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Volumn 5, Issue OCT, 2014, Pages

The importance of podocyte adhesion for a healthy glomerulus

Author keywords

Adhesion and signaling molecules; Cell junction; Extracellular matrix; Nephrotic syndrome; Podocyte

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 12P70; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; TUMOR NECROSIS FACTOR ALPHA;

EID: 84926680826     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2014.00160     Document Type: Review
Times cited : (99)

References (202)
  • 1
    • 34247521820 scopus 로고    scopus 로고
    • Applicability of the glomerular size distribution coefficient in assessing human glomerular volume: the Weibel and Gomez method revisited
    • Samuel T, Hoy WE, Douglas-Denton R, Hughson MD, Bertram JF. Applicability of the glomerular size distribution coefficient in assessing human glomerular volume: the Weibel and Gomez method revisited. J Anat (2007) 210:578-82. doi:10.1111/j.1469-7580.2007.00715.x
    • (2007) J Anat , vol.210 , pp. 578-582
    • Samuel, T.1    Hoy, W.E.2    Douglas-Denton, R.3    Hughson, M.D.4    Bertram, J.F.5
  • 3
    • 0037426760 scopus 로고    scopus 로고
    • Nephron number in patients with primary hypertension
    • Keller G, Zimmer G, Mall G, Ritz E, Amann K. Nephron number in patients with primary hypertension. N Engl J Med (2003) 348:101-8. doi:10.1056/NEJMoa020549
    • (2003) N Engl J Med , vol.348 , pp. 101-108
    • Keller, G.1    Zimmer, G.2    Mall, G.3    Ritz, E.4    Amann, K.5
  • 4
    • 25144500569 scopus 로고    scopus 로고
    • Recurrent glomerulonephritis in the renal allograft: an update of selected areas.
    • Couser W. Recurrent glomerulonephritis in the renal allograft: an update of selected areas. Exp Clin Transplant (2005) 3:283-8.
    • (2005) Exp Clin Transplant , vol.3 , pp. 283-288
    • Couser, W.1
  • 5
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes RO. The extracellular matrix: not just pretty fibrils. Science (2009) 326:1216-9. doi:10.1126/science.1176009
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell (2002) 110:673-87. doi:10.1016/S0092-8674(02)00971-6
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 33645403170 scopus 로고    scopus 로고
    • Hereditary proteinuria syndromes and mechanisms of proteinuria
    • Tryggvason K, Patrakka J, Wartiovaara J. Hereditary proteinuria syndromes and mechanisms of proteinuria. N Engl J Med (2006) 354:1387-401. doi:10.1056/NEJMra052131
    • (2006) N Engl J Med , vol.354 , pp. 1387-1401
    • Tryggvason, K.1    Patrakka, J.2    Wartiovaara, J.3
  • 8
    • 0028171098 scopus 로고
    • Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches
    • Miner JH, Sanes JR. Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches. J Cell Biol (1994) 127:879-91. doi:10.1083/jcb.127.3.879
    • (1994) J Cell Biol , vol.127 , pp. 879-891
    • Miner, J.H.1    Sanes, J.R.2
  • 9
    • 0030919488 scopus 로고    scopus 로고
    • The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform
    • Miner JH, Patton BL, Lentz SI, Gilbert DJ, Snider WD, Jenkins NA, et al. The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform. J Cell Biol (1997) 137:685-701. doi:10.1083/jcb.137.3.685
    • (1997) J Cell Biol , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6
  • 10
    • 0021845459 scopus 로고
    • Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity.
    • Yurchenco PD, Tsilibary EC, Charonis AS, Furthmayr H. Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity. J Biol Chem (1985) 260:7636-44.
    • (1985) J Biol Chem , vol.260 , pp. 7636-7644
    • Yurchenco, P.D.1    Tsilibary, E.C.2    Charonis, A.S.3    Furthmayr, H.4
  • 11
    • 0023818513 scopus 로고
    • The role of Ca2+ binding in the self-aggregation of laminin-nidogen complexes
    • Paulsson M. The role of Ca2+ binding in the self-aggregation of laminin-nidogen complexes. J Biol Chem (1988) 263:5425-30.
    • (1988) J Biol Chem , vol.263 , pp. 5425-5430
    • Paulsson, M.1
  • 12
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol (1999) 144:151-60. doi:10.1083/jcb.144.1.151
    • (1999) J Cell Biol , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6
  • 13
    • 3042790010 scopus 로고    scopus 로고
    • Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation
    • Miner JH, Li C, Mudd JL, Go G, Sutherland AE. Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development (2004) 131:2247-56. doi:10.1242/dev.01112
    • (2004) Development , vol.131 , pp. 2247-2256
    • Miner, J.H.1    Li, C.2    Mudd, J.L.3    Go, G.4    Sutherland, A.E.5
  • 14
    • 0025305486 scopus 로고
    • Terminal short arm domains of basement membrane laminin are critical for its self-assembly
    • Schittny JC, Yurchenco PD. Terminal short arm domains of basement membrane laminin are critical for its self-assembly. J Cell Biol (1990) 110:825-32. doi:10.1083/jcb.110.3.825
    • (1990) J Cell Biol , vol.110 , pp. 825-832
    • Schittny, J.C.1    Yurchenco, P.D.2
  • 15
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
    • Yurchenco PD, Cheng YS. Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. J Biol Chem (1993) 268:17286-99.
    • (1993) J Biol Chem , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2
  • 16
    • 84871801643 scopus 로고    scopus 로고
    • Laminin network formation studied by reconstitution of ternary nodes in solution
    • Purvis A, Hohenester E. Laminin network formation studied by reconstitution of ternary nodes in solution. J Biol Chem (2012) 287:44270-7. doi:10.1074/jbc. M112.418426
    • (2012) J Biol Chem , vol.287 , pp. 44270-44277
    • Purvis, A.1    Hohenester, E.2
  • 17
    • 0028952738 scopus 로고
    • Mapping of network-forming, heparin-binding, and alpha 1 beta 1 integrin-recognition sites within the alpha-chain short arm of laminin-1
    • Colognato-Pyke H, O'Rear JJ, Yamada Y, Carbonetto S, Cheng YS, Yurchenco PD. Mapping of network-forming, heparin-binding, and alpha 1 beta 1 integrin-recognition sites within the alpha-chain short arm of laminin-1. J Biol Chem (1995) 270:9398-406. doi:10.1074/jbc.270.16.9398
    • (1995) J Biol Chem , vol.270 , pp. 9398-9406
    • Colognato-Pyke, H.1    O'Rear, J.J.2    Yamada, Y.3    Carbonetto, S.4    Cheng, Y.S.5    Yurchenco, P.D.6
  • 18
    • 0030613628 scopus 로고    scopus 로고
    • The laminin alpha2-chain short arm mediates cell adhesion through both the alpha1beta1 and alpha2beta1 integrins
    • Colognato H, Maccarrick M, O'Rear JJ, Yurchenco PD. The laminin alpha2-chain short arm mediates cell adhesion through both the alpha1beta1 and alpha2beta1 integrins. J Biol Chem (1997) 272:29330-6. doi:10.1074/jbc.272.46.29330
    • (1997) J Biol Chem , vol.272 , pp. 29330-29336
    • Colognato, H.1    Maccarrick, M.2    O'Rear, J.J.3    Yurchenco, P.D.4
  • 19
    • 0035815633 scopus 로고    scopus 로고
    • Identification of cell-binding sites on the laminin alpha 5 N-terminal domain by site-directed mutagenesis
    • Nielsen PK, Yamada Y. Identification of cell-binding sites on the laminin alpha 5 N-terminal domain by site-directed mutagenesis. J Biol Chem (2001) 276:10906-12. doi:10.1074/jbc. M008743200
    • (2001) J Biol Chem , vol.276 , pp. 10906-10912
    • Nielsen, P.K.1    Yamada, Y.2
  • 20
    • 0037085315 scopus 로고    scopus 로고
    • Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5 chains
    • Garbe JH, Gohring W, Mann K, Timpl R, Sasaki T. Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5 chains. Biochem J (2002) 362:213-21. doi:10.1042/0264-6021:3620213
    • (2002) Biochem J , vol.362 , pp. 213-221
    • Garbe, J.H.1    Gohring, W.2    Mann, K.3    Timpl, R.4    Sasaki, T.5
  • 21
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins
    • Nishiuchi R, Takagi J, Hayashi M, Ido H, Yagi Y, Sanzen N, et al. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins. Matrix Biol (2006) 25:189-97. doi:10.1016/j.matbio.2005.12.001
    • (2006) Matrix Biol , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6
  • 22
    • 4744349621 scopus 로고
    • An unusual congenital and familial congenital malformative combination involving the eye and kidney
    • Pierson M, Cordier J, Hervouuet F, Rauber G. An unusual congenital and familial congenital malformative combination involving the eye and kidney. J Genet Hum (1963) 12:184-213.
