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Volumn 20, Issue 2, 2009, Pages 589-599

Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; TAMM HORSFALL GLYCOPROTEIN; MUCOPROTEIN; TAMM-HORSFALL PROTEIN;

EID: 61949278337     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-08-0876     Document Type: Article
Times cited : (73)

References (35)
  • 1
    • 0022406053 scopus 로고
    • Ultrastructural localization of Tamm-Horsfall glycoprotein (THP) in rat kidney as revealed by protein A-gold immunocytochemistry
    • Bachmann, S., Koeppen-Hagemann, I., and Kriz, W. (1985). Ultrastructural localization of Tamm-Horsfall glycoprotein (THP) in rat kidney as revealed by protein A-gold immunocytochemistry. Histochemistry 83, 531-538.
    • (1985) Histochemistry , vol.83 , pp. 531-538
    • Bachmann, S.1    Koeppen-Hagemann, I.2    Kriz, W.3
  • 3
    • 33749532096 scopus 로고    scopus 로고
    • Defective intracellular trafficking of uromodulin mutant isoforms
    • Bernascone, I. et al. (2006). Defective intracellular trafficking of uromodulin mutant isoforms. Traffic 7, 1567-1579.
    • (2006) Traffic , vol.7 , pp. 1567-1579
    • Bernascone, I.1
  • 4
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida proteins using mass spectrometry
    • Boja, E. S., Hoodbhoy, T., Fales, H. M., and Dean, J. (2003). Structural characterization of native mouse zona pellucida proteins using mass spectrometry. J. Biol. Chem. 278, 34189-34202.
    • (2003) J. Biol. Chem , vol.278 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Dean, J.4
  • 5
    • 0026545275 scopus 로고
    • A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor
    • Bork, P., and Sander, C. (1992). A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor. FEBS Lett. 300, 237-240.
    • (1992) FEBS Lett , vol.300 , pp. 237-240
    • Bork, P.1    Sander, C.2
  • 6
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: A protein structure and structural feature prediction server
    • Cheng, J., Randall, A. Z., Sweredoski, M. J., and Baldi, P. (2005). SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res. 33, W72-76.
    • (2005) Nucleic Acids Res , vol.33
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 7
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondarystructure prediction server
    • Cole, C., Barber, J. D., and Barton, G. J. (2008). The Jpred 3 secondarystructure prediction server. Nucleic Acids Res. 36, W197-201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 8
    • 27844487982 scopus 로고    scopus 로고
    • Mass spectrometric evidence that proteolytic processing of rainbow trout egg vitelline envelope proteins takes place on the egg
    • Darie, C. C., Biniossek, M. L., Gawinowicz, M. A., Milgrom, Y., Thumfart, J. O., Jovine, L., Litscher, E. S., and Wassarman, P. M. (2005). Mass spectrometric evidence that proteolytic processing of rainbow trout egg vitelline envelope proteins takes place on the egg. J. Biol. Chem. 280, 37585-37598.
    • (2005) J. Biol. Chem , vol.280 , pp. 37585-37598
    • Darie, C.C.1    Biniossek, M.L.2    Gawinowicz, M.A.3    Milgrom, Y.4    Thumfart, J.O.5    Jovine, L.6    Litscher, E.S.7    Wassarman, P.M.8
  • 9
    • 2942588629 scopus 로고    scopus 로고
    • Structural characterization of fish egg vitelline envelope proteins by mass spectrometry
    • Darie, C. C., Biniossek, M. L., Jovine, L., Litscher, E. S., and Wassarman, P. M. (2004). Structural characterization of fish egg vitelline envelope proteins by mass spectrometry. Biochemistry 43, 7459-7478.
    • (2004) Biochemistry , vol.43 , pp. 7459-7478
    • Darie, C.C.1    Biniossek, M.L.2    Jovine, L.3    Litscher, E.S.4    Wassarman, P.M.5
  • 10
    • 0019197325 scopus 로고
    • Etude chimique et ultrastructurale de la glycoproteine de Tamm et Horsfall ou uromucoide.
    • Delain, E., Thiery, J. P., Coulaud, D., Joliviere, A., and Hartmann, L. (1980). Etude chimique et ultrastructurale de la glycoproteine de Tamm et Horsfall ou uromucoide. Biologie Cellulaire 39, 31-42.
