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Volumn 91, Issue 6, 2015, Pages 1497-1504

Early Diagnosis of Diabetes through the Eye

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN;

EID: 84946020117     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/php.12524     Document Type: Article
Times cited : (22)

References (98)
  • 1
    • 33846049659 scopus 로고    scopus 로고
    • Insulin and insulin resistance
    • Wilcox, G., (2005) Insulin and insulin resistance. Clin. Biochem. Rev. 26, 19.
    • (2005) Clin. Biochem. Rev. , vol.26 , pp. 19
    • Wilcox, G.1
  • 2
    • 70349675632 scopus 로고    scopus 로고
    • Molecular insights and therapeutic targets for diabetic endothelial dysfunction
    • Xu, J., and, M.-H. Zou, (2009) Molecular insights and therapeutic targets for diabetic endothelial dysfunction. Circulation 120, 1266-1286.
    • (2009) Circulation , vol.120 , pp. 1266-1286
    • Xu, J.1    Zou, M.-H.2
  • 4
    • 84911904102 scopus 로고    scopus 로고
    • The economic burden of elevated blood glucose levels in 2012: Diagnosed and undiagnosed diabetes, gestational diabetes mellitus, and prediabetes
    • Dall, T. M., W. Yang, P. Halder, B. Pang, M. Massoudi, N. Wintfeld, A. P. Semilla, J. Franz, and, P. F. Hogan, (2014) The economic burden of elevated blood glucose levels in 2012: diagnosed and undiagnosed diabetes, gestational diabetes mellitus, and prediabetes. Diabetes Care 37, 3172-3179.
    • (2014) Diabetes Care , vol.37 , pp. 3172-3179
    • Dall, T.M.1    Yang, W.2    Halder, P.3    Pang, B.4    Massoudi, M.5    Wintfeld, N.6    Semilla, A.P.7    Franz, J.8    Hogan, P.F.9
  • 5
    • 0036177713 scopus 로고    scopus 로고
    • Guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus
    • Sacks, D. B., D. E. Bruns, D. E. Goldstein, N. K. Maclaren, J. M. McDonald, and, M. Parrott, (2002) Guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus. Clin. Chem. 48, 436-472.
    • (2002) Clin. Chem. , vol.48 , pp. 436-472
    • Sacks, D.B.1    Bruns, D.E.2    Goldstein, D.E.3    Maclaren, N.K.4    McDonald, J.M.5    Parrott, M.6
  • 6
    • 0041866808 scopus 로고    scopus 로고
    • Hemoglobin variants and hemoglobin A1c analysis: Problem solved?
    • Sacks, D. B., (2003) Hemoglobin variants and hemoglobin A1c analysis: problem solved? Clin. Chem. 49, 1245-1247.
    • (2003) Clin. Chem. , vol.49 , pp. 1245-1247
    • Sacks, D.B.1
  • 7
    • 78650064794 scopus 로고    scopus 로고
    • HbA1c for the diagnosis of diabetes and prediabetes: Is it time for a mid-course correction?
    • Cohen, R. M., S. Haggerty, and, W. H. Herman, (2010) HbA1c for the diagnosis of diabetes and prediabetes: is it time for a mid-course correction? J. Clin. Endocrinol. Metab. 95, 5203-5206.
    • (2010) J. Clin. Endocrinol. Metab. , vol.95 , pp. 5203-5206
    • Cohen, R.M.1    Haggerty, S.2    Herman, W.H.3
  • 9
    • 0020618879 scopus 로고
    • Glycosylated hemoglobin as a long-term parameter in appraising the severity of hemolytic disease
    • Panzer, S., W. Graninger, G. Kronik, P. Bettelheim, and, K. Lechner, (1983) Glycosylated hemoglobin as a long-term parameter in appraising the severity of hemolytic disease. Klin. Wochenschr. 61, 839-843.
    • (1983) Klin. Wochenschr. , vol.61 , pp. 839-843
    • Panzer, S.1    Graninger, W.2    Kronik, G.3    Bettelheim, P.4    Lechner, K.5
  • 10
    • 33747080843 scopus 로고    scopus 로고
    • Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification
    • Dobler, D., N. Ahmed, L. Song, K. E. Eboigbodin, and, P. J. Thornalley, (2006) Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification. Diabetes 55, 1961-1969.
    • (2006) Diabetes , vol.55 , pp. 1961-1969
    • Dobler, D.1    Ahmed, N.2    Song, L.3    Eboigbodin, K.E.4    Thornalley, P.J.5
  • 11
    • 0018761581 scopus 로고
    • Rapid-turnover transport proteins: An index of subclinical protein-energy malnutrition
    • Shetty, P., R. Jung, K. Watrasiewicz, and, W. James, (1979) Rapid-turnover transport proteins: an index of subclinical protein-energy malnutrition. Lancet 314, 230-232.
