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Volumn 2, Issue , 2001, Pages

The relationship between the L1 and L2 domains of the insulin and epidermal growth factor receptors and leucine-rich repeat modules

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; EPIDERMAL GROWTH FACTOR RECEPTOR; INSULIN; INSULIN RECEPTOR; LEUCINE; PECTATE LYASE; RIBONUCLEASE; SOMATOMEDIN C RECEPTOR; SOMATOMEDIN RECEPTOR;

EID: 2942516509     PISSN: 14712105     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2105-2-4     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0001183058 scopus 로고
    • Mobile modules and motifs
    • Bork P: Mobile modules and motifs. Curr Opin Struct Biol 1992,2:413-421
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 413-421
    • Bork, P.1
  • 4
    • 0032410208 scopus 로고    scopus 로고
    • A third fibronectin type-3 domain in the insulin-family receptors
    • Mulhern TD, Booker GW, Cosgrove L: A third fibronectin type-3 domain in the insulin-family receptors. Trends Biochem Sci 1998, 23:465-466
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 465-466
    • Mulhern, T.D.1    Booker, G.W.2    Cosgrove, L.3
  • 5
    • 0032418094 scopus 로고    scopus 로고
    • A third fibronectin type 3 domain in the extracellular region of the insulin receptor family
    • Marino-Buslje C, Mizuguchi K, Siddle K, Blundell TL: A third fibronectin type 3 domain in the extracellular region of the insulin receptor family. FEBS Lett 1998, 441:331-336
    • (1998) FEBS Lett. , vol.441 , pp. 331-336
    • Marino-Buslje, C.1    Mizuguchi, K.2    Siddle, K.3    Blundell, T.L.4
  • 6
    • 0032767919 scopus 로고    scopus 로고
    • Members of the insulin receptor family contain three fibronectin type 3 domains
    • Ward CW: Members of the insulin receptor family contain three fibronectin type 3 domains. Growth Factors 1999, 16:315-322
    • (1999) Growth Factors , vol.16 , pp. 315-322
    • Ward, C.W.1
  • 7
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumour necrosis factor receptor
    • Ward CW, Hoyne PA, Flegg RH: Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumour necrosis factor receptor. Proteins: Struct Funct Genet 1995, 22:141-153
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 9
    • 0032944186 scopus 로고    scopus 로고
    • Structure of the insulin receptor family: Unexpected relationships with other proteins
    • Ward CW, Garrett TPJ, McKern NM, Lawrence LJ: Structure of the insulin receptor family: unexpected relationships with other proteins. Today's Life Sciences 1999, 11:26-32
    • (1999) Today's Life Sciences , vol.11 , pp. 26-32
    • Ward, C.W.1    Garrett, T.P.J.2    McKern, N.M.3    Lawrence, L.J.4
  • 10
    • 0033906634 scopus 로고    scopus 로고
    • Structure and function of the type 1 insulin-like growth factor receptor
    • Adams TE, Epa VC, Garrett TJ, Ward CW: Structure and function of the type 1 insulin-like growth factor receptor. Cell Molec Life Sci. 2000, 57:1050-1093
    • (2000) Cell Molec. Life Sci. , vol.57 , pp. 1050-1093
    • Adams, T.E.1    Epa, V.C.2    Garrett, T.J.3    Ward, C.W.4
  • 11
    • 0027918655 scopus 로고
    • Unusual structural features in the parallel beta-helix in pectate lyases
    • Yoder MD, Lietzke SE, Jurnak F: Unusual structural features in the parallel beta-helix in pectate lyases. Structure 1993, 1:241-251
    • (1993) Structure , vol.1 , pp. 241-251
    • Yoder, M.D.1    Lietzke, S.E.2    Jurnak, F.3
  • 12
    • 0027329090 scopus 로고
    • New domain motif: Pectate lyase C, a secreted plant virulence factor
    • Yoder MD, Keen NT, Jurnak F: New domain motif: pectate lyase C, a secreted plant virulence factor. Science 1993, 260:1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 13
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine repeats
    • Kobe B, Deisenhofer J: Crystal structure of porcine ribonuclease inhibitor, a protein with leucine repeats. Nature 1993,366:751-756
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 14
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B, Deisenhofer J: The leucine-rich repeat: a versatile binding motif. Trends Biochem Sci 1994, 19:415-421
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 16
    • 0032478536 scopus 로고    scopus 로고
    • Structural diversity of leucine-rich repeat proteins
    • Kajava AV: Structural diversity of leucine-rich repeat proteins. J Mol Biol 1998, 277:519-527
    • (1998) J. Mol. Biol. , vol.277 , pp. 519-527
    • Kajava, A.V.1
  • 17
    • 0034306119 scopus 로고    scopus 로고
    • When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
    • Kobe B, Kajava AV: When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem Sci 2000, 25:509-515
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 509-515
    • Kobe, B.1    Kajava, A.V.2
  • 19
    • 0034693799 scopus 로고    scopus 로고
    • The protein tyrosine kinase family of the human genome
    • Robinson DR, Wu Y-M, Lin S-F: The protein tyrosine kinase family of the human genome. Oncogene 2001, 19:5548-5557
    • (2001) Oncogene , vol.19 , pp. 5548-5557
    • Robinson, D.R.1    Wu, Y.-M.2    Lin, S.-F.3
