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Volumn 49, Issue 4, 2000, Pages 249-253

Liv-1 breast cancer protein belongs to new family of histidine-rich membrane proteins with potential to control intracellular ZN2+ homeostasis

Author keywords

Breast cancer; Histidine rich; Metalloprotease; Transmembrane protein; Zinc

Indexed keywords

MEMBRANE PROTEIN; TUMOR PROTEIN;

EID: 0033931310     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540050033087     Document Type: Review
Times cited : (39)

References (26)
  • 2
    • 0343457363 scopus 로고    scopus 로고
    • The LIV-1 gene, implicated in metastatic breast cancer, codes for a histidine-rich transmembrane protein
    • Taylor, K. M., Hadley, L. J., and Nicholson, R. I. (1999). The LIV-1 gene, implicated in metastatic breast cancer, codes for a histidine-rich transmembrane protein. Br. J. Cancer 80 (Suppl 2), 24.
    • (1999) Br. J. Cancer , vol.80 , Issue.SUPPL. 2 , pp. 24
    • Taylor, K.M.1    Hadley, L.J.2    Nicholson, R.I.3
  • 3
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and Falchuk, K. H. (1993) The biochemical basis of zinc physiology. Physiol. Rev. 73, 79-117.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-117
    • Vallee, B.L.1    Falchuk, K.H.2
  • 4
    • 0031953430 scopus 로고    scopus 로고
    • Mammalian zinc transporters
    • McMahon, R. J., and Cousins, R. J. (1998) Mammalian zinc transporters. J. Nutr. 128, 667-670.
    • (1998) J. Nutr. , vol.128 , pp. 667-670
    • McMahon, R.J.1    Cousins, R.J.2
  • 5
    • 0030791257 scopus 로고    scopus 로고
    • Molecular biology of iron and zinc uptake in eukaryotes
    • Eide, D. (1997) Molecular biology of iron and zinc uptake in eukaryotes. Curr. Opin. Cell Biol. 9, 573-577.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 573-577
    • Eide, D.1
  • 6
    • 0033151564 scopus 로고    scopus 로고
    • Zeroing in on zinc uptake in yeast in plants
    • Guerinot, M. L., and Eide, D. (1999) Zeroing in on zinc uptake in yeast in plants. Curr. Opin. Plant Biol. 2, 244-249.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 244-249
    • Guerinot, M.L.1    Eide, D.2
  • 7
    • 0032313517 scopus 로고    scopus 로고
    • Assembly of ion channels
    • Sheng, Z., and Deutsch, C. (1998) Assembly of ion channels. Methods Enzymol. 293, 17-32.
    • (1998) Methods Enzymol. , vol.293 , pp. 17-32
    • Sheng, Z.1    Deutsch, C.2
  • 8
    • 0003425630 scopus 로고    scopus 로고
    • Academic Press, London
    • Conley, E, ed. (1999) Ion Channel Factsbook, Vol 1-4. Academic Press, London.
    • (1999) Ion Channel Factsbook , vol.1-4
    • Conley, E.1
  • 9
    • 0033070866 scopus 로고    scopus 로고
    • Ion channel assembly: Creating structures that function
    • Green, W. N. (1999) Ion channel assembly: Creating structures that function. J. Gen. Physiol. 113, 163-170.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 163-170
    • Green, W.N.1
  • 10
    • 0031794474 scopus 로고    scopus 로고
    • Sequence analyses and phylogenetic characterisation of the ZIP family of metal ion transport proteins
    • Eng, B. H., Guerinot, M. L., Eide, D., and Saier, M. H. Jr. (1998) Sequence analyses and phylogenetic characterisation of the ZIP family of metal ion transport proteins. J. Membr. Biol. 166, 1-7.
    • (1998) J. Membr. Biol. , vol.166 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier M.H., Jr.4
  • 11
    • 0029873677 scopus 로고    scopus 로고
    • ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
    • Palmiter, R. D., Cole, T. B., and Findley, S. D. (1996) ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration. EMBO J. 15, 1784-1791.
    • (1996) EMBO J. , vol.15 , pp. 1784-1791
    • Palmiter, R.D.1    Cole, T.B.2    Findley, S.D.3
  • 13
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper, N. M. (1994) Families of zinc metalloproteases. FEBS Letts. 354, 1-6.
    • (1994) FEBS Letts. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 15
    • 0026451216 scopus 로고
    • Families of metallopeptidases and their relationships
    • Jiang, W., and Bond, J. S. (1992) Families of metallopeptidases and their relationships. FEBS Lett. 312, 112-114.
    • (1992) FEBS Lett. , vol.312 , pp. 112-114
    • Jiang, W.1    Bond, J.S.2
  • 16
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings, N. D., and Barrett, A. J. (1995) Evolutionary families of metallopeptidases. Methods Enzymol. 248, 183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 18
    • 0029095760 scopus 로고
    • Structural features of a superfamily of zinc-endopeptidases: The metzincins
    • Stocker, W., and Bode, W. (1995) Structural features of a superfamily of zinc-endopeptidases: The metzincins. Curr. Opin. Struct. Biol. 5, 383-390.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 383-390
    • Stocker, W.1    Bode, W.2
  • 19
    • 0032509102 scopus 로고    scopus 로고
    • Proline-induced disruption of a transmembrane alpha-helix in its natural environment
    • Nilsson, I., Saaf, A., Whitley, P., Gafvelin, G., Waller, C., and von Heijne, G. (1998) Proline-induced disruption of a transmembrane alpha-helix in its natural environment. J. Mol. Biol. 284, 1165-1175.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1165-1175
    • Nilsson, I.1    Saaf, A.2    Whitley, P.3    Gafvelin, G.4    Waller, C.5    Von Heijne, G.6
  • 20
    • 0025602520 scopus 로고
    • The influence of proline residues on alpha-helical structure
    • Woolfson, D. N., and Williams, D. H. (1990) The influence of proline residues on alpha-helical structure. FEBS Lett. 277, 185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 21
    • 0033369167 scopus 로고    scopus 로고
    • Cloning, expression and vesicular localisation of zinc transporter Dri27/ZnT4 in intestinal tissue and cells
    • Murgia, C., Vespignani, I., Cerase, J., Nobili, F., and Perozzi, G. (1999) Cloning, expression and vesicular localisation of zinc transporter Dri27/ZnT4 in intestinal tissue and cells. Am. J. Physiol. 277, G1231-G1239.
    • (1999) Am. J. Physiol. , vol.277
    • Murgia, C.1    Vespignani, I.2    Cerase, J.3    Nobili, F.4    Perozzi, G.5
  • 23
    • 0030725838 scopus 로고    scopus 로고
    • Zinc metabolism in the brain: Relevance to human neurodegenerative disorders
    • Cuanjungco, M. P., and Lees, G. J. (1997) Zinc metabolism in the brain: Relevance to human neurodegenerative disorders. Neurobiol. Dis. 4, 137-169.
    • (1997) Neurobiol. Dis. , vol.4 , pp. 137-169
    • Cuanjungco, M.P.1    Lees, G.J.2
  • 24
    • 0033575729 scopus 로고    scopus 로고
    • Metal ion transporters and homeostasis
    • Nelson, N. (1999) Metal ion transporters and homeostasis. EMBO J. 18, 4361-4371.
    • (1999) EMBO J. , vol.18 , pp. 4361-4371
    • Nelson, N.1
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.