    • (1979) Lancet , vol.314 , pp. 230-232
    • Shetty, P.1    Jung, R.2    Watrasiewicz, K.3    James, W.4
  • 12
    • 67650094848 scopus 로고    scopus 로고
    • International expert committee report on the role of the A1C assay in the diagnosis of diabetes: Diabetes Care 2009; 32(7): 1327-1334
    • Gillett, M. J., (2009) International expert committee report on the role of the A1C assay in the diagnosis of diabetes: Diabetes Care 2009; 32(7): 1327-1334. Clin. Biochem. Rev. 30, 197-200.
    • (2009) Clin. Biochem. Rev. , vol.30 , pp. 197-200
    • Gillett, M.J.1
  • 13
    • 33748934023 scopus 로고    scopus 로고
    • Cases in primary care laboratory medicine: Glycated haemoglobin (HbA1c) monitoring
    • Reynolds, T. M., W. S. A. Smellie, and, P. J. Twomey, (2006) Cases in primary care laboratory medicine: Glycated haemoglobin (HbA1c) monitoring. BMJ 333, 586.
    • (2006) BMJ , vol.333 , pp. 586
    • Reynolds, T.M.1    Smellie, W.S.A.2    Twomey, P.J.3
  • 14
    • 33244486058 scopus 로고    scopus 로고
    • Case study: Potential pitfalls of using hemoglobin A1c as the sole measure of glycemic control
    • Tran, H. A., D. Silva, and, N. Petrovsky, (2004) Case study: potential pitfalls of using hemoglobin A1c as the sole measure of glycemic control. Clin. Diabetes 22, 141-143.
    • (2004) Clin. Diabetes , vol.22 , pp. 141-143
    • Tran, H.A.1    Silva, D.2    Petrovsky, N.3
  • 15
    • 0035134867 scopus 로고    scopus 로고
    • Effects of hemoglobin variants and chemically modified derivatives on assays for glycohemoglobin
    • Bry, L., P. C. Chen, and, D. B. Sacks, (2001) Effects of hemoglobin variants and chemically modified derivatives on assays for glycohemoglobin. Clin. Chem. 47, 153-163.
    • (2001) Clin. Chem. , vol.47 , pp. 153-163
    • Bry, L.1    Chen, P.C.2    Sacks, D.B.3
  • 17
    • 16244370760 scopus 로고    scopus 로고
    • Effects of hemoglobin C and S traits on glycohemoglobin measurements by eleven methods
    • Roberts, W. L., S. Safar-Pour, B. K. De, C. L. Rohlfing, C. W. Weykamp, and, R. R. Little, (2005) Effects of hemoglobin C and S traits on glycohemoglobin measurements by eleven methods. Clin. Chem. 51, 776-778.
    • (2005) Clin. Chem. , vol.51 , pp. 776-778
    • Roberts, W.L.1    Safar-Pour, S.2    De, B. K.3    Rohlfing, C.L.4    Weykamp, C.W.5    Little, R.R.6
  • 19
    • 40349084011 scopus 로고    scopus 로고
    • Diagnosis and classification of diabetes mellitus
    • Association A. D
    • Association A. D. (2008) Diagnosis and classification of diabetes mellitus. Diabetes Care 31, S55-S60.
    • (2008) Diabetes Care , vol.31 , pp. S55-S60
  • 20
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman, B., T. Ramakrishna, and, C. Mohan Rao, (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 365, 133-136.
    • (1995) FEBS Lett. , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Mohan Rao, C.3
  • 21
    • 0019075085 scopus 로고
    • The quaternary structure of bovine α-crystallin
    • Siezen, R. J., J. G. Bindels, and, H. J. Hoenders, (1980) The quaternary structure of bovine α-crystallin. Eur. J. Biochem. 111, 435-444.
