메뉴 건너뛰기




Volumn 37, Issue 5, 2008, Pages 317-327

Averaged and Depth-Dependent Anisotropy of Articular Cartilage by Microscopic Imaging

Author keywords

anisotropy; cartilage; collagen; ellipse; Fourier transform infrared imaging; magnetic resonance imaging; model; polarized light microscopy; transmission electron microscopy

Indexed keywords

ANISOTROPY; ARTICLE; ARTICULAR CARTILAGE; INFRARED SPECTROSCOPY; JOINT RADIOGRAPHY; MOLECULAR IMAGING; NUCLEAR MAGNETIC RESONANCE IMAGING; POLARIZATION MICROSCOPY; PRIORITY JOURNAL; TRANSMISSION ELECTRON MICROSCOPY;

EID: 40749096367     PISSN: 00490172     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semarthrit.2007.07.001     Document Type: Article
Times cited : (36)

References (73)
  • 1
    • 0034902793 scopus 로고    scopus 로고
    • Quantitative in situ correlation between microscopic MRI and polarized light microscopy studies of articular cartilage
    • Xia Y., Moody J., Burton-Wurster N., and Lust G. Quantitative in situ correlation between microscopic MRI and polarized light microscopy studies of articular cartilage. Osteoarthritis Cartilage 9 (2001) 393-406
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 393-406
    • Xia, Y.1    Moody, J.2    Burton-Wurster, N.3    Lust, G.4
  • 2
    • 0015150915 scopus 로고
    • Articular cartilage: a review and scanning electron microscope study
    • Clarke I.C. Articular cartilage: a review and scanning electron microscope study. J Bone Joint Surg Br 53 (1971) 732-750
    • (1971) J Bone Joint Surg Br , vol.53 , pp. 732-750
    • Clarke, I.C.1
  • 3
    • 0020702090 scopus 로고
    • Structure of proteoglycans from different layers of human articular cartilage
    • Bayliss M., Venn M., Maroudas A., and Ali S.Y. Structure of proteoglycans from different layers of human articular cartilage. Biochem J 209 (1983) 387-400
    • (1983) Biochem J , vol.209 , pp. 387-400
    • Bayliss, M.1    Venn, M.2    Maroudas, A.3    Ali, S.Y.4
  • 4
    • 0026016752 scopus 로고
    • The effect of osmotic and mechanical pressures on water partitioning in articular cartilage
    • Maroudas A., Wachtel E.J., Grushko G., Katz E.P., and Weinberg P. The effect of osmotic and mechanical pressures on water partitioning in articular cartilage. Biochim Biophys Acta 1073 (1991) 285-294
    • (1991) Biochim Biophys Acta , vol.1073 , pp. 285-294
    • Maroudas, A.1    Wachtel, E.J.2    Grushko, G.3    Katz, E.P.4    Weinberg, P.5
  • 5
    • 0028584326 scopus 로고
    • Light and electron microscopical immunohistochemical localization of the small proteoglycan core proteins decorin and biglycan in human knee joint cartilage
    • Miosge N., Flachsbart K., Goetz W., Schultz W., Kresse H., and Herken R. Light and electron microscopical immunohistochemical localization of the small proteoglycan core proteins decorin and biglycan in human knee joint cartilage. Histochem J 26 (1994) 939-945
    • (1994) Histochem J , vol.26 , pp. 939-945
    • Miosge, N.1    Flachsbart, K.2    Goetz, W.3    Schultz, W.4    Kresse, H.5    Herken, R.6
  • 6
    • 0036403676 scopus 로고    scopus 로고
    • Mechano-electrochemical properties of articular cartilage: their inhomogeneities and anisotropies
    • Mow V.C., and Guo X.E. Mechano-electrochemical properties of articular cartilage: their inhomogeneities and anisotropies. Ann Rev Biomed Eng 4 (2002) 175-209
    • (2002) Ann Rev Biomed Eng , vol.4 , pp. 175-209
