메뉴 건너뛰기




Volumn 72, Issue 1, 1999, Pages 16-24

Receptor recognition by histidine 16 of human epidermal growth factor via hydrogen-bond donor/acceptor interactions

Author keywords

Cell proliferation; Ligand receptor interaction; Protein engineering; Rational design; Tyrosine kinase

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; HISTIDINE; IODINE 125; MUTANT PROTEIN; PROTEIN TYROSINE KINASE; RECOMBINANT EPIDERMAL GROWTH FACTOR; RECOMBINANT PROTEIN;

EID: 0032890433     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19990101)72:1<16::AID-JCB3>3.0.CO;2-X     Document Type: Article
Times cited : (4)

References (49)
  • 1
    • 0022179932 scopus 로고
    • Purification of the epidermal growth factor receptor by tyrosine-sepharose affinity chromatography
    • Akiyama T, Kadooka T, Ogawara H. 1985. Purification of the epidermal growth factor receptor by tyrosine-sepharose affinity chromatography. Biochem Biophys Res Commun 131:442-448.
    • (1985) Biochem Biophys Res Commun , vol.131 , pp. 442-448
    • Akiyama, T.1    Kadooka, T.2    Ogawara, H.3
  • 2
    • 0025351528 scopus 로고
    • Induction of sweat glands by epidermal growth factor in murine X-linked anhidrotic ectodermal dysplasia
    • Blecher SR, Kapalanga J, Lalonde D. 1990. Induction of sweat glands by epidermal growth factor in murine X-linked anhidrotic ectodermal dysplasia. Nature 345:542-544.
    • (1990) Nature , vol.345 , pp. 542-544
    • Blecher, S.R.1    Kapalanga, J.2    Lalonde, D.3
  • 4
    • 0025134280 scopus 로고
    • Biochemical properties of site-directed mutants of human epidermal growth factor: Importance of solventexposed hydrophobic residues of the amino-terminal domain in receptor binding
    • Campion SR, Matsunami RK, Engler DA, Niyogi SK. 1990. Biochemical properties of site-directed mutants of human epidermal growth factor: Importance of solventexposed hydrophobic residues of the amino-terminal domain in receptor binding. Biochemistry 29:9988-9993.
    • (1990) Biochemistry , vol.29 , pp. 9988-9993
    • Campion, S.R.1    Matsunami, R.K.2    Engler, D.A.3    Niyogi, S.K.4
  • 5
    • 0027236656 scopus 로고
    • The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor
    • Campion SR, Biamonti C, Montelione GT, Niyogi SK. 1993. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. Prot Engng 6:651-659.
    • (1993) Prot Engng , vol.6 , pp. 651-659
    • Campion, S.R.1    Biamonti, C.2    Montelione, G.T.3    Niyogi, S.K.4
  • 6
    • 0028321326 scopus 로고
    • Interaction of epidermal growth factor with its receptor
    • Cohn WE, Moldave K, editors. New York: Academic Press.
    • Campion SR, Niyogi SK. 1994. Interaction of epidermal growth factor with its receptor. In: Cohn WE, Moldave K, editors. Prog Nucl Acid Res Mol Biol. New York: Academic Press. Vol 49, pp 353-383.
    • (1994) Prog Nucl Acid Res Mol Biol , vol.49 , pp. 353-383
    • Campion, S.R.1    Niyogi, S.K.2
  • 7
    • 0021893825 scopus 로고
    • Binding assays for epidermal growth factor
    • Carpenter G. 1985. Binding assays for epidermal growth factor. Methods Enzymol 109:107-108.
    • (1985) Methods Enzymol , vol.109 , pp. 107-108
    • Carpenter, G.1
  • 8
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter G, Cohen S. 1990. Epidermal growth factor. J Biol Chem 265:7709-7712.
    • (1990) J Biol Chem , vol.265 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 9
    • 0001916717 scopus 로고
    • The epidermal growth factor family
    • Sporn MB, Roberts AB, editors. Berlin: Springer-Verlag
    • Carpenter G, Wahl MI. 1990. The epidermal growth factor family. In: Sporn MB, Roberts AB, editors. Peptide growth factors and their receptors I. Berlin: Springer-Verlag, pp 69-171.
    • (1990) Peptide Growth Factors and Their Receptors I , pp. 69-171
    • Carpenter, G.1    Wahl, M.I.2
  • 11
    • 0024433956 scopus 로고
    • Substitution of lysine for arginine at position 42 of human transforming growth factor α eliminates biological activity without changing internal disulfide bonds