    • (1980) Eur. J. Biochem. , vol.111 , pp. 435-444
    • Siezen, R.J.1    Bindels, J.G.2    Hoenders, H.J.3
  • 22
    • 0025501401 scopus 로고
    • The anaerobic photolysis of lens α-crystallin: Evidence for triplet state mediated photodamage
    • Berger, J. W., and, J. M. Vanderkooi, (1990) The anaerobic photolysis of lens α-crystallin: evidence for triplet state mediated photodamage. Photochem. Photobiol. 52, 855-860.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 855-860
    • Berger, J.W.1    Vanderkooi, J.M.2
  • 23
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat-shock protein family
    • De Jong, W., J. Leunissen, and, C. Voorter, (1993) Evolution of the alpha-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10, 103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.1    Leunissen, J.2    Voorter, C.3
  • 24
    • 77953806476 scopus 로고    scopus 로고
    • The small heat shock protein αa-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis
    • Deng, M., P.-C. Chen, S. Xie, J. Zhao, L. Gong, J. Liu, L. Zhang, S. Sun, J. Liu, and, H. Ma, (2010) The small heat shock protein αA-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis. Biochim. Biophys. Acta 1802, 621-631.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 621-631
    • Deng, M.1    Chen, P.-C.2    Xie, S.3    Zhao, J.4    Gong, L.5    Liu, J.6    Zhang, L.7    Sun, S.8    Liu, J.9    Ma, H.10
  • 25
    • 79451469767 scopus 로고    scopus 로고
    • New focus on alpha-crystallins in retinal neurodegenerative diseases
    • Fort, P. E., and, K. J. Lampi, (2011) New focus on alpha-crystallins in retinal neurodegenerative diseases. Exp. Eye Res. 92, 98-103.
    • (2011) Exp. Eye Res. , vol.92 , pp. 98-103
    • Fort, P.E.1    Lampi, K.J.2
  • 26
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz, J., (2003) Alpha-crystallin. Exp. Eye Res. 76, 145-153.
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 27
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz, J., (1992) Alpha-crystallin can function as a molecular chaperone. Proc. Natl Acad. Sci. 89, 10449-10453.
    • (1992) Proc. Natl Acad. Sci. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 29
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • Van Montfort, R., C. Slingsby, and, E. Vierling, (2002) Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv. Protein Chem. 59, 105-156.
    • (2002) Adv. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 30
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman, B., and, C. M. Rao, (1994) Chaperone-like activity and quaternary structure of alpha-crystallin. J. Biol. Chem. 269, 27264-27268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 32
    • 84880115383 scopus 로고    scopus 로고
    • Heat shock proteins in the human eye
    • Urbak, L., and, H. Vorum, (2011) Heat shock proteins in the human eye. Int. J. Proteomics 2010, 479571.
    • (2011) Int. J. Proteomics , vol.2010 , pp. 479571
    • Urbak, L.1    Vorum, H.2
  • 34
    • 11144324314 scopus 로고    scopus 로고
    • Advanced glycation endproducts - Role in pathology of diabetic complications
    • Ahmed, N., (2005) Advanced glycation endproducts-role in pathology of diabetic complications. Diabetes Res. Clin. Pract. 67, 3-21.
    • (2005) Diabetes Res. Clin. Pract. , vol.67 , pp. 3-21
    • Ahmed, N.1
  • 35
    • 84862645392 scopus 로고    scopus 로고
    • Glycation research in amino acids: A place to call home
    • Rabbani, N., and, P. J. Thornalley, (2012) Glycation research in amino acids: a place to call home. Amino Acids 42, 1087-1096.
    • (2012) Amino Acids , vol.42 , pp. 1087-1096
    • Rabbani, N.1    Thornalley, P.J.2
  • 36
    • 84862688640 scopus 로고    scopus 로고
    • Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
    • Rabbani, N., and, P. J. Thornalley, (2012) Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino Acids 42, 1133-1142.
    • (2012) Amino Acids , vol.42 , pp. 1133-1142
    • Rabbani, N.1    Thornalley, P.J.2
  • 37
    • 84881624747 scopus 로고    scopus 로고
    • Advanced glycation end products
    • Thomas, M. C., (2011) Advanced glycation end products. Contrib. Nephrol. 170, 66-74.
    • (2011) Contrib. Nephrol. , vol.170 , pp. 66-74
    • Thomas, M.C.1
  • 38
    • 76749126235 scopus 로고    scopus 로고
    • Hydroimidazolone modification of human αa-crystallin: Effect on the chaperone function and protein refolding ability
    • Gangadhariah, M. H., B. Wang, M. Linetsky, C. Henning, R. Spanneberg, M. A. Glomb, and, R. H. Nagaraj, (2010) Hydroimidazolone modification of human αA-crystallin: effect on the chaperone function and protein refolding ability. Biochim. Biophys. Acta 1802, 432-441.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 432-441
    • Gangadhariah, M.H.1    Wang, B.2    Linetsky, M.3    Henning, C.4    Spanneberg, R.5    Glomb, M.A.6    Nagaraj, R.H.7
  • 40
    • 0036084953 scopus 로고    scopus 로고
    • Alterations in renal mitochondrial respiration in response to the reactive oxoaldehyde methylglyoxal
    • Rosca, M. G., V. M. Monnier, L. I. Szweda, and, M. F. Weiss, (2002) Alterations in renal mitochondrial respiration in response to the reactive oxoaldehyde methylglyoxal. Am. J. Physiol. Renal. Physiol. 283, F52-F59.