    • (1963) J Genet Hum , vol.12 , pp. 184-213
    • Pierson, M.1    Cordier, J.2    Hervouuet, F.3    Rauber, G.4
  • 23
    • 77956293608 scopus 로고    scopus 로고
    • Mutations in the human laminin beta2 (LAMB2) gene and the associated phenotypic spectrum
    • Matejas V, Hinkes B, Alkandari F, Al-Gazali L, Annexstad E, Aytac MB, et al. Mutations in the human laminin beta2 (LAMB2) gene and the associated phenotypic spectrum. Hum Mutat (2010) 31:992-1002. doi:10.1002/humu.21304
    • (2010) Hum Mutat , vol.31 , pp. 992-1002
    • Matejas, V.1    Hinkes, B.2    Alkandari, F.3    Al-Gazali, L.4    Annexstad, E.5    Aytac, M.B.6
  • 24
    • 0029127384 scopus 로고
    • The renal glomerulus of mice lacking s-laminin/laminin beta 2: nephrosis despite molecular compensation by laminin beta 1
    • Noakes PG, Miner JH, Gautam M, Cunningham JM, Sanes JR, Merlie JP. The renal glomerulus of mice lacking s-laminin/laminin beta 2: nephrosis despite molecular compensation by laminin beta 1. Nat Genet (1995) 10:400-6. doi:10.1038/ng0895-400
    • (1995) Nat Genet , vol.10 , pp. 400-406
    • Noakes, P.G.1    Miner, J.H.2    Gautam, M.3    Cunningham, J.M.4    Sanes, J.R.5    Merlie, J.P.6
  • 25
    • 33746730496 scopus 로고    scopus 로고
    • Proteinuria precedes podocyte abnormalities inLamb2-/- mice, implicating the glomerular basement membrane as an albumin barrier
    • Jarad G, Cunningham J, Shaw AS, Miner JH. Proteinuria precedes podocyte abnormalities inLamb2-/- mice, implicating the glomerular basement membrane as an albumin barrier. J Clin Invest (2006) 116:2272-9. doi:10.1172/JCI28414
    • (2006) J Clin Invest , vol.116 , pp. 2272-2279
    • Jarad, G.1    Cunningham, J.2    Shaw, A.S.3    Miner, J.H.4
  • 26
    • 80053057998 scopus 로고    scopus 로고
    • Forced expression of laminin beta1 in podocytes prevents nephrotic syndrome in mice lacking laminin beta2, a model for Pierson syndrome
    • Suh JH, Jarad G, Vandevoorde RG, Miner JH. Forced expression of laminin beta1 in podocytes prevents nephrotic syndrome in mice lacking laminin beta2, a model for Pierson syndrome. Proc Natl Acad Sci U S A (2011) 108:15348-53. doi:10.1073/pnas.1108269108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15348-15353
    • Suh, J.H.1    Jarad, G.2    Vandevoorde, R.G.3    Miner, J.H.4
  • 27
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • Poschl E, Schlotzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development (2004) 131:1619-28. doi:10.1242/dev.01037
    • (2004) Development , vol.131 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 28
    • 0038469583 scopus 로고    scopus 로고
    • Alport's syndrome, Goodpasture's syndrome, and type IV collagen
    • Hudson BG, Tryggvason K, Sundaramoorthy M, Neilson EG. Alport's syndrome, Goodpasture's syndrome, and type IV collagen. N Engl J Med (2003) 348:2543-56. doi:10.1056/NEJMra022296
    • (2003) N Engl J Med , vol.348 , pp. 2543-2556
    • Hudson, B.G.1    Tryggvason, K.2    Sundaramoorthy, M.3    Neilson, E.G.4
  • 31
    • 84902107236 scopus 로고    scopus 로고
    • Bromine is an essential trace element for assembly of collagen IV scaffolds in tissue development and architecture
    • McCall AS, Cummings CF, Bhave G, Vanacore R, Page-McCaw A, Hudson BG. Bromine is an essential trace element for assembly of collagen IV scaffolds in tissue development and architecture. Cell (2014) 157:1380-92. doi:10.1016/j.cell.2014.05.009
    • (2014) Cell , vol.157 , pp. 1380-1392
    • McCall, A.S.1    Cummings, C.F.2    Bhave, G.3    Vanacore, R.4    Page-McCaw, A.5    Hudson, B.G.6
  • 32
    • 16644399795 scopus 로고    scopus 로고
    • The molecular basis of Goodpasture and Alport syndromes: beacons for the discovery of the collagen IV family
    • Hudson BG. The molecular basis of Goodpasture and Alport syndromes: beacons for the discovery of the collagen IV family. J Am Soc Nephrol (2004) 15:2514-27. doi:10.1097/01.ASN.0000141462.00630.76
    • (2004) J Am Soc Nephrol , vol.15 , pp. 2514-2527
    • Hudson, B.G.1
  • 33
    • 0030730063 scopus 로고    scopus 로고
    • Treatment of X-linked hereditary nephritis in samoyed dogs with angiotensin converting enzyme (ACE) inhibitor
    • Grodecki KM, Gains MJ, Baumal R, Osmond DH, Cotter B, Valli VE, et al. Treatment of X-linked hereditary nephritis in samoyed dogs with angiotensin converting enzyme (ACE) inhibitor. J Comp Pathol (1997) 117:209-25. doi:10.1016/S0021-9975(97)80016-3
    • (1997) J Comp Pathol , vol.117 , pp. 209-225
    • Grodecki, K.M.1    Gains, M.J.2    Baumal, R.3    Osmond, D.H.4    Cotter, B.5    Valli, V.E.6
  • 34
    • 0037248954 scopus 로고    scopus 로고
    • Preemptive ramipril therapy delays renal failure and reduces renal fibrosis in COL4A3-knockout mice with Alport syndrome
    • Gross O, Beirowski B, Koepke ML, Kuck J, Reiner M, Addicks K, et al. Preemptive ramipril therapy delays renal failure and reduces renal fibrosis in COL4A3-knockout mice with Alport syndrome. Kidney Int (2003) 63:438-46. doi:10.1046/j.1523-1755.2003.00779.x
    • (2003) Kidney Int , vol.63 , pp. 438-446
    • Gross, O.1    Beirowski, B.2    Koepke, M.L.3    Kuck, J.4    Reiner, M.5    Addicks, K.6
  • 35
    • 84857109752 scopus 로고    scopus 로고
    • Early angiotensin-converting enzyme inhibition in Alport syndrome delays renal failure and improves life expectancy
    • Gross O, Licht C, Anders HJ, Hoppe B, Beck B, Tonshoff B, et al. Early angiotensin-converting enzyme inhibition in Alport syndrome delays renal failure and improves life expectancy. Kidney Int (2012) 81:494-501. doi:10.1038/ki.2011.407
    • (2012) Kidney Int , vol.81 , pp. 494-501
    • Gross, O.1    Licht, C.2    Anders, H.J.3    Hoppe, B.4    Beck, B.5    Tonshoff, B.6
  • 36
    • 0026006388 scopus 로고
    • Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV
    • Fox JW, Mayer U, Nischt R, Aumailley M, Reinhardt D, Wiedemann H, et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J (1991) 10:3137-46.
    • (1991) EMBO J , vol.10 , pp. 3137-3146
    • Fox, J.W.1    Mayer, U.2    Nischt, R.3    Aumailley, M.4    Reinhardt, D.5    Wiedemann, H.6
  • 38
    • 0033615959 scopus 로고    scopus 로고
    • Perlecan maintains the integrity of cartilage and some basement membranes
    • Costell M, Gustafsson E, Aszodi A, Morgelin M, Bloch W, Hunziker E, et al. Perlecan maintains the integrity of cartilage and some basement membranes. J Cell Biol (1999) 147:1109-22. doi:10.1083/jcb.147.5.1109
    • (1999) J Cell Biol , vol.147 , pp. 1109-1122
    • Costell, M.1    Gustafsson, E.2    Aszodi, A.3    Morgelin, M.4    Bloch, W.5    Hunziker, E.6
  • 39
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • Gautam M, Noakes PG, Moscoso L, Rupp F, Scheller RH, Merlie JP, et al. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell (1996) 85:525-35. doi:10.1016/S0092-8674(00)81253-2
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.3    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6
  • 40
    • 67651089928 scopus 로고    scopus 로고
    • Glomerular filtration is normal in the absence of both agrin and perlecan-heparan sulfate from the glomerular basement membrane
    • Goldberg S, Harvey SJ, Cunningham J, Tryggvason K, Miner JH. Glomerular filtration is normal in the absence of both agrin and perlecan-heparan sulfate from the glomerular basement membrane. Nephrol Dial Transplant (2009) 24:2044-51. doi:10.1093/ndt/gfn758
    • (2009) Nephrol Dial Transplant , vol.24 , pp. 2044-2051
    • Goldberg, S.1    Harvey, S.J.2    Cunningham, J.3    Tryggvason, K.4    Miner, J.H.5
  • 41
    • 22544456862 scopus 로고    scopus 로고
    • Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice
    • Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol (2005) 25:6846-56. doi:10.1128/MCB.25.15.6846-6856.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 6846-6856
    • Bader, B.L.1    Smyth, N.2    Nedbal, S.3    Miosge, N.4    Baranowsky, A.5    Mokkapati, S.6
  • 42
    • 84885357905 scopus 로고    scopus 로고
    • Nanoscale protein architecture of the kidney glomerular basement membrane
    • Suleiman H, Zhang L, Roth R, Heuser JE, Miner JH, Shaw AS, et al. Nanoscale protein architecture of the kidney glomerular basement membrane. Elife (2013) 2:e01149. doi:10.7554/eLife.01149
    • (2013) Elife , vol.2 , pp. e01149
    • Suleiman, H.1    Zhang, L.2    Roth, R.3    Heuser, J.E.4    Miner, J.H.5    Shaw, A.S.6
  • 43
    • 84891418135 scopus 로고    scopus 로고
    • Global analysis reveals the complexity of the human glomerular extracellular matrix.
    • Lennon R, Byron A, Humphries JD, Randles MJ, Carisey A, Murphy S, et al. Global analysis reveals the complexity of the human glomerular extracellular matrix. J Am Soc Nephrol (2014) 25(5):939-51. doi:10.1681/ASN.2013030233
    • (2014) J Am Soc Nephrol , vol.25 , Issue.5 , pp. 939-951
    • Lennon, R.1    Byron, A.2    Humphries, J.D.3    Randles, M.J.4    Carisey, A.5    Murphy, S.6
  • 44
    • 84903562397 scopus 로고    scopus 로고
    • Glomerular cell cross-talk influences composition and assembly of extracellular matrix.
