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Volumn 261, Issue 2, 1996, Pages 255-266

Glycosylated threonine but not 4-hydroxyproline dominates the triple helix stabilizing positions in the sequence of a hydrothermal vent worm cuticle collagen

Author keywords

Collagen like peptide; Glycosylation; Invertebrate collagen; Sequence; Triple helix stability

Indexed keywords

COLLAGEN; COLLAGENASE; CYANOGEN BROMIDE; GALACTOSE; HYDROFLUORIC ACID; HYDROXYPROLINE; THREONINE;

EID: 0030590236     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0457     Document Type: Article
Times cited : (61)

References (31)
  • 1
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella, J., Eaton, M., Brodsky, B. & Berman, H. M. (1994). Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science, 266, 75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 2
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella, J., Brodsky, B. & Berman, H. M. (1995). Hydration structure of a collagen peptide. Structure, 3, 893-906.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 3
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg, R. A. & Prockop, D. J. (1973). The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem. Biophys. Res. Commun. 52, 115-120.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 5
    • 0018270937 scopus 로고
    • Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix-coil transition
    • Bruckner, P., Bächinger, H. P., Timpl, R. & Engel, J. (1978). Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix-coil transition. Eur. J. Biochem. 90, 595-603.
    • (1978) Eur. J. Biochem. , vol.90 , pp. 595-603
    • Bruckner, P.1    Bächinger, H.P.2    Timpl, R.3    Engel, J.4
  • 6
    • 0018391677 scopus 로고
    • Hydroxyproline content and location in relation to collagen thermal stability
    • Burjanadze, T. V. (1979). Hydroxyproline content and location in relation to collagen thermal stability. Biopolymers, 18, 931-938.
    • (1979) Biopolymers , vol.18 , pp. 931-938
    • Burjanadze, T.V.1
  • 7
    • 0027068701 scopus 로고
    • The biology of hydrothermal vent animals: Physiology, biochemistry and autotrophic symbiosis
    • Childress, J. J. & Fisher, C. R. (1992). The biology of hydrothermal vent animals: physiology, biochemistry and autotrophic symbiosis. Oceanogr. Mar. Biol. Annu. Rev. 30, 337-441.
    • (1992) Oceanogr. Mar. Biol. Annu. Rev. , vol.30 , pp. 337-441
    • Childress, J.J.1    Fisher, C.R.2
  • 9
    • 0027469958 scopus 로고
    • Aspects of life development at deep sea hydrothermal vents
    • Gaill, F. (1993). Aspects of life development at deep sea hydrothermal vents. FASEB J. 7, 558-565.
    • (1993) FASEB J. , vol.7 , pp. 558-565
    • Gaill, F.1
  • 10
    • 0025879008 scopus 로고
    • Molecular characterization of cuticle and interstitial collagens from worms collected at deep sea hydrothermal vents
    • Gaill, F., Wiedemann, H., Mann, K., Kühn, K., Timpl, R. & Engel, J. (1991). Molecular characterization of cuticle and interstitial collagens from worms collected at deep sea hydrothermal vents. J. Mol. Biol. 221, 209-223.
    • (1991) J. Mol. Biol. , vol.221 , pp. 209-223
    • Gaill, F.1    Wiedemann, H.2    Mann, K.3    Kühn, K.4    Timpl, R.5    Engel, J.6
  • 11
    • 0028946046 scopus 로고
    • Structural comparison of cuticle and interstitial collagens from annelids living in shallow-sea water and at deep-sea hydrothermal vents
    • Gaill, F., Mann, K., Wiedemann, H., Engel, J. & Timpl, R. (1995). Structural comparison of cuticle and interstitial collagens from annelids living in shallow-sea water and at deep-sea hydrothermal vents. J. Mol. Biol. 246, 284-294.
    • (1995) J. Mol. Biol. , vol.246 , pp. 284-294
    • Gaill, F.1    Mann, K.2    Wiedemann, H.3    Engel, J.4    Timpl, R.5
  • 12
    • 0014429786 scopus 로고
    • Occurrence of glycylhydroxyprolyl sequences in earthworm cuticle collagen
    • Goldstein, A. & Adams, E. (1968). Occurrence of glycylhydroxyprolyl sequences in earthworm cuticle collagen. J. Biol. Chem. 243, 3550-3552.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3550-3552
    • Goldstein, A.1    Adams, E.2
  • 13
    • 0014962874 scopus 로고
    • Glycylhydroxyprolyl sequences in earthworm cuticle collagen: Glycylhydroxyprolylserine
    • Goldstein, A. & Adams, E. (1970). Glycylhydroxyprolyl sequences in earthworm cuticle collagen: glycylhydroxyprolylserine. J. Biol. Chem. 245, 5478-5483.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5478-5483
    • Goldstein, A.1    Adams, E.2
  • 14
    • 0027204045 scopus 로고
    • Evolution of the extracellular matrix in invertebrates
    • Har-El, R. & Tanzer, M. L. (1993). Evolution of the extracellular matrix in invertebrates. FASEB J. 7, 1115-1123.
    • (1993) FASEB J. , vol.7 , pp. 1115-1123
    • Har-El, R.1    Tanzer, M.L.2
  • 16
    • 0015731292 scopus 로고
    • A high resolution PAS stain for polyacrylamide gel electrophoresis
    • Kapitany, R. A. & Zebrowski, E. J. (1973). A high resolution PAS stain for polyacrylamide gel electrophoresis. Anal. Biochem. 56, 361-369.
