메뉴 건너뛰기




Volumn 15, Issue 6, 2004, Pages 1382-1391

Signaling at the slit diaphragm

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADAPTOR PROTEIN; LIGAND; NEPH1 PROTEIN; NEPHRIN; PDZ DOMAIN PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 2542494061     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.ASN.0000130167.30769.55     Document Type: Review
Times cited : (227)

References (118)
  • 1
    • 0035210580 scopus 로고    scopus 로고
    • Caught flat-footed: Podocyte damage and the molecular bases of focal glomerulosclerosis
    • Kerjaschki D: Caught flat-footed: Podocyte damage and the molecular bases of focal glomerulosclerosis. J Clin Invest 108: 1583-1587, 2001
    • (2001) J Clin Invest , vol.108 , pp. 1583-1587
    • Kerjaschki, D.1
  • 2
    • 0034126357 scopus 로고    scopus 로고
    • Getting a foothold in nephrotic syndrome
    • Somlo S, Mundel P: Getting a foothold in nephrotic syndrome. Nat Genet 24: 333-335, 2000
    • (2000) Nat Genet , vol.24 , pp. 333-335
    • Somlo, S.1    Mundel, P.2
  • 4
    • 0346846450 scopus 로고    scopus 로고
    • A molecular look at the glomerular barrier
    • Miner JH: A molecular look at the glomerular barrier. Nephron Exp Nephrol 94: e119-e122, 2003
    • (2003) Nephron Exp Nephrol , vol.94
    • Miner, J.H.1
  • 5
    • 0018267031 scopus 로고
    • Molecular basis of proteinuria of glomerular origin
    • Brenner BM, Hostetter TH, Humes HD: Molecular basis of proteinuria of glomerular origin. N Engl J Med 298: 826-833, 1978
    • (1978) N Engl J Med , vol.298 , pp. 826-833
    • Brenner, B.M.1    Hostetter, T.H.2    Humes, H.D.3
  • 6
    • 0017976656 scopus 로고
    • Glomerular permselectivity: Barrier function based on discrimination of molecular size and charge
    • Brenner BM, Hostetter TH, Humes HD: Glomerular permselectivity: Barrier function based on discrimination of molecular size and charge. Am J Physiol 234: F455-F460, 1978
    • (1978) Am J Physiol , vol.234
    • Brenner, B.M.1    Hostetter, T.H.2    Humes, H.D.3
  • 7
    • 0018764211 scopus 로고
    • Glomerular permeability of macromolecules. Effect of molecular configuration on the fractional clearance of uncharged dextran and neutral horseradish peroxidase in the rat
    • Rennke HG, Venkatachalam MA: Glomerular permeability of macromolecules. Effect of molecular configuration on the fractional clearance of uncharged dextran and neutral horseradish peroxidase in the rat. J Clin Invest 63: 713-717, 1979
    • (1979) J Clin Invest , vol.63 , pp. 713-717
    • Rennke, H.G.1    Venkatachalam, M.A.2
  • 8
    • 0036175951 scopus 로고    scopus 로고
    • Genetic models: Clues for understanding the pathogenesis of idiopathic nephrotic syndrome
    • Antignac C: Genetic models: Clues for understanding the pathogenesis of idiopathic nephrotic syndrome. J Clin Invest 109: 447-449, 2002
    • (2002) J Clin Invest , vol.109 , pp. 447-449
    • Antignac, C.1
  • 9
    • 0032881370 scopus 로고    scopus 로고
    • Discovery of the congenital nephrotic syndrome gene discloses the structure of the mysterious molecular sieve of the kidney
    • Tryggvason K, Ruotsalainen V, Wartiovaara J: Discovery of the congenital nephrotic syndrome gene discloses the structure of the mysterious molecular sieve of the kidney. Int J Dev Biol 43: 445-451, 1999
    • (1999) Int J Dev Biol , vol.43 , pp. 445-451
    • Tryggvason, K.1    Ruotsalainen, V.2    Wartiovaara, J.3
  • 10
    • 0036891810 scopus 로고    scopus 로고
    • Podocyte biology and response to injury
    • Mundel P, Shankland SJ: Podocyte biology and response to injury. J Am Soc Nephrol 13: 3005-3015, 2002
    • (2002) J Am Soc Nephrol , vol.13 , pp. 3005-3015