    • Mow, V.C.1    Guo, X.E.2
  • 7
    • 0014298912 scopus 로고
    • An ultrastructural study of normal young adult human articular cartilage
    • Weiss C., Rosenberg L., and Helfet A.J. An ultrastructural study of normal young adult human articular cartilage. J Bone Joint Surg Am 50 (1968) 663-674
    • (1968) J Bone Joint Surg Am , vol.50 , pp. 663-674
    • Weiss, C.1    Rosenberg, L.2    Helfet, A.J.3
  • 8
    • 0025856481 scopus 로고
    • Three-dimensional collagen architecture in bovine articular cartilage
    • Jeffery A.K., Blunn G.W., Archer C.W., and Bentley G. Three-dimensional collagen architecture in bovine articular cartilage. J Bone Joint Surg Br 73 (1991) 795-801
    • (1991) J Bone Joint Surg Br , vol.73 , pp. 795-801
    • Jeffery, A.K.1    Blunn, G.W.2    Archer, C.W.3    Bentley, G.4
  • 9
    • 0017362911 scopus 로고
    • Chemical composition and swelling of normal and osteoarthritic femoral head cartilage
    • Venn M., and Maroudas A. Chemical composition and swelling of normal and osteoarthritic femoral head cartilage. Ann Rheum Dis 36 (1977) 121-129
    • (1977) Ann Rheum Dis , vol.36 , pp. 121-129
    • Venn, M.1    Maroudas, A.2
  • 10
    • 0018938305 scopus 로고
    • Further studies on the composition of human femoral head cartilage
    • Maroudas A., Bayliss M.T., and Venn M. Further studies on the composition of human femoral head cartilage. Ann Rheum Dis 39 (1980) 514-534
    • (1980) Ann Rheum Dis , vol.39 , pp. 514-534
    • Maroudas, A.1    Bayliss, M.T.2    Venn, M.3
  • 11
    • 0030923403 scopus 로고    scopus 로고
    • Articular cartilage I. Tissue design and chondrocyte matrix interactions
    • Buckwalter J.A., and Mankin H. Articular cartilage I. Tissue design and chondrocyte matrix interactions. J Bone Joint Surg Am 79 (1997) 600-611
    • (1997) J Bone Joint Surg Am , vol.79 , pp. 600-611
    • Buckwalter, J.A.1    Mankin, H.2
  • 12
    • 0020999843 scopus 로고
    • Proteoglycans as organizers of the intercellular matrix
    • Muir H. Proteoglycans as organizers of the intercellular matrix. Biochem Soc Trans 11 (1983) 613-622
    • (1983) Biochem Soc Trans , vol.11 , pp. 613-622
    • Muir, H.1
  • 13
    • 0019538619 scopus 로고
    • Regional histochemical and thickness variations of adult canine articular cartilage
    • Kincaid S.A., and Van Sickle D.C. Regional histochemical and thickness variations of adult canine articular cartilage. Am J Vet Res 42 (1981) 428-432
    • (1981) Am J Vet Res , vol.42 , pp. 428-432
    • Kincaid, S.A.1    Van Sickle, D.C.2
  • 14
    • 0022921867 scopus 로고
    • Composition and glycosaminoglycan metabolism of articular cartilage from habitually loaded and habitually unloaded sites
    • Slowman S.D., and Brandt K.D. Composition and glycosaminoglycan metabolism of articular cartilage from habitually loaded and habitually unloaded sites. Arthritis Rheum 29 (1986) 88-94
    • (1986) Arthritis Rheum , vol.29 , pp. 88-94
    • Slowman, S.D.1    Brandt, K.D.2
  • 15
    • 0023162564 scopus 로고
    • Topographical variation of glycosaminoglycan content and cartilage thickness in canine knee (stifle) joint cartilage. Application of the microspectrophotometric method
    • Kiviranta I., Tammi M., Jurvelin J., and Helminen H.J. Topographical variation of glycosaminoglycan content and cartilage thickness in canine knee (stifle) joint cartilage. Application of the microspectrophotometric method. J Anat 150 (1987) 265-276
