메뉴 건너뛰기




Volumn 29, Issue 2, 1996, Pages 119-167

Structure and distribution of modules in extracellular proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; DATA BASE; EXTRACELLULAR MATRIX; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; REVIEW;

EID: 0029777325     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/s0033583500005783     Document Type: Review
Times cited : (281)

References (95)
  • 1
    • 0027467611 scopus 로고
    • The NMR solution structure of a kunitz-type proteinase inhibitor from the sea anemone stichodactyla helianthus
    • ANTUCH, W., BERNDT, K. D., CHAVEZ, M. A., DELFIN, J. & WÜTHRICH, K. (1993). The NMR solution structure of a kunitz-type proteinase inhibitor from the sea anemone stichodactyla helianthus. Eur. J. Biochem. 212, 675-684.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 675-684
    • Antuch, W.1    Berndt, K.D.2    Chavez, M.A.3    Delfin, J.4    Wüthrich, K.5
  • 2
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 Kd TNF receptor-human TNF-β complex: Implications for TNF receptor activation
    • BANNER, D. W., D'ARCY, A., JANES, W., GENTZ, R., SCHOENFELD, H.-J., BROGER, C., LOETSCHER, H. & LESSLAUER, W. (1993). Crystal structure of the soluble human 55 Kd TNF receptor-human TNF-β complex: Implications for TNF receptor activation. Cell 73, 431-445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.-J.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 6
    • 0001197832 scopus 로고
    • Emerging families of cytokines and receptors
    • BAZAN, J. (1993). Emerging families of cytokines and receptors. Curr. Biol. 3, 603-606.
    • (1993) Curr. Biol. , vol.3 , pp. 603-606
    • Bazan, J.1
  • 7
    • 0024066065 scopus 로고
    • The 2·0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • BODE, W., ENGH, R., MUSIL, D., THIELE, U., HUBER, R., KARSHIKOV, A., BRZIN, J., KOS, J. & TURK, V. (1988). The 2·0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 9
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2·5 Å resolution
    • BODIAN, D. L., JONES, E. Y., HARLOS, K., STUART, D. I. & DAVIS, S. J. (1994). Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2·5 Å resolution. Structure 2, 755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 10
    • 0003338119 scopus 로고
    • Extracellular protein modules
    • BORK, P. & BAIROCH, A. (1995). Extracellular protein modules. TIBS 02 (Supplement).
    • (1995) TIBS , vol.2 , Issue.SUPPL.
    • Bork, P.1    Bairoch, A.2
  • 11
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal domain by bacteria
    • BORK, P. & DOOLITTLE, R. F. (1992). Proposed acquisition of an animal domain by bacteria. Proc. Natl. Acad. Sci. USA 89, 8890-8994.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8890-8994
    • Bork, P.1    Doolittle, R.F.2
  • 12
    • 0028172534 scopus 로고
    • The Immunoglobulin fold. Structural classification, sequence patterns and common core
    • BORK, P., HOLM, L. & SANDER, C. (1994). The Immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 13
    • 0029640799 scopus 로고
    • A phosphotyrosine interaction domain
    • BORK, P. & MARGOLIS, B. (1995). A phosphotyrosine interaction domain. Cell 80, 693-694.
    • (1995) Cell , vol.80 , pp. 693-694
    • Bork, P.1    Margolis, B.2
  • 16
    • 23444449882 scopus 로고
    • Building protein structure and function from modular units
    • CAMPBELL, I. D. & DOWNING, A. K. (1994). Building protein structure and function from modular units. TIBTECH 12, 168-172.
    • (1994) TIBTECH , vol.12 , pp. 168-172
    • Campbell, I.D.1    Downing, A.K.2
  • 17
    • 0028980629 scopus 로고
    • Structure of an antibody lysozyme complex unexpected effect of a conservative mutation
    • CHACKO, S., SILVERTON, E., KAMMORGAN, L., SMITHGILL, S., COHEN, G. & DAVIES, D. (1995). Structure of an antibody lysozyme complex unexpected effect of a conservative mutation. J. Mol. Biol. 245, 261-274.