    • Mundel, P.1    Shankland, S.J.2
  • 11
    • 0033452520 scopus 로고    scopus 로고
    • The role of the podocyte in glomerulosclerosis
    • Kriz W, Lemley KV: The role of the podocyte in glomerulosclerosis. Curr Opin Nephrol Hypertens 8: 489-497, 1999
    • (1999) Curr Opin Nephrol Hypertens , vol.8 , pp. 489-497
    • Kriz, W.1    Lemley, K.V.2
  • 12
    • 0037369891 scopus 로고    scopus 로고
    • Podocyte differentiation and glomerulogenesis
    • Kreidberg JA: Podocyte differentiation and glomerulogenesis. J Am Soc Nephrol 14: 806-814, 2003
    • (2003) J Am Soc Nephrol , vol.14 , pp. 806-814
    • Kreidberg, J.A.1
  • 13
    • 0037207471 scopus 로고    scopus 로고
    • Cell biology of the glomerular podocyte
    • Pavenstadt H, Kriz W, Kretzler M: Cell biology of the glomerular podocyte. Physiol Rev 83: 253-307, 2003
    • (2003) Physiol Rev , vol.83 , pp. 253-307
    • Pavenstadt, H.1    Kriz, W.2    Kretzler, M.3
  • 14
    • 0015953201 scopus 로고
    • Porous substructure of the glomerular slit diaphragm in the rat and mouse
    • Rodewald R, Karnovsky MJ: Porous substructure of the glomerular slit diaphragm in the rat and mouse. J Cell Biol 60: 423-433, 1974
    • (1974) J Cell Biol , vol.60 , pp. 423-433
    • Rodewald, R.1    Karnovsky, M.J.2
  • 19
    • 0032730875 scopus 로고    scopus 로고
    • Unraveling the mechanisms of glomerular ultrafiltration: Nephrin, a key component of the slit diaphragm
    • Tryggvason K: Unraveling the mechanisms of glomerular ultrafiltration: Nephrin, a key component of the slit diaphragm. J Am Soc Nephrol 10: 2440-2445, 1999
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2440-2445
    • Tryggvason, K.1
  • 21
    • 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
    • Putaala H, Soininen R, Kilpelainen P, Wartiovaara J, Tryggvason K: 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: 1-8, 2001
    • (2001) Hum Mol Genet , vol.10 , pp. 1-8
    • Putaala, H.1    Soininen, R.2    Kilpelainen, P.3    Wartiovaara, J.4    Tryggvason, K.5
  • 25
    • 0038641811 scopus 로고    scopus 로고
    • Mice lacking the giant protocadherin mFAT1 exhibit renal slit junction abnormalities and a partially penetrant cyclopia and anophthalmia phenotype
    • Ciani L, Patel A, Allen ND, Ffrench-Constant C: Mice lacking the giant protocadherin mFAT1 exhibit renal slit junction abnormalities and a partially penetrant cyclopia and anophthalmia phenotype. Mol Cell Biol 23: 3575-3582, 2003
    • (2003) Mol Cell Biol , vol.23 , pp. 3575-3582
    • Ciani, L.1    Patel, A.2    Allen, N.D.3    Ffrench-Constant, C.4
  • 31
    • 0035191415 scopus 로고    scopus 로고
    • CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain
    • Shih NY, Li J, Cotran R, Mundel P, Miner JH, Shaw AS: CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain. Am J Pathol 159: 2303-2308, 2001
    • (2001) Am J Pathol , vol.159 , pp. 2303-2308
    • Shih, N.Y.1    Li, J.2    Cotran, R.3    Mundel, P.4    Miner, J.H.5    Shaw, A.S.6
  • 33
    • 0344120816 scopus 로고    scopus 로고
    • CD2-associated protein and glomerular disease
    • Wolf G, Stahl RA: CD2-associated protein and glomerular disease. Lancet 362: 1746-1748, 2003
    • (2003) Lancet , vol.362 , pp. 1746-1748
    • Wolf, G.1    Stahl, R.A.2
  • 38
    • 0346121526 scopus 로고    scopus 로고
    • Molecular basis of the functional podocin-nephrin complex: Mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains
    • Huber TB, Simons M, Hartleben B, Sernetz L, Schmidts M, Gundlach E, Saleem MA, Walz G, Benzing T: Molecular basis of the functional podocin-nephrin complex: Mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains. Hum Mol Genet 12: 3397-3405, 2003