    • (1987) J Anat , vol.150 , pp. 265-276
    • Kiviranta, I.1    Tammi, M.2    Jurvelin, J.3    Helminen, H.J.4
  • 16
    • 0031228045 scopus 로고    scopus 로고
    • Variations in the mechanical properties of cartilage from the canine scapulohumeral joint
    • Korvick D., and Athanasiou K. Variations in the mechanical properties of cartilage from the canine scapulohumeral joint. Am J Vet Res 58 (1997) 949-953
    • (1997) Am J Vet Res , vol.58 , pp. 949-953
    • Korvick, D.1    Athanasiou, K.2
  • 17
    • 0031569981 scopus 로고    scopus 로고
    • Variations in composition of cartilage from the shoulder joints of young adult dogs at risk for developing canine hip dysplasia
    • Farquhar T., Bertram J., Todhunter R.J., Burton-Wurster N., and Lust G. Variations in composition of cartilage from the shoulder joints of young adult dogs at risk for developing canine hip dysplasia. J Am Vet Med Assoc 210 (1997) 1483-1485
    • (1997) J Am Vet Med Assoc , vol.210 , pp. 1483-1485
    • Farquhar, T.1    Bertram, J.2    Todhunter, R.J.3    Burton-Wurster, N.4    Lust, G.5
  • 18
    • 0031896799 scopus 로고    scopus 로고
    • Correlation between biochemical composition and magnetic resonance appearance of articular cartilage
    • Fragonas E., Mlynarik V., Jellus V., Micali F., Piras A., Toffanin R., et al. Correlation between biochemical composition and magnetic resonance appearance of articular cartilage. Osteoarthritis Cartilage 6 (1998) 24-32
    • (1998) Osteoarthritis Cartilage , vol.6 , pp. 24-32
    • Fragonas, E.1    Mlynarik, V.2    Jellus, V.3    Micali, F.4    Piras, A.5    Toffanin, R.6
  • 19
    • 0033087819 scopus 로고    scopus 로고
    • Influence of site and age on biochemical characteristics of the collagen network of equine articular cartilage
    • Brama P.A., TeKoppele J.M., Bank R.A., van Weeren P.R., and Barneveld A. Influence of site and age on biochemical characteristics of the collagen network of equine articular cartilage. Am J Vet Res 60 (1999) 341-345
    • (1999) Am J Vet Res , vol.60 , pp. 341-345
    • Brama, P.A.1    TeKoppele, J.M.2    Bank, R.A.3    van Weeren, P.R.4    Barneveld, A.5
  • 20
    • 0034038540 scopus 로고    scopus 로고
    • Heterogeneity of cartilage laminae in MR imaging
    • Xia Y. Heterogeneity of cartilage laminae in MR imaging. J Magn Reson Imaging 11 (2000) 686-693
    • (2000) J Magn Reson Imaging , vol.11 , pp. 686-693
    • Xia, Y.1
  • 21
    • 0034307816 scopus 로고    scopus 로고
    • Collagen fibrils are differently organized in weight-bearing and not-weight-bearing regions of pig articular cartilage
    • Gomez S., Toffanin R., Bernstorff S., Romanello M., Amenitsch H., Rappolt M., et al. Collagen fibrils are differently organized in weight-bearing and not-weight-bearing regions of pig articular cartilage. J Exp Zool 287 5 (2000) 346-352
    • (2000) J Exp Zool , vol.287 , Issue.5 , pp. 346-352
    • Gomez, S.1    Toffanin, R.2    Bernstorff, S.3    Romanello, M.4    Amenitsch, H.5    Rappolt, M.6
  • 22
    • 0036072785 scopus 로고    scopus 로고
    • Characteristics of topographical heterogeneity of articular cartilage over the joint surface of a humeral head
    • Xia Y., Moody J., Alhadlaq H., Burton-Wurster N., and Lust G. Characteristics of topographical heterogeneity of articular cartilage over the joint surface of a humeral head. Osteoarthritis Cartilage 10 (2002) 370-380