    • Defeo-Jones D, Tai JY, Vuocolo GA, Wegrzyn RJ, Schofield TL, Riemen MA, Oliff A. 1989. Substitution of lysine for arginine at position 42 of human transforming growth factor α eliminates biological activity without changing internal disulfide bonds. Mol Cell Biol 9:4083-4086.
    • (1989) Mol Cell Biol , vol.9 , pp. 4083-4086
    • Defeo-Jones, D.1    Tai, J.Y.2    Vuocolo, G.A.3    Wegrzyn, R.J.4    Schofield, T.L.5    Ma, R.6    Oliff, A.7
  • 12
    • 0026520472 scopus 로고
    • The physiology of transforming growth factor α
    • Derynck R. 1992. The physiology of transforming growth factor α. Adv Cancer Res 58:27-52.
    • (1992) Adv Cancer Res , vol.58 , pp. 27-52
    • Derynck, R.1
  • 13
    • 14844349947 scopus 로고
    • Epidermal growth factor and transforming growth factor α- Differential intracellular routing and processing of ligand-receptor complexes
    • Ebner R, Derynck R. 1991. Epidermal growth factor and transforming growth factor α- differential intracellular routing and processing of ligand-receptor complexes. Cell Regul 8:599-612.
    • (1991) Cell Regul , vol.8 , pp. 599-612
    • Ebner, R.1    Derynck, R.2
  • 14
    • 0026321354 scopus 로고
    • Aromaticity at position 37 in human epidermal growth factor is not obligatory for activity
    • Engler DA, Hauser MR, Cook JS, Niyogi SK. 1991. Aromaticity at position 37 in human epidermal growth factor is not obligatory for activity. Mol Cell Biol 11:2425-2431.
    • (1991) Mol Cell Biol , vol.11 , pp. 2425-2431
    • Engler, D.A.1    Hauser, M.R.2    Cook, J.S.3    Niyogi, S.K.4
  • 16
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction
    • French AR, Tadaki DK, Niyogi SK, Lauffenburger DA. 1995. Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction. J Biol Chem 270:4334-4340.
    • (1995) J Biol Chem , vol.270 , pp. 4334-4340
    • French, A.R.1    Tadaki, D.K.2    Niyogi, S.K.3    Lauffenburger, D.A.4
  • 17
    • 0018745431 scopus 로고
    • The angiogenic activity of the fibroblast and epidermal growth factor
    • Gospodarowicz D, Bialecki H, Thakral TK. 1979. The angiogenic activity of the fibroblast and epidermal growth factor. Exp Eye Res 28:501-514.
    • (1979) Exp Eye Res , vol.28 , pp. 501-514
    • Gospodarowicz, D.1    Bialecki, H.2    Thakral, T.K.3
  • 18
    • 0028618937 scopus 로고
    • Structurefunction relationships for the EGF/TGFα family of mitogens
    • Groenen LC, Nice EC, Burgess AW. 1994. Structurefunction relationships for the EGF/TGFα family of mitogens. Growth Factors 11:235-257.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 19
    • 0000075317 scopus 로고
    • Techniques of transformation of E. coli
    • Glover DM, editor. Oxford: IRL Press.
    • Hanahan D. 1985. Techniques of transformation of E. coli. In: Glover DM, editor. DNA cloning. Oxford: IRL Press. Vol 1, pp 109-135.
    • (1985) DNA Cloning , vol.1 , pp. 109-135
    • Hanahan, D.1
  • 20
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Helmsley A, Arnheim N, Toney MD, Cortopassi G, Galas DJ. 1989. A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucl Acids Res 17:6545-6551.
    • (1989) Nucl Acids Res , vol.17 , pp. 6545-6551
    • Helmsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 22
    • 0026662288 scopus 로고
    • Human epidermal growth factor - High resolution solution structure and comparison with human transforming growth factor α
    • Hommel U, Harvey TS, Driscoll PC, Campbell ID. 1992. Human epidermal growth factor - High resolution solution structure and comparison with human transforming growth factor α. J Mol Biol 227:271-282.
    • (1992) J Mol Biol , vol.227 , pp. 271-282
    • Hommel, U.1    Harvey, T.S.2    Driscoll, P.C.3    Campbell, I.D.4
  • 23
    • 34547383713 scopus 로고
    • Preparation of iodine-131 labeled human growth hormone with high specific activity
    • Hunter WM, Greenwood FC. 1962. Preparation of iodine-131 labeled human growth hormone with high specific activity. Nature 194:495-496.
    • (1962) Nature , vol.194 , pp. 495-496
    • Hunter, W.M.1    Greenwood, F.C.2
