메뉴 건너뛰기




Volumn 108, Issue 1, 1997, Pages 23-33

Glucación no enzimática de proteínas en la diabetes mellitus

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; DIABETES MELLITUS; GLYCOSYLATION; HUMAN; PATHOPHYSIOLOGY; REVIEW;

EID: 0041609941     PISSN: 00257753     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (6)

References (176)
  • 1
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulindependent diabetes mellitus
    • Diabetes Control and Complication Trial Research Group. The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulindependent diabetes mellitus. N Engl J Med 1993; 329: 977-986.
    • (1993) N Engl J Med , vol.329 , pp. 977-986
  • 2
    • 0022853632 scopus 로고
    • The nonenzymatic glycation of proteins and nucleic acids, their importance for the development of diabetic complications, possible molecular basis of aging and autoimmunological processes
    • Krantz S, Lober M, Henschel L. The nonenzymatic glycation of proteins and nucleic acids, their importance for the development of diabetic complications, possible molecular basis of aging and autoimmunological processes. Exp Clin Endocrinol 1986; 88: 257-269.
    • (1986) Exp Clin Endocrinol , vol.88 , pp. 257-269
    • Krantz, S.1    Lober, M.2    Henschel, L.3
  • 3
    • 0015230826 scopus 로고
    • Hemoglobin components in patients with diabetes mellitus
    • Trivelli LA, Ranney HN, Lai HT. Hemoglobin components in patients with diabetes mellitus. N Engl J Med 1971; 284: 353-357.
    • (1971) N Engl J Med , vol.284 , pp. 353-357
    • Trivelli, L.A.1    Ranney, H.N.2    Lai, H.T.3
  • 4
    • 0016547544 scopus 로고
    • Synthesis of hemoglobin A1c in normal and diabetic mice: Potential model of basement membrane thickening
    • Koening RJ, Cerami A. Synthesis of hemoglobin A1c in normal and diabetic mice: potential model of basement membrane thickening. Proc Natl Acad Sci USA 1975; 72: 3.687-3.691.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3687-3691
    • Koening, R.J.1    Cerami, A.2
  • 5
    • 0019984296 scopus 로고
    • Glycosylated hemoglobin in human animal red cells: Role of glucose permeability
    • Higgins PJ, Garlick RL, Bunn HF. Glycosylated hemoglobin in human animal red cells: role of glucose permeability. Diabetes 1982; 31: 743-748.
    • (1982) Diabetes , vol.31 , pp. 743-748
    • Higgins, P.J.1    Garlick, R.L.2    Bunn, H.F.3
  • 6
    • 0020003772 scopus 로고
    • Regulation of hemoglobin A1c formation in human erythrocytes in vitro. Effects of physiologic factors other than glucose
    • Smith RJ, Koenig RJ, Binnerts A, Soeldner JS, Aoki TT. Regulation of hemoglobin A1c formation in human erythrocytes in vitro. Effects of physiologic factors other than glucose. J Clin Invest 1982; 69: 1.164-1168.
    • (1982) J Clin Invest , vol.69 , pp. 1164-1168
    • Smith, R.J.1    Koenig, R.J.2    Binnerts, A.3    Soeldner, J.S.4    Aoki, T.T.5
  • 7
    • 0019488095 scopus 로고
    • Non-enzymatic glycosylation of protein: A form of molecular aging
    • Bunn HF. Non-enzymatic glycosylation of protein: a form of molecular aging. Schweiz Med Wochenschr 1981; 111: 1.503-1.507.
    • (1981) Schweiz Med Wochenschr , vol.111 , pp. 1503-1507
    • Bunn, H.F.1
  • 8
    • 0021702286 scopus 로고
    • National Diabetes Data Group: Report of the Expert Committee on glycosylated haemoglobin
    • Baynes JW, Bunn HF, Goldstein DE. National Diabetes Data Group: Report of the Expert Committee on glycosylated haemoglobin. Diabetes Care 1984; 7: 602-606.
    • (1984) Diabetes Care , vol.7 , pp. 602-606
    • Baynes, J.W.1    Bunn, H.F.2    Goldstein, D.E.3
  • 9
    • 0021950510 scopus 로고
    • Glycosylated haemoglobin measurement and clinical interpretation
    • Ashby JP, Deacon AC, Frier BM. Glycosylated haemoglobin measurement and clinical interpretation. Diabet Med 1985; 2: 83-87.
    • (1985) Diabet Med , vol.2 , pp. 83-87
    • Ashby, J.P.1    Deacon, A.C.2    Frier, B.M.3
  • 11
    • 0026601664 scopus 로고
    • Methods for the analysis of glycated haemoglobins: What is being measured
    • John WG, Bullock DG, McKenzie F. Methods for the analysis of glycated haemoglobins: what is being measured. Diabet Med 1992; 9: 15-19.
    • (1992) Diabet Med , vol.9 , pp. 15-19
    • John, W.G.1    Bullock, D.G.2    McKenzie, F.3
  • 12
    • 0026667483 scopus 로고
    • Glycated haemoglobin: An assessment of high capacity liquid Chromatographic and immunoassay methods
    • Standing SJ, Taylor RP. Glycated haemoglobin: an assessment of high capacity liquid Chromatographic and immunoassay methods. Ann Clin Biochem 1992; 29: 494-505.
    • (1992) Ann Clin Biochem , vol.29 , pp. 494-505
    • Standing, S.J.1    Taylor, R.P.2
  • 14
    • 0028855786 scopus 로고
    • Standardization of glycohemoglobin results and reference values in whole blood studied in 103 laboratories using 20 methods
    • Weykamp CW, Penders TJ, Miedema K, Muskiet FAJ, Van der Slik W. Standardization of glycohemoglobin results and reference values in whole blood studied in 103 laboratories using 20 methods. Clin Chem 1995; 41: 82-86.
    • (1995) Clin Chem , vol.41 , pp. 82-86
    • Weykamp, C.W.1    Penders, T.J.2    Miedema, K.3    Muskiet, F.A.J.4    Van Der Slik, W.5
  • 15
    • 0023180412 scopus 로고
    • Glycated haemoglobin analysis assessment of within and between laboratory performance in large UK region
    • John WG. Glycated haemoglobin analysis assessment of within and between laboratory performance in large UK region Ann Clin Biochem 1987; 24: 453-460.
    • (1987) Ann Clin Biochem , vol.24 , pp. 453-460
    • John, W.G.1
  • 16
    • 0027284774 scopus 로고
    • Blood glucose and glycated haemoglobin measurement in hospital: Which method?
    • Pickup JC, Crook MA, Tuft P. Blood glucose and glycated haemoglobin measurement in hospital: which method? Diabet Med 1993; 10: 402-411.
    • (1993) Diabet Med , vol.10 , pp. 402-411
    • Pickup, J.C.1    Crook, M.A.2    Tuft, P.3
  • 17
    • 0019843239 scopus 로고
    • The standardization of the thiobarbituric acid assay for nonenzymatic glucosylation of human serum albumin
    • Ney KA, Colley KJ, Pizzo SV. The standardization of the thiobarbituric acid assay for nonenzymatic glucosylation of human serum albumin. Ann Biochem 1981; 118: 294-300.
    • (1981) Ann Biochem , vol.118 , pp. 294-300
    • Ney, K.A.1    Colley, K.J.2    Pizzo, S.V.3
  • 18
    • 0018395653 scopus 로고
    • Nonenzymatically glucosylated albumin
    • Day JF, Thorpe SR, Baynes JW. Nonenzymatically glucosylated albumin. J Biol Chem 1979; 254: 595-597.
    • (1979) J Biol Chem , vol.254 , pp. 595-597
    • Day, J.F.1    Thorpe, S.R.2    Baynes, J.W.3
  • 19
    • 0022407525 scopus 로고
    • Use of aminophenylboronic acid affinity chromatography to measure glycosylated albumin levels
    • Rendell M, Kao G, Mecherikunnel P, Petersen B, Duhaney R, Nieremberg J et al. Use of aminophenylboronic acid affinity chromatography to measure glycosylated albumin levels. J Lab Clin Med 1985; 105: 63-69.
    • (1985) J Lab Clin Med , vol.105 , pp. 63-69
    • Rendell, M.1    Kao, G.2    Mecherikunnel, P.3    Petersen, B.4    Duhaney, R.5    Nieremberg, J.6
  • 20
    • 0021246940 scopus 로고
    • Glycosylated haemoglobin and plasma glycoprotein assays by affinity chromatography
    • Willey DG, Rosenthal MA, Caldwell S. Glycosylated haemoglobin and plasma glycoprotein assays by affinity chromatography. Diabetologia 1984; 27: 56-58.
    • (1984) Diabetologia , vol.27 , pp. 56-58
    • Willey, D.G.1    Rosenthal, M.A.2    Caldwell, S.3
  • 21
    • 0021798702 scopus 로고
    • Fluorometric measurement of glycosylated albumin in human serum
    • Hayashi Y, Makino M. Fluorometric measurement of glycosylated albumin in human serum. Clin Chim Acta 1985; 149: 13-19.