    • (2002) Am. J. Physiol. Renal. Physiol. , vol.283 , pp. F52-F59
    • Rosca, M.G.1    Monnier, V.M.2    Szweda, L.I.3    Weiss, M.F.4
  • 42
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • Craig, E. A., J. S. Weissman, and, A. L. Horwich, (1994) Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78, 365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 44
    • 0141567132 scopus 로고
    • The turnover rate of serum albumin in man as measured by I131-tagged albumin
    • Sterling, K., (1951) The turnover rate of serum albumin in man as measured by I131-tagged albumin. J. Clin. Investig. 30, 1228.
    • (1951) J. Clin. Investig. , vol.30 , pp. 1228
    • Sterling, K.1
  • 45
    • 0034175460 scopus 로고    scopus 로고
    • Heat and concentration effects on the small heat shock protein, alpha-crystallin
    • Mandal, K., J. Dillon, and, E. R. Gaillard, (2000) Heat and concentration effects on the small heat shock protein, alpha-crystallin. Photochem. Photobiol. 71, 470-475.
    • (2000) Photochem. Photobiol. , vol.71 , pp. 470-475
    • Mandal, K.1    Dillon, J.2    Gaillard, E.R.3
  • 46
    • 78649903943 scopus 로고    scopus 로고
    • Effect of methylglyoxal modification of human alpha-crystallin on the structure, stability and chaperone function
    • Mukhopadhyay, S., M. Kar, and, K. P. Das, (2010) Effect of methylglyoxal modification of human alpha-crystallin on the structure, stability and chaperone function. Protein. J. 29, 551-556.
    • (2010) Protein. J. , vol.29 , pp. 551-556
    • Mukhopadhyay, S.1    Kar, M.2    Das, K.P.3
  • 47
    • 8644239272 scopus 로고
    • Fluorescence and Raman spectroscopy of the crystalline lens
    • (Edited by B. Masters), Springer-Verlag, New York
    • Bursell, S.E., and, N.T. Yu, (1990) Fluorescence and Raman spectroscopy of the crystalline lens. In Noninvasive Diagnostic Techniques in Ophthalmology, (Edited by B. Masters), pp. 319-341. Springer-Verlag, New York.
    • (1990) Noninvasive Diagnostic Techniques in Ophthalmology , pp. 319-341
    • Bursell, S.E.1    Yu, N.T.2
  • 48
    • 81855182736 scopus 로고    scopus 로고
    • Prognostic potential and tumor growth-inhibiting effect of plasma advanced glycation end products in non-small cell lung carcinoma
    • Bartling, B., H. S. Hofmann, A. Sohst, Y. Hatzky, V. Somoza, R. E. Silber, and, A. Simm, (2011) Prognostic potential and tumor growth-inhibiting effect of plasma advanced glycation end products in non-small cell lung carcinoma. Mol. Med. 17, 980-989.
    • (2011) Mol. Med. , vol.17 , pp. 980-989
    • Bartling, B.1    Hofmann, H.S.2    Sohst, A.3    Hatzky, Y.4    Somoza, V.5    Silber, R.E.6    Simm, A.7
  • 49
    • 84946032641 scopus 로고    scopus 로고
    • Lens fluorescence as a marker of ageing in relation to heritability, diabetes mellitus, and ischaemic heart disease
    • Kessel, L., (2004) Lens fluorescence as a marker of ageing in relation to heritability, diabetes mellitus, and ischaemic heart disease. Dan. Med. Bull. 51, 298.
    • (2004) Dan. Med. Bull. , vol.51 , pp. 298
    • Kessel, L.1
  • 50
    • 0036167208 scopus 로고    scopus 로고
    • Diabetes and advanced glycation endproducts
    • Vlassara, H., and, M. Palace, (2002) Diabetes and advanced glycation endproducts. J. Intern. Med. 251, 87-101.
    • (2002) J. Intern. Med. , vol.251 , pp. 87-101
    • Vlassara, H.1    Palace, M.2
  • 51
    • 34250327529 scopus 로고    scopus 로고
    • Circulating glycotoxins and dietary advanced glycation endproducts: Two links to inflammatory response, oxidative stress, and aging
    • Uribarri, J., W. Cai, M. Peppa, S. Goodman, L. Ferrucci, G. Striker, and, H. Vlassara, (2007) Circulating glycotoxins and dietary advanced glycation endproducts: two links to inflammatory response, oxidative stress, and aging. J. Gerontol. A Biol. Sci. Med. Sci. 62, 427-433.
