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Volumn 2014, Issue , 2014, Pages

Increasing thermal stability of gelatin by UV-induced cross-linking with glucose

Author keywords

[No Author keywords available]

Indexed keywords

GELATIN; GLUCOSE;

EID: 84902166949     PISSN: 16878787     EISSN: 16878795     Source Type: Journal    
DOI: 10.1155/2014/979636     Document Type: Article
Times cited : (38)

References (54)
  • 1
    • 0037484174 scopus 로고    scopus 로고
    • Modelling tissue-specific signaling and organ function in three dimensions
    • 2-s2.0-0037484174 10.1242/jcs.00503
    • Schmeichel K. L., Bissell M. J., Modelling tissue-specific signaling and organ function in three dimensions. Journal of Cell Science 2003 116 12 2377 2388 2-s2.0-0037484174 10.1242/jcs.00503
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2377-2388
    • Schmeichel, K.L.1    Bissell, M.J.2
  • 2
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • 2-s2.0-0035941075 10.1126/science.1064829
    • Cukierman E., Pankov R., Stevens D. R., Yamada K. M., Taking cell-matrix adhesions to the third dimension. Science 2001 294 5547 1708 1712 2-s2.0-0035941075 10.1126/science.1064829
    • (2001) Science , vol.294 , Issue.5547 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 5
    • 77956481502 scopus 로고    scopus 로고
    • Design of three-dimensional biomimetic scaffolds
    • 2-s2.0-77956481502 10.1002/jbm.a.32834
    • Owen S. C., Shoichet M. S., Design of three-dimensional biomimetic scaffolds. Journal of Biomedical Materials Research A 2010 94 4 1321 1331 2-s2.0-77956481502 10.1002/jbm.a.32834
    • (2010) Journal of Biomedical Materials Research A , vol.94 , Issue.4 , pp. 1321-1331
    • Owen, S.C.1    Shoichet, M.S.2
  • 8
    • 47749121495 scopus 로고    scopus 로고
    • Collagen scaffolds for tissue engineering
    • 2-s2.0-47749121495 10.1002/bip.20871
    • Glowacki J., Mizuno S., Collagen scaffolds for tissue engineering. Biopolymers 2008 89 5 338 344 2-s2.0-47749121495 10.1002/bip.20871
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 338-344
    • Glowacki, J.1    Mizuno, S.2
  • 9
    • 0018597290 scopus 로고
    • Quasi-hexagonal molecular packing in collagen fibrils
    • 2-s2.0-0018597290
    • Hulmes D. J. S., Miller A., Quasi-hexagonal molecular packing in collagen fibrils. Nature 1979 282 5741 878 880 2-s2.0-0018597290
    • (1979) Nature , vol.282 , Issue.5741 , pp. 878-880
    • Hulmes, D.J.S.1    Miller, A.2
  • 10
    • 0031692465 scopus 로고    scopus 로고
    • The collagen fibril: The almost crystalline structure
    • 2-s2.0-0031692465 10.1006/jsbi.1998.3976
    • Prockop D. J., Fertala A., The collagen fibril: the almost crystalline structure. Journal of Structural Biology 1998 122 1-2 111 118 2-s2.0-0031692465 10.1006/jsbi.1998.3976
    • (1998) Journal of Structural Biology , vol.122 , Issue.1-2 , pp. 111-118
    • Prockop, D.J.1    Fertala, A.2
  • 12
    • 0015892994 scopus 로고
    • Analysis of the primary structure of collagen for the origins of molecular packing
    • 2-s2.0-0015892994
    • Hulmes D. J. S., Miller A., Parry D. A. D., Analysis of the primary structure of collagen for the origins of molecular packing. Journal of Molecular Biology 1973 79 1 137 148 2-s2.0-0015892994
    • (1973) Journal of Molecular Biology , vol.79 , Issue.1 , pp. 137-148
    • Hulmes, D.J.S.1    Miller, A.2    Parry, D.A.D.3
  • 13
    • 0028324285 scopus 로고
    • Viscoelastic studies of extracellular matrix interactions in a model native collagen gel system
    • 2-s2.0-0028324285
    • Hsu S., Jamieson A. M., Blackwell J., Viscoelastic studies of extracellular matrix interactions in a model native collagen gel system. Biorheology 1994 31 1 21 36 2-s2.0-0028324285
    • (1994) Biorheology , vol.31 , Issue.1 , pp. 21-36
    • Hsu, S.1    Jamieson, A.M.2    Blackwell, J.3
  • 15
    • 40649123205 scopus 로고    scopus 로고
    • Electro-spinning of pure collagen nano-fibres - Just an expensive way to make gelatin?