    • (1985) Clin Chim Acta , vol.149 , pp. 13-19
    • Hayashi, Y.1    Makino, M.2
  • 22
    • 0023392749 scopus 로고
    • Evaluation of the fructosamine test for the measurement of plasma protein glycation
    • Fluckiger R, Woodtli T, Berger W. Evaluation of the fructosamine test for the measurement of plasma protein glycation. Diabetologia 1987; 30: 648-652.
    • (1987) Diabetologia , vol.30 , pp. 648-652
    • Fluckiger, R.1    Woodtli, T.2    Berger, W.3
  • 23
    • 0025169254 scopus 로고
    • Longitudinal changes in serum fructosamine do not parallel those in glycated haemoglobin in young adults with insulin-dependent diabetes
    • Fisken RA, Chan AW, Hanlon A, MacFarlane IA. Longitudinal changes in serum fructosamine do not parallel those in glycated haemoglobin in young adults with insulin-dependent diabetes. Clin Chim Acta 1990; 191: 79-86.
    • (1990) Clin Chim Acta , vol.191 , pp. 79-86
    • Fisken, R.A.1    Chan, A.W.2    Hanlon, A.3    MacFarlane, I.A.4
  • 24
    • 0022219133 scopus 로고
    • Use of protein-based standards in automated colorimetric determinations of fructosamine in serum
    • Baker JR, Metcalf PA, Johnson RN, Newman D, Rietz P. Use of protein-based standards in automated colorimetric determinations of fructosamine in serum. Clin Chem 1985; 31: 1.550-1.554.
    • (1985) Clin Chem , vol.31 , pp. 1550-1554
    • Baker, J.R.1    Metcalf, P.A.2    Johnson, R.N.3    Newman, D.4    Rietz, P.5
  • 25
    • 0021270366 scopus 로고
    • Serum fructosamine concentrations in patients with type II (non-insulin-dependent) diabetes mellitus during changes in management
    • Baker JR, Johnson RN, Scott DJ. Serum fructosamine concentrations in patients with type II (non-insulin-dependent) diabetes mellitus during changes in management. Br Med J 1984; 288: 1.484-1.486.
    • (1984) Br Med J , vol.288 , pp. 1484-1486
    • Baker, J.R.1    Johnson, R.N.2    Scott, D.J.3
  • 28
    • 0018760804 scopus 로고
    • Glycosylated hemoglobin assay and oral glucose tolerance test compared for detection of diabetes mellitus
    • Dods RF, Bolmey C. Glycosylated hemoglobin assay and oral glucose tolerance test compared for detection of diabetes mellitus. Clin Chem 1979; 25: 764-768.
    • (1979) Clin Chem , vol.25 , pp. 764-768
    • Dods, R.F.1    Bolmey, C.2
  • 29
    • 0003512785 scopus 로고
    • Diabetes Mellitus. Report of a WHO Study Group
    • Ginebra: OMS
    • Diabetes Mellitus. Report of a WHO Study Group. Technical Report Series 727. Ginebra: OMS, 1985.
    • (1985) Technical Report Series 727
  • 30
    • 0019505292 scopus 로고
    • Glycohemoglobin: Its use in the follow-up of diabetes and diagnosis of glucose intolerance
    • Lev-Ran A. Glycohemoglobin: its use in the follow-up of diabetes and diagnosis of glucose intolerance. Arch Intern Med 1981; 141: 747-749.
    • (1981) Arch Intern Med , vol.141 , pp. 747-749
    • Lev-Ran, A.1
  • 31
    • 0018778226 scopus 로고
    • Glycohemoglobins and glucose intolerance
    • Lev-Ran A, Vanderlaan WP. Glycohemoglobins and glucose intolerance. JAMA 1979; 241: 912-914.
    • (1979) JAMA , vol.241 , pp. 912-914
    • Lev-Ran, A.1    Vanderlaan, W.P.2
  • 32
    • 0019390834 scopus 로고
    • Glycosylated haemoglobins in the diagnosis of diabetes mellitus and for the assessment of chronic hyperglycemia
    • Boucher BJ, Welch SG, Beer MS. Glycosylated haemoglobins in the diagnosis of diabetes mellitus and for the assessment of chronic hyperglycemia. Diabetologia 1981; 21: 34-36.
    • (1981) Diabetologia , vol.21 , pp. 34-36
    • Boucher, B.J.1    Welch, S.G.2    Beer, M.S.3
  • 34
    • 0021716658 scopus 로고
    • Comparison of glycosylated hemoglobin with oral glucose tolerance test
    • Cederholm J, Ronquist G, Wibell L. Comparison of glycosylated hemoglobin with oral glucose tolerance test. Diabet Metab 1984; 10: 224-229.
    • (1984) Diabet Metab , vol.10 , pp. 224-229
    • Cederholm, J.1    Ronquist, G.2    Wibell, L.3
  • 35
    • 0027373685 scopus 로고
    • Serum fructosamine as a screening test for diabetes in the elderly: A pilot study
    • Cefalu WT, Ettinger WH, Bell-Farrow AD, Rushing JT. Serum fructosamine as a screening test for diabetes in the elderly: a pilot study. J Am Geriatr Soc 1993; 41: 1.090-1.094.
    • (1993) J Am Geriatr Soc , vol.41 , pp. 1090-1094
    • Cefalu, W.T.1    Ettinger, W.H.2    Bell-Farrow, A.D.3    Rushing, J.T.4
  • 37
    • 0021970614 scopus 로고
    • Lack of correlation between glycosylated haemoglobin concentrations and number of daily insulin injections: Cross sectional study in care of ambulatory diabetes
    • Agardh CD, Tallroth G. Lack of correlation between glycosylated haemoglobin concentrations and number of daily insulin injections: cross sectional study in care of ambulatory diabetes. Br Med J 1985; 291: 622.
    • (1985) Br Med J , vol.291 , pp. 622
    • Agardh, C.D.1    Tallroth, G.2
  • 39
    • 0027633424 scopus 로고
    • Oznaczanie hemoglobiny glikozylowanej przydatna metoda kontroli przebiegu cukrzyci typu II u chorych podejrzanych o niepelne wyrownanie
    • Wywial M, Silanczyk A, Wywial R, Jakubowska D, Zmudzinski W, Kokot S. Oznaczanie hemoglobiny glikozylowanej przydatna metoda kontroli przebiegu cukrzyci typu II u chorych podejrzanych o niepelne wyrownanie. Pol Arch Med Wewn 1993; 90: 35-41.
    • (1993) Pol Arch Med Wewn , vol.90 , pp. 35-41
    • Wywial, M.1    Silanczyk, A.2    Wywial, R.3    Jakubowska, D.4    Zmudzinski, W.5    Kokot, S.6
  • 41
    • 0018079591 scopus 로고
    • Glycosylated hemoglobin in normal subjects and subjects with maturity onset diabetes
    • Graf RJ, Halter JB, Porte D. Glycosylated hemoglobin in normal subjects and subjects with maturity onset diabetes. Diabetes 1978; 27: 834-839.
    • (1978) Diabetes , vol.27 , pp. 834-839
    • Graf, R.J.1    Halter, J.B.2    Porte, D.3
  • 42
    • 0018742880 scopus 로고
    • Glycosylation of serum albumin: Elevated glucosyl albumin in diabetic patients
    • Dolhofer R, Wieland OH. Glycosylation of serum albumin: elevated glucosyl albumin in diabetic patients. FEBS Lett 1979; 103: 282-286.
    • (1979) FEBS Lett , vol.103 , pp. 282-286
    • Dolhofer, R.1    Wieland, O.H.2
  • 43
    • 0019251060 scopus 로고
    • Increased glycosylation of serum albumin in diabetes mellitus
    • Dolhofer R, Wieland OH. Increased glycosylation of serum albumin in diabetes mellitus. Diabetes 1980; 29: 417-422.
    • (1980) Diabetes , vol.29 , pp. 417-422
    • Dolhofer, R.1    Wieland, O.H.2
  • 44
    • 0019487251 scopus 로고
    • Different behavior of haemoglobin A1a-c and glucosyl-albumin levels during recovery from diabetic ketoacidosis and non-acidotic coma
    • Dolhofer R, Renner R, Wieland OH. Different behavior of haemoglobin A1a-c and glucosyl-albumin levels during recovery from diabetic ketoacidosis and non-acidotic coma. Diabetologia 1981; 21: 211-215.
    • (1981) Diabetologia , vol.21 , pp. 211-215
    • Dolhofer, R.1    Renner, R.2    Wieland, O.H.3
  • 45
    • 0021241024 scopus 로고
    • Glycosylated albumin and transferrin: Short term markers of blood glucose control
    • Kempf SF, Creech RH, Horn TR. Glycosylated albumin and transferrin: short term markers of blood glucose control. J Pediatr 1984; 105: 394-398.
    • (1984) J Pediatr , vol.105 , pp. 394-398
    • Kempf, S.F.1    Creech, R.H.2    Horn, T.R.3
  • 47
    • 0018835762 scopus 로고
    • Glycosylation of plasma protein and its relation to glycosylated hemoglobin in diabetes
    • Yue DK, Morris K, McLennan S, Turtle JR. Glycosylation of plasma protein and its relation to glycosylated hemoglobin in diabetes. Diabetes 1980; 29: 296-300.