    • (1980) Biologie Cellulaire , vol.39 , pp. 31-42
    • Delain, E.1    Thiery, J.P.2    Coulaud, D.3    Joliviere, A.4    Hartmann, L.5
  • 12
    • 0036914069 scopus 로고    scopus 로고
    • Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy
    • Hart, T. C. et al. (2002). Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy. J. Med. Genet. 39, 882-892.
    • (2002) J. Med. Genet , vol.39 , pp. 882-892
    • Hart, T.C.1
  • 13
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: An ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • Janes, P. W. et al (2005). Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123, 291-304.
    • (2005) Cell , vol.123 , pp. 291-304
    • Janes, P.W.1
  • 15
    • 33748750336 scopus 로고    scopus 로고
    • The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation
    • Jovine, L., Janssen, W. G., Litscher, E. S., and Wassarman, P. M. (2006). The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation. BMC Biochem. 7, 11.
    • (2006) BMC Biochem , vol.7 , pp. 11
    • Jovine, L.1    Janssen, W.G.2    Litscher, E.S.3    Wassarman, P.M.4
  • 16
    • 0036307181 scopus 로고    scopus 로고
    • The ZP domain is a conserved module for polymerization of extracellular proteins
    • Jovine, L., Qi, H., Williams, Z., Litscher, E., and Wassarman, P. M. (2002). The ZP domain is a conserved module for polymerization of extracellular proteins. Nat. Cell Biol. 4, 457-461.
    • (2002) Nat. Cell Biol , vol.4 , pp. 457-461
    • Jovine, L.1    Qi, H.2    Williams, Z.3    Litscher, E.4    Wassarman, P.M.5
  • 18
    • 33845616815 scopus 로고    scopus 로고
    • Structural model of human endoglin, a transmembrane receptor responsible for hereditary hemorrhagic telangiectasia
    • Llorca, O., Trujillo, A., Blanco, F. J., and Bernabeu, C. (2007). Structural model of human endoglin, a transmembrane receptor responsible for hereditary hemorrhagic telangiectasia. J. Mol. Biol. 365, 694-705.
    • (2007) J. Mol. Biol , vol.365 , pp. 694-705
    • Llorca, O.1    Trujillo, A.2    Blanco, F.J.3    Bernabeu, C.4
  • 19
    • 0026671080 scopus 로고
    • Mechanoelectrical transduction, ion movement and water stasis in uromodulin
    • Mattey, M., and Naftalin, L. (1992). Mechanoelectrical transduction, ion movement and water stasis in uromodulin. Experientia 48, 975-980.
    • (1992) Experientia , vol.48 , pp. 975-980
    • Mattey, M.1    Naftalin, L.2
  • 20
    • 0028171579 scopus 로고
    • Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1
    • McAllister, K. A. et al. (1994). Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1. Nat. Genet. 8, 345-351.
    • (1994) Nat. Genet , vol.8 , pp. 345-351
    • McAllister, K.A.1
  • 21
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000). The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 22
    • 4344664015 scopus 로고    scopus 로고
    • Tamm-Horsfall protein is a critical renal defense factor protecting against calcium oxalate crystal formation
    • Mo, L., Huang, H. Y., Zhu, X. H., Shapiro, E., Hasty, D. L., and Wu, X. R. (2004). Tamm-Horsfall protein is a critical renal defense factor protecting against calcium oxalate crystal formation. Kidney Int. 66, 1159-1166.
    • (2004) Kidney Int , vol.66 , pp. 1159-1166
    • Mo, L.1    Huang, H.Y.2    Zhu, X.H.3    Shapiro, E.4    Hasty, D.L.5    Wu, X.R.6
  • 24
    • 17444397116 scopus 로고    scopus 로고
    • Porter: A new, accurate server for protein secondary structure prediction
    • Pollastri, G., and McLysaght, A. (2005). Porter: a new, accurate server for protein secondary structure prediction. Bioinformatics 21, 1719-1720.
    • (2005) Bioinformatics , vol.21 , pp. 1719-1720
    • Pollastri, G.1    McLysaght, A.2
  • 25
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • Pollastri, G., Przybylski, D., Rost, B., and Baldi, P. (2002). Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 47, 228-235.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 26
    • 0141468223 scopus 로고
    • Direct visualization of a mucoprotein component of urine
    • Porter, K. R., and Tamm, I. (1955). Direct visualization of a mucoprotein component of urine. J. Biol. Chem. 212, 135-140.