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 370-380
    • Xia, Y.1    Moody, J.2    Alhadlaq, H.3    Burton-Wurster, N.4    Lust, G.5
  • 23
    • 0037371647 scopus 로고    scopus 로고
    • Imaging the physical and morphological properties of a multi-zone young articular cartilage at microscopic resolution
    • Xia Y., Moody J., Alhadlaq H., and Hu J.N. Imaging the physical and morphological properties of a multi-zone young articular cartilage at microscopic resolution. J Magn Reson Imaging 17 (2003) 365-374
    • (2003) J Magn Reson Imaging , vol.17 , pp. 365-374
    • Xia, Y.1    Moody, J.2    Alhadlaq, H.3    Hu, J.N.4
  • 24
    • 0030306662 scopus 로고    scopus 로고
    • Contrast in NMR imaging and microscopy
    • Xia Y. Contrast in NMR imaging and microscopy. Concepts Magn Reson 8 (1996) 205-225
    • (1996) Concepts Magn Reson , vol.8 , pp. 205-225
    • Xia, Y.1
  • 27
    • 0035163230 scopus 로고    scopus 로고
    • Protocol issues for delayed Gd(DTPA)(2-)-enhanced MRI (dGEMRIC) for clinical evaluation of articular cartilage
    • Burstein D., Velyvis J., Scott K.T., Stock K.W., Kim Y.J., Jaramillo D., et al. Protocol issues for delayed Gd(DTPA)(2-)-enhanced MRI (dGEMRIC) for clinical evaluation of articular cartilage. Magn Reson Med 45 (2001) 36-41
    • (2001) Magn Reson Med , vol.45 , pp. 36-41
    • Burstein, D.1    Velyvis, J.2    Scott, K.T.3    Stock, K.W.4    Kim, Y.J.5    Jaramillo, D.6
  • 28
    • 2442677996 scopus 로고    scopus 로고
    • Detecting structural changes in early experimental osteoarthritis of tibial cartilage by microscopic MRI and polarized light microscopy
    • Alhadlaq H., Xia Y., Moody J.B., and Matyas J. Detecting structural changes in early experimental osteoarthritis of tibial cartilage by microscopic MRI and polarized light microscopy. Ann Rheum Dis 63 (2004) 709-717
    • (2004) Ann Rheum Dis , vol.63 , pp. 709-717
    • Alhadlaq, H.1    Xia, Y.2    Moody, J.B.3    Matyas, J.4
  • 29
    • 27744517267 scopus 로고    scopus 로고
    • Osteoarthritis of the knee: comparison of MR imaging findings with radiographic severity measurements and pain in middle-aged women
    • Hayes C.W., Jamadar D.A., Welch G.W., Jannausch M.L., Lachance L.L., Capul D.C., et al. Osteoarthritis of the knee: comparison of MR imaging findings with radiographic severity measurements and pain in middle-aged women. Radiology 237 (2005) 998-1007
    • (2005) Radiology , vol.237 , pp. 998-1007
    • Hayes, C.W.1    Jamadar, D.A.2    Welch, G.W.3    Jannausch, M.L.4    Lachance, L.L.5    Capul, D.C.6
  • 30
    • 33745161076 scopus 로고    scopus 로고
    • Magnetic resonance imaging (MRI) of articular cartilage in knee osteoarthritis (OA): morphological assessment
    • Eckstein F., Cicuttini F., Raynauld J.P., Waterton J.C., and Peterfy C. Magnetic resonance imaging (MRI) of articular cartilage in knee osteoarthritis (OA): morphological assessment. Osteoarthritis Cartilage 14 Suppl A (2006) A46-A75
    • (2006) Osteoarthritis Cartilage , vol.14 , Issue.SUPPL. A
    • Eckstein, F.1    Cicuttini, F.2    Raynauld, J.P.3    Waterton, J.C.4    Peterfy, C.5
  • 33
    • 33751353597 scopus 로고    scopus 로고
    • Sodium and T1rho MRI for molecular and diagnostic imaging of articular cartilage
    • Borthakur A., Mellon E., Niyogi S., Witschey W., Kneeland J.B., and Reddy R. Sodium and T1rho MRI for molecular and diagnostic imaging of articular cartilage. NMR Biomed 19 (2006) 781-821