    • (1995) J. Mol. Biol. , vol.245 , pp. 261-274
    • Chacko, S.1    Silverton, E.2    Kammorgan, L.3    Smithgill, S.4    Cohen, G.5    Davies, D.6
  • 18
    • 0026580202 scopus 로고
    • Refined solution structure and ligand-binding properties of PDC-109 domain b; a collagen-binding type II domain
    • CONSTANTINE, K. L., MADRID, M., BÁNYAI, L., TREXLER, M., PATTHY, L. & LLINÁS, M. (1992). Refined solution structure and ligand-binding properties of PDC-109 domain b; a collagen-binding type II domain. J. Mol. Biol. 223, 281-298.
    • (1992) J. Mol. Biol. , vol.223 , pp. 281-298
    • Constantine, K.L.1    Madrid, M.2    Bányai, L.3    Trexler, M.4    Patthy, L.5    Llinás, M.6
  • 20
    • 0029020912 scopus 로고
    • 3-dimensional structure of a cysteine-rich repeat from the low-density-lipoprotein receptor
    • DALY, N., SCANLON, M. J., DJORDJEVIC, J. T., KROON, P. A. & SMITH, R. (1995). 3-dimensional structure of a cysteine-rich repeat from the low-density-lipoprotein receptor. Proc. Natl. Acad. Sci. USA 92, 6334-6338.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6334-6338
    • Daly, N.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 21
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • DAOPIN, S., PIEZ, K. A., OGAWA, Y. & DAVIES, D. R. (1994). Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily. Science 257, 369-373.
    • (1994) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 22
    • 0026598960 scopus 로고
    • Human growth hormone and the extracellular domain of its receptor: Crystal structure of the complex
    • DE VOS, A. M., ULTSCH, M. & KOSSIAKOFF, A. A. (1992). Human growth hormone and the extracellular domain of its receptor: Crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 24
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • DOOLITTLE, R. F. (1995). The multiplicity of domains in proteins. Ann. Rev. Biochem. 64, 287-314
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 26
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • DRICKAMER, K. (1992). Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 360, 183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 27
    • 0028813772 scopus 로고
    • 1·8-Å crystal-structure of the C-terminal domain of rabbit serum hemopexin
    • FABER, H. R., GROOM, C. R., BAKER, H. M., MORGAN, W. T., SMITH, A. & BAKER, E. N. (1995). 1·8-Å crystal-structure of the C-terminal domain of rabbit serum hemopexin. Structure 3, 551-559.
    • (1995) Structure , vol.3 , pp. 551-559
    • Faber, H.R.1    Groom, C.R.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 28
    • 0028773130 scopus 로고
    • Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
    • FLETCHER, C. M., HARRISON, R. A., LACHMANN, P. J. & NEUHAUS, D. (1994). Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure 2, 185-199.
    • (1994) Structure , vol.2 , pp. 185-199
    • Fletcher, C.M.1    Harrison, R.A.2    Lachmann, P.J.3    Neuhaus, D.4
  • 29
    • 0027918486 scopus 로고
    • Pancreatic spasmolytic polypeptide: First three-dimensional structure of a member of the mammalian trefoil family of peptides
    • GAJHEDE, M., PETERSEN, T. N., HENRIKSEN, A., PETERSEN, J. F. W., DAUTER, Z., WILSON, K. S. & THIM, L. (1993). Pancreatic spasmolytic polypeptide: first three-dimensional structure of a member of the mammalian trefoil family of peptides. Structure 1, 253-262.
    • (1993) Structure , vol.1 , pp. 253-262
    • Gajhede, M.1    Petersen, T.N.2    Henriksen, A.3    Petersen, J.F.W.4    Dauter, Z.5    Wilson, K.S.6    Thim, L.7
  • 30
    • 0029002967 scopus 로고
    • Polycystic kidney-disease - The complete structure of the PKD1 gene and its protein
    • GLUCKSMANNKUIS, M. A., TAYBER, O., et al. (1995). Polycystic kidney-disease - the complete structure of the PKD1 gene and its protein. Cell 81, 289-298.