    • (2003) Hum Mol Genet , vol.12 , pp. 3397-3405
    • Huber, T.B.1    Simons, M.2    Hartleben, B.3    Sernetz, L.4    Schmidts, M.5    Gundlach, E.6    Saleem, M.A.7    Walz, G.8    Benzing, T.9
  • 39
    • 0642367851 scopus 로고    scopus 로고
    • Signal transduction: Molecular monogamy
    • Endy D, Yaffe MB: Signal transduction: Molecular monogamy. Nature 426: 614-615, 2003
    • (2003) Nature , vol.426 , pp. 614-615
    • Endy, D.1    Yaffe, M.B.2
  • 40
    • 0036518996 scopus 로고    scopus 로고
    • Phosphotyrosine-binding domains in signal transduction
    • Yaffe MB: Phosphotyrosine-binding domains in signal transduction. Nat Rev Mol Cell Biol 3: 177-186, 2002
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 177-186
    • Yaffe, M.B.1
  • 41
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • Yaffe MB, Elia AE: Phosphoserine/threonine-binding domains. Curr Opin Cell Biol 13: 131-138, 2001
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 42
    • 0028953668 scopus 로고
    • Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes
    • Kurihara H, Anderson JM, Farquhar MG: Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes. Am J Physiol 268: F514-F524, 1995
    • (1995) Am J Physiol , vol.268
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 44
    • 0034858027 scopus 로고    scopus 로고
    • Involvement of lipid rafts in nephrin phosphorylation and organization of the glomerular slit diaphragm
    • Simons M, Schwarz K, Kriz W, Miettinen A, Reiser J, Mundel P, Holthofer H: Involvement of lipid rafts in nephrin phosphorylation and organization of the glomerular slit diaphragm. Am J Pathol 159: 1069-1077, 2001
    • (2001) Am J Pathol , vol.159 , pp. 1069-1077
    • Simons, M.1    Schwarz, K.2    Kriz, W.3    Miettinen, A.4    Reiser, J.5    Mundel, P.6    Holthofer, H.7
  • 46
    • 0035182146 scopus 로고    scopus 로고
    • Lupus-like kidney disease in mice deficient in the Src family tyrosine kinases Lyn and Fyn
    • Yu CC, Yen TS, Lowell CA, DeFranco AL: Lupus-like kidney disease in mice deficient in the Src family tyrosine kinases Lyn and Fyn. Curr Biol 11: 34-38, 2001
    • (2001) Curr Biol , vol.11 , pp. 34-38
    • Yu, C.C.1    Yen, T.S.2    Lowell, C.A.3    DeFranco, A.L.4
  • 47
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T: Protein modules and signalling networks. Nature 373: 573-580, 1995
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 48
    • 0035080918 scopus 로고    scopus 로고
    • PhosphoSerine/threonine binding domains: You can't pSERious?
    • Yaffe MB, Smerdon SJ: PhosphoSerine/threonine binding domains: you can't pSERious? Structure (Camb) 9: R33-R38, 2001
    • (2001) Structure (Camb) , vol.9
    • Yaffe, M.B.1    Smerdon, S.J.2
  • 49
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC: The phosphoinositide 3-kinase pathway. Science 296: 1655-1657, 2002
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 50
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J: Mechanisms and consequences of activation of protein kinase B/Akt. Curr Opin Cell Biol 10: 262-267, 1998
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 262-267
    • Downward, J.1
  • 51
    • 0033452520 scopus 로고    scopus 로고
    • The role of the podocyte in glomerulosclerosis
    • Kriz W, Lemley KV: The role of the podocyte in glomerulosclerosis. Curr Opin Nephrol Hypertens 8: 489-497, 1999
    • (1999) Curr Opin Nephrol Hypertens , vol.8 , pp. 489-497
    • Kriz, W.1    Lemley, K.V.2
  • 52
    • 0007617245 scopus 로고
    • How does glomerular epithelial cell injury contribute to progressive glomerular damage?