    • Byron A, Randles MJ, Humphries JD, Mironov A, Hamidi H, Harris S, et al. Glomerular cell cross-talk influences composition and assembly of extracellular matrix. J Am Soc Nephrol (2014) 25(5):953-66. doi:10.1681/ASN.2013070795
    • (2014) J Am Soc Nephrol , vol.25 , Issue.5 , pp. 953-966
    • Byron, A.1    Randles, M.J.2    Humphries, J.D.3    Mironov, A.4    Hamidi, H.5    Harris, S.6
  • 45
    • 84875702158 scopus 로고    scopus 로고
    • Cell-matrix adhesion of podocytes in physiology and disease
    • Sachs N, Sonnenberg A. Cell-matrix adhesion of podocytes in physiology and disease. Nat Rev Nephrol (2013) 9:200-10. doi:10.1038/nrneph.2012.291
    • (2013) Nat Rev Nephrol , vol.9 , pp. 200-210
    • Sachs, N.1    Sonnenberg, A.2
  • 47
    • 84862653023 scopus 로고    scopus 로고
    • Proteomic analysis of alpha4beta1 integrin adhesion complexes reveals alpha-subunit-dependent protein recruitment
    • Byron A, Humphries JD, Craig SE, Knight D, Humphries MJ. Proteomic analysis of alpha4beta1 integrin adhesion complexes reveals alpha-subunit-dependent protein recruitment. Proteomics (2012) 12:2107-14. doi:10.1002/pmic.201100487
    • (2012) Proteomics , vol.12 , pp. 2107-2114
    • Byron, A.1    Humphries, J.D.2    Craig, S.E.3    Knight, D.4    Humphries, M.J.5
  • 50
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6
    • Humphries JD, Byron A, Bass MD, Craig SE, Pinney JW, Knight D, et al. Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci Signal (2009) 2:ra51. doi:10.1126/scisignal.2000396
    • (2009) Sci Signal , vol.2 , pp. ra51
    • Humphries, J.D.1    Byron, A.2    Bass, M.D.3    Craig, S.E.4    Pinney, J.W.5    Knight, D.6
  • 51
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation
    • Kuo JC, Han X, Hsiao CT, Yates JR III, Waterman CM. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation. Nat Cell Biol (2011) 13:383-93. doi:10.1038/ncb2216
    • (2011) Nat Cell Biol , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates J.R, I.I.I.4    Waterman, C.M.5
  • 52
    • 84878598076 scopus 로고    scopus 로고
    • Beta1-and alphav-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments
    • Schiller HB, Hermann MR, Polleux J, Vignaud T, Zanivan S, Friedel CC, et al. Beta1-and alphav-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nat Cell Biol (2013) 15:625-36. doi:10.1038/ncb2747
    • (2013) Nat Cell Biol , vol.15 , pp. 625-636
    • Schiller, H.B.1    Hermann, M.R.2    Polleux, J.3    Vignaud, T.4    Zanivan, S.5    Friedel, C.C.6
  • 53
    • 0034637522 scopus 로고    scopus 로고
    • Integrin modulation by lateral association
    • Woods A, Couchman JR. Integrin modulation by lateral association. J Biol Chem (2000) 275:24233-6. doi:10.1074/jbc. R000001200
    • (2000) J Biol Chem , vol.275 , pp. 24233-24236
    • Woods, A.1    Couchman, J.R.2
  • 54
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • Morgan MR, Humphries MJ, Bass MD. Synergistic control of cell adhesion by integrins and syndecans. Nat Rev Mol Cell Biol (2007) 8:957-69. doi:10.1038/nrm2289
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 55
    • 0025076791 scopus 로고
    • The alpha 1-alpha 6 subunits of integrins are characteristically expressed in distinct segments of developing and adult human nephron
    • Korhonen M, Ylanne J, Laitinen L, Virtanen I. The alpha 1-alpha 6 subunits of integrins are characteristically expressed in distinct segments of developing and adult human nephron. J Cell Biol (1990) 111:1245-54. doi:10.1083/jcb.111.3.1245
    • (1990) J Cell Biol , vol.111 , pp. 1245-1254
    • Korhonen, M.1    Ylanne, J.2    Laitinen, L.3    Virtanen, I.4
  • 56
    • 0026476115 scopus 로고
    • Very late activation-3 integrin is the dominant beta 1-integrin on the glomerular capillary wall: an immunofluorescence study in nephrotic syndrome
    • Baraldi A, Furci L, Zambruno G, Rubbiani E, Annessi G, Lusvarghi E. Very late activation-3 integrin is the dominant beta 1-integrin on the glomerular capillary wall: an immunofluorescence study in nephrotic syndrome. Nephron (1992) 62:382-8. doi:10.1159/000187085
    • (1992) Nephron , vol.62 , pp. 382-388
    • Baraldi, A.1    Furci, L.2    Zambruno, G.3    Rubbiani, E.4    Annessi, G.5    Lusvarghi, E.6
  • 58
    • 84859826518 scopus 로고    scopus 로고
    • Integrin alpha3 mutations with kidney, lung, and skin disease
    • Has C, Sparta G, Kiritsi D, Weibel L, Moeller A, Vega-Warner V, et al. Integrin alpha3 mutations with kidney, lung, and skin disease. N Engl J Med (2012) 366:1508-14. doi:10.1056/NEJMoa1110813
    • (2012) N Engl J Med , vol.366 , pp. 1508-1514
    • Has, C.1    Sparta, G.2    Kiritsi, D.3    Weibel, L.4    Moeller, A.5    Vega-Warner, V.6
  • 59
    • 84870522502 scopus 로고    scopus 로고
    • Gain of glycosylation in integrin alpha3 causes lung disease and nephrotic syndrome
    • Nicolaou N, Margadant C, Kevelam SH, Lilien MR, Oosterveld MJ, Kreft M, et al. Gain of glycosylation in integrin alpha3 causes lung disease and nephrotic syndrome. J Clin Invest (2012) 122:4375-87. doi:10.1172/JCI64100
    • (2012) J Clin Invest , vol.122 , pp. 4375-4387
    • Nicolaou, N.1    Margadant, C.2    Kevelam, S.H.3    Lilien, M.R.4    Oosterveld, M.J.5    Kreft, M.6
  • 62
    • 37849026460 scopus 로고    scopus 로고
    • Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus
    • Kanasaki K, Kanda Y, Palmsten K, Tanjore H, Lee SB, Lebleu VS, et al. Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus. Dev Biol (2008) 313:584-93. doi:10.1016/j.ydbio.2007.10.047
    • (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
  • 63
    • 41149083878 scopus 로고    scopus 로고
    • Beta1 integrin expression by podocytes is required to maintain glomerular structural integrity
    • Pozzi A, Jarad G, Moeckel GW, Coffa S, Zhang X, Gewin L, et al. Beta1 integrin expression by podocytes is required to maintain glomerular structural integrity. Dev Biol (2008) 316:288-301. doi:10.1016/j.ydbio.2008.01.022
    • (2008) Dev Biol , vol.316 , pp. 288-301
    • Pozzi, A.1    Jarad, G.2    Moeckel, G.W.3    Coffa, S.4    Zhang, X.5    Gewin, L.6
  • 64
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration
    • Yauch RL, Berditchevski F, Harler MB, Reichner J, Hemler ME. Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration. Mol Biol Cell (1998) 9:2751-65. doi:10.1091/mbc.9.10.2751
    • (1998) Mol Biol Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1    Berditchevski, F.2    Harler, M.B.3    Reichner, J.4    Hemler, M.E.5
  • 65
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • Karamatic Crew V, Burton N, Kagan A, Green CA, Levene C, Flinter F, et al. CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood (2004) 104:2217-23. doi:10.1182/blood-2004-04-1512
    • (2004) Blood , vol.104 , pp. 2217-2223
    • Karamatic Crew, V.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6
  • 66
    • 53149111544 scopus 로고    scopus 로고
    • Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane
    • Baleato RM, Guthrie PL, Gubler MC, Ashman LK, Roselli S. Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane. Am J Pathol (2008) 173:927-37. doi:10.2353/ajpath.2008.071149
    • (2008) Am J Pathol , vol.173 , pp. 927-937
    • Baleato, R.M.1    Guthrie, P.L.2    Gubler, M.C.3    Ashman, L.K.4    Roselli, S.5
  • 67
    • 84855433172 scopus 로고    scopus 로고
    • Blood pressure influences end-stage renal disease of Cd151 knockout mice
    • Sachs N, Claessen N, Aten J, Kreft M, Teske GJ, Koeman A, et al. Blood pressure influences end-stage renal disease of Cd151 knockout mice. J Clin Invest (2012) 122:348-58. doi:10.1172/JCI58878
    • (2012) J Clin Invest , vol.122 , pp. 348-358
    • Sachs, N.1    Claessen, N.2    Aten, J.3    Kreft, M.4    Teske, G.J.5    Koeman, A.6
  • 68
    • 0028989243 scopus 로고
    • Integrin beta 4 mutations associated with junctional epidermolysis bullosa with pyloric atresia
    • Vidal F, Aberdam D, Miquel C, Christiano AM, Pulkkinen L, Uitto J, et al. Integrin beta 4 mutations associated with junctional epidermolysis bullosa with pyloric atresia. Nat Genet (1995) 10:229-34. doi:10.1038/ng0695-229
    • (1995) Nat Genet , vol.10 , pp. 229-234
    • Vidal, F.1    Aberdam, D.2    Miquel, C.3    Christiano, A.M.4    Pulkkinen, L.5    Uitto, J.6
  • 69
    • 0033918269 scopus 로고    scopus 로고
    • Congenital focal segmental glomerulosclerosis associated with beta4 integrin mutation and epidermolysis bullosa
    • Kambham N, Tanji N, Seigle RL, Markowitz GS, Pulkkinen L, Uitto J, et al. Congenital focal segmental glomerulosclerosis associated with beta4 integrin mutation and epidermolysis bullosa. Am J Kidney Dis (2000) 36:190-6. doi:10.1053/ajkd.2000.8293
    • (2000) Am J Kidney Dis , vol.36 , pp. 190-196
    • Kambham, N.1    Tanji, N.2    Seigle, R.L.3    Markowitz, G.S.4    Pulkkinen, L.5    Uitto, J.6
  • 70
    • 38049032013 scopus 로고    scopus 로고
    • Modification of kidney barrier function by the urokinase receptor
    • Wei C, Moller CC, Altintas MM, Li J, Schwarz K, Zacchigna S, et al. Modification of kidney barrier function by the urokinase receptor. Nat Med (2008) 14:55-63. doi:10.1038/nm1696
    • (2008) Nat Med , vol.14 , pp. 55-63
    • Wei, C.1    Moller, C.C.2    Altintas, M.M.3    Li, J.4    Schwarz, K.5    Zacchigna, S.6
  • 71
    • 84868340975 scopus 로고    scopus 로고
    • Beneficial effects of integrin alphavbeta3-blocking RGD peptides in early but not late phase of experimental glomerulonephritis
    • Amann K, Haas CS, Schussler J, Daniel C, Hartner A, Schocklmann HO. Beneficial effects of integrin alphavbeta3-blocking RGD peptides in early but not late phase of experimental glomerulonephritis. Nephrol Dial Transplant (2012) 27:1755-68. doi:10.1093/ndt/gfr603
    • (2012) Nephrol Dial Transplant , vol.27 , pp. 1755-1768
    • Amann, K.1    Haas, C.S.2    Schussler, J.3    Daniel, C.4    Hartner, A.5    Schocklmann, H.O.6
  • 72
    • 79961132981 scopus 로고    scopus 로고
    • Circulating urokinase receptor as a cause of focal segmental glomerulosclerosis
    • Wei C, El Hindi S, Li J, Fornoni A, Goes N, Sageshima J, et al. Circulating urokinase receptor as a cause of focal segmental glomerulosclerosis. Nat Med (2011) 17:952-60. doi:10.1038/nm.2411
    • (2011) Nat Med , vol.17 , pp. 952-960
    • Wei, C.1    El Hindi, S.2    Li, J.3    Fornoni, A.4    Goes, N.5    Sageshima, J.6
  • 73
    • 5444242206 scopus 로고    scopus 로고
    • The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells
    • Beauvais DM, Burbach BJ, Rapraeger AC. The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells. J Cell Biol (2004) 167:171-81. doi:10.1083/jcb.200404171
    • (2004) J Cell Biol , vol.167 , pp. 171-181
    • Beauvais, D.M.1    Burbach, B.J.2    Rapraeger, A.C.3
  • 74
    • 33845914882 scopus 로고    scopus 로고
    • Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1
    • Hozumi K, Suzuki N, Nielsen PK, Nomizu M, Yamada Y. Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. J Biol Chem (2006) 281:32929-40. doi:10.1074/jbc. M605708200
    • (2006) J Biol Chem , vol.281 , pp. 32929-32940
    • Hozumi, K.1    Suzuki, N.2    Nielsen, P.K.3    Nomizu, M.4    Yamada, Y.5
  • 75
    • 33746067151 scopus 로고    scopus 로고
    • Syndecan-1 regulates alphavbeta5 integrin activity in B82L fibroblasts
    • McQuade KJ, Beauvais DM, Burbach BJ, Rapraeger AC. Syndecan-1 regulates alphavbeta5 integrin activity in B82L fibroblasts. J Cell Sci (2006) 119:2445-56. doi:10.1242/jcs.02970
    • (2006) J Cell Sci , vol.119 , pp. 2445-2456
    • McQuade, K.J.1    Beauvais, D.M.2    Burbach, B.J.3    Rapraeger, A.C.4
  • 76
    • 34248215134 scopus 로고    scopus 로고
    • The short arm of laminin gamma2 chain of laminin-5 (laminin-332) binds syndecan-1 and regulates cellular adhesion and migration by suppressing phosphorylation of integrin beta4 chain
    • Ogawa T, Tsubota Y, Hashimoto J, Kariya Y, Miyazaki K. The short arm of laminin gamma2 chain of laminin-5 (laminin-332) binds syndecan-1 and regulates cellular adhesion and migration by suppressing phosphorylation of integrin beta4 chain. Mol Biol Cell (2007) 18:1621-33. doi:10.1091/mbc. E06-09-0806
    • (2007) Mol Biol Cell , vol.18 , pp. 1621-1633
    • Ogawa, T.1    Tsubota, Y.2    Hashimoto, J.3    Kariya, Y.4    Miyazaki, K.5
  • 78
    • 70549101138 scopus 로고    scopus 로고
    • Integrins: masters and slaves of endocytic transport
    • Caswell PT, Vadrevu S, Norman JC. Integrins: masters and slaves of endocytic transport. Nat Rev Mol Cell Biol (2009) 10:843-53. doi:10.1038/nrm2799
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 843-853
    • Caswell, P.T.1    Vadrevu, S.2    Norman, J.C.3
  • 79
    • 74049160017 scopus 로고    scopus 로고
    • Clathrin mediates integrin endocytosis for focal adhesion disassembly in migrating cells
    • Ezratty EJ, Bertaux C, Marcantonio EE, Gundersen GG. Clathrin mediates integrin endocytosis for focal adhesion disassembly in migrating cells. J Cell Biol (2009) 187:733-47. doi:10.1083/jcb.200904054
    • (2009) J Cell Biol , vol.187 , pp. 733-747
    • Ezratty, E.J.1    Bertaux, C.2    Marcantonio, E.E.3    Gundersen, G.G.4
  • 81
    • 33749441307 scopus 로고    scopus 로고
    • The role of syndecans in disease and wound healing
    • Fears CY, Woods A. The role of syndecans in disease and wound healing. Matrix Biol (2006) 25:443-56. doi:10.1016/j.matbio.2006.07.003
    • (2006) Matrix Biol , vol.25 , pp. 443-456
    • Fears, C.Y.1    Woods, A.2
  • 82
    • 33646076452 scopus 로고    scopus 로고
    • Heparan sulfate in trans potentiates VEGFR-mediated angiogenesis
    • Jakobsson L, Kreuger J, Holmborn K, Lundin L, Eriksson I, Kjellen L, et al. Heparan sulfate in trans potentiates VEGFR-mediated angiogenesis. Dev Cell (2006) 10:625-34. doi:10.1016/j.devcel.2006.03.009
    • (2006) Dev Cell , vol.10 , pp. 625-634
    • Jakobsson, L.1    Kreuger, J.2    Holmborn, K.3    Lundin, L.4    Eriksson, I.5    Kjellen, L.6
  • 83
    • 78349308738 scopus 로고    scopus 로고
    • Podocytes require the engagement of cell surface heparan sulfate proteoglycans for adhesion to extracellular matrices
    • Chen S, Wassenhove-McCarthy D, Yamaguchi Y, Holzman L, Van Kuppevelt TH, Orr AW, et al. Podocytes require the engagement of cell surface heparan sulfate proteoglycans for adhesion to extracellular matrices. Kidney Int (2010) 78:1088-99. doi:10.1038/ki.2010.136
    • (2010) Kidney Int , vol.78 , pp. 1088-1099
    • Chen, S.1    Wassenhove-McCarthy, D.2    Yamaguchi, Y.3    Holzman, L.4    Van Kuppevelt, T.H.5    Orr, A.W.6
  • 85
    • 84867519785 scopus 로고    scopus 로고
    • Soluble FLT1 binds lipid microdomains in podocytes to control cell morphology and glomerular barrier function
    • Jin J, Sison K, Li C, Tian R, Wnuk M, Sung HK, et al. Soluble FLT1 binds lipid microdomains in podocytes to control cell morphology and glomerular barrier function. Cell (2012) 151:384-99. doi:10.1016/j.cell.2012.08.037
    • (2012) Cell , vol.151 , pp. 384-399
    • Jin, J.1    Sison, K.2    Li, C.3    Tian, R.4    Wnuk, M.5    Sung, H.K.6
  • 86
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol (1993) 122:809-23. doi:10.1083/jcb.122.4.809
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 87
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee SH, Blacher RW, Douville PJ, Provost PR, Yurchenco PD, Carbonetto S. Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J Biol Chem (1993) 268:14972-80.
    • (1993) J Biol Chem , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 89
    • 0033839003 scopus 로고    scopus 로고
    • Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies
    • Raats CJ, Van Den Born J, Bakker MA, Oppers-Walgreen B, Pisa BJ, Dijkman HB, et al. Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies. Am J Pathol (2000) 156:1749-65. doi:10.1016/S0002-9440(10)65046-8
    • (2000) Am J Pathol , vol.156 , pp. 1749-1765
    • Raats, C.J.1    Van Den Born, J.2    Bakker, M.A.3    Oppers-Walgreen, B.4    Pisa, B.J.5    Dijkman, H.B.6
  • 90
    • 3543098648 scopus 로고    scopus 로고
    • Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction
    • Kojima K, Davidovits A, Poczewski H, Langer B, Uchida S, Nagy-Bojarski K, et al. Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction. J Am Soc Nephrol (2004) 15:2079-89. doi:10.1097/01.ASN.0000133531.43177.21
    • (2004) J Am Soc Nephrol , vol.15 , pp. 2079-2089
    • Kojima, K.1    Davidovits, A.2    Poczewski, H.3    Langer, B.4    Uchida, S.5    Nagy-Bojarski, K.6
  • 91
    • 78651393398 scopus 로고    scopus 로고
    • Defective glycosylation of alpha-dystroglycan contributes to podocyte flattening
    • Kojima K, Nosaka H, Kishimoto Y, Nishiyama Y, Fukuda S, Shimada M, et al. Defective glycosylation of alpha-dystroglycan contributes to podocyte flattening. Kidney Int (2011) 79:311-6. doi:10.1038/ki.2010.403
    • (2011) Kidney Int , vol.79 , pp. 311-316
    • Kojima, K.1    Nosaka, H.2    Kishimoto, Y.3    Nishiyama, Y.4    Fukuda, S.5    Shimada, M.6
  • 92
    • 79954504238 scopus 로고    scopus 로고
    • Dystroglycan does not contribute significantly to kidney development or function, in health or after injury
    • Jarad G, Pippin JW, Shankland SJ, Kreidberg JA, Miner JH. Dystroglycan does not contribute significantly to kidney development or function, in health or after injury. Am J Physiol Renal Physiol (2011) 300:F811-20. doi:10.1152/ajprenal.00725.2010
    • (2011) Am J Physiol Renal Physiol , vol.300 , pp. F811-F820
    • Jarad, G.1    Pippin, J.W.2    Shankland, S.J.3    Kreidberg, J.A.4    Miner, J.H.5
  • 93
    • 84875439033 scopus 로고    scopus 로고
    • RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover
    • Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, et al. RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover. J Biol Chem (2013) 288:8238-49. doi:10.1074/jbc. M112.438119
    • (2013) J Biol Chem , vol.288 , pp. 8238-8249
    • Goult, B.T.1    Zacharchenko, T.2    Bate, N.3    Tsang, R.4    Hey, F.5    Gingras, A.R.6
  • 94
    • 46649085889 scopus 로고    scopus 로고
    • Talin at a glance
    • Critchley DR, Gingras AR. Talin at a glance. J Cell Sci (2008) 121:1345-7. doi:10.1242/jcs.018085
    • (2008) J Cell Sci , vol.121 , pp. 1345-1347
    • Critchley, D.R.1    Gingras, A.R.2
  • 95
    • 84896795311 scopus 로고    scopus 로고
    • Podocyte-associated talin1 is critical for glomerular filtration barrier maintenance
    • Tian X, Kim JJ, Monkley SM, Gotoh N, Nandez R, Soda K, et al. Podocyte-associated talin1 is critical for glomerular filtration barrier maintenance. J Clin Invest (2014) 124:1098-113. doi:10.1172/JCI69778
    • (2014) J Clin Invest , vol.124 , pp. 1098-1113
    • Tian, X.1    Kim, J.J.2    Monkley, S.M.3    Gotoh, N.4    Nandez, R.5    Soda, K.6
  • 96
    • 36849069902 scopus 로고    scopus 로고
    • Vinculin controls focal adhesion formation by direct interactions with talin and actin
    • Humphries JD, Wang P, Streuli C, Geiger B, Humphries MJ, Ballestrem C. Vinculin controls focal adhesion formation by direct interactions with talin and actin. J Cell Biol (2007) 179:1043-57. doi:10.1083/jcb.200703036
    • (2007) J Cell Biol , vol.179 , pp. 1043-1057
    • Humphries, J.D.1    Wang, P.2    Streuli, C.3    Geiger, B.4    Humphries, M.J.5    Ballestrem, C.6
  • 97
    • 0027399847 scopus 로고
    • Molecular shape of vinculin in aqueous solution
    • Eimer W, Niermann M, Eppe MA, Jockusch BM. Molecular shape of vinculin in aqueous solution. J Mol Biol (1993) 229:146-52. doi:10.1006/jmbi.1993.1014
    • (1993) J Mol Biol , vol.229 , pp. 146-152
    • Eimer, W.1    Niermann, M.2    Eppe, M.A.3    Jockusch, B.M.4
  • 98
    • 0343058961 scopus 로고    scopus 로고
    • The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy
    • Winkler J, Lunsdorf H, Jockusch BM. The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy. J Struct Biol (1996) 116:270-7. doi:10.1006/jsbi.1996.0042
    • (1996) J Struct Biol , vol.116 , pp. 270-277
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 99
    • 18844369343 scopus 로고    scopus 로고
    • Spatial distribution and functional significance of activated vinculin in living cells
    • Chen H, Cohen DM, Choudhury DM, Kioka N, Craig SW. Spatial distribution and functional significance of activated vinculin in living cells. J Cell Biol (2005) 169:459-70. doi:10.1083/jcb.200410100
    • (2005) J Cell Biol , vol.169 , pp. 459-470
    • Chen, H.1    Cohen, D.M.2    Choudhury, D.M.3    Kioka, N.4    Craig, S.W.5
  • 101
    • 84874652706 scopus 로고    scopus 로고
    • Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner
    • Carisey A, Tsang R, Greiner AM, Nijenhuis N, Heath N, Nazgiewicz A, et al. Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner. Curr Biol (2013) 23:271-81. doi:10.1016/j.cub.2013.01.009
    • (2013) Curr Biol , vol.23 , pp. 271-281
    • Carisey, A.1    Tsang, R.2    Greiner, A.M.3    Nijenhuis, N.4    Heath, N.5    Nazgiewicz, A.6
  • 102
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E, Geiger B. Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci (2001) 114:3583-90.