    • (1995) Cell , vol.81 , pp. 289-298
    • Glucksmannkuis, M.A.1    Tayber, O.2
  • 33
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • HARPAZ, Y. & CHOTHIA, C. (1994). Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 34
    • 0026662288 scopus 로고
    • Human epidermal growth factor. High resolution solution structure and comparison with human TGF-α
    • HOMMEL, U., HARVEY, T. S., DRISCOLL, P. C. & CAMPBELL, I. D. (1992). Human epidermal growth factor. High resolution solution structure and comparison with human TGF-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
  • 35
    • 0028351169 scopus 로고
    • Crystal structure of tandem type III fibronectin domains front Drosophila neuroglian at 2·0 Å
    • HUBER, A. H., WANG, Y. E., BIEBER, A. J. & BJORKMAN, P. J. (1994). Crystal structure of tandem type III fibronectin domains front Drosophila neuroglian at 2·0 Å. Neuron 12, 717-731.
    • (1994) Neuron , vol.12 , pp. 717-731
    • Huber, A.H.1    Wang, Y.E.2    Bieber, A.J.3    Bjorkman, P.J.4
  • 38
    • 0027145011 scopus 로고
    • The immunoglobulin superfamily
    • JONES, E. Y. (1993). The immunoglobulin superfamily. Curr. Opin. Struct. Biol. 3, 846-852.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 846-852
    • Jones, E.Y.1
  • 39
    • 0026488252 scopus 로고
    • Crystal structure at 2·8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • JONES, E. Y., DAVIS, S. J., WILLIAMS, A. F., HARLOS, K. & STUART, D. I. (1992). Crystal structure at 2·8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 41
    • 0028205728 scopus 로고
    • Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins
    • KIEFFER, B., DRISCOLL, P. C., CAMPBELL, I. D., WILLIS, A. C., VAN DER MERWE, P. A. & DAVIES, S. J. (1994). Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins. Biochemistry 33, 4471-4482.
    • (1994) Biochemistry , vol.33 , pp. 4471-4482
    • Kieffer, B.1    Driscoll, P.C.2    Campbell, I.D.3    Willis, A.C.4    Van Der Merwe, P.A.5    Davies, S.J.6
  • 42
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • KOBE, B. & DEISENHOFER, J. (1994). The leucine-rich repeat: a versatile binding motif. TIBS 19, 415-421.
    • (1994) TIBS , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 43
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • KOBE, B. & DEISENHOFER, J. (1995). A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 374, 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • KRAULIS, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 46
    • 0028824480 scopus 로고
    • Titins, giant proteins in charge of muscle ultrastructure and elasticity
    • LABEIT, S. & KOLMERER B. (1995). Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 48
    • 0026687920 scopus 로고
    • Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal antiarsonate antibody
    • LASCOMBE, M.-B., ALZARI, P. M., POLJAK, R. J. & NISONOFF, A. (1992). Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal antiarsonate antibody. Proc. Natl. Acad. Sci. USA 89, 9429-9433.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9429-9433
    • Lascombe, M.-B.1    Alzari, P.M.2    Poljak, R.J.3    Nisonoff, A.4
  • 49
    • 0030050396 scopus 로고    scopus 로고
    • 2·0 Å crystal structure of a four domain segment of human fibronectin encompassing the RGD loop and synergy region
    • LEAHY, D. J., AUKHIL, I. & ERICKSON, H. P. (1996). 2·0 Å crystal structure of a four domain segment of human fibronectin encompassing the RGD loop and synergy region Cell 84, 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 50
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18)
    • LEE, J.-O., RIEU, P., ARNAOUT, A. & LIDDINGTON, R. (1995). Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, A.3    Liddington, R.4
  • 52
    • 0028242139 scopus 로고
    • Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy
    • LIEPINSH, E., BERNDT, K. D., SILLARD, R., MUTT, V. & OTTING, G. (1994). Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 239, 137-153.
    • (1994) J. Mol. Biol. , vol.239 , pp. 137-153
    • Liepinsh, E.1    Berndt, K.D.2    Sillard, R.3    Mutt, V.4    Otting, G.5
  • 53
    • 0027943212 scopus 로고
    • Tracing the spread of fibronectin type-III domains in bacterial glycohydrolases
    • LITTLE, E., BORK, P. & DOOLITTLE, R. F. (1994). Tracing the spread of fibronectin type-III domains in bacterial glycohydrolases. J. Mol. Evol. 39, 631-643.
    • (1994) J. Mol. Evol. , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 54
    • 0024351647 scopus 로고
    • Mapping of the Epstein-Barr virus and C3dg binding sites to a common domain on complement receptor type 2
    • LOWELL, C. A., KLICKSTEIN, L. B., CARTER, R. H., MITCHELL, J. A., FEARON, D. T. & AHEARN, J. M. (1989). Mapping of the Epstein-Barr virus and C3dg binding sites to a common domain on complement receptor type 2. J. Exp. Med. 170, 1931-1946.