    • Rennke HG: How does glomerular epithelial cell injury contribute to progressive glomerular damage? Kidney Int Suppl 45: S58-S63, 1994
    • (1994) Kidney Int Suppl , vol.45
    • Rennke, H.G.1
  • 55
    • 0031800504 scopus 로고    scopus 로고
    • Podocytes and the development of segmental glomerulosclerosis
    • Elger M, Kriz W: Podocytes and the development of segmental glomerulosclerosis. Nephrol Dial Transplant 13: 1368-1373, 1998
    • (1998) Nephrol Dial Transplant , vol.13 , pp. 1368-1373
    • Elger, M.1    Kriz, W.2
  • 56
    • 0024514345 scopus 로고
    • Glomerular hypertrophy and epithelial cell injury modulate progressive glomerulosclerosis in the rat
    • Fries JW, Sandstrom DJ, Meyer TW, Rennke HG: Glomerular hypertrophy and epithelial cell injury modulate progressive glomerulosclerosis in the rat. Lab Invest 60: 205-218, 1989
    • (1989) Lab Invest , vol.60 , pp. 205-218
    • Fries, J.W.1    Sandstrom, D.J.2    Meyer, T.W.3    Rennke, H.G.4
  • 57
    • 0031706336 scopus 로고    scopus 로고
    • Progression of glomerular diseases: Is the podocyte the culprit?
    • Kriz W, Gretz N, Lemley KV: Progression of glomerular diseases: Is the podocyte the culprit? Kidney Int 54: 687-697, 1998
    • (1998) Kidney Int , vol.54 , pp. 687-697
    • Kriz, W.1    Gretz, N.2    Lemley, K.V.3
  • 58
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran P, Kowanetz K, Szymkiewicz I, Langdon WY, Dikic I: Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416: 183-187, 2002
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 60
    • 0037040881 scopus 로고    scopus 로고
    • Regulation of collagenase expression during replicative senescence in human fibroblasts by Akt-forkhead signaling
    • Mawal-Dewan M, Lorenzini A, Frisoni L, Zhang H, Cristofalo VJ, Sell C: Regulation of collagenase expression during replicative senescence in human fibroblasts by Akt-forkhead signaling. J Biol Chem 277: 7857-7864, 2002
    • (2002) J Biol Chem , vol.277 , pp. 7857-7864
    • Mawal-Dewan, M.1    Lorenzini, A.2    Frisoni, L.3    Zhang, H.4    Cristofalo, V.J.5    Sell, C.6
  • 61
    • 0037084569 scopus 로고    scopus 로고
    • Genotype/phenotype correlations of NPHS1 and NPHS2 mutations in nephrotic syndrome advocate a functional inter-relationship in glomerular filtration
    • Koziell A, Grech V, Hussain S, Lee G, Lenkkeri U, Tryggvason K, Scambler P: Genotype/phenotype correlations of NPHS1 and NPHS2 mutations in nephrotic syndrome advocate a functional inter-relationship in glomerular filtration. Hum Mol Genet 11: 379-388, 2002
    • (2002) Hum Mol Genet , vol.11 , pp. 379-388
    • Koziell, A.1    Grech, V.2    Hussain, S.3    Lee, G.4    Lenkkeri, U.5    Tryggvason, K.6    Scambler, P.7
  • 63
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D: Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39, 2000
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 64
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E: Functional rafts in cell membranes. Nature 387: 569-572, 1997
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 67
    • 0037379340 scopus 로고    scopus 로고
    • Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and NEPH1
    • Gerke P, Huber TB, Sellin L, Benzing T, Walz G: Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and NEPH1. J Am Soc Nephrol 14: 918-926, 2003
    • (2003) J Am Soc Nephrol , vol.14 , pp. 918-926
    • Gerke, P.1    Huber, T.B.2    Sellin, L.3    Benzing, T.4    Walz, G.5
