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Volumn 24, Issue 2, 2003, Pages 61-80

The Structure of Collagen within Parchment - A Review

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL BONDS; CONFORMATIONS; DETERIORATION; FIBERS; MOLECULAR STRUCTURE; OXIDATION; SCANNING ELECTRON MICROSCOPY; SKIN; STRENGTH OF MATERIALS; TENSILE STRENGTH;

EID: 0142228776     PISSN: 00345806     EISSN: None     Source Type: Journal    
DOI: 10.1515/REST.2003.61     Document Type: Review
Times cited : (77)

References (67)
  • 1
    • 0025208008 scopus 로고
    • Deterioration of skin in museum collections
    • Horie, C. V.: Deterioration of skin in museum collections. Polymer Degradation and Stability 29 (1990): 109-133.
    • (1990) Polymer Degradation and Stability , vol.29 , pp. 109-133
    • Horie, C.V.1
  • 4
    • 0022752968 scopus 로고
    • Fiber orientation in calfskin by laser light scattering or X-ray diffraction and quantitative relation to mechanical properties
    • Kronick, P. L., & P. R. Buechler: Fiber orientation in calfskin by laser light scattering or X-ray diffraction and quantitative relation to mechanical properties. Journal of the American Leather Chemists Association 81 (1986): 221-231.
    • (1986) Journal of the American Leather Chemists Association , vol.81 , pp. 221-231
    • Kronick, P.L.1    Buechler, P.R.2
  • 6
    • 0031910194 scopus 로고    scopus 로고
    • Collagen orientation and molecular spacing during creep and stress-relaxation in soft connective tissues
    • Purslow, P. P., T. J. Wess & D. W. L. Hukins: Collagen orientation and molecular spacing during creep and stress-relaxation in soft connective tissues. Journal of Experimental Biology 201 (1998): 135-142.
    • (1998) Journal of Experimental Biology , vol.201 , pp. 135-142
    • Purslow, P.P.1    Wess, T.J.2    Hukins, D.W.L.3
  • 7
    • 0035978878 scopus 로고    scopus 로고
    • Molecular mechanisms of ageing in connective tissues
    • Bailey, A. J.: Molecular mechanisms of ageing in connective tissues. Mechanisms of Ageing and Development 122 (2001): 735-755.
    • (2001) Mechanisms of Ageing and Development , vol.122 , pp. 735-755
    • Bailey, A.J.1
  • 9
    • 0026740073 scopus 로고
    • The collagen superfamily - Diverse structures and assemblies
    • Hulmes, D. J. S.: The collagen superfamily - diverse structures and assemblies. Essays in Biochemistry 27 (1992): 49-67.
    • (1992) Essays in Biochemistry , vol.27 , pp. 49-67
    • Hulmes, D.J.S.1
  • 11
    • 0002097152 scopus 로고
    • Collagen, The collagen family: Structure, assembly and organisation in the extracellular matrix
    • ed. P.M. Royce & B. Steinmann. New York: Wiley-Liss
    • Kielty, C. M., I. Hopkinson & M. E. Grant: Collagen, The collagen family: Structure, assembly and organisation in the extracellular matrix. Connective Tissue and Its Heritable Disorders, ed. P.M. Royce & B. Steinmann. New York: Wiley-Liss 1993: 103-147.
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 103-147
    • Kielty, C.M.1    Hopkinson, I.2    Grant, M.E.3
  • 12
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani, V., M. Raspanti & A. Ruggeri: Collagen structure and functional implications. Micron 32 (2001): 251-260.
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 13
    • 0020010987 scopus 로고
    • Characterisation of fibrous forms of collagen
    • Brodsky, B., & E. F. Eikenberry: Characterisation of fibrous forms of collagen. Methods in Enzymology 82 (1982): 127-174
    • (1982) Methods in Enzymology , vol.82 , pp. 127-174
    • Brodsky, B.1    Eikenberry, E.F.2
  • 16
    • 0003730253 scopus 로고
    • Paper QQ-1, ed. Breese S.S., Jr., Academic Press, New York
    • Hodge A.J., & J.A. Petruska: Electron Microscopy vol. 1, Paper QQ-1, ed. Breese S.S., Jr., Academic Press, New York (1962)
    • (1962) Electron Microscopy , vol.1
    • Hodge, A.J.1    Petruska, J.A.2
  • 17
    • 0002740030 scopus 로고
    • Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule
    • ed. Ramachandran G.N., Academic Press, New York
    • Hodge A.J. & J.A. Petruska: Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule. Aspects of Protein Structure, ed. Ramachandran G.N., Academic Press, New York (1963): 289-300
    • (1963) Aspects of Protein Structure , pp. 289-300
    • Hodge, A.J.1    Petruska, J.A.2
  • 18
    • 0034651554 scopus 로고    scopus 로고
    • The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen
    • Orgel, J. P., T. J. Wess, & A. Miller: The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen. Structure 8:2 (2000): 137-142.