    • (1973) Anal. Biochem. , vol.56 , pp. 361-369
    • Kapitany, R.A.1    Zebrowski, E.J.2
  • 17
    • 0001922158 scopus 로고
    • Biosynthesis of the collagens
    • (Piez, K. A. & Reddi, A. H., eds), Elsevier, New York
    • Kivirikko, K. I. & Myllylä, R. (1984). Biosynthesis of the collagens. In Extracellular Matrix Biochemistry (Piez, K. A. & Reddi, A. H., eds), pp. 83-118, Elsevier, New York.
    • (1984) Extracellular Matrix Biochemistry , pp. 83-118
    • Kivirikko, K.I.1    Myllylä, R.2
  • 18
    • 0027427773 scopus 로고
    • Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence
    • Long, C. G., Braswell, E., Zhu, D., Apigo, J., Baum, J. & Brodsky, B. (1993). Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence. Biochemistry, 32, 11688-11695.
    • (1993) Biochemistry , vol.32 , pp. 11688-11695
    • Long, C.G.1    Braswell, E.2    Zhu, D.3    Apigo, J.4    Baum, J.5    Brodsky, B.6
  • 19
    • 0025009874 scopus 로고
    • The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane
    • Mann, K., Jander, R., Korsching, E., Kühn, K. & Rauterberg, J. (1990). The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane. FEBS Letters, 273, 168-172.
    • (1990) FEBS Letters , vol.273 , pp. 168-172
    • Mann, K.1    Jander, R.2    Korsching, E.3    Kühn, K.4    Rauterberg, J.5
  • 20
    • 0027097977 scopus 로고
    • Amino-acid sequence and cell-adhesion activity of fibril-forming collagen from the tube worm R. pachyptila living at deep sea hydrothermal vents
    • Mann, K., Gaill, F. & Timpl, R. (1992). Amino-acid sequence and cell-adhesion activity of fibril-forming collagen from the tube worm R. pachyptila living at deep sea hydrothermal vents. Eur. J. Biochem. 210, 839-847.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 839-847
    • Mann, K.1    Gaill, F.2    Timpl, R.3
  • 21
    • 0001941260 scopus 로고
    • Chemistry of the collagens and their tissue distribution
    • (Piez, K. A. & Reddi, A.H., eds), Elsevier, New York
    • Miller, E. J. (1984). Chemistry of the collagens and their tissue distribution. In Extracellular Matrix Biochemistry (Piez, K. A. & Reddi, A.H., eds), pp. 41-81, Elsevier, New York.
    • (1984) Extracellular Matrix Biochemistry , pp. 41-81
    • Miller, E.J.1
  • 22
    • 0014670006 scopus 로고
    • Structures of the d-galactose oligosaccharides from earthworm cuticle collagen
    • Muir, L. & Lee, Y. C. (1969). Structures of the d-galactose oligosaccharides from earthworm cuticle collagen. J. Biol. Chem. 244, 2343-2349.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2343-2349
    • Muir, L.1    Lee, Y.C.2
  • 23
    • 0014938989 scopus 로고
    • Glycopeptides from earthworm cuticle collagen
    • Muir, L. & Lee, Y. C. (1970). Glycopeptides from earthworm cuticle collagen. J. Biol. Chem. 245, 502-509.
    • (1970) J. Biol. Chem. , vol.245 , pp. 502-509
    • Muir, L.1    Lee, Y.C.2
  • 24
    • 0003096348 scopus 로고
    • Molecular and aggregate structures of the collagens
    • (Piez, K. A. & Redd, A. H., eds.), Elsevier, New York
    • Piez, K. A. (1984). Molecular and aggregate structures of the collagens. In Extracellular Matrix Biochemistry (Piez, K. A. & Redd, A. H., eds.), pp. 1-39, Elsevier, New York.
    • (1984) Extracellular Matrix Biochemistry , pp. 1-39
    • Piez, K.A.1
  • 25
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov, P. L. (1982). Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35, 1-104.
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 27
    • 0021763953 scopus 로고
    • High-performance liquid chromatographic separation of glycopeptides from Nereis cuticle collagen
    • Sharma, Y. D. & Tanzer, M. L. (1984). High-performance liquid chromatographic separation of glycopeptides from Nereis cuticle collagen. Anal. Biochem. 141, 205-212.
    • (1984) Anal. Biochem. , vol.141 , pp. 205-212
    • Sharma, Y.D.1    Tanzer, M.L.2
  • 28
    • 0019321242 scopus 로고
    • Studies on the carbohydrate of collagens. Characterization of glucuronic acid-mannose disaccharide unit from Nereis cuticle collagen
    • Spiro, R. G. & Bhoyroo, V. D. (1980). Studies on the carbohydrate of collagens. Characterization of glucuronic acid-mannose disaccharide unit from Nereis cuticle collagen. J. Biol. Chem. 255, 5347-5354.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5347-5354
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 29
    • 0027075371 scopus 로고
    • The nature and origin of the modern hydrothermal vent fauna
    • Tunnicliffe, V. (1992). The nature and origin of the modern hydrothermal vent fauna. Palaios, 7, 338-350.
    • (1992) Palaios , vol.7 , pp. 338-350
    • Tunnicliffe, V.1
  • 31
    • 0021079945 scopus 로고
    • Asparaginyl-glucose: Novel type of carbohydrate linkage
    • Wieland, F., Heitzer, R. & Schäfer, W. (1983). Asparaginyl-glucose: novel type of carbohydrate linkage. Proc. Natl Acad. Sci. USA, 80, 5470-5774.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 5470-5774
    • Wieland, F.1    Heitzer, R.2    Schäfer, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.