  • 69
    • 0037805606 scopus 로고    scopus 로고
    • Nephrin and Nephl co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers
    • Barletta GM, Kovari IA, Verma RK, Kerjaschki D, Holzman LB: Nephrin and Nephl co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers. J Biol Chem 278: 19266-19271, 2003
    • (2003) J Biol Chem , vol.278 , pp. 19266-19271
    • Barletta, G.M.1    Kovari, I.A.2    Verma, R.K.3    Kerjaschki, D.4    Holzman, L.B.5
  • 70
    • 0042242818 scopus 로고    scopus 로고
    • Nephl and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability
    • Liu G, Kaw B, Kurfis J, Rahmanuddin S, Kanwar YS, Chugh SS: Nephl and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability. J Clin Invest 112: 209-221, 2003
    • (2003) J Clin Invest , vol.112 , pp. 209-221
    • Liu, G.1    Kaw, B.2    Kurfis, J.3    Rahmanuddin, S.4    Kanwar, Y.S.5    Chugh, S.S.6
  • 72
    • 0035161741 scopus 로고    scopus 로고
    • Characterization of Drosophila hibris, a gene related to human nephrin
    • Dworak HA, Charles MA, Pellerano LB, Sink H: Characterization of Drosophila hibris, a gene related to human nephrin., Development 128: 4265-4276, 2001
    • (2001) Development , vol.128 , pp. 4265-4276
    • Dworak, H.A.1    Charles, M.A.2    Pellerano, L.B.3    Sink, H.4
  • 74
    • 0027767583 scopus 로고
    • The irregular chiasm C-roughest locus of Drosophila, which affects axonal projections and programmed cell death, encodes a novel immunoglobulin-like protein
    • Ramos RG, Igloi GL, Lichte B, Baumann U, Maier D, Schneider T, Brandstatter JH, Frohlich A, Fischbach KF: The irregular chiasm C-roughest locus of Drosophila, which affects axonal projections and programmed cell death, encodes a novel immunoglobulin-like protein. Genes Dev 7: 2533-2547, 1993
    • (1993) Genes Dev , vol.7 , pp. 2533-2547
    • Ramos, R.G.1    Igloi, G.L.2    Lichte, B.3    Baumann, U.4    Maier, D.5    Schneider, T.6    Brandstatter, J.H.7    Frohlich, A.8    Fischbach, K.F.9
  • 75
    • 0034697954 scopus 로고    scopus 로고
    • Drosophila dumbfounded: A myoblast attractant essential for fusion
    • Ruiz-Gomez M, Coutts N, Price A, Taylor MV, Bate M: Drosophila dumbfounded: A myoblast attractant essential for fusion. Cell 102: 189-198, 2000
    • (2000) Cell , vol.102 , pp. 189-198
    • Ruiz-Gomez, M.1    Coutts, N.2    Price, A.3    Taylor, M.V.4    Bate, M.5
  • 76
    • 0034659374 scopus 로고    scopus 로고
    • Drosophila SNS, a member of the immunoglobulin superfamily that is essential for myoblast fusion
    • Bour BA, Chakravarti M, West JM, Abmayr SM: Drosophila SNS, a member of the immunoglobulin superfamily that is essential for myoblast fusion. Genes Dev 14: 1498-1511, 2000
    • (2000) Genes Dev , vol.14 , pp. 1498-1511
    • Bour, B.A.1    Chakravarti, M.2    West, J.M.3    Abmayr, S.M.4
  • 77
    • 0035173597 scopus 로고    scopus 로고
    • The immunoglobulin-like protein Hibris functions as a dose-dependent regulator of myoblast fusion and is differentially controlled by Ras and Notch signaling
    • Artero RD, Castanon I, Baylies MK: The immunoglobulin-like protein Hibris functions as a dose-dependent regulator of myoblast fusion and is differentially controlled by Ras and Notch signaling. Development 128: 4251-4264, 2001
    • (2001) Development , vol.128 , pp. 4251-4264
    • Artero, R.D.1    Castanon, I.2    Baylies, M.K.3
  • 78