    • (2000) Structure , vol.8 , Issue.2 , pp. 137-142
    • Orgel, J.P.1    Wess, T.J.2    Miller, A.3
  • 19
    • 0034731219 scopus 로고    scopus 로고
    • Changes in collagen structure; drying, dehydrothermal treatment and relation to long term deterioration
    • Wess, T. J., & J. P. Orgel: Changes in collagen structure; drying, dehydrothermal treatment and relation to long term deterioration. Thermochimica Acta 365 (2000): 119-128.
    • (2000) Thermochimica Acta , vol.365 , pp. 119-128
    • Wess, T.J.1    Orgel, J.P.2
  • 20
    • 0142191619 scopus 로고    scopus 로고
    • Analysis of collagen structure in parchment by small angle X-ray diffraction
    • European project SMT4-CT96-2106
    • Wess, T.J.: Analysis of collagen structure in parchment by small angle X-ray diffraction. Handbook in the Micro Analysis of Parchments. European project SMT4-CT96-2106: 269-277.
    • Handbook in the Micro Analysis of Parchments , pp. 269-277
    • Wess, T.J.1
  • 21
    • 0019862889 scopus 로고
    • Proteoglycan-collagen arrangements in developing rat tail tendon
    • Scott, J. E., C. R. Orford & E. W. Hughes: Proteoglycan-collagen arrangements in developing rat tail tendon. Biochemical Journal 195 (1981): 573-581.
    • (1981) Biochemical Journal , vol.195 , pp. 573-581
    • Scott, J.E.1    Orford, C.R.2    Hughes, E.W.3
  • 22
  • 23
    • 0028892860 scopus 로고
    • Tendon response to tensile strength: An ultrastructural investigation of collagen: Proteoglycan interactions in stressed tendon
    • Cribb, A.M., & J. E. Scott: Tendon response to tensile strength: an ultrastructural investigation of collagen: proteoglycan interactions in stressed tendon. Journal of Anatomy 187 (1995): 423-428.
    • (1995) Journal of Anatomy , vol.187 , pp. 423-428
    • Cribb, A.M.1    Scott, J.E.2
  • 24
    • 33745014374 scopus 로고    scopus 로고
    • Peptide sequences in gluteraldehyde-linked proteodermatan sulphate: Collagen fragments from rat tail tendon locate the proteoglycan binding sites
    • Scott, J.E., M. Ritchie, R. W. Glanville & A.D. Cronshaw: Peptide sequences in gluteraldehyde-linked proteodermatan sulphate: collagen fragments from rat tail tendon locate the proteoglycan binding sites. Biochemical Society Transaction 25 (1997): 663.
    • (1997) Biochemical Society Transaction , vol.25 , pp. 663
    • Scott, J.E.1    Ritchie, M.2    Glanville, R.W.3    Cronshaw, A.D.4
  • 25
    • 0018842295 scopus 로고
    • Distribution of macromolecular components in calf dermal connective tissue
    • Tajima, S., & Y. Nagai: Distribution of macromolecular components in calf dermal connective tissue. Connective Tissue Research 7:2 (1980): 65-71.
    • (1980) Connective Tissue Research , vol.7 , Issue.2 , pp. 65-71
    • Tajima, S.1    Nagai, Y.2
  • 26
    • 0031657823 scopus 로고    scopus 로고
    • Supercoiled protein motifs: The collagen triple helix and the α-helical coiled coil
    • Beck, K., & B. Brodsky: Supercoiled protein motifs: the collagen triple helix and the α-helical coiled coil Journal of Structural Biology 122 (1998): 17-29.
