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Volumn 180, Issue 4, 2012, Pages 1431-1440

The Gne M712T mouse as a model for human glomerulopathy

Author keywords

[No Author keywords available]

Indexed keywords

JACALIN; MANNOSAMINE; N ACETYLMANNOSAMINE; N ACETYLMANNOSAMINE KINASE; NEPHRIN; PEANUT AGGLUTININ; PHOSPHOTRANSFERASE; PODOCALYXIN; SIALIC ACID; SIALIDASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE; WHEAT GERM AGGLUTININ;

EID: 84859064418     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2011.12.023     Document Type: Article
Times cited : (27)

References (82)
  • 1
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • A. Varki Sialic acids as ligands in recognition phenomena FASEB J 11 1997 248 255
    • (1997) FASEB J , vol.11 , pp. 248-255
    • Varki, A.1
  • 3
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • A. Varki Sialic acids in human health and disease Trends Mol Med 14 2008 351 360
    • (2008) Trends Mol Med , vol.14 , pp. 351-360
    • Varki, A.1
  • 4
    • 70349878950 scopus 로고    scopus 로고
    • Sialic acids as regulators of molecular and cellular interactions
    • R. Schauer Sialic acids as regulators of molecular and cellular interactions Curr Opin Struct Biol 19 2009 507 514
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 507-514
    • Schauer, R.1
  • 5
    • 0029990367 scopus 로고    scopus 로고
    • In vivo enzymatic removal of alpha 2>6-linked sialic acid from the glomerular filtration barrier results in podocyte charge alteration and glomerular injury
    • H. Gelberg, L. Healy, H. Whiteley, L.A. Miller, E. Vimr In vivo enzymatic removal of alpha 2>6-linked sialic acid from the glomerular filtration barrier results in podocyte charge alteration and glomerular injury Lab Invest 74 1996 907 920
    • (1996) Lab Invest , vol.74 , pp. 907-920
    • Gelberg, H.1    Healy, L.2    Whiteley, H.3    Miller, L.A.4    Vimr, E.5
  • 6
    • 34249867986 scopus 로고    scopus 로고
    • Sizing up sialic acid in glomerular disease
    • S.E. Quaggin Sizing up sialic acid in glomerular disease J Clin Invest 117 2007 1480 1483
    • (2007) J Clin Invest , vol.117 , pp. 1480-1483
    • Quaggin, S.E.1
  • 7
    • 0015876502 scopus 로고
    • Glomerular sialic acid and proteinuria in human renal disease
    • E.B. Blau, J.E. Haas Glomerular sialic acid and proteinuria in human renal disease Lab Invest 28 1973 477 481
    • (1973) Lab Invest , vol.28 , pp. 477-481
    • Blau, E.B.1    Haas, J.E.2
  • 8
    • 0023121603 scopus 로고
    • Ultrastructural alterations in the sialic acid distribution in minimal change disease and membranous glomerulonephritis
    • J. Quatacker, M. Praet, E. Matthys Ultrastructural alterations in the sialic acid distribution in minimal change disease and membranous glomerulonephritis Pathol Res Pract 182 1987 188 194
    • (1987) Pathol Res Pract , vol.182 , pp. 188-194
    • Quatacker, J.1    Praet, M.2    Matthys, E.3
  • 9
    • 2342580146 scopus 로고    scopus 로고
    • Aberrant glycosylation in IgA nephropathy (IgAN)
    • R. Coppo, A. Amore Aberrant glycosylation in IgA nephropathy (IgAN) Kidney Int 65 2004 1544 1547
    • (2004) Kidney Int , vol.65 , pp. 1544-1547
    • Coppo, R.1    Amore, A.2
  • 10
    • 76749143681 scopus 로고    scopus 로고
    • Aberrantly glycosylated IgA1 induces mesangial cells to produce platelet-activating factor that mediates nephrin loss in cultured podocytes
    • R. Coppo, V. Fonsato, S. Balegno, E. Ricotti, E. Loiacono, R. Camilla, L. Peruzzi, A. Amore, B. Bussolati, G. Camussi Aberrantly glycosylated IgA1 induces mesangial cells to produce platelet-activating factor that mediates nephrin loss in cultured podocytes Kidney Int 77 2010 417 427