    • (2007) J. Gerontol. A Biol. Sci. Med. Sci. , vol.62 , pp. 427-433
    • Uribarri, J.1    Cai, W.2    Peppa, M.3    Goodman, S.4    Ferrucci, L.5    Striker, G.6    Vlassara, H.7
  • 52
    • 33845295849 scopus 로고    scopus 로고
    • Benfotiamine prevents macro-and microvascular endothelial dysfunction and oxidative stress following a meal rich in advanced glycation end products in individuals with type 2 diabetes
    • Stirban, A., M. Negrean, B. Stratmann, T. Gawlowski, T. Horstmann, C. Götting, K. Kleesiek, M. Mueller-Roesel, T. Koschinsky, and, J. Uribarri, (2006) Benfotiamine prevents macro-and microvascular endothelial dysfunction and oxidative stress following a meal rich in advanced glycation end products in individuals with type 2 diabetes. Diabetes Care 29, 2064-2071.
    • (2006) Diabetes Care , vol.29 , pp. 2064-2071
    • Stirban, A.1    Negrean, M.2    Stratmann, B.3    Gawlowski, T.4    Horstmann, T.5    Götting, C.6    Kleesiek, K.7    Mueller-Roesel, M.8    Koschinsky, T.9    Uribarri, J.10
  • 53
    • 0030176306 scopus 로고    scopus 로고
    • Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids, and enzymatic detoxification-a role in pathogenesis and antiproliferative chemotherapy
    • Thornalley, P. J., (1996) Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27, 565-573.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 565-573
    • Thornalley, P.J.1
  • 54
    • 0001489682 scopus 로고
    • An enzyme concerned with the formation of hydroxy acids from ketonic aldehydes
    • Dakin, H., and, H. Dudley, (1913) An enzyme concerned with the formation of hydroxy acids from ketonic aldehydes. J. Biol. Chem. 14, 155-157.
    • (1913) J. Biol. Chem. , vol.14 , pp. 155-157
    • Dakin, H.1    Dudley, H.2
  • 55
    • 0028292698 scopus 로고
    • Glyoxalase system in clinical diabetes mellitus and correlation with diabetic com pl icat ions
    • McLellan, A. C., and, J. Thornalley, (1994) Glyoxalase system in clinical diabetes mellitus and correlation with diabetic com pl icat ions. Clin. Sci. 87, 21-29.
    • (1994) Clin. Sci. , vol.87 , pp. 21-29
    • McLellan, A.C.1    Thornalley, J.2
  • 56
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: Chemistry, biochemistry, toxicology and biological implications
    • Kalapos, M. P., (1999) Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 110, 145-175.
    • (1999) Toxicol. Lett. , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 57
    • 0026541136 scopus 로고
    • Autofluorescence of the crystalline lens in early and late onset diabetes
    • Sparrow, J. M., A. J. Bron, N. A. Brown, and, H. A. Neil, (1992) Autofluorescence of the crystalline lens in early and late onset diabetes. Br. J. Ophthalmol. 76, 25-31.
    • (1992) Br. J. Ophthalmol. , vol.76 , pp. 25-31
    • Sparrow, J.M.1    Bron, A.J.2    Brown, N.A.3    Neil, H.A.4
  • 58
    • 0025422647 scopus 로고
    • Front surface fluorescence measurements of the age-related change in the human lens
    • Liang, J. N., (1990) Front surface fluorescence measurements of the age-related change in the human lens. Curr. Eye Res. 9, 399-405.
    • (1990) Curr. Eye Res. , vol.9 , pp. 399-405
    • Liang, J.N.1
  • 59
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P. I., and, A. Squire, (1999) Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-52.
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 61
    • 0000103624 scopus 로고
    • Emerging biomedical and advanced applications of time-resolved fluorescence spectroscopy
    • Lakowicz, J. R., P. A. Koen, H. Szmacinski, I. Gryczynski, and, J. Kus̈ba, (1994) Emerging biomedical and advanced applications of time-resolved fluorescence spectroscopy. J. Fluoresc. 4, 117-136.