    • (1998) Journal of Structural Biology , vol.122 , pp. 17-29
    • Beck, K.1    Brodsky, B.2
  • 30
    • 0031692465 scopus 로고    scopus 로고
    • The collagen fibril: The almost crystalline structure
    • Prockop, D. J., & A. Fertala: The collagen fibril: the almost crystalline structure. Journal of Structural Biology 122 (1998): 111-118.
    • (1998) Journal of Structural Biology , vol.122 , pp. 111-118
    • Prockop, D.J.1    Fertala, A.2
  • 31
    • 27844463782 scopus 로고
    • Effect of cross-links on the quarter-staggered molecular structure of fiber-forming collagen: A finite-element analysis
    • Vanderby jr, R., C. Chen & A. C. Vailas: Effect of cross-links on the quarter-staggered molecular structure of fiber-forming collagen: a finite-element analysis Biomimetics 3:2 (1995): 91-104.
    • (1995) Biomimetics , vol.3 , Issue.2 , pp. 91-104
    • Vanderby R., Jr.1    Chen, C.2    Vailas, A.C.3
  • 32
    • 0020031151 scopus 로고
    • Covalent crosslinking between molecules of type I and type III collagen
    • Henkel, W., & R. W. Glanville: Covalent crosslinking between molecules of type I and type III collagen. European Journal of Biochemistry 122 (1982): 205-213.
    • (1982) European Journal of Biochemistry , vol.122 , pp. 205-213
    • Henkel, W.1    Glanville, R.W.2
  • 33
    • 0029814082 scopus 로고    scopus 로고
    • Cross-link analysis of the C-telopeptide domain from type in collagen
    • Henkel, W.: Cross-link analysis of the C-telopeptide domain from type in collagen. Biochemical Journal 318 (1996): 497-503.
    • (1996) Biochemical Journal , vol.318 , pp. 497-503
    • Henkel, W.1
  • 34
    • 0023069839 scopus 로고
    • The collagens: An overview and update
    • Miller, E. J., & S. Gay: The collagens: an overview and update. Methods in Enzymology 144 (1987): 3-19.
    • (1987) Methods in Enzymology , vol.144 , pp. 3-19
    • Miller, E.J.1    Gay, S.2
  • 35
    • 0036007873 scopus 로고    scopus 로고
    • Insights on the conformational stability of collagen
    • Jenkins, C. L., & R. T. Raines: Insights on the conformational stability of collagen. Natural Product Reports. 19 (2002): 49-59.
    • (2002) Natural Product Reports , vol.19 , pp. 49-59
    • Jenkins, C.L.1    Raines, R.T.2
  • 36
    • 0015232048 scopus 로고
    • Identification of three genetically distinct collagens by cyanogen bromide cleavage in insoluble human skin and cartilage collagen
    • Miller, E. J., Epstein Jr, E. H. & K.A. Piez: Identification of three genetically distinct collagens by cyanogen bromide cleavage in insoluble human skin and cartilage collagen. Biochemical and Biophysical Research Communications 42 (1971): 1024-1029.
    • (1971) Biochemical and Biophysical Research Communications , vol.42 , pp. 1024-1029
    • Miller, E.J.1    Epstein Jr, E.H.2    Piez, K.A.3
  • 37
    • 0036445444 scopus 로고    scopus 로고
    • Structure of type I and type III heterotypic collagen fibrils: An X-ray diffraction study
    • Cameron, G. J., I.L. Alberts, J. H. Laing & T. J. Wess: Structure of type I and type III heterotypic collagen fibrils: an X-ray diffraction study. Journal of Structural Biology 137 (2002): 15-22.
    • (2002) Journal of Structural Biology , vol.137 , pp. 15-22
    • Cameron, G.J.1    Alberts, I.L.2    Laing, J.H.3    Wess, T.J.4
  • 38
    • 0028904399 scopus 로고
    • Structure of the type I collagen molecule based on conformational energy computations: The triple stranded helix and the N-terminal telopeptide
    • Vitagliano, L., G. Nemethy, A. Zagari & H. A. Scheraga: Structure of the type I collagen molecule based on conformational energy computations: the triple stranded helix and the N-terminal telopeptide. Journal of Molecular Biology 247 (1995): 69-80.
    • (1995) Journal of Molecular Biology , vol.247 , pp. 69-80
    • Vitagliano, L.1    Nemethy, G.2    Zagari, A.3    Scheraga, H.A.4
  • 40
    • 0142253833 scopus 로고
    • The preparation of leather and parchment by the Dead Sea scrolls community
    • Poole J. B., & R. Reed: The preparation of leather and parchment by the Dead Sea scrolls community. Technology and Culture 3:1 (1962): 1-26.