    • (1989) J. Exp. Med. , vol.170 , pp. 1931-1946
    • Lowell, C.A.1    Klickstein, L.B.2    Carter, R.H.3    Mitchell, J.A.4    Fearon, D.T.5    Ahearn, J.M.6
  • 55
    • 0026496886 scopus 로고
    • The three dimensional structure of the tenth type in module of fibronectin: An insight into RGD mediated interactions
    • MAIN, A. L., BARON, M., HARVEY, T. S., BOYD, J. & CAMPBELL, I. D. (1992). The three dimensional structure of the tenth type in module of fibronectin: an insight into RGD mediated interactions. Cell 71, 671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Baron, M.2    Harvey, T.S.3    Boyd, J.4    Campbell, I.D.5
  • 56
    • 0025728020 scopus 로고
    • A new superfamily of cell surface proteins related to the nerve growth factor receptor
    • MALLETT, S. & BARCLAY, A. N. (1991). A new superfamily of cell surface proteins related to the nerve growth factor receptor. Immunology Today 12, 220-227.
    • (1991) Immunology Today , vol.12 , pp. 220-227
    • Mallett, S.1    Barclay, A.N.2
  • 57
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • MARTINEZ, S. E., HUANG, D., SZCZEPANIAK, A., CRAMER, W. A. & SMITH, J. L. (1994). Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2, 95-105.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 58
    • 0027251256 scopus 로고
    • A structural superfamily of growth factors containing a cystine knot motif
    • MCDONALD, N. Q. & HENDRICKSON, W. A. (1993). A structural superfamily of growth factors containing a cystine knot motif. Cell 73, 421-424.
    • (1993) Cell , vol.73 , pp. 421-424
    • Mcdonald, N.Q.1    Hendrickson, W.A.2
  • 59
    • 0025986121 scopus 로고
    • New-protein fold revealed by a 2·3-Å resolution crystal-structure of nerve growth-factor
    • MCDONALD, N. Q., LAPATTO, R., MURRAYRUST, J., GUNNING, J., WLODAWER, A. & BLUNDELL, T. L. (1991). New-protein fold revealed by a 2·3-Å resolution crystal-structure of nerve growth-factor. Nature 354, 411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • Mcdonald, N.Q.1    Lapatto, R.2    Murrayrust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 60
    • 0027377708 scopus 로고
    • Molecular modelling of the norrie disease protein predicts a cystine knot growth-factor tertiary structure
    • MEITINGER, T., MEINDL, A., BORK, P., ROST, B., SANDER, C., HASSEMANN, M. & MURKEN, J. (1993). Molecular modelling of the norrie disease protein predicts a cystine knot growth-factor tertiary structure. Nature Genetics 5, 376-380.
    • (1993) Nature Genetics , vol.5 , pp. 376-380
    • Meitinger, T.1    Meindl, A.2    Bork, P.3    Rost, B.4    Sander, C.5    Hassemann, M.6    Murken, J.7
  • 61
    • 0028094639 scopus 로고
    • Structure of the extracellular domain of human tissue factor: Location of the factor VIIa bínding site
    • MULLER, Y. A., ULTSCH, M. H., KELLEY, R. F. & DE VOS, A. M. (1994). Structure of the extracellular domain of human tissue factor: location of the factor VIIa bínding site. Biochemistry 33, 10864-10870.
    • (1994) Biochemistry , vol.33 , pp. 10864-10870
    • Muller, Y.A.1    Ultsch, M.H.2    Kelley, R.F.3    De Vos, A.M.4
  • 62
    • 0026744790 scopus 로고
    • Crystal-structure of human platelet-derived growth factor-BB
    • OEFNER, C., DARCY, A., WINKLER, F. K., EGGIMANN, B. & HOSANG, M. (1992). Crystal-structure of human platelet-derived growth factor-BB. EMBO J. 11, 3921-3926.
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    Darcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 63
    • 0028956981 scopus 로고
    • Solution structure of the epithelial cadherin domain responsible for selective cell-adhesion
    • OVERDUIN, M., HARVER, T. S., BAGBY, S., TONG, K. I., YAU, P., TAKEICHI, M. & IKURA, M. (1995). Solution structure of the epithelial cadherin domain responsible for selective cell-adhesion. Science 267, 386-389.