    • (2010) Kidney Int , vol.77 , pp. 417-427
    • Coppo, R.1    Fonsato, V.2    Balegno, S.3    Ricotti, E.4    Loiacono, E.5    Camilla, R.6    Peruzzi, L.7    Amore, A.8    Bussolati, B.9    Camussi, G.10
  • 11
    • 0035796487 scopus 로고    scopus 로고
    • Anuria, omphalocele, and perinatal lethality in mice lacking the CD34-related protein podocalyxin
    • R. Doyonnas, D.B. Kershaw, C. Duhme, H. Merkens, S. Chelliah, T. Graf, K.M. McNagny Anuria, omphalocele, and perinatal lethality in mice lacking the CD34-related protein podocalyxin J Exp Med 194 2001 13 27
    • (2001) J Exp Med , vol.194 , pp. 13-27
    • Doyonnas, R.1    Kershaw, D.B.2    Duhme, C.3    Merkens, H.4    Chelliah, S.5    Graf, T.6    McNagny, K.M.7
  • 12
    • 0021262325 scopus 로고
    • Identification and characterization of podocalyxinthe major sialoprotein of the renal glomerular epithelial cell
    • D. Kerjaschki, D.J. Sharkey, M.G. Farquhar Identification and characterization of podocalyxinthe major sialoprotein of the renal glomerular epithelial cell J Cell Biol 98 1984 1591 1596
    • (1984) J Cell Biol , vol.98 , pp. 1591-1596
    • Kerjaschki, D.1    Sharkey, D.J.2    Farquhar, M.G.3
  • 13
    • 0035750621 scopus 로고    scopus 로고
    • Gene structure and alternative splicing of murine podocalyxin: A member of the CD34 sialomucin family
    • J. Li, Y. Li, P.D. Brophy, D.B. Kershawt Gene structure and alternative splicing of murine podocalyxin: a member of the CD34 sialomucin family DNA Seq 12 2001 407 412
    • (2001) DNA Seq , vol.12 , pp. 407-412
    • Li, J.1    Li, Y.2    Brophy, P.D.3    Kershawt, D.B.4
  • 14
  • 15
    • 0034954343 scopus 로고    scopus 로고
    • Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
    • T. Takeda, T. McQuistan, R.A. Orlando, M.G. Farquhar Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton J Clin Invest 108 2001 289 301
    • (2001) J Clin Invest , vol.108 , pp. 289-301
    • Takeda, T.1    McQuistan, T.2    Orlando, R.A.3    Farquhar, M.G.4
  • 16
    • 0021999179 scopus 로고
    • Reduced sialylation of podocalyxinthe major sialoprotein of the rat kidney glomerulusin aminonucleoside nephrosis
    • D. Kerjaschki, A.T. Vernillo, M.G. Farquhar Reduced sialylation of podocalyxinthe major sialoprotein of the rat kidney glomerulusin aminonucleoside nephrosis Am J Pathol 118 1985 343 349
    • (1985) Am J Pathol , vol.118 , pp. 343-349
    • Kerjaschki, D.1    Vernillo, A.T.2    Farquhar, M.G.3
  • 17
    • 0026729987 scopus 로고
    • The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulfate-treated rats contain the tight junction protein ZO-1
    • H. Kurihara, J.M. Anderson, D. Kerjaschki, M.G. Farquhar The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulfate-treated rats contain the tight junction protein ZO-1 Am J Pathol 141 1992 805 816
    • (1992) Am J Pathol , vol.141 , pp. 805-816
    • Kurihara, H.1    Anderson, J.M.2    Kerjaschki, D.3    Farquhar, M.G.4
  • 18
    • 0017333586 scopus 로고
    • Pathogenesis of polycation-induced alterations ("fusion") of glomerular epithelium
    • M.W. Seiler, H.G. Rennke, M.A. Venkatachalam, R.S. Cotran Pathogenesis of polycation-induced alterations ("fusion") of glomerular epithelium Lab Invest 36 1977 48 61
    • (1977) Lab Invest , vol.36 , pp. 48-61
    • Seiler, M.W.1    Rennke, H.G.2    Venkatachalam, M.A.3    Cotran, R.S.4
  • 19
    • 0018119667 scopus 로고
    • Scanning electron microscopy of the kidney glomerular epithelium after treatment with polycations in situ and in vitro
    • P.M. Andrews Scanning electron microscopy of the kidney glomerular epithelium after treatment with polycations in situ and in vitro Am J Anat 153 1978 291 303