    • 0037423919 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein SYG-1 determines the location of specific synapses in C. elegans
    • Shen K, Bargmann CI: The immunoglobulin superfamily protein SYG-1 determines the location of specific synapses in C. elegans. Cell 112: 619-630, 2003
    • (2003) Cell , vol.112 , pp. 619-630
    • Shen, K.1    Bargmann, C.I.2
  • 79
    • 0036080664 scopus 로고    scopus 로고
    • Podocyte slit-diaphragm protein nephrin is linked to the actin cytoskeleton
    • Yuan H, Takeuchi E, Salant DJ: Podocyte slit-diaphragm protein nephrin is linked to the actin cytoskeleton. Am J Physiol Renal Physiol 282: F585-F591, 2002
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Yuan, H.1    Takeuchi, E.2    Salant, D.J.3
  • 80
    • 0036791605 scopus 로고    scopus 로고
    • Co-localization of nephrin, podocin, and the actin cytoskeleton: Evidence for a role in podocyte foot process formation
    • Saleem MA, Ni L, Witherden I, Tryggvason K, Ruotsalainen V, Mundel P, Mathieson PW: Co-localization of nephrin, podocin, and the actin cytoskeleton: Evidence for a role in podocyte foot process formation. Am J Pathol 161: 1459-1466, 2002
    • (2002) Am J Pathol , vol.161 , pp. 1459-1466
    • Saleem, M.A.1    Ni, L.2    Witherden, I.3    Tryggvason, K.4    Ruotsalainen, V.5    Mundel, P.6    Mathieson, P.W.7
  • 81
  • 82
    • 0036783544 scopus 로고    scopus 로고
    • CD2-associated protein directly interacts with the actin cytoskeleton
    • Lehtonen S, Zhao F, Lehtonen E: CD2-associated protein directly interacts with the actin cytoskeleton. Am J Physiol Renal Physiol 283: F734-F743, 2002
    • (2002) Am J Physiol Renal Physiol , vol.283
    • Lehtonen, S.1    Zhao, F.2    Lehtonen, E.3
  • 83
    • 0345282940 scopus 로고    scopus 로고
    • Actin filament organization of foot processes in rat podocytes
    • Ichimura K, Kurihara H, Sakai T: Actin filament organization of foot processes in rat podocytes. J Histochem Cytochem 51: 1589-1600, 2003
    • (2003) J Histochem Cytochem , vol.51 , pp. 1589-1600
    • Ichimura, K.1    Kurihara, H.2    Sakai, T.3
  • 84
    • 0037093347 scopus 로고    scopus 로고
    • Mechanism of the process formation; podocytes vs. neurons
    • Kobayashi N: Mechanism of the process formation; podocytes vs. neurons. Microsc Res Tech 57: 217-223, 2002
    • (2002) Microsc Res Tech , vol.57 , pp. 217-223
    • Kobayashi, N.1
  • 85
    • 0024209817 scopus 로고
    • Ultrastructural organization of contractile and cytoskeletal proteins in glomerular podocytes of chicken, rat, and man
    • Drenckhahn D, Franke RP: Ultrastructural organization of contractile and cytoskeletal proteins in glomerular podocytes of chicken, rat, and man. Lab Invest 59: 673-682, 1988
    • (1988) Lab Invest , vol.59 , pp. 673-682
    • Drenckhahn, D.1    Franke, R.P.2
  • 86
    • 0037590956 scopus 로고    scopus 로고
    • Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85
    • Hutchings NJ, Clarkson N, Chalkley R, Barclay AN, Brown MH: Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. J Biol Chem 278: 22396-22403, 2003
    • (2003) J Biol Chem , vol.278 , pp. 22396-22403
    • Hutchings, N.J.1    Clarkson, N.2    Chalkley, R.3    Barclay, A.N.4    Brown, M.H.5
  • 87
    • 0038498066 scopus 로고    scopus 로고
    • A Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton
    • Lynch DK, Winata SC, Lyons RJ, Hughes WE, Lehrbach GM, Wasinger V, Corthals G, Cordwell S, Daly RJ: A Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton. J Biol Chem 278: 21805-21813, 2003