    • (2001) J Cell Sci , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 104
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown MC, Perrotta JA, Turner CE. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J Cell Biol (1996) 135:1109-23. doi:10.1083/jcb.135.4.1109
    • (1996) J Cell Biol , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 105
    • 0031847578 scopus 로고    scopus 로고
    • Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin
    • Brown MC, Perrotta JA, Turner CE. Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin. Mol Biol Cell (1998) 9:1803-16. doi:10.1091/mbc.9.7.1803
    • (1998) Mol Biol Cell , vol.9 , pp. 1803-1816
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 106
    • 84855737428 scopus 로고    scopus 로고
    • The C terminus of talin links integrins to cell cycle progression
    • Wang P, Ballestrem C, Streuli CH. The C terminus of talin links integrins to cell cycle progression. J Cell Biol (2011) 195:499-513. doi:10.1083/jcb.201104128
    • (2011) J Cell Biol , vol.195 , pp. 499-513
    • Wang, P.1    Ballestrem, C.2    Streuli, C.H.3
  • 107
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: adapting to change
    • Brown MC, Turner CE. Paxillin: adapting to change. Physiol Rev (2004) 84:1315-39. doi:10.1152/physrev.00002.2004
    • (2004) Physiol Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 109
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions
    • Schaller MD. Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions. J Cell Sci (2010) 123:1007-13. doi:10.1242/jcs.045112
    • (2010) J Cell Sci , vol.123 , pp. 1007-1013
    • Schaller, M.D.1
  • 110
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic D, Furuta Y, Kanazawa S, Takeda N, Sobue K, Nakatsuji N, et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature (1995) 377:539-44. doi:10.1038/377539a0
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1    Furuta, Y.2    Kanazawa, S.3    Takeda, N.4    Sobue, K.5    Nakatsuji, N.6
  • 111
    • 77954599877 scopus 로고    scopus 로고
    • Inhibition of podocyte FAK protects against proteinuria and foot process effacement
    • Ma H, Togawa A, Soda K, Zhang J, Lee S, Ma M, et al. Inhibition of podocyte FAK protects against proteinuria and foot process effacement. J Am Soc Nephrol (2010) 21:1145-56. doi:10.1681/ASN.2009090991
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1145-1156
    • Ma, H.1    Togawa, A.2    Soda, K.3    Zhang, J.4    Lee, S.5    Ma, M.6
  • 112
    • 84902590772 scopus 로고    scopus 로고
    • Laminin alpha2-mediated focal adhesion kinase activation triggers Alport glomerular pathogenesis
    • Delimont D, Dufek BM, Meehan DT, Zallocchi M, Gratton MA, Phillips G, et al. Laminin alpha2-mediated focal adhesion kinase activation triggers Alport glomerular pathogenesis. PLoS One (2014) 9:e99083. doi:10.1371/journal.pone.0099083
    • (2014) PLoS One , vol.9 , pp. e99083
    • Delimont, D.1    Dufek, B.M.2    Meehan, D.T.3    Zallocchi, M.4    Gratton, M.A.5    Phillips, G.6
  • 113
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase
    • Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, Coppolino MG, Radeva G, Filmus J, et al. Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. Nature (1996) 379:91-6. doi:10.1038/379091a0
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3    Coppolino, M.G.4    Radeva, G.5    Filmus, J.6
  • 114
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas CG, Gregory SL, Brown NH. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J Cell Biol (2001) 152:1007-18. doi:10.1083/jcb.152.5.1007
    • (2001) J Cell Biol , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 115
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BD. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol (2002) 12:787-97. doi:10.1016/S0960-9822(02)00810-2
    • (2002) Curr Biol , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 116
    • 75049085759 scopus 로고    scopus 로고
    • The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!
    • Wickstrom SA, Lange A, Montanez E, Fassler R. The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase! EMBO J (2010) 29:281-91. doi:10.1038/emboj.2009.376
    • (2010) EMBO J , vol.29 , pp. 281-291
    • Wickstrom, S.A.1    Lange, A.2    Montanez, E.3    Fassler, R.4
  • 117
    • 79957552048 scopus 로고    scopus 로고
    • Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase
    • Fukuda K, Knight JD, Piszczek G, Kothary R, Qin J. Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase. J Biol Chem (2011) 286:21886-95. doi:10.1074/jbc. M111.240093
    • (2011) J Biol Chem , vol.286 , pp. 21886-21895
    • Fukuda, K.1    Knight, J.D.2    Piszczek, G.3    Kothary, R.4    Qin, J.5
  • 118
    • 80055062698 scopus 로고    scopus 로고
    • Integrin-linked kinase: not so "pseudo" after all
    • Hannigan GE, McDonald PC, Walsh MP, Dedhar S. Integrin-linked kinase: not so "pseudo" after all. Oncogene (2011) 30:4375-85. doi:10.1038/onc.2011.177
    • (2011) Oncogene , vol.30 , pp. 4375-4385
    • Hannigan, G.E.1    McDonald, P.C.2    Walsh, M.P.3    Dedhar, S.4
  • 119
    • 84867885462 scopus 로고    scopus 로고
    • ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling
    • Qin J, Wu C. ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling. Curr Opin Cell Biol (2012) 24:607-13. doi:10.1016/j.ceb.2012.06.003
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 607-613
    • Qin, J.1    Wu, C.2
  • 120
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos SN, Turner CE. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol (2000) 151:1435-48. doi:10.1083/jcb.151.7.1435
    • (2000) J Cell Biol , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 121
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji S, Suzuki A, Sugiyama Y, Koide Y, Yoshida M, Kanamori H, et al. A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J Cell Biol (2001) 153:1251-64. doi:10.1083/jcb.153.6.1251
    • (2001) J Cell Biol , vol.153 , pp. 1251-1264
    • Yamaji, S.1    Suzuki, A.2    Sugiyama, Y.3    Koide, Y.4    Yoshida, M.5    Kanamori, H.6
  • 122
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu Y, Li F, Goicoechea S, Wu C. The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol Cell Biol (1999) 19:2425-34.