    • (1980) Diabetes , vol.29 , pp. 296-300
    • Yue, D.K.1    Morris, K.2    McLennan, S.3    Turtle, J.R.4
  • 48
    • 2542554372 scopus 로고
    • Evolución de parámetros de glucación proteica a lo largo de la gestación en pacientes diabéticas
    • Grande C, Díez JJ, De la Morena ML, Ezquieta B, Luna R, Pallardo LF. Evolución de parámetros de glucación proteica a lo largo de la gestación en pacientes diabéticas. Endocrinología 1989; 36: 322-326.
    • (1989) Endocrinología , vol.36 , pp. 322-326
    • Grande, C.1    Díez, J.J.2    De La Morena, M.L.3    Ezquieta, B.4    Luna, R.5    Pallardo, L.F.6
  • 49
    • 0019798973 scopus 로고
    • Elevated maternal hemoglobin A1c in early pregnancy and major congenital anomalies in infants of diabetic mothers
    • Miller E, Hare JW, Cloherty JP, Dunn PJ, Gleason RE, Soeldner S et al. Elevated maternal hemoglobin A1c in early pregnancy and major congenital anomalies in infants of diabetic mothers. N Engl J Med 1981; 304: 1.331-1.334.
    • (1981) N Engl J Med , vol.304 , pp. 1331-1334
    • Miller, E.1    Hare, J.W.2    Cloherty, J.P.3    Dunn, P.J.4    Gleason, R.E.5    Soeldner, S.6
  • 50
    • 0021177841 scopus 로고
    • Risk of minor and major fetal malformations in diabetics with high haemoglobin A1c values in early pregnancy
    • Ylinen K, Aula P, Stenman UH, Kesäniemi-Kuokkanen T, Teramo K. Risk of minor and major fetal malformations in diabetics with high haemoglobin A1c values in early pregnancy. Br Med J 1984; 289: 345-346.
    • (1984) Br Med J , vol.289 , pp. 345-346
    • Ylinen, K.1    Aula, P.2    Stenman, U.H.3    Kesäniemi-Kuokkanen, T.4    Teramo, K.5
  • 51
    • 0024297636 scopus 로고
    • Hemoglobina glucosilada y fructosamina sanguíneas y péptido C en el líquido amniótico de gestantes diabéticas: Relación con el peso fetal
    • Barc
    • Díez JJ, Pallardo LF, Grande C. Hemoglobina glucosilada y fructosamina sanguíneas y péptido C en el líquido amniótico de gestantes diabéticas: relación con el peso fetal. Med Clin (Barc) 1988; 90: 484-489.
    • (1988) Med Clin , vol.90 , pp. 484-489
    • Díez, J.J.1    Pallardo, L.F.2    Grande, C.3
  • 52
    • 0019729926 scopus 로고
    • Stability of hemoglobin A1c levels on repetitive determination in diabetic outpatients
    • Dunn PJ, Cole RA, Soeldner JS, Gleason RE. Stability of hemoglobin A1c levels on repetitive determination in diabetic outpatients. J Clin Endocrinol Metab 1981; 52: 1.019-1.022.
    • (1981) J Clin Endocrinol Metab , vol.52 , pp. 1019-1022
    • Dunn, P.J.1    Cole, R.A.2    Soeldner, J.S.3    Gleason, R.E.4
  • 53
    • 0026659456 scopus 로고
    • Direct evidence for the alterations in protein structure and conformation upon in vitro nonenzymatic glycosylation
    • Watala C, Gwozdzinski K, Malek M. Direct evidence for the alterations in protein structure and conformation upon in vitro nonenzymatic glycosylation. Int J Biochem 1992; 24: 1.295-1.302.
    • (1992) Int J Biochem , vol.24 , pp. 1295-1302
    • Watala, C.1    Gwozdzinski, K.2    Malek, M.3
  • 56
    • 0021231172 scopus 로고
    • Nonenzymatic glycosylation and phatogenesis of diabetic complications
    • Brownlee M, Vlassara H, Cerami A. Nonenzymatic glycosylation and phatogenesis of diabetic complications. Ann Intern Med 1984; 101: 527-537.
    • (1984) Ann Intern Med , vol.101 , pp. 527-537
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 57
    • 0023950461 scopus 로고
    • Advanced glycosylation and products in tissue and the biochemical basis of diabetic complications
    • Brownlee M, Cerami A, Vlassara H. Advanced glycosylation and products in tissue and the biochemical basis of diabetic complications. N Engl J Med 1988; 318: 1.315-1.321.
    • (1988) N Engl J Med , vol.318 , pp. 1315-1321
    • Brownlee, M.1    Cerami, A.2    Vlassara, H.3
  • 58
    • 0024272467 scopus 로고
    • Collagen browning and cross-linking are increased in chronic experimental hyperglycemia
    • Monnier VM, Sell DR, Abdul-Karim FW, Emancipator SN. Collagen browning and cross-linking are increased in chronic experimental hyperglycemia. Diabet 1988; 37: 867-872.
    • (1988) Diabet , vol.37 , pp. 867-872
    • Monnier, V.M.1    Sell, D.R.2    Abdul-Karim, F.W.3    Emancipator, S.N.4
  • 59
    • 0026347369 scopus 로고
    • Advanced nonenzymatic glycation endproducts (AGE): Their relevance to aging and the pathogenesis of late diabetic complications
    • Sensi M, Pricci F, Andreani D, Di Mario U. Advanced nonenzymatic glycation endproducts (AGE): their relevance to aging and the pathogenesis of late diabetic complications. Diabetes Res 1991; 16: 1-9.
    • (1991) Diabetes Res , vol.16 , pp. 1-9
    • Sensi, M.1    Pricci, F.2    Andreani, D.3    Di Mario, U.4
  • 60
    • 11944272384 scopus 로고
    • Glycation products and the pathogenesis of diabetic complications
    • Brownlee M. Glycation products and the pathogenesis of diabetic complications. Diabet Care 1992; 15: 1.835-1.843.
    • (1992) Diabet Care , vol.15 , pp. 1835-1843
    • Brownlee, M.1
  • 61
    • 0027913005 scopus 로고
    • Glycosylation non-enzymatique des proteines. Complications du diabete, du vieillissement et de l'insuffisance renale
    • Monnier V. Glycosylation non-enzymatique des proteines. Complications du diabete, du vieillissement et de l'insuffisance renale. Presse Med 1993; 22: 1.413-1.418.
    • (1993) Presse Med , vol.22 , pp. 1413-1418
    • Monnier, V.1
  • 62
    • 0027137507 scopus 로고
    • Review of diabetes: Identification of markers for early detection, glycemic control, and monitoring clinical complications
    • Wu JT. Review of diabetes: identification of markers for early detection, glycemic control, and monitoring clinical complications. J Clin Lab Anal 1993; 7: 293-300.
    • (1993) J Clin Lab Anal , vol.7 , pp. 293-300
    • Wu, J.T.1
  • 64
    • 0026356684 scopus 로고
    • Pentosidine: A molecular marker for the cumulative damage to proteins in diabetes, aging, and uremia
    • Sell DR, Nagaraj RH, Grandhee SK, Odetti P, Lapolla A, Fogarty J et al. Pentosidine: a molecular marker for the cumulative damage to proteins in diabetes, aging, and uremia. Diabet Metab Rev 1991; 7: 239-251.
    • (1991) Diabet Metab Rev , vol.7 , pp. 239-251
    • Sell, D.R.1    Nagaraj, R.H.2    Grandhee, S.K.3    Odetti, P.4    Lapolla, A.5    Fogarty, J.6
  • 65
    • 0027515855 scopus 로고
    • Presence of 3-deoxyglucosone, a potent crosslinking intermediated of Maillard reaction, in diabetic serum
    • Niwa T, Takeda N, Yoshizumi H, Tatematsu A, Ohara M, Tomiyama S et al. Presence of 3-deoxyglucosone, a potent crosslinking intermediated of Maillard reaction, in diabetic serum. Biochem Biophys Res Comm 1993; 196: 837-843.
    • (1993) Biochem Biophys Res Comm , vol.196 , pp. 837-843
    • Niwa, T.1    Takeda, N.2    Yoshizumi, H.3    Tatematsu, A.4    Ohara, M.5    Tomiyama, S.6
  • 66
    • 0023940640 scopus 로고
    • Cachectin/TNF and IL-1 induced by glucose-modified proteins: Role in normal tissue remodeling
    • Vlassara H, Brownlee M, Manogue K, Dinarello CA, Pasagian A, Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science 1988; 240: 1.546-1.548.
    • (1988) Science , vol.240 , pp. 1546-1548
    • Vlassara, H.1    Brownlee, M.2    Manogue, K.3    Dinarello, C.A.4    Pasagian, A.5
  • 67
    • 0027176945 scopus 로고
    • Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
    • Schmidt AM, Yan SD, Brett J, Mora R, Nowygrod R, Stern D. Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. J Clin Invest 1993; 91: 2.155-2.168.
    • (1993) J Clin Invest , vol.91 , pp. 2155-2168
    • Schmidt, A.M.1    Yan, S.D.2    Brett, J.3    Mora, R.4    Nowygrod, R.5    Stern, D.6
  • 68
    • 0004818738 scopus 로고
    • High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules
    • Vlassara H, Brownlee M, Cerami A. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci USA 1985; 82: 5.588-5.592.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 69
    • 0024851555 scopus 로고
    • Macrophage/monocyte receptor for non-enzymatically glycosylated proteins is upregulated by cachectin/tumor necrosis factor
    • Vlassara H, Moldawer L, Chan B. Macrophage/monocyte receptor for non-enzymatically glycosylated proteins is upregulated by cachectin/tumor necrosis factor. J Clin Invest 1989; 84: 1.813-1.820.