    • 2-s2.0-40649123205 10.1016/j.biomaterials.2008.02.009
    • Zeugolis D. I., Khew S. T., Yew E. S. Y., Ekaputra A. K., Tong Y. W., Yung L. Y. L., Hutmacher D. W., Sheppard C., Raghunath M., Electro-spinning of pure collagen nano-fibres-just an expensive way to make gelatin? Biomaterials 2008 29 15 2293 2305 2-s2.0-40649123205 10.1016/j.biomaterials.2008.02.009
    • (2008) Biomaterials , vol.29 , Issue.15 , pp. 2293-2305
    • Zeugolis, D.I.1    Khew, S.T.2    Yew, E.S.Y.3    Ekaputra, A.K.4    Tong, Y.W.5    Yung, L.Y.L.6    Hutmacher, D.W.7    Sheppard, C.8    Raghunath, M.9
  • 16
    • 0141873096 scopus 로고
    • The long range reorganization of gelatin to the collagen structure
    • 2-s2.0-0141873096
    • Veis A., Anesey J., Cohen J., The long range reorganization of gelatin to the collagen structure. Archives of Biochemistry and Biophysics 1961 94 1 20 31 2-s2.0-0141873096
    • (1961) Archives of Biochemistry and Biophysics , vol.94 , Issue.1 , pp. 20-31
    • Veis, A.1    Anesey, J.2    Cohen, J.3
  • 18
    • 0034333644 scopus 로고    scopus 로고
    • Gelatin based resorbable sponge as a carrier matrix for human mesenchymal stem cells in cartilage regeneration therapy
    • Ponticiello M. S., Schinagl R. M., Kadiyala S., Barry F. P., Gelatin based resorbable sponge as a carrier matrix for human mesenchymal stem cells in cartilage regeneration therapy. Journal of Biomedical Materials Research 2000 52 246 255
    • (2000) Journal of Biomedical Materials Research , vol.52 , pp. 246-255
    • Ponticiello, M.S.1    Schinagl, R.M.2    Kadiyala, S.3    Barry, F.P.4
  • 20
    • 3242700527 scopus 로고    scopus 로고
    • Making tissue engineering scaffolds work. Review: The application of solid freeform fabrication technology to the production of tissue engineering scaffolds
    • 2-s2.0-0142227984
    • Sachlos E., Czernuszka J. T., Making tissue engineering scaffolds work. Review: the application of solid freeform fabrication technology to the production of tissue engineering scaffolds. European Cells and Materials Journal 2003 5 29 39 2-s2.0-0142227984
    • (2003) European Cells and Materials Journal , vol.5 , pp. 29-39
    • Sachlos, E.1    Czernuszka, J.T.2
  • 21
    • 84873634183 scopus 로고    scopus 로고
    • Enhanced redifferentiation of chondrocytes on microperiodic silk/gelatin scaffolds: Toward tailor-made tissue engineering
    • 10.1021/bm301193t
    • Das S., Pati F., Chameettachal S., Pahwa S., Ray A. R., Dhara S., Ghosh S., Enhanced redifferentiation of chondrocytes on microperiodic silk/gelatin scaffolds: toward tailor-made tissue engineering. Biomacromolecules 2013 14 2 311 321 10.1021/bm301193t
    • (2013) Biomacromolecules , vol.14 , Issue.2 , pp. 311-321
    • Das, S.1    Pati, F.2    Chameettachal, S.3    Pahwa, S.4    Ray, A.R.5    Dhara, S.6    Ghosh, S.7
  • 22
    • 84879886422 scopus 로고    scopus 로고
    • Structure-property-processing correlations in freeze-cast composite scaffolds
    • 10.1016/j.actbio.2013.01.012
    • Hunger P. M., Donius A. E., Wegst U. G., Structure-property-processing correlations in freeze-cast composite scaffolds. Acta Biomaterialia 2013 9 5 6338 6348 10.1016/j.actbio.2013.01.012
    • (2013) Acta Biomaterialia , vol.9 , Issue.5 , pp. 6338-6348
    • Hunger, P.M.1    Donius, A.E.2    Wegst, U.G.3
  • 23
    • 23944463701 scopus 로고    scopus 로고
    • In vitro characterization of chitosan-gelatin scaffolds for tissue engineering
    • 2-s2.0-23944463701 10.1016/j.biomaterials.2005.05.036