    • (2006) NMR Biomed , vol.19 , pp. 781-821
    • Borthakur, A.1    Mellon, E.2    Niyogi, S.3    Witschey, W.4    Kneeland, J.B.5    Reddy, R.6
  • 37
    • 0031809322 scopus 로고    scopus 로고
    • Relaxation anisotropy in cartilage by NMR microscopy (μMRI) at 14 μm resolution
    • Xia Y. Relaxation anisotropy in cartilage by NMR microscopy (μMRI) at 14 μm resolution. Magn Reson Med 39 (1998) 941-949
    • (1998) Magn Reson Med , vol.39 , pp. 941-949
    • Xia, Y.1
  • 38
    • 0027177336 scopus 로고
    • Effects of collagen orientation on MR imaging characteristics of bovine articular cartilage
    • Rubenstein J.D., Kim J.K., Morava-Protzner I., Stanchev P.L., and Henkelman R.M. Effects of collagen orientation on MR imaging characteristics of bovine articular cartilage. Radiology 188 (1993) 219-226
    • (1993) Radiology , vol.188 , pp. 219-226
    • Rubenstein, J.D.1    Kim, J.K.2    Morava-Protzner, I.3    Stanchev, P.L.4    Henkelman, R.M.5
  • 39
    • 0033814727 scopus 로고    scopus 로고
    • Magic angle effect in MRI of articular cartilage-a review
    • Xia Y. Magic angle effect in MRI of articular cartilage-a review. Invest Radiol 35 (2000) 602-621
    • (2000) Invest Radiol , vol.35 , pp. 602-621
    • Xia, Y.1
  • 40
    • 0036708126 scopus 로고    scopus 로고
    • Orientational dependence of T2 relaxation in articular cartilage: a microscopic MRI (μMRI) study
    • Xia Y., Moody J., and Alhadlaq H. Orientational dependence of T2 relaxation in articular cartilage: a microscopic MRI (μMRI) study. Magn Reson Med 48 (2002) 460-469
    • (2002) Magn Reson Med , vol.48 , pp. 460-469
    • Xia, Y.1    Moody, J.2    Alhadlaq, H.3
  • 42
    • 0343619350 scopus 로고    scopus 로고
    • Visualization of pressure distribution within loaded joint cartilage by application of angle-sensitive NMR microscopy
    • Gründer W., Kanowski M., Wagner M., and Werner A. Visualization of pressure distribution within loaded joint cartilage by application of angle-sensitive NMR microscopy. Magn Reson Med 43 (2000) 884-891
    • (2000) Magn Reson Med , vol.43 , pp. 884-891
    • Gründer, W.1    Kanowski, M.2    Wagner, M.3    Werner, A.4
  • 43
    • 0035667838 scopus 로고    scopus 로고
    • Biochemical (and functional) imaging of articular cartilage
    • Gray M.L., Burstein D., and Xia Y. Biochemical (and functional) imaging of articular cartilage. Semin Musculoskelet Radiol 5 (2001) 329-344
    • (2001) Semin Musculoskelet Radiol , vol.5 , pp. 329-344
    • Gray, M.L.1    Burstein, D.2    Xia, Y.3
  • 44
    • 0034741671 scopus 로고    scopus 로고
    • T2 relaxation reveals spatial collagen architecture in articular cartilage: a comparative quantitative MRI and polarized light microscopic study
    • Nieminen M.T., Rieppo J., Toyras J., Hakumaki J.M., Silvennoinen J., Hyttinen M.M., et al. T2 relaxation reveals spatial collagen architecture in articular cartilage: a comparative quantitative MRI and polarized light microscopic study. Magn Reson Med 46 (2001) 487-493
    • (2001) Magn Reson Med , vol.46 , pp. 487-493
    • Nieminen, M.T.1    Rieppo, J.2    Toyras, J.3    Hakumaki, J.M.4    Silvennoinen, J.5    Hyttinen, M.M.6
  • 45
    • 0034999398 scopus 로고    scopus 로고
    • Bilaminar pattern of tibial condyle cartilage layer on the fat-suppressed 3D gradient echo images: artifact or structural and biochemical difference in composition of cartilage?