    • (1989) J Clin Invest , vol.84 , pp. 1813-1820
    • Vlassara, H.1    Moldawer, L.2    Chan, B.3
  • 70
    • 0025689060 scopus 로고
    • Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophage-derived cell line RAW 264.7
    • Radoff S, Cerami A, Vlassara H. Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophage-derived cell line RAW 264.7. Diabetes 1990; 39: 1.510-1.518.
    • (1990) Diabetes , vol.39 , pp. 1510-1518
    • Radoff, S.1    Cerami, A.2    Vlassara, H.3
  • 71
    • 0027420670 scopus 로고
    • Advanced glycosylation endproduct-specific receptors on human and rat T-lymphocytes mediate synthesis of interferon gamma: Role in tissue remodeling
    • Imani F, Horii Y, Suthanthiran M, Skolnik EY, Makita Z, Sharma V et al. Advanced glycosylation endproduct-specific receptors on human and rat T-lymphocytes mediate synthesis of interferon gamma: role in tissue remodeling. J Exp Med 1993; 178: 2.165-2.172.
    • (1993) J Exp Med , vol.178 , pp. 2165-2172
    • Imani, F.1    Horii, Y.2    Suthanthiran, M.3    Skolnik, E.Y.4    Makita, Z.5    Sharma, V.6
  • 72
    • 0027718105 scopus 로고
    • Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues
    • Brett J, Schmitdt AM, Yan SD, Zou YS, Weidman E, Pinsky D et al. Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues. Am J Pathol 1993; 143: 1.699-1.712.
    • (1993) Am J Pathol , vol.143 , pp. 1699-1712
    • Brett, J.1    Schmitdt, A.M.2    Yan, S.D.3    Zou, Y.S.4    Weidman, E.5    Pinsky, D.6
  • 73
    • 0027290572 scopus 로고
    • Identification of aortic endothelial cell binding proteins for Amadori adducts in glycated albumin
    • Wu VY, Cohen MP. Identification of aortic endothelial cell binding proteins for Amadori adducts in glycated albumin. Biochem Biophys Res Comm 1993; 30: 1.131-1.136.
    • (1993) Biochem Biophys Res Comm , vol.30 , pp. 1131-1136
    • Wu, V.Y.1    Cohen, M.P.2
  • 75
    • 0000571086 scopus 로고
    • Modification of DNA by reducing sugars: A possible mechanism for nucleic acid aging and age-related dysfunction in gene expresion
    • Bucala R, Model P, Cerami A. Modification of DNA by reducing sugars: a possible mechanism for nucleic acid aging and age-related dysfunction in gene expresion. Proc Natl Acad Sci USA 1984; 81: 105-109.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 105-109
    • Bucala, R.1    Model, P.2    Cerami, A.3
  • 76
  • 81
    • 0026675759 scopus 로고
    • Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM
    • Sell DR, Lapolla A, Odetti P, Fogarty J, Monnier VM. Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM. Diabetes 1992; 41: 1.286-1.292.
    • (1992) Diabetes , vol.41 , pp. 1286-1292
    • Sell, D.R.1    Lapolla, A.2    Odetti, P.3    Fogarty, J.4    Monnier, V.M.5
  • 82
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • McCance DR, Dyer DG, Dunn JA, Bailie KE, Thorpe SR, Baynes JW et al. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 1993; 91: 2.470-2.478.
    • (1993) J Clin Invest , vol.91 , pp. 2470-2478
    • McCance, D.R.1    Dyer, D.G.2    Dunn, J.A.3    Bailie, K.E.4    Thorpe, S.R.5    Baynes, J.W.6
  • 83
    • 0027448330 scopus 로고
    • Stiffening of connective tissue in elderly diabetic patients: Relevance to diabetic nephropathy and oxidative stress
    • Aoki Y, Yazaki K, Shirotori K, Yanagisawa Y, Oguchi H, Kiyosawa K et al. Stiffening of connective tissue in elderly diabetic patients: relevance to diabetic nephropathy and oxidative stress. Diabetologia 1993; 36: 79-83.
    • (1993) Diabetologia , vol.36 , pp. 79-83
    • Aoki, Y.1    Yazaki, K.2    Shirotori, K.3    Yanagisawa, Y.4    Oguchi, H.5    Kiyosawa, K.6
  • 84
    • 0023932850 scopus 로고
    • The effect of nonenzymatic glycosilation on the binding of the main noncollagenous NC1 domain at to type IV collagen
    • Tsilbary EC, Charonis AS, Reger LA, Wonlhueter RM, Furcht LT. The effect of nonenzymatic glycosilation on the binding of the main noncollagenous NC1 domain at to type IV collagen. J Biol Chem 1988; 263: 4.302-4.308.
    • (1988) J Biol Chem , vol.263 , pp. 4302-4308
    • Tsilbary, E.C.1    Charonis, A.S.2    Reger, L.A.3    Wonlhueter, R.M.4    Furcht, L.T.5
  • 85
    • 0026723061 scopus 로고
    • Structural and functional changes of laminin and type IV collagen after nonenzymatic glycation
    • Charonis AS, Tsilibary EC. Structural and functional changes of laminin and type IV collagen after nonenzymatic glycation. Diabetes 1992; 41 (Supl 2): 49-51.
    • (1992) Diabetes , vol.41 , Issue.2 SUPPL. , pp. 49-51
    • Charonis, A.S.1    Tsilibary, E.C.2
  • 86
    • 0022921495 scopus 로고
    • Glycosylation of low density lipoprotein in patients with type 1 diabetes: Correlations with other parameters of glycaemic control
    • Lyons TJ, Patrick JS, Baines JW, Colwell JA, Lopes-Virella MF. Glycosylation of low density lipoprotein in patients with type 1 diabetes: correlations with other parameters of glycaemic control. Diabetologia 1986; 29: 685-689.
    • (1986) Diabetologia , vol.29 , pp. 685-689
    • Lyons, T.J.1    Patrick, J.S.2    Baines, J.W.3    Colwell, J.A.4    Lopes-Virella, M.F.5
  • 88
    • 0026703165 scopus 로고
    • Lipoprotein glycation and its metabolic consequences
    • Lyons TJ. Lipoprotein glycation and its metabolic consequences. Diabetes 1992; 41 (Supl 2): 67-73.
    • (1992) Diabetes , vol.41 , Issue.2 SUPPL. , pp. 67-73
    • Lyons, T.J.1
  • 89
    • 0027537768 scopus 로고
    • Glycation and oxidation: A role in the pathogenesis of atherosclerosis
    • Lyons TJ. Glycation and oxidation: a role in the pathogenesis of atherosclerosis. Am J Cardiol 1993; 71: 26B-31B.
    • (1993) Am J Cardiol , vol.71
    • Lyons, T.J.1
  • 90
    • 84945735124 scopus 로고
    • Glycated LDL concentrations in non-diabetic and diabetic subjects measured with monoclonal antibodies reactive with glycated apolipoprotein B epitopes
    • Cohen MP, Lautenslager G, Shea E. Glycated LDL concentrations in non-diabetic and diabetic subjects measured with monoclonal antibodies reactive with glycated apolipoprotein B epitopes. Eur J Clin Chem Biochem 1993; 31: 707-713.
    • (1993) Eur J Clin Chem Biochem , vol.31 , pp. 707-713
    • Cohen, M.P.1    Lautenslager, G.2    Shea, E.3
  • 91
    • 0020068937 scopus 로고
    • Surface binding, internalization and degradation by cultured human fibroblasts of low density lipoproteins isolated from type 1 (insulin-dependent) diabetic patients: Changes with metabolic control
    • Lopes-Virella MF, Sherer GK, Lees AM, Wohlthann H, Mayfield R, Sagel J et al. Surface binding, internalization and degradation by cultured human fibroblasts of low density lipoproteins isolated from type 1 (insulin-dependent) diabetic patients: changes with metabolic control. Diabetologia 1982; 22: 430-436.
    • (1982) Diabetologia , vol.22 , pp. 430-436
    • Lopes-Virella, M.F.1    Sherer, G.K.2    Lees, A.M.3    Wohlthann, H.4    Mayfield, R.5    Sagel, J.6
  • 92
    • 0026343582 scopus 로고
    • Metabolic consequences of the nonenzymatic glucosilation of apolipoproteins
    • Ponsin G, Calvo C, Berthezene F. Metabolic consequences of the nonenzymatic glucosilation of apolipoproteins. Diabet Metab 1991; 17: 497-502.
    • (1991) Diabet Metab , vol.17 , pp. 497-502
    • Ponsin, G.1    Calvo, C.2    Berthezene, F.3
  • 93
    • 0027315839 scopus 로고
    • Modified low density lipoproteins from diabetic patients causes cholesterol accumulation in human intimai aortic cells
    • Sobenin IA, Tertov W, Koschinsky T, Bunting CE, Slavina ES, Dedov II et al. Modified low density lipoproteins from diabetic patients causes cholesterol accumulation in human intimai aortic cells. Atherosclerosis 1993; 100: 41-54.