    • Huang Y., Onyeri S., Siewe M., Moshfeghian A., Madihally S. V., In vitro characterization of chitosan-gelatin scaffolds for tissue engineering. Biomaterials 2005 26 36 7616 7627 2-s2.0-23944463701 10.1016/j.biomaterials. 2005.05.036
    • (2005) Biomaterials , vol.26 , Issue.36 , pp. 7616-7627
    • Huang, Y.1    Onyeri, S.2    Siewe, M.3    Moshfeghian, A.4    Madihally, S.V.5
  • 24
    • 84866009498 scopus 로고    scopus 로고
    • Ultraviolet-B radiation induced cross-linking improves physical properties of cold- and warm-water fish gelatin gels and films
    • 10.1111/j.1750-3841.2012.02839.x
    • Otoni C. G., Avena-Bustillos R. J. A., Chiou B. S., Bilbao-Sainz C., Bechtel P. J., McHugh T. H., Ultraviolet-B radiation induced cross-linking improves physical properties of cold- and warm-water fish gelatin gels and films. Journal of Food Science 2012 77 9 E215 E223 10.1111/j.1750-3841.2012. 02839.x
    • (2012) Journal of Food Science , vol.77 , Issue.9
    • Otoni, C.G.1    Avena-Bustillos, R.J.A.2    Chiou, B.S.3    Bilbao-Sainz, C.4    Bechtel, P.J.5    McHugh, T.H.6
  • 25
    • 17044460126 scopus 로고    scopus 로고
    • Sugar cross-linked gelatin for controlled release: Microspheres and disks
    • 2-s2.0-17044460126 10.1016/S0142-9612(98)00034-9
    • Cortesi R., Nastruzzi C., Davis S. S., Sugar cross-linked gelatin for controlled release: microspheres and disks. Biomaterials 1998 19 18 1641 1649 2-s2.0-17044460126 10.1016/S0142-9612(98)00034-9
    • (1998) Biomaterials , vol.19 , Issue.18 , pp. 1641-1649
    • Cortesi, R.1    Nastruzzi, C.2    Davis, S.S.3
  • 27
    • 0031693632 scopus 로고    scopus 로고
    • Cross-linking of proteins by Maillard processes - Model reactions of D-glucose or methylglyoxal with butylamine and guanidine derivatives
    • 2-s2.0-0031693632 10.1016/S0968-0896(98)00058-3
    • Lederer M. O., Gerum F., Severin T., Cross-linking of proteins by Maillard processes-model reactions of D-glucose or methylglyoxal with butylamine and guanidine derivatives. Bioorganic and Medicinal Chemistry 1998 6 7 993 1002 2-s2.0-0031693632 10.1016/S0968-0896(98)00058-3
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.7 , pp. 993-1002
    • Lederer, M.O.1    Gerum, F.2    Severin, T.3
  • 28
    • 40449094797 scopus 로고    scopus 로고
    • Soft textural and emulsifiable gelatin formed by conjugating with fatty-acylated saccharide
    • 2-s2.0-40449094797 10.1271/bbb.70237
    • Nakajima K., Sato M., Hattori M., Yoshida T., Yoshimura K., Takahashi K., Soft textural and emulsifiable gelatin formed by conjugating with fatty-acylated saccharide. Bioscience, Biotechnology and Biochemistry 2008 72 2 295 302 2-s2.0-40449094797 10.1271/bbb.70237
    • (2008) Bioscience, Biotechnology and Biochemistry , vol.72 , Issue.2 , pp. 295-302
    • Nakajima, K.1    Sato, M.2    Hattori, M.3    Yoshida, T.4    Yoshimura, K.5    Takahashi, K.6
  • 29
    • 80052626092 scopus 로고    scopus 로고
    • Effect of xylose on the molecular and particle size distribution of peanut hydrolysate in Maillard reaction system
    • 2-s2.0-80052626092 10.1002/jsfa.4487
    • Su G., Cui C., Ren J., Yang B., Zhao M., Effect of xylose on the molecular and particle size distribution of peanut hydrolysate in Maillard reaction system. Journal of the Science of Food and Agriculture 2011 91 13 2457 2462 2-s2.0-80052626092 10.1002/jsfa.4487
    • (2011) Journal of the Science of Food and Agriculture , vol.91 , Issue.13 , pp. 2457-2462