    • Trattnig S., Mlynarik V., Jung B., Bader T., Sulzbacher I., Herneth A., et al. Bilaminar pattern of tibial condyle cartilage layer on the fat-suppressed 3D gradient echo images: artifact or structural and biochemical difference in composition of cartilage?. Magn Reson Imaging 19 (2001) 187-192
    • (2001) Magn Reson Imaging , vol.19 , pp. 187-192
    • Trattnig, S.1    Mlynarik, V.2    Jung, B.3    Bader, T.4    Sulzbacher, I.5    Herneth, A.6
  • 46
    • 0036898923 scopus 로고    scopus 로고
    • Detection of changes in cartilage water content using MRI T2-mapping in vivo
    • Liess C., Lusse S., Karger N., Heller M., and Gluer C.C. Detection of changes in cartilage water content using MRI T2-mapping in vivo. Osteoarthritis Cartilage 10 (2002) 907-913
    • (2002) Osteoarthritis Cartilage , vol.10 , pp. 907-913
    • Liess, C.1    Lusse, S.2    Karger, N.3    Heller, M.4    Gluer, C.C.5
  • 47
    • 0036939395 scopus 로고    scopus 로고
    • MR microscopy of articular cartilage at 1.5 T: orientation and site dependence of laminar structures
    • Yoshioka H., Haishi T., Uematsu T., Matsuda Y., Anno I., Echigo J., et al. MR microscopy of articular cartilage at 1.5 T: orientation and site dependence of laminar structures. Skeletal Radiol 31 (2002) 505-510
    • (2002) Skeletal Radiol , vol.31 , pp. 505-510
    • Yoshioka, H.1    Haishi, T.2    Uematsu, T.3    Matsuda, Y.4    Anno, I.5    Echigo, J.6
  • 49
    • 0002466727 scopus 로고
    • Methods applicable to the study of both fresh and fixed materials
    • Jones R.M. (Ed), Hafner Publishing Co, New York
    • Bennett H.S. Methods applicable to the study of both fresh and fixed materials. In: Jones R.M. (Ed). McClung's handbook of microscopic technique. 3rd ed. (1967), Hafner Publishing Co, New York
    • (1967) McClung's handbook of microscopic technique. 3rd ed.
    • Bennett, H.S.1
  • 50
    • 0029876353 scopus 로고    scopus 로고
    • Decreased birefringence of the superficial zone collagen network in the canine knee (stifle) articular cartilage after long distance running training, detected by quantitative polarized light microscopy
    • Arokoski J.P., Hyttinen M.M., Lapveteläinen T., Takacs P., Kosztaczky B., Modis L., et al. Decreased birefringence of the superficial zone collagen network in the canine knee (stifle) articular cartilage after long distance running training, detected by quantitative polarized light microscopy. Ann Rheum Dis 55 (1996) 253-264
    • (1996) Ann Rheum Dis , vol.55 , pp. 253-264
    • Arokoski, J.P.1    Hyttinen, M.M.2    Lapveteläinen, T.3    Takacs, P.4    Kosztaczky, B.5    Modis, L.6
  • 51
    • 0028872085 scopus 로고
    • New polarized light microscope with precision universal compensator
    • Oldenbourg R., and Mei G. New polarized light microscope with precision universal compensator. J Microsc 180 Pt. 2 (1995) 140-147
    • (1995) J Microsc , vol.180 , Issue.PART 2 , pp. 140-147
    • Oldenbourg, R.1    Mei, G.2
  • 53
    • 27744498116 scopus 로고    scopus 로고
    • Fourier transform infrared imaging spectroscopic analysis of tissue engineered cartilage: histologic and biochemical correlations
    • Kim M., Bi X., Horton W.E., Spencer R.G., and Camacho N.P. Fourier transform infrared imaging spectroscopic analysis of tissue engineered cartilage: histologic and biochemical correlations. J Biomed Opt 10 (2005) 031105-031106
    • (2005) J Biomed Opt , vol.10 , pp. 031105-031106
    • Kim, M.1    Bi, X.2    Horton, W.E.3    Spencer, R.G.4    Camacho, N.P.5
  • 54
    • 0343092088 scopus 로고    scopus 로고
    • Orientation of the infrared transition moments for an alpha-helix
    • Marsh D., Muller M., and Schmitt F.J. Orientation of the infrared transition moments for an alpha-helix. Biophys J 78 (2000) 2499-2510
    • (2000) Biophys J , vol.78 , pp. 2499-2510