    • (1993) Atherosclerosis , vol.100 , pp. 41-54
    • Sobenin, I.A.1    Tertov, W.2    Koschinsky, T.3    Bunting, C.E.4    Slavina, E.S.5    Dedov, I.I.6
  • 94
    • 0025540553 scopus 로고
    • Free radical generation by early glycation products: A mechanism for accelerated atherogenesis in diabetes
    • Mullarkey CJ, Edelstein D, Brownlee M. Free radical generation by early glycation products: a mechanism for accelerated atherogenesis in diabetes. Biochem Biophys Res Comm 1990; 173: 932-939.
    • (1990) Biochem Biophys Res Comm , vol.173 , pp. 932-939
    • Mullarkey, C.J.1    Edelstein, D.2    Brownlee, M.3
  • 95
    • 0025758118 scopus 로고
    • Oxidized low density lipoproteins- A role in the pathogenesis of atherosclerosis in diabetes?
    • Lyons TJ. Oxidized low density lipoproteins- a role in the pathogenesis of atherosclerosis in diabetes? Diabet Med 1991; 8: 411-419.
    • (1991) Diabet Med , vol.8 , pp. 411-419
    • Lyons, T.J.1
  • 96
    • 0020616462 scopus 로고
    • Low density lipoprotein cytotoxity induced by free radical peroxidation of lipid
    • Morel DW, Hessler JR, Chisol GM. Low density lipoprotein cytotoxity induced by free radical peroxidation of lipid. J Lipid Res 1983; 24: 1.070-1.076.
    • (1983) J Lipid Res , vol.24 , pp. 1070-1076
    • Morel, D.W.1    Hessler, J.R.2    Chisol, G.M.3
  • 97
    • 0027183867 scopus 로고
    • Glycosylated low density lipoprotein is more sensitive to oxidation: Implications for the diabetic patient?
    • Bowie A, Owens D, Collins P, Johnson A, Tomkin GH. Glycosylated low density lipoprotein is more sensitive to oxidation: implications for the diabetic patient? Atherosclerosis 1993; 102: 63-67.
    • (1993) Atherosclerosis , vol.102 , pp. 63-67
    • Bowie, A.1    Owens, D.2    Collins, P.3    Johnson, A.4    Tomkin, G.H.5
  • 98
    • 0026657680 scopus 로고
    • Immune mechanisms of atherosclerosis in diabetes mellitus
    • Lopes-Virella MF, Virella G. Immune mechanisms of atherosclerosis in diabetes mellitus. Diabetes 1992; 41 (Supl 2): 86-91.
    • (1992) Diabetes , vol.41 , Issue.2 SUPPL. , pp. 86-91
    • Lopes-Virella, M.F.1    Virella, G.2
  • 99
    • 0026783776 scopus 로고
    • Lipoprotein-immune complexes and diabetic vascular complications
    • Gisinger CH, Lopes-Virella MF. Lipoprotein-immune complexes and diabetic vascular complications. Diabetes 1992; 41 (Supl 2): 92-96.
    • (1992) Diabetes , vol.41 , Issue.2 SUPPL. , pp. 92-96
    • Gisinger, C.H.1    Lopes-Virella, M.F.2
  • 100
    • 0021889184 scopus 로고
    • Plasma apo-lipoproteins A-I, A-II, B, C-I, and e are glycosylated in hyperglycemic diabetic subjects
    • Curtiss LK, Witztum JL. Plasma apo-lipoproteins A-I, A-II, B, C-I, and E are glycosylated in hyperglycemic diabetic subjects. Diabetes 1985; 34: 452-461.
    • (1985) Diabetes , vol.34 , pp. 452-461
    • Curtiss, L.K.1    Witztum, J.L.2
  • 101
    • 0025038731 scopus 로고
    • Nonenzymatic glycosylation of HDL resulting in inhibition of high-affinity binding to cultured human fibroblasts
    • Duell PB, Oram JF, Bierman EL. Nonenzymatic glycosylation of HDL resulting in inhibition of high-affinity binding to cultured human fibroblasts. Diabetes 1990; 39: 1.257-1.263.
    • (1990) Diabetes , vol.39 , pp. 1257-1263
    • Duell, P.B.1    Oram, J.F.2    Bierman, E.L.3
  • 102
    • 0026013131 scopus 로고
    • Noenzymatic glycosylation of HDL and impaired HDL-receptor-mediated cholesterol efflux
    • Duell PB, Oram JF, Bierman EL. Noenzymatic glycosylation of HDL and impaired HDL-receptor-mediated cholesterol efflux. Diabetes 1991; 40: 377-384.
    • (1991) Diabetes , vol.40 , pp. 377-384
    • Duell, P.B.1    Oram, J.F.2    Bierman, E.L.3
  • 103
    • 84952619562 scopus 로고
    • Association in vivo of glycated apolipoprotein A-I with high density lipoproteins
    • Calvo C, Verdugo C. Association in vivo of glycated apolipoprotein A-I with high density lipoproteins. Eur J Clin Chem Clin Biochem 1992; 30: 3-5.
    • (1992) Eur J Clin Chem Clin Biochem , vol.30 , pp. 3-5
    • Calvo, C.1    Verdugo, C.2
  • 104
    • 84943464639 scopus 로고
    • Decreased activation of lecitin. cholesterol acyltransferase by glycated apolipoprotein A-I
    • Calvo C, Ulloa N, Del Pozo R, Verdugo C. Decreased activation of lecitin. cholesterol acyltransferase by glycated apolipoprotein A-I. Eur J Clin Chem Clin Biochem 1993; 31: 217-220.
    • (1993) Eur J Clin Chem Clin Biochem , vol.31 , pp. 217-220
    • Calvo, C.1    Ulloa, N.2    Del Pozo, R.3    Verdugo, C.4
  • 105
    • 0019920378 scopus 로고
    • Nonenzymatic glucosilation of high-density lipoprotein accelerates its catabolism in guinea pigs
    • Witztum JL, Fisher M, Pietro T, Steinbrecher UP, Elam RL. Nonenzymatic glucosilation of high-density lipoprotein accelerates its catabolism in guinea pigs. Diabetes 1982; 31: 1.029-1.032.
    • (1982) Diabetes , vol.31 , pp. 1029-1032
    • Witztum, J.L.1    Fisher, M.2    Pietro, T.3    Steinbrecher, U.P.4    Elam, R.L.5
  • 106
    • 0025359177 scopus 로고
    • Glycation of very low density lipoprotein form rat plasma impairs its catabolism
    • Mamo JC, Szeto L, Steiner G. Glycation of very low density lipoprotein form rat plasma impairs its catabolism. Diabetologia 1990; 33: 339-345.
    • (1990) Diabetologia , vol.33 , pp. 339-345
    • Mamo, J.C.1    Szeto, L.2    Steiner, G.3
  • 107
    • 0020975006 scopus 로고
    • Covalent attachement of soluble proteins by nonenzymatically glycosylated collagen. role in the situ formation of immune complex
    • Brownlee M, Pongor S, Cerami A. Covalent attachement of soluble proteins by nonenzymatically glycosylated collagen. role in the situ formation of immune complex. J Exp Med 1983; 158: 1.739-1.744.
    • (1983) J Exp Med , vol.158 , pp. 1739-1744
    • Brownlee, M.1    Pongor, S.2    Cerami, A.3
  • 108
    • 0021886497 scopus 로고
    • Nonenzymatic glycosylation products on collagen covalently trap low-density lipoprotein
    • Brownlee M, Vlassara H, Cerami A. Nonenzymatic glycosylation products on collagen covalently trap low-density lipoprotein. Diabetes 1985; 34: 938-941.
    • (1985) Diabetes , vol.34 , pp. 938-941
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 110
    • 0026713726 scopus 로고
    • Advanced glycosylation endproducts block the antiproliferative effect of nitric oxide. Role in the vascular and renal complications of diabetes mellitus
    • Hogan M, Cerami A, Bucala R. Advanced glycosylation endproducts block the antiproliferative effect of nitric oxide. Role in the vascular and renal complications of diabetes mellitus. J Clin Invest 1992; 90: 1.110-1.115.
    • (1992) J Clin Invest , vol.90 , pp. 1110-1115
    • Hogan, M.1    Cerami, A.2    Bucala, R.3
  • 111
    • 85047676110 scopus 로고
    • Diminished arterial elasticity in diabetes: Association with fluorescent advanced glycosylation end products in collagen
    • Airaksinen KE, Salmela PI, Linnaluoto MK, Ikaheimo MJ, Ahola K, Ryhanen LJ. Diminished arterial elasticity in diabetes: association with fluorescent advanced glycosylation end products in collagen. Crdiovasc Res 1993; 27: 942-945.
    • (1993) Crdiovasc Res , vol.27 , pp. 942-945
    • Airaksinen, K.E.1    Salmela, P.I.2    Linnaluoto, M.K.3    Ikaheimo, M.J.4    Ahola, K.5    Ryhanen, L.J.6
  • 112
    • 0027291535 scopus 로고
    • Aminoguanidine treatment increases elasticity and decreasaes fluid filtration of large arteries from diabetics rats
    • Huijberts MS, Wolffenbuttel BH, Boudier HA, Crijns FR, Kruseman AC, Poitevin P et al. Aminoguanidine treatment increases elasticity and decreasaes fluid filtration of large arteries from diabetics rats. J Clin Invest 1993; 92: 1.407-1.411.