    • (1994) J. Fluoresc. , vol.4 , pp. 117-136
    • Lakowicz, J.R.1    Koen, P.A.2    Szmacinski, H.3    Gryczynski, I.4    Kus̈ba, J.5
  • 62
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem, J. M., and, L. Brand, (1985) Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 54, 43-71.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 63
    • 0000839617 scopus 로고    scopus 로고
    • Photochromicity and fluorescence lifetimes of green fluorescent protein
    • Striker, G., V. Subramaniam, C. A. Seidel, and, A. Volkmer, (1999) Photochromicity and fluorescence lifetimes of green fluorescent protein. J. Phys. Chem. B 103, 8612-8617.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8612-8617
    • Striker, G.1    Subramaniam, V.2    Seidel, C.A.3    Volkmer, A.4
  • 64
    • 0036879209 scopus 로고    scopus 로고
    • Time-resolved and steady-state fluorescence spectroscopic studies of the human lens with comparison to argpyrimidine, pentosidine and 3-OH-kynurenine
    • Kessel, L., S. Kalinin, R. H. Nagaraj, M. Larsen, and, L. B. Å. Johansson, (2002) Time-resolved and steady-state fluorescence spectroscopic studies of the human lens with comparison to argpyrimidine, pentosidine and 3-OH-kynurenine. Photochem. Photobiol. 76, 549-554.
    • (2002) Photochem. Photobiol. , vol.76 , pp. 549-554
    • Kessel, L.1    Kalinin, S.2    Nagaraj, R.H.3    Larsen, M.4    Johansson, L.B.Å.5
  • 65
    • 17744398249 scopus 로고    scopus 로고
    • Impact of UVR-A on whole human lenses, supernatants of buffered human lens homogenates, and purified argpyrimidine and 3-OH-kynurenine
    • Kessel, L., S. Kalinin, V. Soroka, M. Larsen, and, L. B. Johansson, (2005) Impact of UVR-A on whole human lenses, supernatants of buffered human lens homogenates, and purified argpyrimidine and 3-OH-kynurenine. Acta Ophthalmol. Scand. 83, 221-227.
    • (2005) Acta Ophthalmol. Scand. , vol.83 , pp. 221-227
    • Kessel, L.1    Kalinin, S.2    Soroka, V.3    Larsen, M.4    Johansson, L.B.5
  • 66
    • 84946042489 scopus 로고    scopus 로고
    • Lens fluorescence in newly diagnosed type 2 diabetic patients
    • I. S. Group
    • Kessel, L., and, M. Larsen, and I. S. Group (2003) Lens fluorescence in newly diagnosed type 2 diabetic patients. Invest. Ophthalmol. Vis. Sci. 44, 3471.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 3471
    • Kessel, L.1    Larsen, M.2
  • 67
    • 0029353377 scopus 로고
    • Age-related changes in the human lens as monitored by detection of porphyrin excited states
    • Roberts, J. E., S. J. Atherton, E. R. Gaillard, and, J. Dillon, (1995) Age-related changes in the human lens as monitored by detection of porphyrin excited states. Photochem. Photobiol. 62, 339-341.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 339-341
    • Roberts, J.E.1    Atherton, S.J.2    Gaillard, E.R.3    Dillon, J.4
  • 68
    • 84994997529 scopus 로고
    • Fluorescence lifetimes of ocular lens chromophores
    • Borkman, R., J. Tassin, and, S. Lerman, (1980) Fluorescence lifetimes of ocular lens chromophores. Photochem. Photobiol. 31, 519-521.
    • (1980) Photochem. Photobiol. , vol.31 , pp. 519-521
    • Borkman, R.1    Tassin, J.2    Lerman, S.3
  • 70
    • 0027289609 scopus 로고
    • Picosecond fluorescence decay in photolyzed lens protein alpha-crystallin
    • Borkman, R. F., A. Douhal, and, K. Yoshihara, (1993) Picosecond fluorescence decay in photolyzed lens protein alpha-crystallin. Biochemistry 32, 4787-4792.
    • (1993) Biochemistry , vol.32 , pp. 4787-4792
    • Borkman, R.F.1    Douhal, A.2    Yoshihara, K.3
  • 71
    • 0018192767 scopus 로고
    • Fluorescence spectra of tryptophan residues in human and bovine lens proteins
    • Borkman, R. F., and, S. Lerman, (1978) Fluorescence spectra of tryptophan residues in human and bovine lens proteins. Exp. Eye Res. 26, 705-713.
    • (1978) Exp. Eye Res. , vol.26 , pp. 705-713
    • Borkman, R.F.1    Lerman, S.2
  • 73
    • 0017521840 scopus 로고
    • Ultraviolet action spectrum for fluorogen production in the ocular lens
    • Borkman, R. F., A. Dalrymple, and, S. Lerman, (1977) Ultraviolet action spectrum for fluorogen production in the ocular lens. Photochem. Photobiol. 26, 129-132.