    • Su, G.1    Cui, C.2    Ren, J.3    Yang, B.4    Zhao, M.5
  • 30
    • 0037024093 scopus 로고    scopus 로고
    • Synergistic effects of glucose and ultraviolet irradiation on the physical properties of collagen
    • 10.1002/jbm.10111
    • Ohan M. P., Weadock K. S., Dunn M. G., Synergistic effects of glucose and ultraviolet irradiation on the physical properties of collagen. Journal of Biomedical Materials Research 2002 60 3 384 391 10.1002/jbm.10111
    • (2002) Journal of Biomedical Materials Research , vol.60 , Issue.3 , pp. 384-391
    • Ohan, M.P.1    Weadock, K.S.2    Dunn, M.G.3
  • 31
    • 33746920337 scopus 로고    scopus 로고
    • Advanced glycation end products: Sparking the development of diabetic vascular injury
    • 2-s2.0-33746920337 10.1161/CIRCULATIONAHA.106.621854
    • Goldin A., Beckman J. A., Schmidt A. M., Creager M. A., Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 2006 114 6 597 605 2-s2.0-33746920337 10.1161/CIRCULATIONAHA.106. 621854
    • (2006) Circulation , vol.114 , Issue.6 , pp. 597-605
    • Goldin, A.1    Beckman, J.A.2    Schmidt, A.M.3    Creager, M.A.4
  • 34
    • 33747068274 scopus 로고    scopus 로고
    • Spectral study of the photolysis of aqueous thiamine hydrochloride and ascorbic acid solutions in the presence and absence of riboflavin
    • 2-s2.0-33747068274
    • Vaid F. H. M., Shaikh R. H., Ansari I. A., Ahmad I., Spectral study of the photolysis of aqueous thiamine hydrochloride and ascorbic acid solutions in the presence and absence of riboflavin. Journal of the Chemical Society of Pakistan 2005 27 3 227 232 2-s2.0-33747068274
    • (2005) Journal of the Chemical Society of Pakistan , vol.27 , Issue.3 , pp. 227-232
    • Vaid, F.H.M.1    Shaikh, R.H.2    Ansari, I.A.3    Ahmad, I.4
  • 35
    • 58149364663 scopus 로고
    • Use of a free radical method to evaluate antioxidant activity
    • 2-s2.0-58149364663
    • Brand-Williams W., Cuvelier M. E., Berset C., Use of a free radical method to evaluate antioxidant activity. LWT: Food Science and Technology 1995 28 1 25 30 2-s2.0-58149364663
    • (1995) LWT: Food Science and Technology , vol.28 , Issue.1 , pp. 25-30
    • Brand-Williams, W.1    Cuvelier, M.E.2    Berset, C.3
  • 36
    • 0001505441 scopus 로고
    • The amino acid composition of mammalian collagen and gelatin
    • 2-s2.0-0001505441
    • EASTOE J. E., The amino acid composition of mammalian collagen and gelatin. The Biochemical Journal 1955 61 4 589 600 2-s2.0-0001505441
    • (1955) The Biochemical Journal , vol.61 , Issue.4 , pp. 589-600
    • Eastoe, J.E.1
  • 37
    • 33747624165 scopus 로고    scopus 로고
    • A potential role for cyclized quinones derived from dopamine, DOPA, and 3,4-dihydroxyphenylacetic acid in proteasomal inhibition
    • 2-s2.0-33747624165 10.1124/mol.106.024703
    • Zafar K. S., Siegel D., Ross D., A potential role for cyclized quinones derived from dopamine, DOPA, and 3,4-dihydroxyphenylacetic acid in proteasomal inhibition. Molecular Pharmacology 2006 70 3 1079 1086 2-s2.0-33747624165 10.1124/mol.106.024703
    • (2006) Molecular Pharmacology , vol.70 , Issue.3 , pp. 1079-1086
    • Zafar, K.S.1    Siegel, D.2    Ross, D.3
  • 38
    • 0029394848 scopus 로고
    • Physical crosslinking of collagen fibers: Comparison of ultraviolet irradiation and dehydrothermal treatment
    • 2-s2.0-0029394848 10.1002/jbm.820291108