    • (1978) Am J Anat , vol.153 , pp. 291-303
    • Andrews, P.M.1
  • 20
    • 0022629279 scopus 로고
    • Alterations in the sialic acid content of the rat glomerular filter in aminonucleoside nephrosis
    • J. Quatacker Alterations in the sialic acid content of the rat glomerular filter in aminonucleoside nephrosis Virchows Arch B Cell Pathol Incl Mol Pathol 50 1986 237 247
    • (1986) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.50 , pp. 237-247
    • Quatacker, J.1
  • 21
    • 0030827128 scopus 로고    scopus 로고
    • A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
    • S. Hinderlich, R. Stasche, R. Zeitler, W. Reutter A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase J Biol Chem 272 1997 24313 24318
    • (1997) J Biol Chem , vol.272 , pp. 24313-24318
    • Hinderlich, S.1    Stasche, R.2    Zeitler, R.3    Reutter, W.4
  • 23
    • 0039546871 scopus 로고    scopus 로고
    • Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme
    • R. Seppala, V.P. Lehto, W.A. Gahl Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme Am J Hum Genet 64 1999 1563 1569
    • (1999) Am J Hum Genet , vol.64 , pp. 1563-1569
    • Seppala, R.1    Lehto, V.P.2    Gahl, W.A.3
  • 24
    • 0021320516 scopus 로고
    • "Rimmed vacuole myopathy" sparing the quadriceps A unique disorder in Iranian Jews
    • Z. Argov, R. Yarom "Rimmed vacuole myopathy" sparing the quadriceps A unique disorder in Iranian Jews J Neurol Sci 64 1984 33 43
    • (1984) J Neurol Sci , vol.64 , pp. 33-43
    • Argov, Z.1    Yarom, R.2
  • 27
    • 70249085865 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathy: A decade of progress
    • M. Huizing, D.M. Krasnewich Hereditary inclusion body myopathy: a decade of progress Biochim Biophys Acta 1792 2009 881 887
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 881-887
    • Huizing, M.1    Krasnewich, D.M.2
  • 30
    • 0035077631 scopus 로고    scopus 로고
    • Biosynthesis of N-acetylneuraminic acid in cells lacking UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
    • S. Hinderlich, M. Berger, O.T. Keppler, M. Pawlita, W. Reutter Biosynthesis of N-acetylneuraminic acid in cells lacking UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Biol Chem 382 2001 291 297
    • (2001) Biol Chem , vol.382 , pp. 291-297
    • Hinderlich, S.1    Berger, M.2    Keppler, O.T.3    Pawlita, M.4    Reutter, W.5
  • 33
    • 0031004717 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human podocalyxin-like protein Orthologous relationship to rabbit PCLP1 and rat podocalyxin
    • D.B. Kershaw, S.G. Beck, B.L. Wharram, J.E. Wiggins, M. Goyal, P.E. Thomas, R.C. Wiggins Molecular cloning and characterization of human podocalyxin-like protein Orthologous relationship to rabbit PCLP1 and rat podocalyxin J Biol Chem 272 1997 15708 15714
    • (1997) J Biol Chem , vol.272 , pp. 15708-15714
    • Kershaw, D.B.1    Beck, S.G.2    Wharram, B.L.3    Wiggins, J.E.4    Goyal, M.5    Thomas, P.E.6    Wiggins, R.C.7
  • 34
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • T.D. Schmittgen, K.J. Livak Analyzing real-time PCR data by the comparative C(T) method Nat Protoc 3 2008 1101 1108
    • (2008) Nat Protoc , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 35
    • 0023470854 scopus 로고
    • Structure and development of the glomerular capillary wall and basement membrane
    • D.R. Abrahamson Structure and development of the glomerular capillary wall and basement membrane Am J Physiol 253 1987 F783 F794
    • (1987) Am J Physiol , vol.253
    • Abrahamson, D.R.1
  • 36
    • 0030717738 scopus 로고    scopus 로고