  • 20
    • 0029645408 scopus 로고
    • Modeling of the three-dimensional structure of proteins with typical leucine-rich repeats
    • Kajava AV, Vassart G, Wodak SJ: Modeling of the three-dimensional structure of proteins with typical leucine-rich repeats. Structure 1995, 3:867-877
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 21
    • 0034142114 scopus 로고    scopus 로고
    • Super-motifs and evolution of tandem leucine-rich repeats within the small proteoglycans-biglycan, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin
    • Matsushima N, Ohyanagi T, Tanaka T, Kretsinger RH: Super-motifs and evolution of tandem leucine-rich repeats within the small proteoglycans-biglycan, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin. Proteins: Struct Funct Genet 2000, 38:210-225
    • (2000) Proteins: Struct. Funct. Genet. , vol.38 , pp. 210-225
    • Matsushima, N.1    Ohyanagi, T.2    Tanaka, T.3    Kretsinger, R.H.4
  • 22
    • 0033256246 scopus 로고    scopus 로고
    • Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L-monocytogenes
    • Marino M, Braun L, Cossart P, Ghosh P: Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L-monocytogenes. Molecular Cell 1999,4:1063-1072
    • (1999) Molecular Cell , vol.4 , pp. 1063-1072
    • Marino, M.1    Braun, L.2    Cossart, P.3    Ghosh, P.4
  • 23
    • 0025242953 scopus 로고
    • The trypanosome leucine repeat gene in the variant surface glycoprotein expression site encodes a putative metal-binding domain and a region resembling protein-binding domains of yeast, Drosophila, and mammalian proteins
    • Smiley BL, Stadnyk AW, Myler PJ, Stuart K: The trypanosome leucine repeat gene in the variant surface glycoprotein expression site encodes a putative metal-binding domain and a region resembling protein-binding domains of yeast, Drosophila, and mammalian proteins. Mol Cell Biol 1990, 10:6436-6444
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6436-6444
    • Smiley, B.L.1    Stadnyk, A.W.2    Myler, P.J.3    Stuart, K.4
  • 24
    • 0029257437 scopus 로고
    • Functional implications for structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat B, Heffron SE, Yoder MD, Lietzky SE, Jurnak F: Functional implications for structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 1995, 107:963-976
    • (1995) Plant Physiol. , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzky, S.E.4    Jurnak, F.5
  • 25
    • 0029257535 scopus 로고
    • The parallel β helix and other coiled folds
    • Yoder MD, Jurnak F: The parallel β helix and other coiled folds. FASEB J 1995, 9:335-342
    • (1995) FASEB J. , vol.9 , pp. 335-342
    • Yoder, M.D.1    Jurnak, F.2
  • 27
    • 0024342417 scopus 로고
    • Functional analysis of the ligand binding site of EGF-receptor utilizing chimeric chicken/human receptor molecules
    • Lax I, Bellot F, Howk R, Ullrich A, Givol D, Schlessinger J: Functional analysis of the ligand binding site of EGF-receptor utilizing chimeric chicken/human receptor molecules. EMBO J 1989,8:421-427
    • (1989) EMBO J. , vol.8 , pp. 421-427
    • Lax, I.1    Bellot, F.2    Howk, R.3    Ullrich, A.4    Givol, D.5    Schlessinger, J.6
  • 28
    • 0027519152 scopus 로고
    • A 40-kDa epidermal growth factor/transforming growth factor alpha-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor
    • Kohda D, Odaka M, Lax I, Kawasaki H, Suzuki K, Ullrich A, Schlessinger J, Inagaki F: A 40-kDa epidermal growth factor/transforming growth factor alpha-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J Biol Chem 1993, 268:1976-1981
    • (1993) J. Biol. Chem. , vol.268 , pp. 1976-1981
    • Kohda, D.1    Odaka, M.2    Lax, I.3    Kawasaki, H.4    Suzuki, K.5    Ullrich, A.6    Schlessinger, J.7    Inagaki, F.8
  • 29
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA
    • Price SR, Evans PR, Nagai K: Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA. Nature 1998, 394:645-650
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evans, P.R.2    Nagai, K.3
  • 30
    • 0023241481 scopus 로고
    • On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors
    • Bajaj M, Waterfield MD, Schlessinger J, Taylor WR, Blundell T: On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. Biochim.Biophys. Acta 1987, 916:220-226
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 220-226
    • Bajaj, M.1    Waterfield, M.D.2    Schlessinger, J.3    Taylor, W.R.4    Blundell, T.5
  • 31
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O: A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 1984,12:387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 34
    • 0031594282 scopus 로고    scopus 로고
    • The three-dimensional structure of Aspergillus niger pectin lyase B at 1.7 Å resolution
    • Vitali J, Schick B, Kester HCM, Visser J, Jurnak F: The three-dimensional structure of Aspergillus niger pectin lyase B at 1.7 Å resolution. Plant Physiol. 1998, 116:69-80
    • (1998) Plant Physiol. , vol.116 , pp. 69-80
    • Vitali, J.1    Schick, B.2    Kester, H.C.M.3    Visser, J.4    Jurnak, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.