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Volumn 236, Issue 1, 1998, Pages 18-23

Protein size resolution in human eye lenses by dynamic light scattering after in vivo measurements

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLIN; LENS PROTEIN;

EID: 0031938909     PISSN: 0721832X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004170050037     Document Type: Article
Times cited : (8)

References (16)
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    • Benedek, G.B.1
  • 3
    • 0001001048 scopus 로고
    • Species specificity of the crystallins and the albuminoid of the aging lens
    • Bours J (1980) Species specificity of the crystallins and the albuminoid of the aging lens. Comp Biochem Physiol 65B:215-222
    • (1980) Comp Biochem Physiol , vol.65 B , pp. 215-222
    • Bours, J.1
  • 5
    • 6844233805 scopus 로고
    • Diagnostic methods and tissue parameter investigations together with measurement results (in vivo)
    • Proceedings of Biomedical Optics, SPIE OE/LASE '94
    • Dierks K, Dieckmann M (1994) Diagnostic methods and tissue parameter investigations together with measurement results (in vivo). Proceedings of Biomedical Optics, SPIE OE/LASE '94, Ophthalmic Technologies IV:2126-2143
    • (1994) Ophthalmic Technologies , vol.4 , pp. 2126-2143
    • Dierks, K.1    Dieckmann, M.2
  • 6
    • 0001942609 scopus 로고
    • Light scattering apparatus
    • Pecora R (ed) Plenum Press, New York
    • Ford NC (1985) Light scattering apparatus. In: Pecora R (ed) Dynamic light scattering. Plenum Press, New York
    • (1985) Dynamic Light Scattering
    • Ford, N.C.1
  • 7
    • 0024415226 scopus 로고
    • Die Scheimpflug-Photographie der Linse
    • Hockwin O (1989) Die Scheimpflug-Photographie der Linse. Fortschr Ophthalmol 86:304-311
    • (1989) Fortschr Ophthalmol , vol.86 , pp. 304-311
    • Hockwin, O.1
  • 8
  • 9
    • 0022902805 scopus 로고
    • In vivo measurement of the aging rabbit lens using quasielastic light scattering
    • Libondi T, Magnante P, Chylack LT, Benedek GB (1986) In vivo measurement of the aging rabbit lens using quasielastic light scattering. Curr Eye Res 5:411-419
    • (1986) Curr Eye Res , vol.5 , pp. 411-419
    • Libondi, T.1    Magnante, P.2    Chylack, L.T.3    Benedek, G.B.4
  • 11
    • 0005482587 scopus 로고    scopus 로고
    • A single wavelength cross-correlation technique which suppresses multiple scattering
    • Photon correlation and scattering
    • Meyer WV et al. (1996) A single wavelength cross-correlation technique which suppresses multiple scattering. In: Photon correlation and scattering, OSA Tech Digest Ser (Optical Society of America) 14:104-107
    • (1996) OSA Tech Digest Ser (Optical Society of America) , vol.14 , pp. 104-107
    • Meyer, W.V.1
  • 12
    • 0020176708 scopus 로고
    • A general purpose constrained regularization program for inverting noisy non-linear algebraic and integral equations
    • Provencher SW (1982) A general purpose constrained regularization program for inverting noisy non-linear algebraic and integral equations. Comput Phys Comm 27:229-242o
    • (1982) Comput Phys Comm , vol.27
    • Provencher, S.W.1
  • 13
    • 0016698522 scopus 로고
    • Observation of protein diffusivity in intact human and bovine eye lenses with application to cataract
    • Tanaka T, Benedek GB (1975) Observation of protein diffusivity in intact human and bovine eye lenses with application to cataract. Invest Ophthalmol 6:449-456
    • (1975) Invest Ophthalmol , vol.6 , pp. 449-456
    • Tanaka, T.1    Benedek, G.B.2
  • 14
    • 0017359691 scopus 로고
    • In vivo observation of protein diffusivity in rabbit lenses
    • Tanaka T, Ishimoto C (1977) In vivo observation of protein diffusivity in rabbit lenses. Invest Ophthalmol 16:135
    • (1977) Invest Ophthalmol , vol.16 , pp. 135
    • Tanaka, T.1    Ishimoto, C.2
  • 16
    • 0024309379 scopus 로고
    • Packing interaction in the eye-lens: Structural analysis, internal symmetry and lattice interactions in the bovine IVa-crystallin
    • White HE, Driessen HPC, Slingsby C, Moss DS, Lindley PF (1989) Packing interaction in the eye-lens: structural analysis, internal symmetry and lattice interactions in the bovine IVa-crystallin. J Mol Biol 207:217-235
    • (1989) J Mol Biol , vol.207 , pp. 217-235
    • White, H.E.1    Driessen, H.P.C.2    Slingsby, C.3    Moss, D.S.4    Lindley, P.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.