    • Morphogenesis of the glomerular filter: The synchronous assembly and maturation of two distinct extracellular matrices
    • K.J. McCarthy Morphogenesis of the glomerular filter: the synchronous assembly and maturation of two distinct extracellular matrices Microsc Res Tech 39 1997 233 253
    • (1997) Microsc Res Tech , vol.39 , pp. 233-253
    • McCarthy, K.J.1
  • 37
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific reagents and biological recognition molecules
    • N. Sharon Lectins: carbohydrate-specific reagents and biological recognition molecules J Biol Chem 282 2007 2753 2764
    • (2007) J Biol Chem , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 38
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • T. Iskratsch, A. Braun, K. Paschinger, I.B. Wilson Specificity analysis of lectins and antibodies using remodeled glycoproteins Anal Biochem 386 2009 133 146
    • (2009) Anal Biochem , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.4
  • 39
    • 0020488865 scopus 로고
    • Specificity of isolectins of wheat germ agglutinin for sialyloligosaccharides: A 360-MHz proton nuclear magnetic resonance binding study
    • K.A. Kronis, J.P. Carver Specificity of isolectins of wheat germ agglutinin for sialyloligosaccharides: a 360-MHz proton nuclear magnetic resonance binding study Biochemistry 21 1982 3050 3057
    • (1982) Biochemistry , vol.21 , pp. 3050-3057
    • Kronis, K.A.1    Carver, J.P.2
  • 41
    • 0016702060 scopus 로고
    • The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea)
    • R. Lotan, E. Skutelsky, D. Danon, N. Sharon The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea) J Biol Chem 250 1975 8518 8523
    • (1975) J Biol Chem , vol.250 , pp. 8518-8523
    • Lotan, R.1    Skutelsky, E.2    Danon, D.3    Sharon, N.4
  • 42
    • 0025045974 scopus 로고
    • Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: Application of jacalin-agarose
    • G.L. Hortin, B.L. Trimpe Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose Anal Biochem 188 1990 271 277
    • (1990) Anal Biochem , vol.188 , pp. 271-277
    • Hortin, G.L.1    Trimpe, B.L.2
  • 43
    • 29444435597 scopus 로고    scopus 로고
    • Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: Quantitative analysis by frontal affinity chromatography
    • K. Tachibana, S. Nakamura, H. Wang, H. Iwasaki, K. Maebara, L. Cheng, J. Hirabayashi, H. Narimatsu Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography Glycobiology 16 2006 46 53
    • (2006) Glycobiology , vol.16 , pp. 46-53
    • Tachibana, K.1    Nakamura, S.2    Wang, H.3    Iwasaki, H.4    Maebara, K.5    Cheng, L.6    Hirabayashi, J.7    Narimatsu, H.8
  • 45
    • 0029839882 scopus 로고    scopus 로고
    • Does the lectin Helix pomatia agglutinin bind to hyaluronic acid in breast and colon cancer?
    • U. Schumacher, B.S. Mitchell, S.A. Brooks, B. Delpech, A.J. Leathem Does the lectin Helix pomatia agglutinin bind to hyaluronic acid in breast and colon cancer? Acta Histochem 98 1996 435 440
    • (1996) Acta Histochem , vol.98 , pp. 435-440
    • Schumacher, U.1    Mitchell, B.S.2    Brooks, S.A.3    Delpech, B.4    Leathem, A.J.5
  • 46
    • 0026481151 scopus 로고
    • Carbohydrate binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4)
    • K.D. Puri, B. Gopalakrishnan, A. Surolia Carbohydrate binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4) FEBS Lett 312 1992 208 212
    • (1992) FEBS Lett , vol.312 , pp. 208-212
    • Puri, K.D.1    Gopalakrishnan, B.2    Surolia, A.3
  • 47
    • 33645403170 scopus 로고    scopus 로고
    • Hereditary proteinuria syndromes and mechanisms of proteinuria