    • (1993) J Clin Invest , vol.92 , pp. 1407-1411
    • Huijberts, M.S.1    Wolffenbuttel, B.H.2    Boudier, H.A.3    Crijns, F.R.4    Kruseman, A.C.5    Poitevin, P.6
  • 114
    • 0027732183 scopus 로고
    • Immunohistochemical localization of advanced glycosylation end products in coronary atheroma and cardiac tissue in diabetes mellitus
    • Nakamura Y, Horii Y, Nishino T, Sakaguchi Y, Kagoshima T, Dohi K et al. Immunohistochemical localization of advanced glycosylation end products in coronary atheroma and cardiac tissue in diabetes mellitus. Am J Pathol 1993; 143: 1.649-1.656.
    • (1993) Am J Pathol , vol.143 , pp. 1649-1656
    • Nakamura, Y.1    Horii, Y.2    Nishino, T.3    Sakaguchi, Y.4    Kagoshima, T.5    Dohi, K.6
  • 115
    • 0021236835 scopus 로고
    • Endothelial and smooth muscle cells alters LDL in vitro by free radical oxidation
    • Morel DW, DiCorleto PE, Chilsom G. Endothelial and smooth muscle cells alters LDL in vitro by free radical oxidation. Arteriosclerosis 1984; 4: 357-364.
    • (1984) Arteriosclerosis , vol.4 , pp. 357-364
    • Morel, D.W.1    DiCorleto, P.E.2    Chilsom, G.3
  • 116
    • 0027367204 scopus 로고
    • Coagulation activation in diabetes mellitus: The role of hyperglycaemia and therapeutic prospects
    • Ceriello A. Coagulation activation in diabetes mellitus: the role of hyperglycaemia and therapeutic prospects. Diabetologia 1993; 36: 1.119-1.125.
    • (1993) Diabetologia , vol.36 , pp. 1119-1125
    • Ceriello, A.1
  • 117
  • 118
    • 0024468052 scopus 로고
    • Endothelial receptor-mediated binding of glucose-modified is associated with increased monolayer permeability and modulation of cell surface coagulant properties
    • Esposito C, Gerlach H, Brett J, Stern D, Vlassara H. Endothelial receptor-mediated binding of glucose-modified is associated with increased monolayer permeability and modulation of cell surface coagulant properties. J Exp Med 1989; 170: 1.387-1-407.
    • (1989) J Exp Med , vol.170 , pp. 1387-1407
    • Esposito, C.1    Gerlach, H.2    Brett, J.3    Stern, D.4    Vlassara, H.5
  • 119
    • 0000555820 scopus 로고
    • Recombinant tumor necrosis factor induces procoagulant activity in cultured human vascular endothelium: Characterization and comparison with the actions of interleukin 1
    • Bevilacqua MP, Pober JS, Majeau GR, Fiers W, Cotran RS, Gimbrone MA Jr. Recombinant tumor necrosis factor induces procoagulant activity in cultured human vascular endothelium: characterization and comparison with the actions of interleukin 1. Proc Natl Acad Sci 1986; 83: 4.533-4.537.
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 4533-4537
    • Bevilacqua, M.P.1    Pober, J.S.2    Majeau, G.R.3    Fiers, W.4    Cotran, R.S.5    Gimbrone Jr., M.A.6
  • 120
    • 0021255358 scopus 로고
    • Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation: Possible role in fibrin deposition in diabetes
    • Brownlee M, Vlassara H, Cerami A. Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation: possible role in fibrin deposition in diabetes. Diabetes 1984; 33: 532-535.
    • (1984) Diabetes , vol.33 , pp. 532-535
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 122
    • 0026743264 scopus 로고
    • Hyperglycaemia alters the physico-chemical properties of proteins in erythrocyte membranes of diabetic patients
    • Watala C. Hyperglycaemia alters the physico-chemical properties of proteins in erythrocyte membranes of diabetic patients. Int J Biochem 1992; 24: 1.755-1.761.
    • (1992) Int J Biochem , vol.24 , pp. 1755-1761
    • Watala, C.1
  • 123
    • 0026726130 scopus 로고
    • The association between erythrocyte internal viscosity, protein non-enzymatic glycosylation and erithrocyte membrane dynamic properties in juvenile diabetes mellitus
    • Watala C, Witas H, Olszowska L, Piasecki W. The association between erythrocyte internal viscosity, protein non-enzymatic glycosylation and erithrocyte membrane dynamic properties in juvenile diabetes mellitus. Int J Exp Pathol 1992; 73: 655-663.
    • (1992) Int J Exp Pathol , vol.73 , pp. 655-663
    • Watala, C.1    Witas, H.2    Olszowska, L.3    Piasecki, W.4
  • 124
    • 0027342655 scopus 로고
    • Role of nonenzymatic glycosilation of proteins in disorders of erythrocytes and blood platelets in diabetes mellitus
    • Watala C. Role of nonenzymatic glycosilation of proteins in disorders of erythrocytes and blood platelets in diabetes mellitus. Acta Haematol Pol 1993; 24: 95-101.
    • (1993) Acta Haematol Pol , vol.24 , pp. 95-101
    • Watala, C.1
  • 126
    • 0018160553 scopus 로고
    • Reduced erythrocyte deforambility in diabetes
    • McMillan DE, Utterback NG, LaPuma J. Reduced erythrocyte deforambility in diabetes. Diabetes 1978; 27: 895-901.
    • (1978) Diabetes , vol.27 , pp. 895-901
    • McMillan, D.E.1    Utterback, N.G.2    LaPuma, J.3
  • 127
    • 0027667833 scopus 로고
    • Immunochemical determination of advanced glycation end products in erythrocyte peripheral-membrane proteins from diabetic patients
    • Kuwajima S. Immunochemical determination of advanced glycation end products in erythrocyte peripheral-membrane proteins from diabetic patients. Hokkaido Igaku Zasshi 1993; 68: 695-704.
    • (1993) Hokkaido Igaku Zasshi , vol.68 , pp. 695-704
    • Kuwajima, S.1
  • 128
    • 0025324232 scopus 로고
    • Glycation of the human erythrocyte glucose transporte in vitro and its functional consequences
    • Bilan PJ, Klip A. Glycation of the human erythrocyte glucose transporte in vitro and its functional consequences. Biochem J 1990; 268: 661-667.
    • (1990) Biochem J , vol.268 , pp. 661-667
    • Bilan, P.J.1    Klip, A.2
  • 129
    • 0027325597 scopus 로고
    • The erythrocyte calcium pump is inhibited by non-enzymatic glycation: Studies in situ and with the purified enzyme
    • González Flecha FL, Castello PR, Caride AJ, Gagliardino JJ, Rossi JP. The erythrocyte calcium pump is inhibited by non-enzymatic glycation: studies in situ and with the purified enzyme. Biochem J 1993; 293: 369-375.
    • (1993) Biochem J , vol.293 , pp. 369-375
    • González Flecha, F.L.1    Castello, P.R.2    Caride, A.J.3    Gagliardino, J.J.4    Rossi, J.P.5
  • 130
    • 0026777243 scopus 로고
    • Increased glycated Cu,Zn-superoxide dismutase levels in erythrocytes of patients with insulin-dependent diabetes mellitus
    • Kawamura N, Ookawara T, Suzuki K, Konishi K, Mino M, Taniguchi N. Increased glycated Cu,Zn-superoxide dismutase levels in erythrocytes of patients with insulin-dependent diabetes mellitus. J Clin Endocrinol Metab 1992; 74: 1.352-1.354.
    • (1992) J Clin Endocrinol Metab , vol.74 , pp. 1352-1354
    • Kawamura, N.1    Ookawara, T.2    Suzuki, K.3    Konishi, K.4    Mino, M.5    Taniguchi, N.6
  • 131
    • 0025088921 scopus 로고
    • Impairment by glycation of immunoglobulin G Fc fragment function
    • Dolhofer Bliesener R, Gerbitz KD. Impairment by glycation of immunoglobulin G Fc fragment function. Scand J Clin Lab Invest 1990; 50: 739-746.
    • (1990) Scand J Clin Lab Invest , vol.50 , pp. 739-746
    • Dolhofer Bliesener, R.1    Gerbitz, K.D.2
  • 132
    • 0025003795 scopus 로고
    • Effect of nonenzymatic glycation on the structure of immunoglobulin G
    • Dohofer Bliesener R, Gerbitz KD. Effect of nonenzymatic glycation on the structure of immunoglobulin G, Biol Chem Hoppe Seyler 1990; 371: 693-697.
    • (1990) Biol Chem Hoppe Seyler , vol.371 , pp. 693-697
    • Dohofer Bliesener, R.1    Gerbitz, K.D.2
  • 133
    • 0025969283 scopus 로고
    • Nonenzymatic glycosilation of immunoglobulin G impairs complement fixation
    • Hennessey PJ, Black CT, Andrassy RJ. Nonenzymatic glycosilation of immunoglobulin G impairs complement fixation. JPEN J Parent Enterai Nutr 1991; 15: 60-64.