    • (1995) Science , vol.267 , pp. 386-389
    • Overduin, M.1    Harver, T.S.2    Bagby, S.3    Tong, K.I.4    Yau, P.5    Takeichi, M.6    Ikura, M.7
  • 64
    • 0026148460 scopus 로고
    • Exons - Original building blocks of proteins
    • PATTHY, L. (1991). Exons - original building blocks of proteins, Bioessays 13, 187-192.
    • (1991) Bioessays , vol.13 , pp. 187-192
    • Patthy, L.1
  • 65
    • 0027487510 scopus 로고
    • Modular design of proteases of coagulation, fibrinolysis, and complement activation: Implications for protein engineering and structure-function studies
    • PATTHY, L. (1993). Modular design of proteases of coagulation, fibrinolysis, and complement activation: implications for protein engineering and structure-function studies. Methods. Enzymol. 222, 10-21.
    • (1993) Methods. Enzymol. , vol.222 , pp. 10-21
    • Patthy, L.1
  • 66
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • PAWSON, T. (1995). Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 67
    • 0016242709 scopus 로고
    • The three-dimensional structure of the Fab' fragment of a human myeloma immunoglobulin at 2·0-Å resolution
    • POLJAK, R. J., AMZEL, L. M., CHEN, B. L., PHIZACKERLEY, R. P. & SAUL, F. (1974). The three-dimensional structure of the Fab' fragment of a human myeloma immunoglobulin at 2·0-Å resolution. Proc. Nat. Acad. Sci. USA 71, 3440-3444.
    • (1974) Proc. Nat. Acad. Sci. USA , vol.71 , pp. 3440-3444
    • Poljak, R.J.1    Amzel, L.M.2    Chen, B.L.3    Phizackerley, R.P.4    Saul, F.5
  • 71
    • 0026706824 scopus 로고
    • Crystal structure of human immunoglobulin fragment fab new refined at 2·0 Å resolution
    • SAUL, F. A. & POLJAK, R. J. (1992). Crystal structure of human immunoglobulin fragment fab new refined at 2·0 Å resolution. PROTEINS 14, 363-371.
    • (1992) Proteins , vol.14 , pp. 363-371
    • Saul, F.A.1    Poljak, R.J.2
  • 73
    • 0029645288 scopus 로고
    • The solution structure and backbone dynamics of the fibronectin type 1 and epidermal growth factor-like pair of modules of tissue-type plasminogen activator
    • SMITH, B. O., DOWNING, A. K., DRISCOLL, P. C., DUDGEON, T. J. & CAMPBELL, I. D. (1995). The solution structure and backbone dynamics of the fibronectin type 1 and epidermal growth factor-like pair of modules of tissue-type plasminogen activator. Structure 3, 823-833.
    • (1995) Structure , vol.3 , pp. 823-833
    • Smith, B.O.1    Downing, A.K.2    Driscoll, P.C.3    Dudgeon, T.J.4    Campbell, I.D.5
  • 74
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • SMITH, C. A., FARRAH, T. & GOODWIN, R. G. (1994). The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell 76, 959-962.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 75
    • 0028032203 scopus 로고
    • X-ray structure of a growth hormone-prolactinreceptor complex
    • SOMERS, W., ULTSCH, M., DE VOS, A. M. & KOSSIAKOFF, A. A. (1994). X-ray structure of a growth hormone-prolactinreceptor complex. Nature 372, 478-481.
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 77
    • 0022259920 scopus 로고
    • The LDL receptor gene - A mosaic of exons shared with different proteins
    • SUDHOF, T. C., GOLDSTEIN, J. L., BROWN, M. S. & RUSSELL, D. W. (1985). The LDL receptor gene - a mosaic of exons shared with different proteins. Science 228, 815-822.
    • (1985) Science , vol.228 , pp. 815-822
    • Sudhof, T.C.1    Goldstein, J.L.2    Brown, M.S.3    Russell, D.W.4
  • 80
    • 0027049523 scopus 로고
    • Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2
    • TORMO, J., STADLER, E., SKERN, T., AUER, H., KANZLER, O., BETZEL, C., BLAAS, D. & FITA, I. (1992). Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2. Protein Science 1, 1154-1161.