    • (1962) Technology and Culture , vol.3 , Issue.1 , pp. 1-26
    • Poole, J.B.1    Reed, R.2
  • 42
  • 43
    • 0022756702 scopus 로고
    • Effects of beaming and tanning on collagen stability, studies by differential scanning calorimetry
    • Kronick P.L., & P. R. Buechler: Effects of beaming and tanning on collagen stability, studies by differential scanning calorimetry. Journal of the American Leather Chemists Association 81 (1986): 213-220.
    • (1986) Journal of the American Leather Chemists Association , vol.81 , pp. 213-220
    • Kronick, P.L.1    Buechler, P.R.2
  • 46
    • 0011145993 scopus 로고
    • The role of microorganisms in the decay of parchment
    • Strzelczyk, A. B., & J. Karbowska: The role of microorganisms in the decay of parchment. Acta Microbiologica Polonica 43:2 (1994): 165-174.
    • (1994) Acta Microbiologica Polonica , vol.43 , Issue.2 , pp. 165-174
    • Strzelczyk, A.B.1    Karbowska, J.2
  • 49
    • 0002554982 scopus 로고
    • Amino acid analysis of leather. Preliminary studies in deterioration, accelerated ageing and conservation of vegetable tanned leather
    • Larsen, R., V. Barkholt & K. Neilsen: Amino acid analysis of leather. Preliminary studies in deterioration, accelerated ageing and conservation of vegetable tanned leather. Das Leder 40 (1989): 153-158.
    • (1989) Das Leder , vol.40 , pp. 153-158
    • Larsen, R.1    Barkholt, V.2    Neilsen, K.3
  • 50
    • 0142191612 scopus 로고
    • The possible link between collagen sequence and structure and its oxidative deterioration pattern
    • STEP Leather Project
    • Larsen, R.: The possible link between collagen sequence and structure and its oxidative deterioration pattern. STEP Leather Project. European Commission DG XII Research Report No. 1 (1994): 59.
    • (1994) European Commission DG XII Research Report No. 1 , vol.1 , pp. 59
    • Larsen, R.1
  • 51
    • 0142191607 scopus 로고
    • A study of the oxidative degradation of gelatin and collagen by aqueous hydrogen peroxide solutions
    • Deasy, C.L., & S. C. Michele sr: A study of the oxidative degradation of gelatin and collagen by aqueous hydrogen peroxide solutions. Journal of the American Leather Chemists Association 60 (1965): 665-674.
    • (1965) Journal of the American Leather Chemists Association , vol.60 , pp. 665-674
    • Deasy, C.L.1    Michele Sr, S.C.2
  • 52
    • 0142191606 scopus 로고    scopus 로고
    • Detection of radicals in collagen and parchment produced by natural and artificial deterioration
    • European project SMT4-CT96-2106
    • Hansen, D. J., K. Nielsen & S. B. Rasmussen: Detection of radicals in collagen and parchment produced by natural and artificial deterioration. Handbook in the Micro Analysis of Parchments. European project SMT4-CT96-2106 (1999): 227-236.
    • (1999) Handbook in the Micro Analysis of Parchments , pp. 227-236
    • Hansen, D.J.1    Nielsen, K.2    Rasmussen, S.B.3
  • 53
    • 0030452782 scopus 로고    scopus 로고
    • EPR detection of free radicals in UV-irradiated skin: Mouse versus human
    • Jurkiewicz, B. A., & G. R. Buettner: EPR detection of free radicals in UV-irradiated skin: mouse versus human. Photochemistry and Photobiology 64:6 (1996): 918-922.
    • (1996) Photochemistry and Photobiology , vol.64 , Issue.6 , pp. 918-922
    • Jurkiewicz, B.A.1    Buettner, G.R.2
  • 54
    • 0028056803 scopus 로고
    • Ultraviolet light-induced free radical formation in skin: An electron paramagnetic resonance study
    • Jurkiewicz, B.A., & G. R. Buettner: Ultraviolet light-induced free radical formation in skin: an electron paramagnetic resonance study. Photochemistry and Photobiology 59:1 (1994): 1-4.