    • (2003) J Biol Chem , vol.278 , pp. 21805-21813
    • Lynch, D.K.1    Winata, S.C.2    Lyons, R.J.3    Hughes, W.E.4    Lehrbach, G.M.5    Wasinger, V.6    Corthals, G.7    Cordwell, S.8    Daly, R.J.9
  • 88
    • 0037241232 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse
    • Badour K, Zhang J, Shi F, McGavin MK, Rampersad V, Hardy LA, Field D, Siminovitch KA: The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse. Immunity 18: 141-154, 2003
    • (2003) Immunity , vol.18 , pp. 141-154
    • Badour, K.1    Zhang, J.2    Shi, F.3    McGavin, M.K.4    Rampersad, V.5    Hardy, L.A.6    Field, D.7    Siminovitch, K.A.8
  • 89
    • 0027322037 scopus 로고
    • Divalency of the monoclonal antibody 5-1-6 is required for induction of proteinuria in rats
    • Narisawa M, Kawachi H, Oite T, Shimizu F: Divalency of the monoclonal antibody 5-1-6 is required for induction of proteinuria in rats. Clin Exp Immunol 92: 522-526, 1993
    • (1993) Clin Exp Immunol , vol.92 , pp. 522-526
    • Narisawa, M.1    Kawachi, H.2    Oite, T.3    Shimizu, F.4
  • 95
    • 0036209849 scopus 로고    scopus 로고
    • Nephrin dissociates from actin, and its expression is reduced in early experimental membranous nephropathy
    • Yuan H, Takeuchi E, Taylor GA, McLaughlin M, Brown D, Salant DJ: Nephrin dissociates from actin, and its expression is reduced in early experimental membranous nephropathy. J Am Soc Nephrol 13: 946-956, 2002
    • (2002) J Am Soc Nephrol , vol.13 , pp. 946-956
    • Yuan, H.1    Takeuchi, E.2    Taylor, G.A.3    McLaughlin, M.4    Brown, D.5    Salant, D.J.6
  • 96
    • 0344708488 scopus 로고    scopus 로고
    • Complement mediates nephrin redistribution and actin dissociation in experimental membranous nephropathy
    • Saran AM, Yuan H, Takeuchi E, McLaughlin M, Salant DJ: Complement mediates nephrin redistribution and actin dissociation in experimental membranous nephropathy. Kidney Int 64: 2072-2078, 2003
    • (2003) Kidney Int , vol.64 , pp. 2072-2078
    • Saran, A.M.1    Yuan, H.2    Takeuchi, E.3    McLaughlin, M.4    Salant, D.J.5
  • 97
    • 0035863159 scopus 로고    scopus 로고
    • Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin
    • Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, Asuncion FJ, Kennedy MB: Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. J Neurosci 21: 423-433, 2001
    • (2001) J Neurosci , vol.21 , pp. 423-433
    • Walikonis, R.S.1    Oguni, A.2    Khorosheva, E.M.3    Jeng, C.J.4    Asuncion, F.J.5    Kennedy, M.B.6
  • 99
    • 0025008077 scopus 로고
    • The tight junction protein ZO-1 is concentrated along slit diaphragms of the glomerular epithelium
    • Schnabel E, Anderson JM, Farquhar MG: The tight junction protein ZO-1 is concentrated along slit diaphragms of the glomerular epithelium. J Cell Biol 111: 1255-1263, 1990
    • (1990) J Cell Biol , vol.111 , pp. 1255-1263
    • Schnabel, E.1    Anderson, J.M.2    Farquhar, M.G.3
  • 100
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung AY, Sheng M: PDZ domains: Structural modules for protein complex assembly. J Biol Chem 277: 5699-5702, 2002
    • (2002) J Biol Chem , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 102
    • 0033851771 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: Lessons from mutant animals and proteins
    • Mitic LL, Van Itallie CM, Anderson JM: Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins. Am J Physiol Gastrointest Liver Physiol 279: G250-G254, 2000