    • (1977) Photochem. Photobiol. , vol.26 , pp. 129-132
    • Borkman, R.F.1    Dalrymple, A.2    Lerman, S.3
  • 74
    • 0019424366 scopus 로고
    • Fluorescence lifetimes of chromophores in intact human lenses and lens protection
    • Borkman, R. F., J. D. Tassin, and, S. Lerman, (1981) Fluorescence lifetimes of chromophores in intact human lenses and lens protection. Exp. Eye Res. 32, 313-322.
    • (1981) Exp. Eye Res. , vol.32 , pp. 313-322
    • Borkman, R.F.1    Tassin, J.D.2    Lerman, S.3
  • 75
    • 0017059827 scopus 로고
    • Spectroscopic evaluation and classification of the normal, aging, and cataractous lens. (with 1 color plate)
    • Lerman, S., and, R. Borkman, (1976) Spectroscopic evaluation and classification of the normal, aging, and cataractous lens. (with 1 color plate). Ophthalmic Res. 8, 335-353.
    • (1976) Ophthalmic Res. , vol.8 , pp. 335-353
    • Lerman, S.1    Borkman, R.2
  • 77
    • 0017167627 scopus 로고
    • Accleration of an aging parameter (fluorogen) in the ocular lens
    • Lerman, S., J. Jr Kuck, R. Borkman, and, E. Saker, (1976) Accleration of an aging parameter (fluorogen) in the ocular lens. Ann. Ophthalmol. 8, 558.
    • (1976) Ann. Ophthalmol. , vol.8 , pp. 558
    • Lerman, S.1    Kuck, Jr.J.2    Borkman, R.3    Saker, E.4
  • 78
    • 0018118537 scopus 로고
    • Photoacoustic, fluorescence and light transmission spectra of normal, aging and cataractous lenses
    • Lerman, S., B. Yamanashi, R. Palmer, J. Roark, and, R. Borkman, (1978) Photoacoustic, fluorescence and light transmission spectra of normal, aging and cataractous lenses. Ophthalmic Res. 10, 168-176.
    • (1978) Ophthalmic Res. , vol.10 , pp. 168-176
    • Lerman, S.1    Yamanashi, B.2    Palmer, R.3    Roark, J.4    Borkman, R.5
  • 80
    • 0025410113 scopus 로고
    • Time resolved spectroscopic studies on the intact human lens
    • Dillon, J., and, S. J. Atherton, (1990) Time resolved spectroscopic studies on the intact human lens. Photochem. Photobiol. 51, 465-468.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 465-468
    • Dillon, J.1    Atherton, S.J.2
  • 82
    • 0038023149 scopus 로고    scopus 로고
    • Advanced glycation endproducts as UVA photosensitizers of tryptophan and ascorbic acid: Consequences for the lens
    • de La Rochette, A., I. Birlouez-Aragon, E. Silva, and, P. Morliere, (2003) Advanced glycation endproducts as UVA photosensitizers of tryptophan and ascorbic acid: consequences for the lens. Biochim. Biophys. Acta 1621, 235-241.
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 235-241
    • De La Rochette, A.1    Birlouez-Aragon, I.2    Silva, E.3    Morliere, P.4
  • 83
    • 34249809404 scopus 로고    scopus 로고
    • Photosensitizing activity of advanced glycation endproducts on tryptophan, glucose 6-phosphate dehydrogenase, human serum albumin and ascorbic acid evaluated at low oxygen pressure
    • Fuentealba, D., M. Galvez, E. Alarcon, E. Lissi, and, E. Silva, (2007) Photosensitizing activity of advanced glycation endproducts on tryptophan, glucose 6-phosphate dehydrogenase, human serum albumin and ascorbic acid evaluated at low oxygen pressure. Photochem. Photobiol. 83, 563-569.
    • (2007) Photochem. Photobiol. , vol.83 , pp. 563-569
    • Fuentealba, D.1    Galvez, M.2    Alarcon, E.3    Lissi, E.4    Silva, E.5
  • 84
    • 0036904719 scopus 로고    scopus 로고
    • Glycated proteins can enhance photooxidative stress in aged and diabetic lenses
    • Argirova, M. D., and, W. Breipohl, (2002) Glycated proteins can enhance photooxidative stress in aged and diabetic lenses. Free Radical Res. 36, 1251-1259.