    • K. Tryggvason, J. Patrakka, J. Wartiovaara Hereditary proteinuria syndromes and mechanisms of proteinuria N Engl J Med 354 2006 1387 1401
    • (2006) N Engl J Med , vol.354 , pp. 1387-1401
    • Tryggvason, K.1    Patrakka, J.2    Wartiovaara, J.3
  • 52
    • 33644806727 scopus 로고    scopus 로고
    • Morphological and functional evidence for an important role of the endothelial cell glycocalyx in the glomerular barrier
    • M. Jeansson, B. Haraldsson Morphological and functional evidence for an important role of the endothelial cell glycocalyx in the glomerular barrier Am J Physiol Renal Physiol 290 2006 F111 F116
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Jeansson, M.1    Haraldsson, B.2
  • 53
    • 0021354241 scopus 로고
    • Size and charge selective permeability defects induced in glomerular basement membrane by a polycation
    • J.L. Barnes, R.A. Radnik, E.P. Gilchrist, M.A. Venkatachalam Size and charge selective permeability defects induced in glomerular basement membrane by a polycation Kidney Int 25 1984 11 19
    • (1984) Kidney Int , vol.25 , pp. 11-19
    • Barnes, J.L.1    Radnik, R.A.2    Gilchrist, E.P.3    Venkatachalam, M.A.4
  • 54
    • 0020535249 scopus 로고
    • Anionic sites in basement membranes Differences in their electrostatic properties in continuous and fenestrated capillaries
    • A.S. Charonis, S.L. Wissig Anionic sites in basement membranes Differences in their electrostatic properties in continuous and fenestrated capillaries Microvasc Res 25 1983 265 285
    • (1983) Microvasc Res , vol.25 , pp. 265-285
    • Charonis, A.S.1    Wissig, S.L.2
  • 55
    • 0031937492 scopus 로고    scopus 로고
    • The charge for going by foot: Modifying the surface of podocytes
    • H. Pavenstdt The charge for going by foot: modifying the surface of podocytes Exp Nephrol 6 1998 98 103
    • (1998) Exp Nephrol , vol.6 , pp. 98-103
    • Pavenstdt, H.1
  • 56
    • 0017286132 scopus 로고
    • Alterations of the glomerular epithelium in acute aminonucleoside nephrosis Evidence for formation of occluding junctions and epithelial cell detachment
    • J.P. Caulfield, J.J. Reid, M.G. Farquhar Alterations of the glomerular epithelium in acute aminonucleoside nephrosis Evidence for formation of occluding junctions and epithelial cell detachment Lab Invest 34 1976 43 59
    • (1976) Lab Invest , vol.34 , pp. 43-59
    • Caulfield, J.P.1    Reid, J.J.2    Farquhar, M.G.3
  • 57
    • 0037338437 scopus 로고    scopus 로고
    • Pathophysiology of proteinuria
    • G. D'Amico, C. Bazzi Pathophysiology of proteinuria Kidney Int 63 2003 809 825
    • (2003) Kidney Int , vol.63 , pp. 809-825
    • D'Amico, G.1    Bazzi, C.2
  • 58
    • 0343416250 scopus 로고    scopus 로고
    • The stressed neonatal kidney: From pathophysiology to clinical management of neonatal vasomotor nephropathy
    • P. Tóth-Heyn, A. Drukker, J.P. Guignard The stressed neonatal kidney: from pathophysiology to clinical management of neonatal vasomotor nephropathy Pediatr Nephrol 14 2000 227 239
    • (2000) Pediatr Nephrol , vol.14 , pp. 227-239
    • Tóth-Heyn, P.1    Drukker, A.2    Guignard, J.P.3
  • 59
    • 0024573781 scopus 로고
    • Biogenesis of podocalyxinthe major glomerular sialoglycoproteinin the newborn rat kidney
    • E. Schnabel, G. Dekan, A. Miettinen, M.G. Farquhar Biogenesis of podocalyxinthe major glomerular sialoglycoproteinin the newborn rat kidney Eur J Cell Biol 48 1989 313 326
    • (1989) Eur J Cell Biol , vol.48 , pp. 313-326
    • Schnabel, E.1    Dekan, G.2    Miettinen, A.3    Farquhar, M.G.4
  • 61
    • 37849026460 scopus 로고    scopus 로고
    • Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus
    • K. Kanasaki, Y. Kanda, K. Palmsten, H. Tanjore, S.B. Lee, V.S. Lebleu, V.H. Gattone Jr, R. Kalluri Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus Dev Biol 313 2008 584 593
    • (2008) Dev Biol , vol.313 , pp. 584-593
    • Kanasaki, K.1    Kanda, Y.2    Palmsten, K.3    Tanjore, H.4    Lee, S.B.5    Lebleu, V.S.6    Gattone, Jr.V.H.7    Kalluri, R.8
  • 63
    • 78651252297 scopus 로고    scopus 로고
    • Podocyte-secreted angiopoietin-like-4 mediates proteinuria in glucocorticoid-sensitive nephrotic syndrome
    • L.C. Clement, C. Avila-Casado, C. Mace, E. Soria, W.W. Bakker, S. Kersten, S.S. Chugh Podocyte-secreted angiopoietin-like-4 mediates proteinuria in glucocorticoid-sensitive nephrotic syndrome Nat Med 17 2011 117 122
    • (2011) Nat Med , vol.17 , pp. 117-122
    • Clement, L.C.1    Avila-Casado, C.2    MacE, C.3    Soria, E.4    Bakker, W.W.5    Kersten, S.6    Chugh, S.S.7
  • 65
    • 0035164681 scopus 로고    scopus 로고
    • The murine nephrin gene is specifically expressed in kidney, brain and pancreas: Inactivation of the gene leads to massive proteinuria and neonatal death
    • H. Putaala, R. Soininen, P. Kilpelinen, J. Wartiovaara, K. Tryggvason The murine nephrin gene is specifically expressed in kidney, brain and pancreas: inactivation of the gene leads to massive proteinuria and neonatal death Hum Mol Genet 10 2001 1 8
    • (2001) Hum Mol Genet , vol.10 , pp. 1-8
    • Putaala, H.1    Soininen, R.2    Kilpelinen, P.3    Wartiovaara, J.4    Tryggvason, K.5
  • 67
    • 33947203263 scopus 로고    scopus 로고
    • Identification of N-linked glycosylation sites in human nephrin using mass spectrometry
    • J. Khoshnoodi, S. Hill, K. Tryggvason, B. Hudson, D.B. Friedman Identification of N-linked glycosylation sites in human nephrin using mass spectrometry J Mass Spectrom 42 2007 370 379
    • (2007) J Mass Spectrom , vol.42 , pp. 370-379
    • Khoshnoodi, J.1    Hill, S.2    Tryggvason, K.3    Hudson, B.4    Friedman, D.B.5
  • 68
    • 0032730875 scopus 로고    scopus 로고
    • Unraveling the mechanisms of glomerular ultrafiltration: Nephrin, a key component of the slit diaphragm
    • K. Tryggvason Unraveling the mechanisms of glomerular ultrafiltration: nephrin, a key component of the slit diaphragm J Am Soc Nephrol 10 1999 2440 2445
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2440-2445
    • Tryggvason, K.1
  • 69
    • 0036238921 scopus 로고    scopus 로고
    • N-linked glycosylation is critical for the plasma membrane localization of nephrin
    • K. Yan, J. Khoshnoodi, V. Ruotsalainen, K. Tryggvason N-linked glycosylation is critical for the plasma membrane localization of nephrin J Am Soc Nephrol 13 2002 1385 1389
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1385-1389
    • Yan, K.1    Khoshnoodi, J.2    Ruotsalainen, V.3    Tryggvason, K.4
  • 70
    • 45749155148 scopus 로고    scopus 로고
    • Characterization of mouse sialyltransferase genes: Their evolution and diversity
    • S. Takashima Characterization of mouse sialyltransferase genes: their evolution and diversity Biosci Biotechnol Biochem 72 2008 1155 1167
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 1155-1167
    • Takashima, S.1
  • 71
    • 0141703289 scopus 로고    scopus 로고
    • Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal i and II
    • S. Takashima, S. Tsuji, M. Tsujimoto Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II J Biochem 134 2003 287 296
    • (2003) J Biochem , vol.134 , pp. 287-296
    • Takashima, S.1    Tsuji, S.2    Tsujimoto, M.3
  • 72
    • 0030974649 scopus 로고    scopus 로고
    • Mouse beta-galactoside alpha 2,3-sialyltransferases: Comparison of in vitro substrate specificities and tissue specific expression