    • (1991) JPEN J Parent Enterai Nutr , vol.15 , pp. 60-64
    • Hennessey, P.J.1    Black, C.T.2    Andrassy, R.J.3
  • 134
    • 0027332915 scopus 로고
    • Glycation increases the vascular clearance rate of IgG in mice
    • Kennedy DM, Skillen AW, Self CH. Glycation increases the vascular clearance rate of IgG in mice. Clin Exp Immunol 1993; 94: 447-451.
    • (1993) Clin Exp Immunol , vol.94 , pp. 447-451
    • Kennedy, D.M.1    Skillen, A.W.2    Self, C.H.3
  • 135
  • 136
    • 13644281454 scopus 로고
    • Pathogenesis of diabetic microangiopathy: An overview
    • Barnett AH. Pathogenesis of diabetic microangiopathy: an overview. Am J Med 1991; 90 (Supl 6A): 67-73.
    • (1991) Am J Med , vol.90 , Issue.SUPPL. 6A , pp. 67-73
    • Barnett, A.H.1
  • 137
    • 0026814383 scopus 로고
    • Advanced glycosylation end products (AGE) and diabetic nephropathy
    • Brouhard BH. Advanced glycosylation end products (AGE) and diabetic nephropathy. Diabet Care 1992; 15: 302-303.
    • (1992) Diabet Care , vol.15 , pp. 302-303
    • Brouhard, B.H.1
  • 138
    • 0026034080 scopus 로고
    • Diabetic Nephropathy: Can the natural history be modified?
    • Narins RG. Diabetic Nephropathy: can the natural history be modified? Am J Med 1991; 21 (Supl 2A): 70-75.
    • (1991) Am J Med , vol.21 , Issue.SUPPL. 2A , pp. 70-75
    • Narins, R.G.1
  • 139
    • 0027169317 scopus 로고
    • Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy
    • Beisswenger PJ, Moore LL, Brinck Johnsen T, Curphey TJ. Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy. J Clin Invest 1993; 92: 212-217.
    • (1993) J Clin Invest , vol.92 , pp. 212-217
    • Beisswenger, P.J.1    Moore, L.L.2    Brinck Johnsen, T.3    Curphey, T.J.4
  • 140
    • 0026042328 scopus 로고
    • Human and rat mesangial cell receptors for glucose-modified proteins: Potential role in kidney tissue remodelling and diabetic nephropathy
    • Skolnick EY, Yang Z, Makita Z, Radoff S, Kirstein M, Vlassara H. Human and rat mesangial cell receptors for glucose-modified proteins: potential role in kidney tissue remodelling and diabetic nephropathy. J Exp Med 1991; 174: 931-939.
    • (1991) J Exp Med , vol.174 , pp. 931-939
    • Skolnick, E.Y.1    Yang, Z.2    Makita, Z.3    Radoff, S.4    Kirstein, M.5    Vlassara, H.6
  • 141
    • 0025852573 scopus 로고
    • Effects of nonenzymatic glycosylation of mesangial matrix on proliferation of mesangial cells
    • Crowley ST, Brownlee M, Edelstein D, Satriano JA, Morit T, Singhal PC et al. Effects of nonenzymatic glycosylation of mesangial matrix on proliferation of mesangial cells. Diabetes 1991; 40: 540-547.
    • (1991) Diabetes , vol.40 , pp. 540-547
    • Crowley, S.T.1    Brownlee, M.2    Edelstein, D.3    Satriano, J.A.4    Morit, T.5    Singhal, P.C.6
  • 142
    • 0027258770 scopus 로고
    • Cellular mechanisms of lipid injury in the glomerulus
    • Schlondorff D. Cellular mechanisms of lipid injury in the glomerulus. Am J Kidney Dis 1993; 22: 72-82.
    • (1993) Am J Kidney Dis , vol.22 , pp. 72-82
    • Schlondorff, D.1
  • 143
    • 0027438533 scopus 로고
    • Effects of glycated albumin on mesangial cells: Evidence for a role in diabetic nephropathy
    • Ziyadeh EN, Cohen MP. Effects of glycated albumin on mesangial cells: evidence for a role in diabetic nephropathy. Mol Cell Biochem 1993; 125: 19-25.
    • (1993) Mol Cell Biochem , vol.125 , pp. 19-25
    • Ziyadeh, E.N.1    Cohen, M.P.2
  • 144
    • 0027196250 scopus 로고
    • Renal tubular basement membrane and collagen type IV in diabetes mellitus
    • Ziyadeh FN. Renal tubular basement membrane and collagen type IV in diabetes mellitus. Kidney Int 1993; 43: 114-120.
    • (1993) Kidney Int , vol.43 , pp. 114-120
    • Ziyadeh, F.N.1
  • 145
    • 0028057677 scopus 로고
    • Amadori glucose adducts modulate mesangial cell growth and collagen gene expression
    • Cohen MP, Ziyadeh FN. Amadori glucose adducts modulate mesangial cell growth and collagen gene expression. Kidney Int 1994; 45: 475-487.
    • (1994) Kidney Int , vol.45 , pp. 475-487
    • Cohen, M.P.1    Ziyadeh, F.N.2
  • 146
    • 0027203240 scopus 로고
    • Nonenzymatic advanced glycation in the lens membranes
    • Liang JN. Nonenzymatic advanced glycation in the lens membranes. Exp Eye Res 1993; 57: 45-49.
    • (1993) Exp Eye Res , vol.57 , pp. 45-49
    • Liang, J.N.1
  • 147
    • 0026534769 scopus 로고
    • Glycation of human lens proteins: Preferential glycation of alpha a subunits
    • Swamy MS, Abraham A, Abraham EC. Glycation of human lens proteins: preferential glycation of alpha A subunits. Exp Eye Res 1992; 54: 337-345.
    • (1992) Exp Eye Res , vol.54 , pp. 337-345
    • Swamy, M.S.1    Abraham, A.2    Abraham, E.C.3
  • 148
    • 0026451590 scopus 로고
    • Glycation and insolubility of human lens protein
    • Kamei A. Glycation and insolubility of human lens protein. Chem Pharm Bull Tokyo 1992; 40: 2.787-2.791.
    • (1992) Chem Pharm Bull Tokyo , vol.40 , pp. 2787-2791
    • Kamei, A.1
  • 149
    • 0026539828 scopus 로고
    • Glycation of cristallins in lenses from aging and diabetic individuals
    • Van Boekel MA, Hoenders HJ. Glycation of cristallins in lenses from aging and diabetic individuals. FEBS Lett 1992; 314: 1-4.
    • (1992) FEBS Lett , vol.314 , pp. 1-4
    • Van Boekel, M.A.1    Hoenders, H.J.2
  • 150
    • 0026484264 scopus 로고
    • Glycation of lens membrane intrinsic proteins
    • Swamy MS, Abraham EC. Glycation of lens membrane intrinsic proteins. Curr Eye Res 1992; 11: 833-842.
    • (1992) Curr Eye Res , vol.11 , pp. 833-842
    • Swamy, M.S.1    Abraham, E.C.2
  • 151
    • 0024406557 scopus 로고
    • Nonenzymatic glycosilation (glycation) of lens crystallins in diabetes and aging
    • Abraham EC, Swamy MS, Perry RE: Nonenzymatic glycosilation (glycation) of lens crystallins in diabetes and aging. Prog Clin Biol Res 1989; 304: 123-139.
    • (1989) Prog Clin Biol Res , vol.304 , pp. 123-139
    • Abraham, E.C.1    Swamy, M.S.2    Perry, R.E.3
  • 152
    • 0027400290 scopus 로고
    • Glycation mediated lens cyrstallin aggregation and cross-linking by various sugars and sugar phosphates in vitro
    • Swamy MS, Tsai C, Abraham A, Abraham EC. Glycation mediated lens cyrstallin aggregation and cross-linking by various sugars and sugar phosphates in vitro. Exp Eye Res 1993; 56: 177-185.
    • (1993) Exp Eye Res , vol.56 , pp. 177-185
    • Swamy, M.S.1    Tsai, C.2    Abraham, A.3    Abraham, E.C.4
  • 153
    • 0027428896 scopus 로고
    • The effect of diabetes and dietary ascorbate supplementation on the oxidative modification of rat lens beta L crystallin
    • Jones RH, Hothersall JS. The effect of diabetes and dietary ascorbate supplementation on the oxidative modification of rat lens beta L crystallin. Biochem Med Metab Biol 1993; 50: 197-209.
    • (1993) Biochem Med Metab Biol , vol.50 , pp. 197-209
    • Jones, R.H.1    Hothersall, J.S.2
  • 154
    • 0026529770 scopus 로고
    • Prevention of cataract in diabetic rats by aspirin, paracetamol (acetaminophen) and ibuprofen
    • Blakytny R, Harding JJ. Prevention of cataract in diabetic rats by aspirin, paracetamol (acetaminophen) and ibuprofen. Exp Eye Res 1992; 54: 509-518.
    • (1992) Exp Eye Res , vol.54 , pp. 509-518
    • Blakytny, R.1    Harding, J.J.2
  • 155
    • 0025174842 scopus 로고
    • End-stage renal disease and diabetes catalyze the formation of a pentose-derived cross-link from aging human collagen
    • Sell DR, Monnier VM. End-stage renal disease and diabetes catalyze the formation of a pentose-derived cross-link from aging human collagen. J Clin Invest 1990; 85: 380-384.