    • (1999) Mol Cell Biol , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 123
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y, Huang Y, Zhang Y, Hua Y, Wu C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol (2001) 153:585-98. doi:10.1083/jcb.153.3.585
    • (2001) J Cell Biol , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 125
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y, Wu S, Shi X, Chen K, Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell (2003) 113:37-47. doi:10.1016/S0092-8674(03)00163-6
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 126
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
    • Larjava H, Plow EF, Wu C. Kindlins: essential regulators of integrin signalling and cell-matrix adhesion. EMBO Rep (2008) 9:1203-8. doi:10.1038/embor.2008.202
    • (2008) EMBO Rep , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2    Wu, C.3
  • 127
    • 79952802913 scopus 로고    scopus 로고
    • Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins
    • Qu H, Tu Y, Shi X, Larjava H, Saleem MA, Shattil SJ, et al. Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins. J Cell Sci (2011) 124:879-91. doi:10.1242/jcs.076976
    • (2011) J Cell Sci , vol.124 , pp. 879-891
    • Qu, H.1    Tu, Y.2    Shi, X.3    Larjava, H.4    Saleem, M.A.5    Shattil, S.J.6
  • 128
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai T, Li S, Docheva D, Grashoff C, Sakai K, Kostka G, et al. Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev (2003) 17:926-40. doi:10.1101/gad.255603
    • (2003) Genes Dev , vol.17 , pp. 926-940
    • Sakai, T.1    Li, S.2    Docheva, D.3    Grashoff, C.4    Sakai, K.5    Kostka, G.6
  • 129
    • 70350345546 scopus 로고    scopus 로고
    • Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling
    • Montanez E, Wickstrom SA, Altstatter J, Chu H, Fassler R. Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling. EMBO J (2009) 28:3132-44. doi:10.1038/emboj.2009.295
    • (2009) EMBO J , vol.28 , pp. 3132-3144
    • Montanez, E.1    Wickstrom, S.A.2    Altstatter, J.3    Chu, H.4    Fassler, R.5
  • 130
    • 23744490092 scopus 로고    scopus 로고
    • PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage
    • Li S, Bordoy R, Stanchi F, Moser M, Braun A, Kudlacek O, et al. PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage. J Cell Sci (2005) 118:2913-21. doi:10.1242/jcs.02422
    • (2005) J Cell Sci , vol.118 , pp. 2913-2921
    • Li, S.1    Bordoy, R.2    Stanchi, F.3    Moser, M.4    Braun, A.5    Kudlacek, O.6
  • 131
    • 70350064314 scopus 로고    scopus 로고
    • Integrin-linked kinase is an adaptor with essential functions during mouse development
    • Lange A, Wickstrom SA, Jakobson M, Zent R, Sainio K, Fassler R. Integrin-linked kinase is an adaptor with essential functions during mouse development. Nature (2009) 461:1002-6. doi:10.1038/nature08468
    • (2009) Nature , vol.461 , pp. 1002-1006
    • Lange, A.1    Wickstrom, S.A.2    Jakobson, M.3    Zent, R.4    Sainio, K.5    Fassler, R.6
  • 132
    • 33746491157 scopus 로고    scopus 로고
    • Essential role of integrin-linked kinase in podocyte biology: bridging the integrin and slit diaphragm signaling
    • Dai C, Stolz DB, Bastacky SI, St-Arnaud R, Wu C, Dedhar S, et al. Essential role of integrin-linked kinase in podocyte biology: bridging the integrin and slit diaphragm signaling. J Am Soc Nephrol (2006) 17:2164-75. doi:10.1681/ASN.2006010033
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2164-2175
    • Dai, C.1    Stolz, D.B.2    Bastacky, S.I.3    St-Arnaud, R.4    Wu, C.5    Dedhar, S.6
  • 133
    • 33646356720 scopus 로고    scopus 로고
    • Podocyte-specific deletion of integrin-linked kinase results in severe glomerular basement membrane alterations and progressive glomerulosclerosis
    • El-Aouni C, Herbach N, Blattner SM, Henger A, Rastaldi MP, Jarad G, et al. Podocyte-specific deletion of integrin-linked kinase results in severe glomerular basement membrane alterations and progressive glomerulosclerosis. J Am Soc Nephrol (2006) 17:1334-44. doi:10.1681/ASN.2005090921
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1334-1344
    • El-Aouni, C.1    Herbach, N.2    Blattner, S.M.3    Henger, A.4    Rastaldi, M.P.5    Jarad, G.6
  • 134
    • 0035152114 scopus 로고    scopus 로고
    • The distribution and regulation of integrin-linked kinase in normal and diabetic kidneys
    • Guo L, Sanders PW, Woods A, Wu C. The distribution and regulation of integrin-linked kinase in normal and diabetic kidneys. Am J Pathol (2001) 159:1735-42. doi:10.1016/S0002-9440(10)63020-9
    • (2001) Am J Pathol , vol.159 , pp. 1735-1742
    • Guo, L.1    Sanders, P.W.2    Woods, A.3    Wu, C.4
  • 136
    • 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 (1974) 60:423-33. doi:10.1083/jcb.60.2.423
    • (1974) J Cell Biol , vol.60 , pp. 423-433
    • Rodewald, R.1    Karnovsky, M.J.2
  • 137
    • 0002965692 scopus 로고
    • Glomerular permeability. I. Ferritin transfer across the normal glomerular capillary wall.
    • Farquhar MG, Wissig SL, Palade GE. Glomerular permeability. I. Ferritin transfer across the normal glomerular capillary wall. J Exp Med (1961) 113:47-66. doi:10.1084/jem.113.1.47
    • (1961) J Exp Med , vol.113 , pp. 47-66
    • Farquhar, M.G.1    Wissig, S.L.2    Palade, G.E.3
  • 138
    • 0016282517 scopus 로고
    • The permeability of glomerular capillaries to graded dextrans. Identification of the basement membrane as the primary filtration barrier.
    • Caulfield JP, Farquhar MG. The permeability of glomerular capillaries to graded dextrans. Identification of the basement membrane as the primary filtration barrier. J Cell Biol (1974) 63:883-903. doi:10.1083/jcb.63.3.883
    • (1974) J Cell Biol , vol.63 , pp. 883-903
    • Caulfield, J.P.1    Farquhar, M.G.2
  • 139
    • 0032015551 scopus 로고    scopus 로고
    • Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome
    • Kestila M, Lenkkeri U, Mannikko M, Lamerdin J, McCready P, Putaala H, et al. Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome. Mol Cell (1998) 1:575-82. doi:10.1016/S1097-2765(00)80057-X
    • (1998) Mol Cell , vol.1 , pp. 575-582
    • Kestila, M.1    Lenkkeri, U.2    Mannikko, M.3    Lamerdin, J.4    McCready, P.5    Putaala, H.6
  • 141
    • 78649829302 scopus 로고    scopus 로고
    • Imaging of the porous ultrastructure of the glomerular epithelial filtration slit
    • Gagliardini E, Conti S, Benigni A, Remuzzi G, Remuzzi A. Imaging of the porous ultrastructure of the glomerular epithelial filtration slit. J Am Soc Nephrol (2010) 21:2081-9. doi:10.1681/ASN.2010020199
    • (2010) J Am Soc Nephrol , vol.21 , pp. 2081-2089
    • Gagliardini, E.1    Conti, S.2    Benigni, A.3    Remuzzi, G.4    Remuzzi, A.5
  • 142
    • 0017286132 scopus 로고
    • Alterations of the glomerular epithelium in acute aminonucleoside nephrosis. Evidence for formation of occluding junctions and epithelial cell detachment.
    • Caulfield JP, Reid JJ, Farquhar MG. Alterations of the glomerular epithelium in acute aminonucleoside nephrosis. Evidence for formation of occluding junctions and epithelial cell detachment. Lab Invest (1976) 34:43-59.
    • (1976) Lab Invest , vol.34 , pp. 43-59
    • Caulfield, J.P.1    Reid, J.J.2    Farquhar, M.G.3
  • 143
    • 0018171211 scopus 로고
    • Differentiation of epithelial foot processes and filtration slits: sequential appearance of occluding junctions, epithelial polyanion, and slit membranes in developing glomeruli
    • Reeves W, Caulfield JP, Farquhar MG. Differentiation of epithelial foot processes and filtration slits: sequential appearance of occluding junctions, epithelial polyanion, and slit membranes in developing glomeruli. Lab Invest (1978) 39:90-100.
    • (1978) Lab Invest , vol.39 , pp. 90-100
    • Reeves, W.1    Caulfield, J.P.2    Farquhar, M.G.3
  • 144
    • 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 (2003) 23:3575-82. doi:10.1128/MCB.23.10.3575-3582.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 3575-3582
    • Ciani, L.1    Patel, A.2    Allen, N.D.3    Ffrench-Constant, C.4
  • 145
    • 0033958396 scopus 로고    scopus 로고
    • The glomerular slit diaphragm is a modified adherens junction
    • Reiser J, Kriz W, Kretzler M, Mundel P. The glomerular slit diaphragm is a modified adherens junction. J Am Soc Nephrol (2000) 11:1-8.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 1-8
    • Reiser, J.1    Kriz, W.2    Kretzler, M.3    Mundel, P.4
  • 147
    • 0036841804 scopus 로고    scopus 로고
    • Up-regulation of connexin43 in glomerular podocytes in response to injury
    • Yaoita E, Yao J, Yoshida Y, Morioka T, Nameta M, Takata T, et al. Up-regulation of connexin43 in glomerular podocytes in response to injury. Am J Pathol (2002) 161:1597-606. doi:10.1016/S0002-9440(10)64438-0
    • (2002) Am J Pathol , vol.161 , pp. 1597-1606
    • Yaoita, E.1    Yao, J.2    Yoshida, Y.3    Morioka, T.4    Nameta, M.5    Takata, T.6
  • 148
    • 84908619384 scopus 로고    scopus 로고
    • A brief overview on IRM function across evolution.