    • Marsh, D.1    Muller, M.2    Schmitt, F.J.3
  • 56
    • 0042229087 scopus 로고    scopus 로고
    • Polarization artefacts of an FTIR microscope and the consequences for intensity measurements on anisotropic materials
    • Coats A.M., Hukins D.W., Imrie C.T., and Aspden R.M. Polarization artefacts of an FTIR microscope and the consequences for intensity measurements on anisotropic materials. J Microscopy 211 Pt. 1 (2003) 63-66
    • (2003) J Microscopy , vol.211 , Issue.PART 1 , pp. 63-66
    • Coats, A.M.1    Hukins, D.W.2    Imrie, C.T.3    Aspden, R.M.4
  • 57
    • 27944441245 scopus 로고    scopus 로고
    • A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS)
    • Bi X., Li G., Doty S.B., and Camacho N.P. A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS). Osteoarthritis Cartilage 13 (2005) 1050-1058
    • (2005) Osteoarthritis Cartilage , vol.13 , pp. 1050-1058
    • Bi, X.1    Li, G.2    Doty, S.B.3    Camacho, N.P.4
  • 58
    • 18144375926 scopus 로고    scopus 로고
    • Fourier transform infrared imaging spectroscopy analysis of collagenase-induced cartilage degradation
    • West P.A., Torzilli P.A., Chen C., Lin P., and Camacho N.P. Fourier transform infrared imaging spectroscopy analysis of collagenase-induced cartilage degradation. J Biomed Opt 10 (2005) 14015
    • (2005) J Biomed Opt , vol.10 , pp. 14015
    • West, P.A.1    Torzilli, P.A.2    Chen, C.3    Lin, P.4    Camacho, N.P.5
  • 59
    • 34249997492 scopus 로고    scopus 로고
    • The depth-dependent anisotropy of articular cartilage by Fourier-transform infrared imaging (FTIRI)
    • (in press)
    • Xia Y., Ramakrishnan N., and Bidthanapally A. The depth-dependent anisotropy of articular cartilage by Fourier-transform infrared imaging (FTIRI). Osteoarthritis Cartilage (2007) (in press)
    • (2007) Osteoarthritis Cartilage
    • Xia, Y.1    Ramakrishnan, N.2    Bidthanapally, A.3
  • 60
    • 0014349202 scopus 로고
    • The significance of the fine structure of articular cartilage
    • Bullough P., and Goodfellow J. The significance of the fine structure of articular cartilage. J Bone Joint Surg Br 50 (1968) 852-857
    • (1968) J Bone Joint Surg Br , vol.50 , pp. 852-857
    • Bullough, P.1    Goodfellow, J.2
  • 61
    • 0014837347 scopus 로고
    • The distribution of collagen in human articular cartilage with some of its physiological implications
    • Muir H., Bullough P., and Maroudas A. The distribution of collagen in human articular cartilage with some of its physiological implications. J Bone Joint Surg Br 52 (1970) 554-563
    • (1970) J Bone Joint Surg Br , vol.52 , pp. 554-563
    • Muir, H.1    Bullough, P.2    Maroudas, A.3
  • 62
    • 0017333778 scopus 로고
    • The collagen fibril organization in human articular cartilage
    • Minns R.J., and Steven F.S. The collagen fibril organization in human articular cartilage. J Anat 123 (1977) 437-457
    • (1977) J Anat , vol.123 , pp. 437-457
    • Minns, R.J.1    Steven, F.S.2
  • 63
    • 0021346891 scopus 로고
    • Morphological and functional interrelationships of articular cartilage matrices
    • Poole C.A., Flint M.H., and Beaumont B.W. Morphological and functional interrelationships of articular cartilage matrices. J Anat 138 Pt. 1 (1984) 113-138
    • (1984) J Anat , vol.138 , Issue.PART 1 , pp. 113-138
    • Poole, C.A.1    Flint, M.H.2    Beaumont, B.W.3
  • 64
    • 0021799462 scopus 로고
    • Matrix compartments on the growth plate of the proximal tibia of rats
    • Eggle P.S., Herrmann W., Hunziker E.B., and Schenk R.K. Matrix compartments on the growth plate of the proximal tibia of rats. Anat Rec 211 (1985) 246-257
    • (1985) Anat Rec , vol.211 , pp. 246-257
    • Eggle, P.S.1    Herrmann, W.2    Hunziker, E.B.3    Schenk, R.K.4
  • 65
    • 0025094277 scopus 로고