    • (1990) J Clin Invest , vol.85 , pp. 380-384
    • Sell, D.R.1    Monnier, V.M.2
  • 156
    • 0027451507 scopus 로고
    • Differential effects of type 2 (non-insulin-dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane
    • Sell DR, Carlson EC, Monnier VM. Differential effects of type 2 (non-insulin-dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane. Diabetologia 1993; 36: 936-941.
    • (1993) Diabetologia , vol.36 , pp. 936-941
    • Sell, D.R.1    Carlson, E.C.2    Monnier, V.M.3
  • 157
    • 0024340373 scopus 로고
    • Cutaneous manifestations of diabetes mellitus
    • Huntley AC. Cutaneous manifestations of diabetes mellitus. Dermatol Clin 1989; 7: 531-546.
    • (1989) Dermatol Clin , vol.7 , pp. 531-546
    • Huntley, A.C.1
  • 158
    • 0025997576 scopus 로고
    • Effect of non-enzymatic glycosylation and heating on browning of human stratum corneun and nail
    • Sueki H, Nozaki S, Numuzawa S, Aoki K, Kiroiwa Y, Fujisawa R. Effect of non-enzymatic glycosylation and heating on browning of human stratum corneun and nail. Dermatologica 1991; 183: 197-202.
    • (1991) Dermatologica , vol.183 , pp. 197-202
    • Sueki, H.1    Nozaki, S.2    Numuzawa, S.3    Aoki, K.4    Kiroiwa, Y.5    Fujisawa, R.6
  • 160
    • 0025871181 scopus 로고
    • The in vivo and in vitro inhibition of protein glycosylation and diabetic vascular basement membrane thickening by pyridoxal-5′-phosphate
    • Hayakawa M, Shibata M. The in vivo and in vitro inhibition of protein glycosylation and diabetic vascular basement membrane thickening by pyridoxal-5′-phosphate. J Nutr Sci Vitaminol Tokyo 1991; 37: 149-159.
    • (1991) J Nutr Sci Vitaminol Tokyo , vol.37 , pp. 149-159
    • Hayakawa, M.1    Shibata, M.2
  • 162
    • 0026482622 scopus 로고
    • Lipoate prevents glucose-induced protein modifications
    • Suzuki YJ, Tsuchiya M, Packer L. Lipoate prevents glucose-induced protein modifications. Free Radic Res Commun 1992; 17: 211-217.
    • (1992) Free Radic Res Commun , vol.17 , pp. 211-217
    • Suzuki, Y.J.1    Tsuchiya, M.2    Packer, L.3
  • 163
    • 0026759447 scopus 로고
    • Captopril inhibits the fluorescence development associated with glycation of proteins
    • Le Guen CA, Bain S, Barnett AH, Lunec J. Captopril inhibits the fluorescence development associated with glycation of proteins. Agents Actions 1992; 36: 264-270.
    • (1992) Agents Actions , vol.36 , pp. 264-270
    • Le Guen, C.A.1    Bain, S.2    Barnett, A.H.3    Lunec, J.4
  • 164
    • 0026025718 scopus 로고
    • Vitamin e reduction of protein glycosylation in diabetes. New prospect for prevention of diabetic complications?
    • Ceriello A, Giugliano D, Quatraro A, Donzella C, Dipalo G, Lefebvre PJ. Vitamin E reduction of protein glycosylation in diabetes. New prospect for prevention of diabetic complications? Diabet Care 1991; 14: 68-72.
    • (1991) Diabet Care , vol.14 , pp. 68-72
    • Ceriello, A.1    Giugliano, D.2    Quatraro, A.3    Donzella, C.4    Dipalo, G.5    Lefebvre, P.J.6
  • 165
    • 0026562860 scopus 로고
    • New insights on non-enzymatic glycosylation may lead to therapeutic approches for the prevention of diabetic complications
    • Ceriello A, Quatraro A, Giugliano D. New insights on non-enzymatic glycosylation may lead to therapeutic approches for the prevention of diabetic complications. Diabet Med 1992; 9: 297-299.
    • (1992) Diabet Med , vol.9 , pp. 297-299
    • Ceriello, A.1    Quatraro, A.2    Giugliano, D.3
  • 166
    • 0026513031 scopus 로고
    • Effect of vitamin C on glycoslation of proteins
    • Davie SJ, Gould BJ, Yudkin JS. Effect of vitamin C on glycoslation of proteins. Diabetes 1992; 41: 167-173.
    • (1992) Diabetes , vol.41 , pp. 167-173
    • Davie, S.J.1    Gould, B.J.2    Yudkin, J.S.3
  • 167
    • 0023204254 scopus 로고
    • In vitro inhibition of nonenzymic glycosylation induced by aspirin
    • Sensi M, Bruno MR, Pozzilli P. In vitro inhibition of nonenzymic glycosylation induced by aspirin. Med Sci Res 1987; 15: 99-100.
    • (1987) Med Sci Res , vol.15 , pp. 99-100
    • Sensi, M.1    Bruno, M.R.2    Pozzilli, P.3
  • 168
    • 0026073393 scopus 로고
    • Effect of alpha-glucosidase inhibition on the nonenzymatic glycation of glomerular basement membrane
    • Cohen MP, Klepser H, Wu VY. Effect of alpha-glucosidase inhibition on the nonenzymatic glycation of glomerular basement membrane. Gen Pharmacol 1991; 22: 515-519.
    • (1991) Gen Pharmacol , vol.22 , pp. 515-519
    • Cohen, M.P.1    Klepser, H.2    Wu, V.Y.3
  • 169
    • 0027169182 scopus 로고
    • Dlysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats
    • Sensi M, De Rossi MG, Celi FS, Cristina A, Rosati C, Perrett D et al. Dlysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats. Diabetologia 1993; 36: 797-801.
    • (1993) Diabetologia , vol.36 , pp. 797-801
    • Sensi, M.1    De Rossi, M.G.2    Celi, F.S.3    Cristina, A.4    Rosati, C.5    Perrett, D.6
  • 170
    • 0026575313 scopus 로고
    • Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine
    • Edelstein D, Brownlee M. Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes 1992; 41: 26-29.
    • (1992) Diabetes , vol.41 , pp. 26-29
    • Edelstein, D.1    Brownlee, M.2
  • 171
    • 0027179586 scopus 로고
    • Glycosylated hemoglobin concentrations and vitamin E, vitamin C, and beta-carotene intake in diabetic and nondiabetic older adults
    • Shoff SM, Mares-Perlman JA, Cruickshanks KJ, Klein R, Klein BE, Ritter LL. Glycosylated hemoglobin concentrations and vitamin E, vitamin C, and beta-carotene intake in diabetic and nondiabetic older adults. Am J Clin Nutr 1993; 58: 412-416.
    • (1993) Am J Clin Nutr , vol.58 , pp. 412-416
    • Shoff, S.M.1    Mares-Perlman, J.A.2    Cruickshanks, K.J.3    Klein, R.4    Klein, B.E.5    Ritter, L.L.6
  • 172
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of accelerated diabetic retinopathy
    • Hammes HP, Martin S, Federlin K, Gersen K, Brownlee M. Aminoguanidine treatment inhibits the development of accelerated diabetic retinopathy. Proc Natl Acad Sci 1991; 88: 11.555-11.558.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 11555-11558
    • Hammes, H.P.1    Martin, S.2    Federlin, K.3    Gersen, K.4    Brownlee, M.5
  • 173
    • 0028107538 scopus 로고
    • Aminoguanidine inhibits the development of accelerated diabetic retinopathy in the spontaneous hypertensive rat
    • Hammes HP, Brownle M, Edelstein D, Saleck M, Martin S, Federlin K. Aminoguanidine inhibits the development of accelerated diabetic retinopathy in the spontaneous hypertensive rat. Diabetologia 1994; 37: 32-35.
    • (1994) Diabetologia , vol.37 , pp. 32-35
    • Hammes, H.P.1    Brownle, M.2    Edelstein, D.3    Saleck, M.4    Martin, S.5    Federlin, K.6
  • 174
    • 0026571089 scopus 로고
    • Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats
    • Vagishashi S, Kamijo M, Baba M, Yagihashi N, Nagai K. Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats. Diabetes 1992; 41: 47-52.
    • (1992) Diabetes , vol.41 , pp. 47-52
    • Vagishashi, S.1    Kamijo, M.2    Baba, M.3    Yagihashi, N.4    Nagai, K.5
  • 175
    • 0026728117 scopus 로고
    • Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotoin-diabetic rats
    • Cameron NE, Cotter MA, Dines K, Love A. Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotoin-diabetic rats. Diabetologia 1992; 35: 946-950.
    • (1992) Diabetologia , vol.35 , pp. 946-950
    • Cameron, N.E.1    Cotter, M.A.2    Dines, K.3    Love, A.4
  • 176
    • 0027273039 scopus 로고
    • Potential therapeutic approaches to the treatment or prevention of diabetic neuropathy: Evidence form experimental studies
    • Cameron NE, Cotter MA. Potential therapeutic approaches to the treatment or prevention of diabetic neuropathy: evidence form experimental studies. Diabet Med 1993; 10: 593-605.
    • (1993) Diabet Med , vol.10 , pp. 593-605
    • Cameron, N.E.1    Cotter, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.