    • M. Kono, Y. Ohyama, Y.C. Lee, T. Hamamoto, N. Kojima, S. Tsuji Mouse beta-galactoside alpha 2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression Glycobiology 7 1997 469 479
    • (1997) Glycobiology , vol.7 , pp. 469-479
    • Kono, M.1    Ohyama, Y.2    Lee, Y.C.3    Hamamoto, T.4    Kojima, N.5    Tsuji, S.6
  • 73
    • 33748755610 scopus 로고    scopus 로고
    • Roles for UDP-GlcNAc 2-epimerase/ManNAc 6-kinase outside of sialic acid biosynthesis: Modulation of sialyltransferase and BiP expression GM3 and GD3 biosynthesis, proliferation, and apoptosis, and ERK1/2 phosphorylation
    • Z. Wang, Z. Sun, A.V. Li, K.J. Yarema Roles for UDP-GlcNAc 2-epimerase/ManNAc 6-kinase outside of sialic acid biosynthesis: modulation of sialyltransferase and BiP expression GM3 and GD3 biosynthesis, proliferation, and apoptosis, and ERK1/2 phosphorylation J Biol Chem 281 2006 27016 27028
    • (2006) J Biol Chem , vol.281 , pp. 27016-27028
    • Wang, Z.1    Sun, Z.2    Li, A.V.3    Yarema, K.J.4
  • 75
    • 77953969650 scopus 로고    scopus 로고
    • Sialic acid utilisation and synthesis in the neonatal rat revisited
    • P.I. Duncan, F. Raymond, A. Fuerholz, N. Sprenger Sialic acid utilisation and synthesis in the neonatal rat revisited PLoS One 4 2009 e8241
    • (2009) PLoS One , vol.4 , pp. 8241
    • Duncan, P.I.1    Raymond, F.2    Fuerholz, A.3    Sprenger, N.4
  • 76
    • 33750887047 scopus 로고    scopus 로고
    • Focal and segmental glomerulosclerosis
    • N. Daskalakis, M.P. Winn Focal and segmental glomerulosclerosis Cell Mol Life Sci 63 2006 2506 2511
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2506-2511
    • Daskalakis, N.1    Winn, M.P.2
  • 77
    • 33646807123 scopus 로고    scopus 로고
    • New insights into the pathogenesis of membranous glomerulonephritis
    • P. Ronco, H. Debiec New insights into the pathogenesis of membranous glomerulonephritis Curr Opin Nephrol Hypertens 15 2006 258 263
    • (2006) Curr Opin Nephrol Hypertens , vol.15 , pp. 258-263
    • Ronco, P.1    Debiec, H.2
  • 78
    • 68949192362 scopus 로고    scopus 로고
    • Clinical approach to lupus nephritis: Recent advances
    • C. Molino, F. Fabbian, C. Longhini Clinical approach to lupus nephritis: recent advances Eur J Intern Med 20 2009 447 453
    • (2009) Eur J Intern Med , vol.20 , pp. 447-453
    • Molino, C.1    Fabbian, F.2    Longhini, C.3
  • 79
    • 27644551257 scopus 로고    scopus 로고
    • Genetics of idiopathic nephrotic syndrome
    • A.N. Vats Genetics of idiopathic nephrotic syndrome Indian J Pediatr 72 2005 777 783
    • (2005) Indian J Pediatr , vol.72 , pp. 777-783
    • Vats, A.N.1
  • 81
    • 0032999845 scopus 로고    scopus 로고
    • Effects of human alpha-1-acid glycoprotein on aminonucleoside-induced minimal change nephrosis in rats
    • E. Muchitsch, L. Pichler, H.P. Schwarz, W. Ulrich Effects of human alpha-1-acid glycoprotein on aminonucleoside-induced minimal change nephrosis in rats Nephron 81 1999 194 199
    • (1999) Nephron , vol.81 , pp. 194-199
    • Muchitsch, E.1    Pichler, L.2    Schwarz, H.P.3    Ulrich, W.4
  • 82
    • 33646178816 scopus 로고    scopus 로고
    • Beneficial effects of orosomucoid on the glomerular barrier in puromycin aminonucleoside-induced nephrosis
    • C. Hjalmarsson, M.E. Lidell, B. Haraldsson Beneficial effects of orosomucoid on the glomerular barrier in puromycin aminonucleoside-induced nephrosis Nephrol Dial Transplant 21 2006 1223 1230
    • (2006) Nephrol Dial Transplant , vol.21 , pp. 1223-1230
    • Hjalmarsson, C.1    Lidell, M.E.2    Haraldsson, B.3


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