  • 25
    • 0023852787 scopus 로고
    • Growth factor control of epidermal growth factor receptor kinase activity via an intramolecular mechanism
    • Koland JG, Cerione RA. 1988. Growth factor control of epidermal growth factor receptor kinase activity via an intramolecular mechanism. J Biol Chem 263:2230-2237.
    • (1988) J Biol Chem , vol.263 , pp. 2230-2237
    • Koland, J.G.1    Cerione, R.A.2
  • 26
    • 0023930686 scopus 로고
    • Chicken epidermal growth factor (EGF) receptor- CDNA cloning, expression in mouse cells and differential binding of EGF and transforming growth factor α
    • Lax I, Johnson A, Howk R, Sap J, Bellot F, Winkler M, Ullrich A, Vennstrom B, Schlessinger J, Givol D. 1988. Chicken epidermal growth factor (EGF) receptor- cDNA cloning, expression in mouse cells and differential binding of EGF and transforming growth factor α. Mol Cell Biol 8:1970-1978.
    • (1988) Mol Cell Biol , vol.8 , pp. 1970-1978
    • Lax, I.1    Johnson, A.2    Howk, R.3    Sap, J.4    Bellot, F.5    Winkler, M.6    Ullrich, A.7    Vennstrom, B.8    Schlessinger, J.9    Givol, D.10
  • 27
    • 0028985308 scopus 로고
    • Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by Nitrogen-15 relaxation measurements
    • Li Y-C, Montelione GT. 1995. Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by Nitrogen-15 relaxation measurements. Biochemistry 34:2408-2423.
    • (1995) Biochemistry , vol.34 , pp. 2408-2423
    • Li, Y.-C.1    Montelione, G.T.2
  • 28
    • 0025372023 scopus 로고
    • Development of mammary hyperplasia and neoplasia in MMTV-TGFα transgenic mice
    • Matsui Y, Halter SA, Holt JT, Hogan BLM, Coffey RJ. 1990. Development of mammary hyperplasia and neoplasia in MMTV-TGFα transgenic mice. Cell 61:1147-1155.
    • (1990) Cell , vol.61 , pp. 1147-1155
    • Matsui, Y.1    Halter, S.A.2    Holt, J.T.3    Blm, H.4    Coffey, R.J.5
  • 29
    • 0029063575 scopus 로고
    • Tissue- And transformati on-specific phospho-tyrosyl proteins in verbB-transformed cells
    • McManus MJ, Connolly DC, Maihle NJ. 1995. Tissue- and transformati on-specific phospho-tyrosyl proteins in verbB-transformed cells. J Virol 69:3631-3638.
    • (1995) J Virol , vol.69 , pp. 3631-3638
    • McManus, M.J.1    Connolly, D.C.2    Maihle, N.J.3
  • 31
    • 0028909692 scopus 로고
    • Epidermal growth factor receptor expression is abnormal in murine polycystic kidney
    • Orellana SA, Sweeney WE, Neff CD, Avner ED. 1995. Epidermal growth factor receptor expression is abnormal in murine polycystic kidney. Kidney Int 47:490-499.
    • (1995) Kidney Int , vol.47 , pp. 490-499
    • Orellana, S.A.1    Sweeney, W.E.2    Neff, C.D.3    Avner, E.D.4
  • 34
    • 0028909329 scopus 로고
    • Contribution of the transforming growth factor α B-loop β-sheet to binding and activation of the epidermal growth factor receptor
    • Richter A, Drummond DR, MacGarvie J, Puddicombe SM, Chamberlin SG, Davies DE. 1995. Contribution of the transforming growth factor α B-loop β-sheet to binding and activation of the epidermal growth factor receptor. J Biol Chem 270:1612-1616.
    • (1995) J Biol Chem , vol.270 , pp. 1612-1616
    • Richter, A.1    Drummond, D.R.2    MacGarvie, J.3    Puddicombe, S.M.4    Chamberlin, S.G.5    Davies, D.E.6
  • 37
    • 0027103174 scopus 로고
    • Pseudomonas exotoxin A-epidermal growth factor mutant chimeric protein as an indicator for identifying amino acid residues important in EGF-receptor interaction
    • Shiah H-S, Chen T-Y, Chang C-M, Chow JT, Kung H-S, Hwang J. 1992. Pseudomonas exotoxin A-epidermal growth factor mutant chimeric protein as an indicator for identifying amino acid residues important in EGF-receptor interaction. J Biol Chem 267:24034-24040.
    • (1992) J Biol Chem , vol.267 , pp. 24034-24040
    • Shiah, H.-S.1    Chen, T.-Y.2    Chang, C.-M.3    Chow, J.T.4    Kung, H.-S.5    Hwang, J.6
  • 38
    • 0027527696 scopus 로고
    • Rieger syndrome revisited- Experimental approaches using pharmacological and antisense strategies to abrogate EGF and TGFα functions resulting in dysmorphogenesis during embryonic mouse craniofacial morphogenesis