    • The organisation of collagen fibrils in the superficial zones of articular cartilage
    • Clark J.M. The organisation of collagen fibrils in the superficial zones of articular cartilage. J Anat 171 (1990) 117-130
    • (1990) J Anat , vol.171 , pp. 117-130
    • Clark, J.M.1
  • 66
    • 0032970772 scopus 로고    scopus 로고
    • Concerning the ultrastructural origin of large-scale swelling in articular cartilage
    • Chen M.H., and Broom N.D. Concerning the ultrastructural origin of large-scale swelling in articular cartilage. J Anat 194 Pt. 3 (1999) 445-461
    • (1999) J Anat , vol.194 , Issue.PART 3 , pp. 445-461
    • Chen, M.H.1    Broom, N.D.2
  • 67
    • 0034784267 scopus 로고    scopus 로고
    • Quantification of the graphical details of collagen fibrils in transmission electron micrographs
    • Xia Y., and Elder K. Quantification of the graphical details of collagen fibrils in transmission electron micrographs. J Microsc 204 Pt. 1 (2001) 3-16
    • (2001) J Microsc , vol.204 , Issue.PART 1 , pp. 3-16
    • Xia, Y.1    Elder, K.2
  • 68
    • 7744245802 scopus 로고    scopus 로고
    • The structural adaptations in compressed articular cartilage by microscopic MRI (μMRI) T2 anisotropy
    • Alhadlaq H., and Xia Y. The structural adaptations in compressed articular cartilage by microscopic MRI (μMRI) T2 anisotropy. Osteoarthritis Cartilage 12 (2004) 887-894
    • (2004) Osteoarthritis Cartilage , vol.12 , pp. 887-894
    • Alhadlaq, H.1    Xia, Y.2
  • 69
    • 27644466703 scopus 로고    scopus 로고
    • Modifications of orientational dependence of microscopic magnetic resonance imaging T(2) anisotropy in compressed articular cartilage
    • Alhadlaq H.A., and Xia Y. Modifications of orientational dependence of microscopic magnetic resonance imaging T(2) anisotropy in compressed articular cartilage. J Magn Reson Imaging 22 (2005) 665-673
    • (2005) J Magn Reson Imaging , vol.22 , pp. 665-673
    • Alhadlaq, H.A.1    Xia, Y.2
  • 70
    • 0014665671 scopus 로고
    • The correlation of fixed negative charge with glycosaminoglycan content of human articular cartilage
    • Maroudas A., Muir H., and Wingham J. The correlation of fixed negative charge with glycosaminoglycan content of human articular cartilage. Biochim Biophys Acta 177 (1969) 492-500
    • (1969) Biochim Biophys Acta , vol.177 , pp. 492-500
    • Maroudas, A.1    Muir, H.2    Wingham, J.3
  • 71
    • 0019858003 scopus 로고
    • Variations in the composition of bovine hip articular cartilage with distance from the articular surface
    • Franzen A., Inerot S., Hejderup S.O., and Heinegard D. Variations in the composition of bovine hip articular cartilage with distance from the articular surface. Biochem J 195 (1981) 535-543
    • (1981) Biochem J , vol.195 , pp. 535-543
    • Franzen, A.1    Inerot, S.2    Hejderup, S.O.3    Heinegard, D.4
  • 72
    • 0026334767 scopus 로고
    • On the adaptive structures of the collagen fibrils of bone and cartilage
    • Volpi M., and Katz E.P. On the adaptive structures of the collagen fibrils of bone and cartilage. J Biomech 24 Suppl 1 (1991) 67-77
    • (1991) J Biomech , vol.24 , Issue.SUPPL. 1 , pp. 67-77
    • Volpi, M.1    Katz, E.P.2
  • 73
    • 0034841435 scopus 로고    scopus 로고
    • Depth-dependent compressive properties of normal aged human femoral head articular cartilage: relationship to fixed charge density
    • Chen S.S., Falcovitz Y.H., Schneiderman R., Maroudas A., and Sah R.L. Depth-dependent compressive properties of normal aged human femoral head articular cartilage: relationship to fixed charge density. Osteoarthritis Cartilage 9 (2001) 561-569
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 561-569
    • Chen, S.S.1    Falcovitz, Y.H.2    Schneiderman, R.3    Maroudas, A.4    Sah, R.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.