    • (1992) Protein Science , vol.1 , pp. 1154-1161
    • Tormo, J.1    Stadler, E.2    Skern, T.3    Auer, H.4    Kanzler, O.5    Betzel, C.6    Blaas, D.7    Fita, I.8
  • 81
    • 0025770980 scopus 로고
    • The structures of domains of blood proteins
    • TULINSKY (1991). The structures of domains of blood proteins. Thromb. & Haemo. 66, 16-31.
    • (1991) Thromb. & Haemo. , vol.66 , pp. 16-31
    • Tulinsky1
  • 82
    • 0026781840 scopus 로고
    • Refined crystal structure of the influenza virus N9 neuraminidase-NC41 fab complex
    • TULIP, W. R., VARGHESE, J. N., LAVER, W. G., WEBSTER, R. G. & COLMAN, P. M. (1992). Refined crystal structure of the influenza virus N9 neuraminidase-NC41 fab complex. J. Mol. Biol. 227, 122-148.
    • (1992) J. Mol. Biol. , vol.227 , pp. 122-148
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Webster, R.G.4    Colman, P.M.5
  • 83
    • 0028172935 scopus 로고
    • Calcium-dependent interaction between gamma-carboxyglumtamic acid-containing and N-terminal epidermal growth factor-like modules in factor-X
    • VALCARCE, C., HOLMGREN, A. & STENFLO, J. (1994). Calcium-dependent interaction between gamma-carboxyglumtamic acid-containing and N-terminal epidermal growth factor-like modules in factor-X. J. Biol. Chem. 269, 26011-26016.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26011-26016
    • Valcarce, C.1    Holmgren, A.2    Stenflo, J.3
  • 84
    • 0344564905 scopus 로고
    • Autonomous function of structural domains on human tissue-type plasminogen activator
    • VAN ZONNEVELD, A. J., VEERMAN, H. & PANNEKOEK, H. (1986). Autonomous function of structural domains on human tissue-type plasminogen activator. Proc. Natl. Acad. Sci. 83, 4670-4674.
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 4670-4674
    • Van Zonneveld, A.J.1    Veerman, H.2    Pannekoek, H.3
  • 85
    • 0027325517 scopus 로고
    • Extracellular matrix 2: Role of extracellular matrix molecules and their receptors in the nervous system
    • VENSTROM, K. A. & REICHARDT, L. F. (1993). Extracellular matrix 2: role of extracellular matrix molecules and their receptors in the nervous system. FASEB J. 7, 997-1003.
    • (1993) FASEB J. , vol.7 , pp. 997-1003
    • Venstrom, K.A.1    Reichardt, L.F.2
  • 89
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumour necrosis factor receptor
    • WARD, C. W., HOYNE, P. A. & FLEGG, R. H. (1995). Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumour necrosis factor receptor. PROTEINS 22, 141-153.
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 90
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • WEIS, W. I., DRICKAMER, K. & HENDRICKSON, W. A. (1992). Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 91
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • WILLIAMS, A. F. & BARCLAY, A. N. (1988). The immunoglobulin superfamily - domains for cell surface recognition. Ana. Rev. Immunol. 6, 381-405.
    • (1988) Ana. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 92
    • 0028213715 scopus 로고
    • Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity
    • WILLIAMS, M. J., PHAN, I., HARVEY, T. S., ROSTAGNO, A., GOLD, L. I. & CAMPBELL, I. D. (1994). Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity. J. Mol. Biol. 235, 1302-1311.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1302-1311
    • Williams, M.J.1    Phan, I.2    Harvey, T.S.3    Rostagno, A.4    Gold, L.I.5    Campbell, I.D.6
  • 94
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • WILSON, I. A. & STANFIELD, R. L. (1994). Antibody-antigen interactions: new structures and new conformational changes. Cur. Opin. in Struct. Biol. 4, 857-867.
    • (1994) Cur. Opin. in Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 95
    • 0028773646 scopus 로고
    • Structure of human chorionic-conadotropin at 2·6-angstrom resolution from MAD analysis of the selenomethionyl protein
    • WU, H., LUSTBADER, J. W., LIU, Y., CANFIELD, R. E. & HENDRICKSON, W. A. (1994). Structure of human chorionic-conadotropin at 2·6-angstrom resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.