) CD24 is a marker of exosomes secreted into urine and amniotic fluid. Kidney Int 72: 1095-1102.
    • (2007) Kidney Int , vol.72 , pp. 1095-1102
    • Keller, S.1    Rupp, C.2    Stoeck, A.3    Runz, S.4    Fogel, M.5
  • 47
    • 34247872835 scopus 로고    scopus 로고
    • Rapid isolation of urinary exosomal biomarkers using a nanomembrane ultrafiltration concentrator
    • Cheruvanky A, Zhou H, Pisitkun T, Kopp JB, Knepper MA, et al. (2007) Rapid isolation of urinary exosomal biomarkers using a nanomembrane ultrafiltration concentrator. Am J Physiol Renal Physiol 292: F1657-1661.
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Cheruvanky, A.1    Zhou, H.2    Pisitkun, T.3    Kopp, J.B.4    Knepper, M.A.5
  • 48
    • 77957557995 scopus 로고    scopus 로고
    • Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome
    • Rood IM, Deegens JK, Merchant ML, Tamboer WP, Wilkey DW, et al. (2010) Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome. Kidney Int 78: 810-816.
    • (2010) Kidney Int , vol.78 , pp. 810-816
    • Rood, I.M.1    Deegens, J.K.2    Merchant, M.L.3    Tamboer, W.P.4    Wilkey, D.W.5
  • 49
    • 84866721319 scopus 로고    scopus 로고
    • Characterization of a nanoparticulate drug delivery system using scanning ion occlusion sensing
    • Yang L, Broom MF, Tucker IG, (2012) Characterization of a nanoparticulate drug delivery system using scanning ion occlusion sensing. Pharm Res 29: 2578-2586.
    • (2012) Pharm Res , vol.29 , pp. 2578-2586
    • Yang, L.1    Broom, M.F.2    Tucker, I.G.3
  • 50
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes-vesicular carriers for intercellular communication
    • Simons M, Raposo G, (2009) Exosomes-vesicular carriers for intercellular communication. Curr Opin Cell Biol 21: 575-581.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 51
    • 59749089917 scopus 로고    scopus 로고
    • Comparative analysis of oligosaccharide specificities of fucose-specific lectins from Aspergillus oryzae and Aleuria aurantia using frontal affinity chromatography
    • Matsumura K, Higashida K, Hata Y, Kominami J, Nakamura-Tsuruta S, et al. (2009) Comparative analysis of oligosaccharide specificities of fucose-specific lectins from Aspergillus oryzae and Aleuria aurantia using frontal affinity chromatography. Anal Biochem 386: 217-221.
    • (2009) Anal Biochem , vol.386 , pp. 217-221
    • Matsumura, K.1    Higashida, K.2    Hata, Y.3    Kominami, J.4    Nakamura-Tsuruta, S.5
  • 52
    • 84859820446 scopus 로고    scopus 로고
    • Differential release of high mannose structural isoforms by fungal and bacterial endo-beta-N-acetylglucosaminidases
    • Gerlach JQ, Kilcoyne M, Farrell MP, Kane M, Joshi L, (2012) Differential release of high mannose structural isoforms by fungal and bacterial endo-beta-N-acetylglucosaminidases. Mol Biosyst 8: 1472-1481.
    • (2012) Mol Biosyst , vol.8 , pp. 1472-1481
    • Gerlach, J.Q.1    Kilcoyne, M.2    Farrell, M.P.3    Kane, M.4    Joshi, L.5
  • 53
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: current perspectives
    • Simpson RJ, Jensen SS, Lim JW, (2008) Proteomic profiling of exosomes: current perspectives. Proteomics 8: 4083-4099.
    • (2008) Proteomics , vol.8 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 54
    • 77954692713 scopus 로고    scopus 로고
    • Recognition of galactose-deficient O-glycans in the hinge region of IgA1 by N-acetylgalactosamine-specific snail lectins: a comparative binding study
    • Gomes MM, Suzuki H, Brooks MT, Tomana M, Moldoveanu Z, et al. (2010) Recognition of galactose-deficient O-glycans in the hinge region of IgA1 by N-acetylgalactosamine-specific snail lectins: a comparative binding study. Biochemistry 49: 5671-5682.