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Mitic, L.L.1    Van Itallie, C.M.2    Anderson, J.M.3
  • 103
    • 0033560065 scopus 로고    scopus 로고
    • PDZ domains: Fundamental building blocks in the organization of protein complexes at the plasma membrane
    • Fanning AS, Anderson JM: PDZ domains: Fundamental building blocks in the organization of protein complexes at the plasma membrane. J Clin Invest 103: 767-772, 1999
    • (1999) J Clin Invest , vol.103 , pp. 767-772
    • Fanning, A.S.1    Anderson, J.M.2
  • 104
    • 0036832157 scopus 로고    scopus 로고
    • Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1
    • Fanning AS, Ma TY, Anderson JM: Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1. FASEB J 16: 1835-1837, 2002
    • (2002) FASEB J , vol.16 , pp. 1835-1837
    • Fanning, A.S.1    Ma, T.Y.2    Anderson, J.M.3
  • 106
    • 0033662964 scopus 로고    scopus 로고
    • Evaluation of a new tool for exploring podocyte biology: Mouse nphs1 5′ flanking region drives LacZ expression in podocytes
    • Moeller MJ, Kovari IA, Holzman LB: Evaluation of a new tool for exploring podocyte biology: Mouse nphs1 5′ flanking region drives LacZ expression in podocytes. J Am Soc Nephrol 11: 2306-2314, 2000
    • (2000) J Am Soc Nephrol , vol.11 , pp. 2306-2314
    • Moeller, M.J.1    Kovari, I.A.2    Holzman, L.B.3
  • 108
    • 0038311846 scopus 로고    scopus 로고
    • Vertebrate and invertebrate TRPV-like mechanoreceptors
    • Mutai H, Heller S: Vertebrate and invertebrate TRPV-like mechanoreceptors. Cell Calcium 33: 471-478, 2003
    • (2003) Cell Calcium , vol.33 , pp. 471-478
    • Mutai, H.1    Heller, S.2
  • 109
    • 0037607542 scopus 로고    scopus 로고
    • Transducing touch in Caenorhabditis elegans
    • Goodman MB, Schwarz EM: Transducing touch in Caenorhabditis elegans. Annu Rev Physiol 65: 429-452, 2003
    • (2003) Annu Rev Physiol , vol.65 , pp. 429-452
    • Goodman, M.B.1    Schwarz, E.M.2
  • 111
    • 0029990765 scopus 로고    scopus 로고
    • Stability and leakiness: Opposing challenges to the glomerulus
    • Kriz W, Kretzler M, Provoost AP, Shirato I: Stability and leakiness: Opposing challenges to the glomerulus. Kidney Int 49: 1570-1574, 1996
    • (1996) Kidney Int , vol.49 , pp. 1570-1574
    • Kriz, W.1    Kretzler, M.2    Provoost, A.P.3    Shirato, I.4
  • 112
    • 0037389827 scopus 로고    scopus 로고
    • Why the kidney glomerulus does not clog: A gel permeation/diffusion hypothesis of renal function
    • Smithies O: Why the kidney glomerulus does not clog: A gel permeation/diffusion hypothesis of renal function. Proc Natl Acad Sci U S A 100: 4108-4113, 2003
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4108-4113
    • Smithies, O.1
  • 115
    • 0028817922 scopus 로고
    • Basic fibroblast growth factor augments podocyte injury and induces glomerulosclerosis in rats with experimental membranous nephropathy
    • Floege J, Kriz W, Schulze M, Susani M, Kerjaschki D, Mooney A, Couser WG, Koch KM: Basic fibroblast growth factor augments podocyte injury and induces glomerulosclerosis in rats with experimental membranous nephropathy. J Clin Invest 96: 2809-2819, 1995
    • (1995) J Clin Invest , vol.96 , pp. 2809-2819
    • Floege, J.1    Kriz, W.2    Schulze, M.3    Susani, M.4    Kerjaschki, D.5    Mooney, A.6    Couser, W.G.7    Koch, K.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.