    • (1955) J. Biol. Chem , vol.212 , pp. 135-140
    • Porter, K.R.1    Tamm, I.2
  • 27
    • 63149157585 scopus 로고    scopus 로고
    • Raghava, G.P.S. (2002). APSSP 2, a combination method for protein secondary structure prediction based on neural network and example based learning. CASP5, A-132.
    • Raghava, G.P.S. (2002). APSSP 2, a combination method for protein secondary structure prediction based on neural network and example based learning. CASP5, A-132.
  • 29
    • 0141620216 scopus 로고    scopus 로고
    • Tamm-Horsfall glycoprotein: Biology and clinical relevance
    • Serafini-Cessi, F., Malagolini, N., and Cavallone, D. (2003). Tamm-Horsfall glycoprotein: biology and clinical relevance. Am. J. Kidney Dis. 42, 658 -676.
    • (2003) Am. J. Kidney Dis , vol.42 , pp. 658-676
    • Serafini-Cessi, F.1    Malagolini, N.2    Cavallone, D.3
  • 30
    • 84964109501 scopus 로고    scopus 로고
    • Tamm,I.,andHorsfall,F. L. (1950). Characterisation and separation of an inhibitor of viral hemagglutination present in urine. Proc. Soc. Exp. Biol. Med. 108-114.
    • Tamm,I.,andHorsfall,F. L. (1950). Characterisation and separation of an inhibitor of viral hemagglutination present in urine. Proc. Soc. Exp. Biol. Med. 108-114.
  • 31
    • 0034255358 scopus 로고    scopus 로고
    • DbClustal: Rapid and reliable global multiple alignments of protein sequences detected by database searches
    • Thompson, J. D., Plewniak, F., Thierry, J., and Poch, O. (2000). DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches. Nucleic Acids Res. 28, 2919-2926.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2919-2926
    • Thompson, J.D.1    Plewniak, F.2    Thierry, J.3    Poch, O.4
  • 32
    • 17344364928 scopus 로고    scopus 로고
    • Mutations in the human alpha-tectorin gene cause autosomal dominant non-syndromic hearing impairment
    • Verhoeven, K. et al. (1998). Mutations in the human alpha-tectorin gene cause autosomal dominant non-syndromic hearing impairment. Nat. Genet. 19, 60-62.
    • (1998) Nat. Genet , vol.19 , pp. 60-62
    • Verhoeven, K.1
  • 33
    • 54049085798 scopus 로고    scopus 로고
    • Zona pellucida glycoproteins
    • Wassarman, P. M. (2008). Zona pellucida glycoproteins. J. Biol. Chem. 283, 24285-24289.
    • (2008) J. Biol. Chem , vol.283 , pp. 24285-24289
    • Wassarman, P.M.1
  • 34
    • 0023090684 scopus 로고
    • Uromucoid (Tamm-Horsfall glycoprotein) forms different polymeric arrangements on a filter surface under different physicochemical conditions
    • Wiggins, R. C. (1987). Uromucoid (Tamm-Horsfall glycoprotein) forms different polymeric arrangements on a filter surface under different physicochemical conditions. Clin. Chim. Acta 162, 329-340.
    • (1987) Clin. Chim. Acta , vol.162 , pp. 329-340
    • Wiggins, R.C.1
  • 35
    • 0344629667 scopus 로고    scopus 로고
    • Mutation of a conserved hydrophobic patch prevents incorporation of ZP3 into the zona pellucida surrounding mouse eggs
    • Zhao, M., Gold, L., Dorward, H., Liang, L. F., Hoodbhoy, T., Boja, E., Fales, H. M., and Dean, J. (2003). Mutation of a conserved hydrophobic patch prevents incorporation of ZP3 into the zona pellucida surrounding mouse eggs. Mol. Cell Biol. 23, 8982-8991.
    • (2003) Mol. Cell Biol , vol.23 , pp. 8982-8991
    • Zhao, M.1    Gold, L.2    Dorward, H.3    Liang, L.F.4    Hoodbhoy, T.5    Boja, E.6    Fales, H.M.7    Dean, J.8


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