    • (2002) Free Radical Res. , vol.36 , pp. 1251-1259
    • Argirova, M.D.1    Breipohl, W.2
  • 85
    • 67649970874 scopus 로고    scopus 로고
    • Tryptophan metabolites from young human lenses and the photooxidation of ascorbic acid by UVA light
    • Ortwerth, B. J., J. Bhattacharyya, and, E. Shipova, (2009) Tryptophan metabolites from young human lenses and the photooxidation of ascorbic acid by UVA light. Invest. Ophthalmol. Vis. Sci. 50, 3311-3319.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 3311-3319
    • Ortwerth, B.J.1    Bhattacharyya, J.2    Shipova, E.3
  • 86
    • 32444433859 scopus 로고    scopus 로고
    • Endogenous UVA-photosensitizers: Mediators of skin photodamage and novel targets for skin photoprotection
    • Wondrak, G. T., M. K. Jacobson, and, E. L. Jacobson, (2006) Endogenous UVA-photosensitizers: mediators of skin photodamage and novel targets for skin photoprotection. Photochem. Photobiol. Sci. 5, 215-237.
    • (2006) Photochem. Photobiol. Sci. , vol.5 , pp. 215-237
    • Wondrak, G.T.1    Jacobson, M.K.2    Jacobson, E.L.3
  • 87
    • 0033066479 scopus 로고    scopus 로고
    • Generation of active oxygen species from advanced glycation end-products (AGEs) during ultraviolet light A (UVA) irradiation and a possible mechanism for cell damaging
    • Masaki, H., Y. Okano, and, H. Sakurai, (1999) Generation of active oxygen species from advanced glycation end-products (AGEs) during ultraviolet light A (UVA) irradiation and a possible mechanism for cell damaging. Biochim. Biophys. Acta 1428, 45-56.
    • (1999) Biochim. Biophys. Acta , vol.1428 , pp. 45-56
    • Masaki, H.1    Okano, Y.2    Sakurai, H.3
  • 88
    • 0031127237 scopus 로고    scopus 로고
    • The relative UV sensitizer activity of purified advanced glycation endproducts
    • Ortwerth, B. J., M. Prabhakaram, R. H. Nagaraj, and, M. Linetsky, (1997) The relative UV sensitizer activity of purified advanced glycation endproducts. Photochem. Photobiol. 65, 666-672.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 666-672
    • Ortwerth, B.J.1    Prabhakaram, M.2    Nagaraj, R.H.3    Linetsky, M.4
  • 90
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E., N. Vedenkina, and, M. Ivkova, (1973) Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18, 263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.1    Vedenkina, N.2    Ivkova, M.3
  • 91
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y., and, M. D. Barkley, (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 92
    • 84946074540 scopus 로고    scopus 로고
    • Time resolved autofluorescence - A new diagnostic tool in ophthalmology
    • Schweitzer, D., (2011) Time resolved autofluorescence-a new diagnostic tool in ophthalmology. Acta Ophthalmol. 89.
    • (2011) Acta Ophthalmol. , vol.89
    • Schweitzer, D.1
  • 93
    • 65949117223 scopus 로고    scopus 로고
    • Vivo and in vitro investigations of retinal fluorophores in age-related macular degeneration by fluorescence lifetime imaging
    • 71832S-71832S-71812. International Society for Optics and Photonics
    • Hammer, M., S. Quick, M. Klemm, S. Schenke, N. Mata, A. Eitner, and, D. Schweitzer,. In vivo and in vitro investigations of retinal fluorophores in age-related macular degeneration by fluorescence lifetime imaging. pp. 71832S-71832S-71812. International Society for Optics and Photonics, Proceedings of the SPIE BiOS: Biomedical Optics2009.
    • (2009) Proceedings of the SPIE BiOS: Biomedical Optics
    • Hammer, M.1    Quick, S.2    Klemm, M.3    Schenke, S.4    Mata, N.5    Eitner, A.6    Schweitzer, D.7
  • 96
    • 27744603114 scopus 로고    scopus 로고
    • Limits of the confocal laser-scanning technique in measurements of time-resolved autofluorescence of the ocular fundus
    • Schweitzer, D., M. Hammer, and, F. Schweitzer, (2005) Limits of the confocal laser-scanning technique in measurements of time-resolved autofluorescence of the ocular fundus. Biomed. Tech. 50, 263-267.
    • (2005) Biomed. Tech. , vol.50 , pp. 263-267
    • Schweitzer, D.1    Hammer, M.2    Schweitzer, F.3
  • 98
    • 0036770672 scopus 로고    scopus 로고
    • Cataract extraction and age-related macular degeneration: Associations, diagnosis and management
    • Velez, G., and, J. J. Weiter, (2002) Cataract extraction and age-related macular degeneration: associations, diagnosis and management. Semin. Ophthalmol. 17, 187-195.
    • (2002) Semin. Ophthalmol. , vol.17 , pp. 187-195
    • Velez, G.1    Weiter, J.J.2


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