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Volumn 379, Issue 3, 2009, Pages 706-709

Clustering of disease-causing mutations on the domain-domain interfaces of ABCC6

Author keywords

ABC transporters; Genetic disease; Homology model; Missense mutations; Pseudoxanthoma elasticum

Indexed keywords

ABC TRANSPORTER; PROTEIN ABCC6; UNCLASSIFIED DRUG;

EID: 58549107012     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.12.142     Document Type: Article
Times cited : (34)

References (28)
  • 3
    • 0034705145 scopus 로고    scopus 로고
    • Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter
    • Ringpfeil F., Lebwohl M.G., Christiano A.M., and Uitto J. Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter. Proc. Natl. Acad. Sci. USA 97 (2000) 6001-6006
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6001-6006
    • Ringpfeil, F.1    Lebwohl, M.G.2    Christiano, A.M.3    Uitto, J.4
  • 4
    • 58549119111 scopus 로고    scopus 로고
    • Jiang Q, Endo M, Dibra F, Wang K, Uitto J. Pseudoxanthoma elasticum is a metabolic disease. J. Invest. Dermatol. (2008) [Epub ahead of print] PMID: 18685618.
    • Jiang Q, Endo M, Dibra F, Wang K, Uitto J. Pseudoxanthoma elasticum is a metabolic disease. J. Invest. Dermatol. (2008) [Epub ahead of print] PMID: 18685618.
  • 5
    • 45849111436 scopus 로고    scopus 로고
    • Does the absence of ABCC6 (multidrug resistance protein 6) in patients with Pseudoxanthoma elasticum prevent the liver from providing sufficient vitamin K to the periphery?
    • Borst P., van de Wetering K., and Schlingemann R. Does the absence of ABCC6 (multidrug resistance protein 6) in patients with Pseudoxanthoma elasticum prevent the liver from providing sufficient vitamin K to the periphery?. Cell Cycle 7 (2008) 1575-1579
    • (2008) Cell Cycle , vol.7 , pp. 1575-1579
    • Borst, P.1    van de Wetering, K.2    Schlingemann, R.3
  • 6
    • 0037053355 scopus 로고    scopus 로고
    • Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6)
    • Iliás A., Urban Z., Seidl T.L., Le Saux O., Sinkó E., Boyd C.D., Sarkadi B., and Váradi A. Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6). J. Biol. Chem. 277 (2002) 16860-16867
    • (2002) J. Biol. Chem. , vol.277 , pp. 16860-16867
    • Iliás, A.1    Urban, Z.2    Seidl, T.L.3    Le Saux, O.4    Sinkó, E.5    Boyd, C.D.6    Sarkadi, B.7    Váradi, A.8
  • 7
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., and Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 443 (2006) 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 8
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson R.J., and Locher K.P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581 (2007) 935-938
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 9
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks J.K., Wooding C., and Linton K.J. Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein. FASEB J. 21 (2007) 3937-3948
    • (2007) FASEB J. , vol.21 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 10
    • 33846827217 scopus 로고    scopus 로고
    • Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: a molecular modeling study
    • Li Y.F., Polgar O., Okada M., Esser L., Bates S.E., and Xia D. Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: a molecular modeling study. J. Mol. Graph. Model. 25 (2007) 837-851
    • (2007) J. Mol. Graph. Model. , vol.25 , pp. 837-851
    • Li, Y.F.1    Polgar, O.2    Okada, M.3    Esser, L.4    Bates, S.E.5    Xia, D.6
  • 11
    • 41649122089 scopus 로고    scopus 로고
    • Homology modeling of breast cancer resistance protein (ABCG2)
    • Hazai E., and Bikádi Z. Homology modeling of breast cancer resistance protein (ABCG2). J. Struct. Biol. 162 (2008) 63-74
    • (2008) J. Struct. Biol. , vol.162 , pp. 63-74
    • Hazai, E.1    Bikádi, Z.2
  • 13
    • 44649096868 scopus 로고    scopus 로고
    • Molecular model of the outward facing state of the human multidrug resistance protein 4 (MRP4/ABCC4)
    • Ravna A.W., and Sager G. Molecular model of the outward facing state of the human multidrug resistance protein 4 (MRP4/ABCC4). Bioorg. Med. Chem. Lett. 18 (2008) 3481-3483
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3481-3483
    • Ravna, A.W.1    Sager, G.2
  • 14
    • 38549085409 scopus 로고    scopus 로고
    • Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5)
    • Ravna A.W., Sylte I., and Sager G. Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5). Theor. Biol. Med. Model. 4 (2007) 33
    • (2007) Theor. Biol. Med. Model. , vol.4 , pp. 33
    • Ravna, A.W.1    Sylte, I.2    Sager, G.3
  • 15
    • 54049100453 scopus 로고    scopus 로고
    • A molecular model of a putative substrate releasing conformation of multidrug resistance protein 5 (MRP5)
    • [Epub ahead of print]
    • Ravna A.W., Sylte I., and Sager G. A molecular model of a putative substrate releasing conformation of multidrug resistance protein 5 (MRP5). Eur. J. Med. Chem. (2008) [Epub ahead of print]
    • (2008) Eur. J. Med. Chem.
    • Ravna, A.W.1    Sylte, I.2    Sager, G.3
  • 16
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos A.W., Hegedus T., Aleksandrov A.A., He L., Cui L., Dokholyan N.V., and Riordan J.R. Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc. Natl. Acad. Sci. USA 105 (2008) 3256-3261
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5    Dokholyan, N.V.6    Riordan, J.R.7
  • 17
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., and Hunt J.F. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10 (2002) 139-149
    • (2002) Mol. Cell. , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 18
    • 38449085899 scopus 로고    scopus 로고
    • Protein interactions and disease phenotypes in the ABC transporter superfamily
    • Kelly L., Karchin R., and Sali A. Protein interactions and disease phenotypes in the ABC transporter superfamily. Pac. Symp. Biocomput. (2007) 51-63
    • (2007) Pac. Symp. Biocomput. , pp. 51-63
    • Kelly, L.1    Karchin, R.2    Sali, A.3
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewein S., Jumpertz T., Holland I.B., and Schmitt L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24 (2004) 1901-1910
    • (2004) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 26
    • 0031026369 scopus 로고    scopus 로고
    • Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters
    • Tusnády G.E., Bakos E., Váradi A., and Sarkadi B. Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters. FEBS Lett. 402 (1997) 1-3
    • (1997) FEBS Lett. , vol.402 , pp. 1-3
    • Tusnády, G.E.1    Bakos, E.2    Váradi, A.3    Sarkadi, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.