    • Slavkin HC. 1993. Rieger syndrome revisited- experimental approaches using pharmacological and antisense strategies to abrogate EGF and TGFα functions resulting in dysmorphogenesis during embryonic mouse craniofacial morphogenesis. Am J Med Genet 47:689-697.
    • (1993) Am J Med Genet , vol.47 , pp. 689-697
    • Slavkin, H.C.1
  • 39
    • 0021958679 scopus 로고
    • Autocrine growth factors and cancer
    • Sporn MB, Roberts AB. 1985. Autocrine growth factors and cancer. Nature 313:745-747.
    • (1985) Nature , vol.313 , pp. 745-747
    • Sporn, M.B.1    Roberts, A.B.2
  • 40
    • 0026675933 scopus 로고
    • Autocrine secretion-10 years later
    • Sporn MB, Roberts AB. 1992. Autocrine secretion-10 years later. Ann Intern Med 117:408-414.
    • (1992) Ann Intern Med , vol.117 , pp. 408-414
    • Sporn, M.B.1    Roberts, A.B.2
  • 41
    • 0018023210 scopus 로고
    • Establishment of epithelial cell lines following exposure of cultured tracheal epithelium to 12-O-tetradecanoyl-phorbol13-acetate
    • Steele VE, Marchok AC, Nettesheim P. 1978. Establishment of epithelial cell lines following exposure of cultured tracheal epithelium to 12-O-tetradecanoyl-phorbol13-acetate. Cancer Res 38:3563-3565.
    • (1978) Cancer Res , vol.38 , pp. 3563-3565
    • Steele, V.E.1    Marchok, A.C.2    Nettesheim, P.3
  • 42
    • 0029810873 scopus 로고    scopus 로고
    • Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor
    • Summerfield AE, Hudnall AK, Lukas TJ, Guyer CA, Staros JV. 1996. Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor. J Biol Chem 271:19656-19659.
    • (1996) J Biol Chem , vol.271 , pp. 19656-19659
    • Summerfield, A.E.1    Hudnall, A.K.2    Lukas, T.J.3    Guyer, C.A.4    Staros, J.V.5
  • 43
    • 0005657017 scopus 로고    scopus 로고
    • Epidermal growth factor-Cellular and molecular function
    • Leroith D, Bondi C, editors Greenwich, CT/London, England: JAI Press Inc.
    • Tadaki DK, Niyogi SK. 1996. Epidermal growth factor-Cellular and molecular function. In: Leroith D, Bondi C, editors. Growth factors and cytokines in health and disease. Greenwich, CT/London, England: JAI Press Inc. Vol 1A, pp 85-121.
    • (1996) Growth Factors and Cytokines in Health and Disease , vol.1 A , pp. 85-121
    • Tadaki, D.K.1    Niyogi, S.K.2
  • 44
    • 0024477057 scopus 로고
    • 1H-NMR study of human transforming growth factor α - Structure and pH-dependent conformational interconversion
    • 1H-NMR study of human transforming growth factor α - structure and pH-dependent conformational interconversion. Eur J Biochem 179:629-637.
    • (1989) Eur J Biochem , vol.179 , pp. 629-637
    • Tappin, M.J.1    Cooke, R.M.2    Fitton, J.E.3    Campbell, I.D.4
  • 45
    • 0018117704 scopus 로고
    • Repopulation of denuded tracheal grafts with normal, preneoplastic and neoplastic epithelial cell populations
    • Terzaghi M, Nettesheim P, Williams ML. 1978. Repopulation of denuded tracheal grafts with normal, preneoplastic and neoplastic epithelial cell populations. Cancer Res 38:4546-4553.
    • (1978) Cancer Res , vol.38 , pp. 4546-4553
    • Terzaghi, M.1    Nettesheim, P.2    Williams, M.L.3
  • 46
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A, Schlessinger J. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 48
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer P, Hunter T, Lindberg R. 1994. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol 10:251-337.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.3
  • 49
    • 0000402821 scopus 로고
    • Cytotoxicity and viability assays
    • Freshney RI, editor. Oxford/Washington DC: IRL Press
    • Wilson AP. 1992. Cytotoxicity and viability assays. In: Freshney RI, editor. Animal cell culture - A practical approach. Oxford/Washington DC: IRL Press, pp 183-216.
    • (1992) Animal Cell Culture - A Practical Approach , pp. 183-216
    • Wilson, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.