    • (2010) Biochemistry , vol.49 , pp. 5671-5682
    • Gomes, M.M.1    Suzuki, H.2    Brooks, M.T.3    Tomana, M.4    Moldoveanu, Z.5
  • 55
    • 79953292210 scopus 로고    scopus 로고
    • Aberrantly glycosylated IgA1 as a factor in the pathogenesis of IgA nephropathy
    • Tanaka M, Seki G, Someya T, Nagata M, Fujita T, (2011) Aberrantly glycosylated IgA1 as a factor in the pathogenesis of IgA nephropathy. Clin Dev Immunol 2011: 470803.
    • (2011) Clin Dev Immunol , vol.2011 , pp. 470803
    • Tanaka, M.1    Seki, G.2    Someya, T.3    Nagata, M.4    Fujita, T.5
  • 56
    • 78651393398 scopus 로고    scopus 로고
    • Defective glycosylation of alpha-dystroglycan contributes to podocyte flattening
    • Kojima K, Nosaka H, Kishimoto Y, Nishiyama Y, Fukuda S, et al. (2011) Defective glycosylation of alpha-dystroglycan contributes to podocyte flattening. Kidney Int 79: 311-316.
    • (2011) Kidney Int , vol.79 , pp. 311-316
    • Kojima, K.1    Nosaka, H.2    Kishimoto, Y.3    Nishiyama, Y.4    Fukuda, S.5
  • 57
    • 77955274627 scopus 로고    scopus 로고
    • Glycosphingolipids
    • In: Varki A, Cummings RD, Esko JD, Freeze HH, et al. editors, 2 edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
    • Schnaar RL, Suzuki A, Stanley P (2009) Glycosphingolipids. In: Varki A, Cummings RD, Esko JD, Freeze HH, et al. editors. Essentials of Glycobiology, 2 edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press.
    • (2009) Essentials of Glycobiology
    • Schnaar, R.L.1    Suzuki, A.2    Stanley, P.3
  • 58
    • 0030333179 scopus 로고    scopus 로고
    • Alterations of Tamm-Horsfall protein immunoreactivity after partial desialylation and deglycosylation
    • Grabska T, Baginski T, Kubicz A, Kokot M, Kokot F, et al. (1996) Alterations of Tamm-Horsfall protein immunoreactivity after partial desialylation and deglycosylation. Arch Immunol Ther Exp (Warsz) 44: 241-248.
    • (1996) Arch Immunol Ther Exp (Warsz) , vol.44 , pp. 241-248
    • Grabska, T.1    Baginski, T.2    Kubicz, A.3    Kokot, M.4    Kokot, F.5
  • 59
    • 0002970919 scopus 로고
    • A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses
    • Tamm I, Horsfall FL Jr, (1952) A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses. J Exp Med 95: 71-97.
    • (1952) J Exp Med , vol.95 , pp. 71-97
    • Tamm, I.1    Horsfall Jr., F.L.2
  • 60
    • 36349015388 scopus 로고    scopus 로고
    • Altered glycosylation of Tamm-Horsfall glycoprotein derived from renal allograft recipients leads to changes in its biological function
    • Wu TH, Hsieh SC, Li KJ, Wu CH, Yu CL, et al. (2008) Altered glycosylation of Tamm-Horsfall glycoprotein derived from renal allograft recipients leads to changes in its biological function. Transpl Immunol 18: 237-245.
    • (2008) Transpl Immunol , vol.18 , pp. 237-245
    • Wu, T.H.1    Hsieh, S.C.2    Li, K.J.3    Wu, C.H.4    Yu, C.L.5
  • 61
    • 84859384612 scopus 로고    scopus 로고
    • Construction of a natural mucin microarray and interrogation for biologically relevant glyco-epitopes
    • Kilcoyne M, Gerlach JQ, Gough R, Gallagher ME, Kane M, et al. (2012) Construction of a natural mucin microarray and interrogation for biologically relevant glyco-epitopes. Anal Chem 84: 3330-3338.
    • (2012) Anal Chem , vol.84 , pp. 3330-3338
    • Kilcoyne, M.1    Gerlach, J.Q.2    Gough, R.3    Gallagher, M.E.4    Kane, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.