    • Weadock K. S., Miller E. J., Bellincampi L. D., Zawadsky J. P., Dunn M. G., Physical crosslinking of collagen fibers: comparison of ultraviolet irradiation and dehydrothermal treatment. Journal of Biomedical Materials Research 1995 29 11 1373 1379 2-s2.0-0029394848 10.1002/jbm.820291108
    • (1995) Journal of Biomedical Materials Research , vol.29 , Issue.11 , pp. 1373-1379
    • Weadock, K.S.1    Miller, E.J.2    Bellincampi, L.D.3    Zawadsky, J.P.4    Dunn, M.G.5
  • 39
    • 0013822618 scopus 로고
    • Ultraviolet light-induced change in collagen macromolecules
    • 2-s2.0-0013822618
    • Fujimori E., Ultraviolet light-induced change in collagen macromolecules. Biopolymers: Peptide Science Section 1965 3 2 115 119 2-s2.0-0013822618
    • (1965) Biopolymers: Peptide Science Section , vol.3 , Issue.2 , pp. 115-119
    • Fujimori, E.1
  • 40
    • 0000360170 scopus 로고
    • The effect of ultraviolet irradiation on soluble collagen
    • Cooper D. R., Davidson R. J., The effect of ultraviolet irradiation on soluble collagen. Biochemical Journal 1965 97 139 147
    • (1965) Biochemical Journal , vol.97 , pp. 139-147
    • Cooper, D.R.1    Davidson, R.J.2
  • 41
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • 2-s2.0-0024448151
    • Gill S. C., Von Hippel P. H., Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry 1989 182 2 319 326 2-s2.0-0024448151
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 42
    • 0025182889 scopus 로고
    • Tyrosine formation from phenylalanine by ultraviolet irradiation
    • 2-s2.0-0025182889
    • Ishimitsu S., Fujimoto S., Ohara A., Tyrosine formation from phenylalanine by ultraviolet irradiation. Chemical and Pharmaceutical Bulletin 1990 38 5 1417 1418 2-s2.0-0025182889
    • (1990) Chemical and Pharmaceutical Bulletin , vol.38 , Issue.5 , pp. 1417-1418
    • Ishimitsu, S.1    Fujimoto, S.2    Ohara, A.3
  • 44
    • 0001078755 scopus 로고
    • The photolysis ( = 254 nm) of tyrosine in aqueous solutions in the absence and presence of oxygen. The reaction of tyrosine with singlet oxygen
    • 2-s2.0-0001078755
    • Jin F., Leitich J., von Sonntag C., The photolysis ( = 254 nm) of tyrosine in aqueous solutions in the absence and presence of oxygen. The reaction of tyrosine with singlet oxygen. Journal of Photochemistry and Photobiology A: Chemistry 1995 92 3 147 153 2-s2.0-0001078755
    • (1995) Journal of Photochemistry and Photobiology A: Chemistry , vol.92 , Issue.3 , pp. 147-153
    • Jin, F.1    Leitich, J.2    Von Sonntag, C.3
  • 46
    • 33748472655 scopus 로고    scopus 로고
    • Spectroscopic studies into the influence of UV radiation on elastin hydrolysates in water solution
    • 2-s2.0-33748472655 10.1016/j.jphotobiol.2006.05.005
    • Sionkowska A., Skopinska J., Wisniewski M., Leznicki A., Fisz J., Spectroscopic studies into the influence of UV radiation on elastin hydrolysates in water solution. Journal of Photochemistry and Photobiology B: Biology 2006 85 1 79 84 2-s2.0-33748472655 10.1016/j.jphotobiol.2006.05.005
    • (2006) Journal of Photochemistry and Photobiology B: Biology , vol.85 , Issue.1 , pp. 79-84
    • Sionkowska, A.1    Skopinska, J.2    Wisniewski, M.3    Leznicki, A.4    Fisz, J.5
  • 47
    • 0017267089 scopus 로고
    • Photo-induced formation of peroxide in saccharides and related compounds
    • 2-s2.0-0017267089
    • Kubota H., Ogiwara Y., Matsuzaki K., Photo-induced formation of peroxide in saccharides and related compounds. Polymer Journal 1976 8 6 557 563 2-s2.0-0017267089
    • (1976) Polymer Journal , vol.8 , Issue.6 , pp. 557-563