    • Helmstadter M, Hohne M, Huber TB. A brief overview on IRM function across evolution. J Neurogenet (2014). doi:10.3109/01677063.2014.918976
    • (2014) J Neurogenet
    • Helmstadter, M.1    Hohne, M.2    Huber, T.B.3
  • 150
    • 69649091814 scopus 로고    scopus 로고
    • Sns and Kirre, the Drosophila orthologs of nephrin and Neph1, direct adhesion, fusion and formation of a slit diaphragm-like structure in insect nephrocytes
    • Zhuang S, Shao H, Guo F, Trimble R, Pearce E, Abmayr SM. Sns and Kirre, the Drosophila orthologs of nephrin and Neph1, direct adhesion, fusion and formation of a slit diaphragm-like structure in insect nephrocytes. Development (2009) 136:2335-44. doi:10.1242/dev.031609
    • (2009) Development , vol.136 , pp. 2335-2344
    • Zhuang, S.1    Shao, H.2    Guo, F.3    Trimble, R.4    Pearce, E.5    Abmayr, S.M.6
  • 152
    • 84893506782 scopus 로고    scopus 로고
    • Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis
    • Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, et al. Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis. Cell (2014) 156:482-94. doi:10.1016/j.cell.2014.01.004
    • (2014) Cell , vol.156 , pp. 482-494
    • Ozkan, E.1    Chia, P.H.2    Wang, R.R.3    Goriatcheva, N.4    Borek, D.5    Otwinowski, Z.6
  • 154
    • 54049142085 scopus 로고    scopus 로고
    • Nephrin mutations can cause childhood-onset steroid-resistant nephrotic syndrome
    • Philippe A, Nevo F, Esquivel EL, Reklaityte D, Gribouval O, Tete MJ, et al. Nephrin mutations can cause childhood-onset steroid-resistant nephrotic syndrome. J Am Soc Nephrol (2008) 19:1871-8. doi:10.1681/ASN.2008010059
    • (2008) J Am Soc Nephrol , vol.19 , pp. 1871-1878
    • Philippe, A.1    Nevo, F.2    Esquivel, E.L.3    Reklaityte, D.4    Gribouval, O.5    Tete, M.J.6
  • 155
    • 0034121030 scopus 로고    scopus 로고
    • Primary structure of mouse and rat nephrin cDNA and structure and expression of the mouse gene
    • Putaala H, Sainio K, Sariola H, Tryggvason K. Primary structure of mouse and rat nephrin cDNA and structure and expression of the mouse gene. J Am Soc Nephrol (2000) 11:991-1001.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 991-1001
    • Putaala, H.1    Sainio, K.2    Sariola, H.3    Tryggvason, K.4
  • 156
    • 0034948819 scopus 로고    scopus 로고
    • Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN
    • Donoviel DB, Freed DD, Vogel H, Potter DG, Hawkins E, Barrish JP, et al. Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN. Mol Cell Biol (2001) 21:4829-36. doi:10.1128/MCB.21.14.4829-4836.2001
    • (2001) Mol Cell Biol , vol.21 , pp. 4829-4836
    • Donoviel, D.B.1    Freed, D.D.2    Vogel, H.3    Potter, D.G.4    Hawkins, E.5    Barrish, J.P.6
  • 157
    • 0034034757 scopus 로고    scopus 로고
    • NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome
    • Boute N, Gribouval O, Roselli S, Benessy F, Lee H, Fuchshuber A, et al. NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nat Genet (2000) 24:349-54. doi:10.1038/74166
    • (2000) Nat Genet , vol.24 , pp. 349-354
    • Boute, N.1    Gribouval, O.2    Roselli, S.3    Benessy, F.4    Lee, H.5    Fuchshuber, A.6
  • 158
    • 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, et al. Molecular basis of the functional podocin-nephrin complex: mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains. Hum Mol Genet (2003) 12:3397-405. doi:10.1093/hmg/ddg360
    • (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
  • 159
    • 0033536599 scopus 로고    scopus 로고
    • Congenital nephrotic syndrome in mice lacking CD2-associated protein
    • Shih NY, Li J, Karpitskii V, Nguyen A, Dustin ML, Kanagawa O, et al. Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science (1999) 286:312-5. doi:10.1126/science.286.5438.312
    • (1999) Science , vol.286 , pp. 312-315
    • Shih, N.Y.1    Li, J.2    Karpitskii, V.3    Nguyen, A.4    Dustin, M.L.5    Kanagawa, O.6
  • 160
    • 35848956602 scopus 로고    scopus 로고
    • Basic science meets clinical medicine: identification of a CD2AP-deficient patient
    • Akilesh S, Koziell A, Shaw AS. Basic science meets clinical medicine: identification of a CD2AP-deficient patient. Kidney Int (2007) 72:1181-3. doi:10.1038/sj.ki.5002575
    • (2007) Kidney Int , vol.72 , pp. 1181-1183
    • Akilesh, S.1    Koziell, A.2    Shaw, A.S.3
  • 161
    • 34147130656 scopus 로고    scopus 로고
    • CD2AP/CIN85 balance determines receptor tyrosine kinase signaling response in podocytes
    • Tossidou I, Kardinal C, Peters I, Kriz W, Shaw A, Dikic I, et al. CD2AP/CIN85 balance determines receptor tyrosine kinase signaling response in podocytes. J Biol Chem (2007) 282:7457-64. doi:10.1074/jbc. M608519200
    • (2007) J Biol Chem , vol.282 , pp. 7457-7464
    • Tossidou, I.1    Kardinal, C.2    Peters, I.3    Kriz, W.4    Shaw, A.5    Dikic, I.6
  • 162
    • 22244466451 scopus 로고    scopus 로고
    • Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex
    • Lehtonen S, Ryan JJ, Kudlicka K, Iino N, Zhou H, Farquhar MG. Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex. Proc Natl Acad Sci U S A (2005) 102:9814-9. doi:10.1073/pnas.0504166102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9814-9819
    • Lehtonen, S.1    Ryan, J.J.2    Kudlicka, K.3    Iino, N.4    Zhou, H.5    Farquhar, M.G.6
  • 163
    • 84876089986 scopus 로고    scopus 로고
    • Cadherin adhesome at a glance
    • Zaidel-Bar R. Cadherin adhesome at a glance. J Cell Sci (2013) 126:373-8. doi:10.1242/jcs.111559
    • (2013) J Cell Sci , vol.126 , pp. 373-378
    • Zaidel-Bar, R.1
  • 164
    • 84884670045 scopus 로고    scopus 로고
    • The podocyte slit diaphragm-from a thin grey line to a complex signalling hub
    • Grahammer F, Schell C, Huber TB. The podocyte slit diaphragm-from a thin grey line to a complex signalling hub. Nat Rev Nephrol (2013) 9:587-98. doi:10.1038/nrneph.2013.169
    • (2013) Nat Rev Nephrol , vol.9 , pp. 587-598
    • Grahammer, F.1    Schell, C.2    Huber, T.B.3
  • 165
    • 84902257083 scopus 로고    scopus 로고
    • Advances in slit diaphragm signaling
    • New LA, Martin CE, Jones N. Advances in slit diaphragm signaling. Curr Opin Nephrol Hypertens (2014) 23:420-30. doi:10.1097/01.mnh.0000447018.28852.b6
    • (2014) Curr Opin Nephrol Hypertens , vol.23 , pp. 420-430
    • New, L.A.1    Martin, C.E.2    Jones, N.3
  • 166
    • 0037743504 scopus 로고    scopus 로고
    • Fyn binds to and phosphorylates the kidney slit diaphragm component nephrin
    • Verma R, Wharram B, Kovari I, Kunkel R, Nihalani D, Wary KK, et al. Fyn binds to and phosphorylates the kidney slit diaphragm component nephrin. J Biol Chem (2003) 278:20716-23. doi:10.1074/jbc. M301689200
    • (2003) J Biol Chem , vol.278 , pp. 20716-20723
    • Verma, R.1    Wharram, B.2    Kovari, I.3    Kunkel, R.4    Nihalani, D.5    Wary, K.K.6
  • 167
    • 33645746950 scopus 로고    scopus 로고
    • Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes
    • Jones N, Blasutig IM, Eremina V, Ruston JM, Bladt F, Li H, et al. Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes. Nature (2006) 440:818-23. doi:10.1038/nature04662
    • (2006) Nature , vol.440 , pp. 818-823
    • Jones, N.1    Blasutig, I.M.2    Eremina, V.3    Ruston, J.M.4    Bladt, F.5    Li, H.6
  • 168
    • 33646401549 scopus 로고    scopus 로고
    • Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization
    • Verma R, Kovari I, Soofi A, Nihalani D, Patrie K, Holzman LB. Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization. J Clin Invest (2006) 116:1346-59. doi:10.1172/JCI27414
    • (2006) J Clin Invest , vol.116 , pp. 1346-1359
    • Verma, R.1    Kovari, I.2    Soofi, A.3    Nihalani, D.4    Patrie, K.5    Holzman, L.B.6
  • 169
    • 84863066779 scopus 로고    scopus 로고
    • Crk1/2-dependent signaling is necessary for podocyte foot process spreading in mouse models of glomerular disease
    • George B, Verma R, Soofi AA, Garg P, Zhang J, Park TJ, et al. Crk1/2-dependent signaling is necessary for podocyte foot process spreading in mouse models of glomerular disease. J Clin Invest (2012) 122:674-92. doi:10.1172/JCI60070
    • (2012) J Clin Invest , vol.122 , pp. 674-692
    • George, B.1    Verma, R.2    Soofi, A.A.3    Garg, P.4    Zhang, J.5    Park, T.J.6
  • 170
    • 84901919445 scopus 로고    scopus 로고
    • Crk1/2 and CrkL form a hetero-oligomer and functionally complement each other during podocyte morphogenesis
    • George B, Fan Q, Dlugos CP, Soofi AA, Zhang J, Verma R, et al. Crk1/2 and CrkL form a hetero-oligomer and functionally complement each other during podocyte morphogenesis. Kidney Int (2014) 85:1382-94. doi:10.1038/ki.2013.556
    • (2014) Kidney Int , vol.85 , pp. 1382-1394
    • George, B.1    Fan, Q.2    Dlugos, C.P.3    Soofi, A.A.4    Zhang, J.5    Verma, R.6
  • 171
    • 37549036286 scopus 로고    scopus 로고
    • Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization
    • Garg P, Verma R, Nihalani D, Johnstone DB, Holzman LB. Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization. Mol Cell Biol (2007) 27:8698-712. doi:10.1128/MCB.00948-07
    • (2007) Mol Cell Biol , vol.27 , pp. 8698-8712
    • Garg, P.1    Verma, R.2    Nihalani, D.3    Johnstone, D.B.4    Holzman, L.B.5
  • 172
    • 84870605054 scopus 로고    scopus 로고
    • The adaptor protein Grb2 is not essential for the establishment of the glomerular filtration barrier
    • Bisson N, Ruston J, Jeansson M, Vanderlaan R, Hardy WR, Du J, et al. The adaptor protein Grb2 is not essential for the establishment of the glomerular filtration barrier. PLoS One (2012) 7:e50996. doi:10.1371/journal.pone.0050996
    • (2012) PLoS One , vol.7 , pp. e50996
    • Bisson, N.1    Ruston, J.2    Jeansson, M.3    Vanderlaan, R.4    Hardy, W.R.5    Du, J.6
  • 173
    • 0038788840 scopus 로고    scopus 로고
    • Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling
    • Huber TB, Hartleben B, Kim J, Schmidts M, Schermer B, Keil A, et al. Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling. Mol Cell Biol (2003) 23:4917-28. doi:10.1128/MCB.23.14.4917-4928.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 4917-4928