    • (1994) Photochemistry and Photobiology , vol.59 , Issue.1 , pp. 1-4
    • Jurkiewicz, B.A.1    Buettner, G.R.2
  • 55
    • 0142191605 scopus 로고
    • Degradation of collagen by metal ion-hydrogen peroxide systems I. Evidence for a free radical catalysed depolymerisation mechanism
    • Deasy, C. L.: Degradation of collagen by metal ion-hydrogen peroxide systems I. Evidence for a free radical catalysed depolymerisation mechanism. Journal of the American Leather Chemists Association 62 (1967): 258-269.
    • (1967) Journal of the American Leather Chemists Association , vol.62 , pp. 258-269
    • Deasy, C.L.1
  • 57
    • 0001378397 scopus 로고
    • Dead Sea Scroll parchments: Unfolding of the collagen molecules and racemisation of aspartic acid
    • Weiner, S., Z. Kustanovich, E. Gil-Av & W. Traub: Dead Sea Scroll parchments: unfolding of the collagen molecules and racemisation of aspartic acid. Nature 287 (1980): 820-823.
    • (1980) Nature , vol.287 , pp. 820-823
    • Weiner, S.1    Kustanovich, Z.2    Gil-Av, E.3    Traub, W.4
  • 58
    • 0033682146 scopus 로고    scopus 로고
    • Gelatin-gluteraldehyde supramolecular structures studied by laser light scattering
    • Sharma, J., & H. B. Bohidar: Gelatin-gluteraldehyde supramolecular structures studied by laser light scattering. European Polymer Journal 36 (2000): 409-1418.
    • (2000) European Polymer Journal , vol.36 , pp. 409-1418
    • Sharma, J.1    Bohidar, H.B.2
  • 59
    • 0020764859 scopus 로고
    • The structure and properties of solid gelatin and the principles of their modification
    • Koslov, P. V., & G. I. Burdygina: The structure and properties of solid gelatin and the principles of their modification. Polymer 24 (1983): 651-665.
    • (1983) Polymer , vol.24 , pp. 651-665
    • Koslov, P.V.1    Burdygina, G.I.2
  • 60
    • 0142191604 scopus 로고    scopus 로고
    • Examination of heat damaged parchment. Master thesis. Copenhagen: School of Conservation
    • Hassel, B.: Examination of heat damaged parchment. Master thesis. Copenhagen: School of Conservation, The Royal Danish Academy of Fine Arts 2001.
    • (2001) The Royal Danish Academy of Fine Arts
    • Hassel, B.1
  • 62
    • 0017111428 scopus 로고
    • Reconstitution of collagen-fold structure with stretching of gelatin film
    • Tanioka, A., K. Miyasaka & K. Ishikawa: Reconstitution of collagen-fold structure with stretching of gelatin film. Biopolymers 15 (1976): 1505-1511.
    • (1976) Biopolymers , vol.15 , pp. 1505-1511
    • Tanioka, A.1    Miyasaka, K.2    Ishikawa, K.3
  • 65
    • 0026472641 scopus 로고
    • Modification in amino acids of Dead Sea Scrolls parchments
    • Sobel, H., & H. Ajie: Modification in amino acids of Dead Sea Scrolls parchments. Free Radical Biology and Medicine 13 (1992): 701-702.
    • (1992) Free Radical Biology and Medicine , vol.13 , pp. 701-702
    • Sobel, H.1    Ajie, H.2
  • 66
    • 0021212838 scopus 로고
    • Participation of the α2(I) chain of bovine skin collagen in the formation of mature crosslinks
    • Heidemann, E., & N. Linnert: Participation of the α2(I) chain of bovine skin collagen in the formation of mature crosslinks. Hoppe-Seyler's Zeitschrift fur Physiologische Chemie. 365 (1984): 781-789.
    • (1984) Hoppe-Seyler's Zeitschrift fur Physiologische Chemie , vol.365 , pp. 781-789
    • Heidemann, E.1    Linnert, N.2
  • 67
    • 0036483747 scopus 로고    scopus 로고
    • Racemisation of aspartic acid in human proteins
    • Ritz-Timme, S., & M. J. Collins: Racemisation of aspartic acid in human proteins. Ageing Research Reviews 1 (2002): 43-59.
    • (2002) Ageing Research Reviews , vol.1 , pp. 43-59
    • Ritz-Timme, S.1    Collins, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.