    • Kubota, H.1    Ogiwara, Y.2    Matsuzaki, K.3
  • 48
    • 37049137019 scopus 로고
    • Photodegradation of carbohydrates. Part IV: Direct photolysis of d-glucose in aqueous solution
    • 10.1039/J29690000455 2-s2.0-37049137019
    • Phillips G. O., Rickards T., Photodegradation of carbohydrates. Part IV: direct photolysis of d-glucose in aqueous solution. Journal of the Chemical Society B: Physical Organic 1969 455 461 10.1039/J29690000455 2-s2.0-37049137019
    • (1969) Journal of the Chemical Society B: Physical Organic , pp. 455-461
    • Phillips, G.O.1    Rickards, T.2
  • 49
    • 4243357294 scopus 로고
    • Photochemical processes for water treatment
    • 2-s2.0-4243357294
    • Legrini O., Oliveros E., Braun A. M., Photochemical processes for water treatment. Chemical Reviews 1993 93 2 671 698 2-s2.0-4243357294
    • (1993) Chemical Reviews , vol.93 , Issue.2 , pp. 671-698
    • Legrini, O.1    Oliveros, E.2    Braun, A.M.3
  • 50
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II: Modification of amino acids
    • 2-s2.0-0023655407
    • Davies K. J., Delsignore M. E., Lin S. W., Protein damage and degradation by oxygen radicals. II: modification of amino acids. Journal of Biological Chemistry 1987 262 20 9902 9907 2-s2.0-0023655407
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9902-9907
    • Davies, K.J.1    Delsignore, M.E.2    Lin, S.W.3
  • 51
    • 21844438003 scopus 로고    scopus 로고
    • Porous scaffold design for tissue engineering
    • 2-s2.0-21844438003 10.1038/nmat1421
    • Hollister S. J., Porous scaffold design for tissue engineering. Nature Materials 2005 4 7 518 524 2-s2.0-21844438003 10.1038/nmat1421
    • (2005) Nature Materials , vol.4 , Issue.7 , pp. 518-524
    • Hollister, S.J.1
  • 52
    • 67650699256 scopus 로고    scopus 로고
    • Beating behavior of primary neonatal cardiomyocytes and cardiac-differentiated P19.CL6 cells on different extracellular matrix components
    • 2-s2.0-67650699256 10.1007/s10047-009-0449-4
    • Miskon A., Ehashi T., Mahara A., Uyama H., Yamaoka T., Beating behavior of primary neonatal cardiomyocytes and cardiac-differentiated P19.CL6 cells on different extracellular matrix components. Journal of Artificial Organs 2009 12 2 111 117 2-s2.0-67650699256 10.1007/s10047-009-0449-4
    • (2009) Journal of Artificial Organs , vol.12 , Issue.2 , pp. 111-117
    • Miskon, A.1    Ehashi, T.2    Mahara, A.3    Uyama, H.4    Yamaoka, T.5
  • 53
    • 0042657552 scopus 로고
    • The antigenicity of collagen
    • 2-s2.0-0042657552
    • Waksman B. H., Mason H. L., The antigenicity of collagen. Journal of Immunology 1949 63 4 427 433 2-s2.0-0042657552
    • (1949) Journal of Immunology , vol.63 , Issue.4 , pp. 427-433
    • Waksman, B.H.1    Mason, H.L.2
  • 54
    • 0020466583 scopus 로고
    • Age-related differences in human skin collagen: Solubility in solvent, susceptibility to pepsin digestion, and the spectrum of the solubilized polymeric collagen molecules
    • 2-s2.0-0020466583
    • Miyahara T., Murai A., Tanaka T., Age-related differences in human skin collagen: solubility in solvent, susceptibility to pepsin digestion, and the spectrum of the solubilized polymeric collagen molecules. Journals of Gerontology 1982 37 6 651 655 2-s2.0-0020466583
    • (1982) Journals of Gerontology , vol.37 , Issue.6 , pp. 651-655
    • Miyahara, T.1    Murai, A.2    Tanaka, T.3


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