    • Huber, T.B.1    Hartleben, B.2    Kim, J.3    Schmidts, M.4    Schermer, B.5    Keil, A.6
  • 174
    • 39349104907 scopus 로고    scopus 로고
    • Nephrin mediates actin reorganization via phosphoinositide 3-kinase in podocytes
    • Zhu J, Sun N, Aoudjit L, Li H, Kawachi H, Lemay S, et al. Nephrin mediates actin reorganization via phosphoinositide 3-kinase in podocytes. Kidney Int (2008) 73:556-66. doi:10.1038/sj.ki.5002691
    • (2008) Kidney Int , vol.73 , pp. 556-566
    • Zhu, J.1    Sun, N.2    Aoudjit, L.3    Li, H.4    Kawachi, H.5    Lemay, S.6
  • 176
    • 84864313966 scopus 로고    scopus 로고
    • Inhibitory effects of Robo2 on nephrin: a crosstalk between positive and negative signals regulating podocyte structure
    • Fan X, Li Q, Pisarek-Horowitz A, Rasouly HM, Wang X, Bonegio RG, et al. Inhibitory effects of Robo2 on nephrin: a crosstalk between positive and negative signals regulating podocyte structure. Cell Rep (2012) 2:52-61. doi:10.1016/j.celrep.2012.06.002
    • (2012) Cell Rep , vol.2 , pp. 52-61
    • Fan, X.1    Li, Q.2    Pisarek-Horowitz, A.3    Rasouly, H.M.4    Wang, X.5    Bonegio, R.G.6
  • 177
    • 84887479804 scopus 로고    scopus 로고
    • AKT2 is essential to maintain podocyte viability and function during chronic kidney disease
    • Canaud G, Bienaime F, Viau A, Treins C, Baron W, Nguyen C, et al. AKT2 is essential to maintain podocyte viability and function during chronic kidney disease. Nat Med (2013) 19:1288-96. doi:10.1038/nm.3313
    • (2013) Nat Med , vol.19 , pp. 1288-1296
    • Canaud, G.1    Bienaime, F.2    Viau, A.3    Treins, C.4    Baron, W.5    Nguyen, C.6
  • 178
    • 77957657608 scopus 로고    scopus 로고
    • Insulin signaling to the glomerular podocyte is critical for normal kidney function
    • Welsh GI, Hale LJ, Eremina V, Jeansson M, Maezawa Y, Lennon R, et al. Insulin signaling to the glomerular podocyte is critical for normal kidney function. Cell Metab (2010) 12:329-40. doi:10.1016/j.cmet.2010.08.015
    • (2010) Cell Metab , vol.12 , pp. 329-340
    • Welsh, G.I.1    Hale, L.J.2    Eremina, V.3    Jeansson, M.4    Maezawa, Y.5    Lennon, R.6
  • 179
    • 0034051681 scopus 로고    scopus 로고
    • Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis
    • Kaplan JM, Kim SH, North KN, Rennke H, Correia LA, Tong HQ, et al. Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. Nat Genet (2000) 24:251-6. doi:10.1038/73456
    • (2000) Nat Genet , vol.24 , pp. 251-256
    • Kaplan, J.M.1    Kim, S.H.2    North, K.N.3    Rennke, H.4    Correia, L.A.5    Tong, H.Q.6
  • 180
  • 181
    • 84878733723 scopus 로고    scopus 로고
    • Inverted formin 2 regulates actin dynamics by antagonizing Rho/diaphanous-related formin signaling
    • Sun H, Schlondorff J, Higgs HN, Pollak MR. Inverted formin 2 regulates actin dynamics by antagonizing Rho/diaphanous-related formin signaling. J Am Soc Nephrol (2013) 24:917-29. doi:10.1681/ASN.2012080834
    • (2013) J Am Soc Nephrol , vol.24 , pp. 917-929
    • Sun, H.1    Schlondorff, J.2    Higgs, H.N.3    Pollak, M.R.4
  • 182
    • 84891703184 scopus 로고    scopus 로고
    • Rac1 activation in podocytes induces rapid foot process effacement and proteinuria
    • Yu H, Suleiman H, Kim AH, Miner JH, Dani A, Shaw AS, et al. Rac1 activation in podocytes induces rapid foot process effacement and proteinuria. Mol Cell Biol (2013) 33:4755-64. doi:10.1128/MCB.00730-13
    • (2013) Mol Cell Biol , vol.33 , pp. 4755-4764
    • Yu, H.1    Suleiman, H.2    Kim, A.H.3    Miner, J.H.4    Dani, A.5    Shaw, A.S.6
  • 183
    • 57349168398 scopus 로고    scopus 로고
    • Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease
    • Shibata S, Nagase M, Yoshida S, Kawarazaki W, Kurihara H, Tanaka H, et al. Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease. Nat Med (2008) 14:1370-6. doi:10.1038/nm.1879
    • (2008) Nat Med , vol.14 , pp. 1370-1376
    • Shibata, S.1    Nagase, M.2    Yoshida, S.3    Kawarazaki, W.4    Kurihara, H.5    Tanaka, H.6
  • 185
    • 84888382854 scopus 로고    scopus 로고
    • Divergent functions of the Rho GTPases Rac1 and Cdc42 in podocyte injury
    • Blattner SM, Hodgin JB, Nishio M, Wylie SA, Saha J, Soofi AA, et al. Divergent functions of the Rho GTPases Rac1 and Cdc42 in podocyte injury. Kidney Int (2013) 84:920-30. doi:10.1038/ki.2013.175
    • (2013) Kidney Int , vol.84 , pp. 920-930
    • Blattner, S.M.1    Hodgin, J.B.2    Nishio, M.3    Wylie, S.A.4    Saha, J.5    Soofi, A.A.6
  • 187
    • 84905658896 scopus 로고    scopus 로고
    • aPKClambda maintains the integrity of the glomerular slit diaphragm through trafficking of nephrin to the cell surface.
    • Satoh D, Hirose T, Harita Y, Daimon C, Harada T, Kurihara H, et al. aPKClambda maintains the integrity of the glomerular slit diaphragm through trafficking of nephrin to the cell surface. J Biochem (2014) 156(2):115-28. doi:10.1093/jb/mvu022
    • (2014) J Biochem , vol.156 , Issue.2 , pp. 115-128
    • Satoh, D.1    Hirose, T.2    Harita, Y.3    Daimon, C.4    Harada, T.5    Kurihara, H.6
  • 189
    • 79956081242 scopus 로고    scopus 로고
    • Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane
    • Arif E, Wagner MC, Johnstone DB, Wong HN, George B, Pruthi PA, et al. Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Mol Cell Biol (2011) 31:2134-50. doi:10.1128/MCB.05051-11
    • (2011) Mol Cell Biol , vol.31 , pp. 2134-2150
    • Arif, E.1    Wagner, M.C.2    Johnstone, D.B.3    Wong, H.N.4    George, B.5    Pruthi, P.A.6
  • 190
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett (2007) 581:644-50. doi:10.1016/j.febslet.2007.01.021
    • (2007) FEBS Lett , vol.581 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 192
    • 22844436647 scopus 로고    scopus 로고
    • TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function
    • Reiser J, Polu KR, Moller CC, Kenlan P, Altintas MM, Wei C, et al. TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function. Nat Genet (2005) 37:739-44. doi:10.1038/ng1592
    • (2005) Nat Genet , vol.37 , pp. 739-744
    • Reiser, J.1    Polu, K.R.2    Moller, C.C.3    Kenlan, P.4    Altintas, M.M.5    Wei, C.6
  • 193
    • 20844461826 scopus 로고    scopus 로고
    • A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis
    • Winn MP, Conlon PJ, Lynn KL, Farrington MK, Creazzo T, Hawkins AF, et al. A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis. Science (2005) 308:1801-4. doi:10.1126/science.1106215
    • (2005) Science , vol.308 , pp. 1801-1804
    • Winn, M.P.1    Conlon, P.J.2    Lynn, K.L.3    Farrington, M.K.4    Creazzo, T.5    Hawkins, A.F.6
  • 194
    • 84878611663 scopus 로고    scopus 로고
    • Fluid shear stress on endothelial cells modulates mechanical tension across VE-cadherin and PECAM-1
    • Conway DE, Breckenridge MT, Hinde E, Gratton E, Chen CS, Schwartz MA. Fluid shear stress on endothelial cells modulates mechanical tension across VE-cadherin and PECAM-1. Curr Biol (2013) 23:1024-30. doi:10.1016/j.cub.2013.04.049
    • (2013) Curr Biol , vol.23 , pp. 1024-1030
    • Conway, D.E.1    Breckenridge, M.T.2    Hinde, E.3    Gratton, E.4    Chen, C.S.5    Schwartz, M.A.6
  • 195
    • 84455208254 scopus 로고    scopus 로고
    • The podocyte as a target for therapies-new and old
    • Mathieson PW. The podocyte as a target for therapies-new and old. Nat Rev Nephrol (2012) 8:52-6. doi:10.1038/nrneph.2011.171
    • (2012) Nat Rev Nephrol , vol.8 , pp. 52-56
    • Mathieson, P.W.1
  • 196
    • 77956297974 scopus 로고    scopus 로고
    • Spironolactone ameliorates podocytic adhesive capacity via restoring integrin alpha 3 expression in streptozotocin-induced diabetic rats
    • Lin S, Li D, Jia J, Zheng Z, Jia Z, Shang W. Spironolactone ameliorates podocytic adhesive capacity via restoring integrin alpha 3 expression in streptozotocin-induced diabetic rats. J Renin Angiotensin Aldosterone Syst (2010) 11:149-57. doi:10.1177/1470320310369603
    • (2010) J Renin Angiotensin Aldosterone Syst , vol.11 , pp. 149-157
    • Lin, S.1    Li, D.2    Jia, J.3    Zheng, Z.4    Jia, Z.5    Shang, W.6
  • 199
    • 84862686491 scopus 로고    scopus 로고
    • Integrins as therapeutic targets
    • Goodman SL, Picard M. Integrins as therapeutic targets. Trends Pharmacol Sci (2012) 33:405-12. doi:10.1016/j.tips.2012.04.002
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 405-412
    • Goodman, S.L.1    Picard, M.2
  • 200
    • 84901399937 scopus 로고    scopus 로고
    • Feasibility of repairing glomerular basement membrane defects in Alport syndrome
    • Lin X, Suh JH, Go G, Miner JH. Feasibility of repairing glomerular basement membrane defects in Alport syndrome. J Am Soc Nephrol (2014) 25:687-92. doi:10.1681/ASN.2013070798
    • (2014) J Am Soc Nephrol , vol.25 , pp. 687-692
    • Lin, X.1    Suh, J.H.2    Go, G.3    Miner, J.H.4
  • 201
    • 3042623796 scopus 로고    scopus 로고
    • Defective trafficking of nephrin missense mutants rescued by a chemical chaperone
    • Liu XL, Done SC, Yan K, Kilpelainen P, Pikkarainen T, Tryggvason K. Defective trafficking of nephrin missense mutants rescued by a chemical chaperone. J Am Soc Nephrol (2004) 15:1731-8. doi:10.1097/01.ASN.0000129826.28932.FD
    • (2004) J Am Soc Nephrol , vol.15 , pp. 1731-1738
    • Liu, X.L.1    Done, S.C.2    Yan, K.3    Kilpelainen, P.4    Pikkarainen, T.5    Tryggvason, K.6
  • 202
    • 84898069665 scopus 로고    scopus 로고
    • Slit diaphragm protein Neph1 and its signaling: a novel therapeutic target for protection of podocytes against glomerular injury
    • Arif E, Rathore YS, Kumari B, Ashish F, Wong HN, Holzman LB, et al. Slit diaphragm protein Neph1 and its signaling: a novel therapeutic target for protection of podocytes against glomerular injury. J Biol Chem (2014) 289:9502-18. doi:10.1074/jbc. M113.505743
    • (2014) J Biol Chem , vol.289 , pp. 9502-9518
    • Arif, E.1    Rathore, Y.S.2    Kumari, B.3    Ashish, F.4    Wong, H.N.5    Holzman, L.B.6


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