메뉴 건너뛰기




Volumn 10, Issue , 2009, Pages

Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells

Author keywords

[No Author keywords available]

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; 4 [5 (4 METHYL 1 PIPERAZINYL)[2,5' BI 1H BENZIMIDAZOL] 2' YL]PHENOL; BOVINE SERUM ALBUMIN; FRUCTOSE; GLUCOSE; LACTATE DEHYDROGENASE; LIPOCORTIN 5; NITROBLUE TETRAZOLIUM; PROPIDIUM IODIDE; REACTIVE OXYGEN METABOLITE; RIBOSE; XYLOSE; ADVANCED GLYCATION END PRODUCT;

EID: 63249093042     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-10-10     Document Type: Article
Times cited : (187)

References (64)
  • 1
    • 0018395653 scopus 로고
    • Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum
    • 762083
    • Day JF Thorpe SR Baynes JW Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum J Biol Chem 1979, 254(3):595-597 762083
    • (1979) J Biol Chem , vol.254 , Issue.3 , pp. 595-597
    • Day, J.F.1    Thorpe, S.R.2    Baynes, J.W.3
  • 2
    • 0032980115 scopus 로고    scopus 로고
    • The Clinical Significance of Glycation
    • J TP The Clinical Significance of Glycation Clin Lab 1999, 45:263-273
    • (1999) Clin Lab , vol.45 , pp. 263-273
    • J, T.P.1
  • 4
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • 443307 8514859 10.1172/JCI116482
    • McCance DR Dyer DG Dunn JA Bailie KE Thorpe SR Baynes JW Lyons TJ Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus J Clin Invest 1993, 91(6):2470-2478 443307 8514859 10.1172/JCI116482
    • (1993) J Clin Invest , vol.91 , Issue.6 , 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    Lyons, T.J.7
  • 5
    • 0025892834 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • 10.2337/diabetes.40.8.1010 1907246
    • Lyons TJ Silvestri G Dunn JA Dyer DG Baynes JW Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts Diabetes 1991, 40(8):1010-1015 10.2337/diabetes.40.8.1010 1907246
    • (1991) Diabetes , vol.40 , Issue.8 , pp. 1010-1015
    • Lyons, T.J.1    Silvestri, G.2    Dunn, J.A.3    Dyer, D.G.4    Baynes, J.W.5
  • 6
    • 0032910949 scopus 로고    scopus 로고
    • Alterations in nonenzymatic biochemistry in uremia: Origin and significance of "carbonyl stress" in long-term uremic complications
    • 10.1046/j.1523-1755.1999.00302.x 9987064
    • Miyata T van Ypersele de Strihou C Kurokawa K Baynes JW Alterations in nonenzymatic biochemistry in uremia: Origin and significance of "carbonyl stress" in long-term uremic complications Kidney Int 1999, 55(2):389-399 10.1046/j.1523-1755.1999.00302.x 9987064
    • (1999) Kidney Int , vol.55 , Issue.2 , pp. 389-399
    • Miyata, T.1    van Ypersele de Strihou, C.2    Kurokawa, K.3    Baynes, J.W.4
  • 7
    • 0029165873 scopus 로고
    • Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins
    • 10.1007/BF01886793 8590604
    • Westwood ME Thornalley PJ Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins J Protein Chem 1995, 14(5):359-372 10.1007/BF01886793 8590604
    • (1995) J Protein Chem , vol.14 , Issue.5 , pp. 359-372
    • Westwood, M.E.1    Thornalley, P.J.2
  • 8
    • 0034887436 scopus 로고    scopus 로고
    • AGES in brain ageing: AGE-inhibitors as neuroprotective and anti-dementia drugs?
    • 10.1023/A:1010052800347 11708614
    • Dukic-Stefanovic S Schinzel R Riederer P Munch G AGES in brain ageing: AGE-inhibitors as neuroprotective and anti-dementia drugs? Biogerontology 2001, 2(1):19-34 10.1023/A:1010052800347 11708614
    • (2001) Biogerontology , vol.2 , Issue.1 , pp. 19-34
    • Dukic-Stefanovic, S.1    Schinzel, R.2    Riederer, P.3    Munch, G.4
  • 9
    • 33644870582 scopus 로고    scopus 로고
    • Degradation of glycated bovine serum albumin in microglial cells
    • 10.1016/j.freeradbiomed.2005.10.061 16540397
    • Stolzing A Widmer R Jung T Voss P Grune T Degradation of glycated bovine serum albumin in microglial cells Free Radic Biol Med 2006, 40(6):1017-1027 10.1016/j.freeradbiomed.2005.10.061 16540397
    • (2006) Free Radic Biol Med , vol.40 , Issue.6 , pp. 1017-1027
    • Stolzing, A.1    Widmer, R.2    Jung, T.3    Voss, P.4    Grune, T.5
  • 11
    • 0034609951 scopus 로고    scopus 로고
    • Kinetin inhibits protein oxidation and glycoxidation in vitro
    • 10.1006/bbrc.2000.3616 11027621
    • Verbeke P Siboska GE Clark BF Rattan SI Kinetin inhibits protein oxidation and glycoxidation in vitro Biochem Biophys Res Commun 2000, 276(3):1265-1270 10.1006/bbrc.2000.3616 11027621
    • (2000) Biochem Biophys Res Commun , vol.276 , Issue.3 , pp. 1265-1270
    • Verbeke, P.1    Siboska, G.E.2    Clark, B.F.3    Rattan, S.I.4
  • 12
    • 0028324241 scopus 로고
    • Glycation of albumin: Reaction with glucose, fructose, galactose, ribose or glyceraldehyde measured using four methods
    • 10.1016/0165-022X(94)90025-6 8040561
    • Syrovy I Glycation of albumin: Reaction with glucose, fructose, galactose, ribose or glyceraldehyde measured using four methods J Biochem Biophys Methods 1994, 28(2):115-121 10.1016/0165-022X(94)90025-6 8040561
    • (1994) J Biochem Biophys Methods , vol.28 , Issue.2 , pp. 115-121
    • Syrovy, I.1
  • 13
    • 0029995384 scopus 로고    scopus 로고
    • Kinetics of nonenzymatic glycation of ribonuclease A leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-Amadori studies
    • 10.1021/bi9525942 8664253
    • Khalifah RG Todd P Booth AA Yang SX Mott JD Hudson BG Kinetics of nonenzymatic glycation of ribonuclease A leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-Amadori studies Biochemistry 1996, 35(15):4645-4654 10.1021/bi9525942 8664253
    • (1996) Biochemistry , vol.35 , Issue.15 , pp. 4645-4654
    • Khalifah, R.G.1    Todd, P.2    Booth, A.A.3    Yang, S.X.4    Mott, J.D.5    Hudson, B.G.6
  • 14
    • 0023705750 scopus 로고
    • Glycation induces expansion of the molecular packing of collagen
    • 10.1016/0022-2836(88)90015-0 3143838
    • Tanaka S Avigad G Brodsky B Eikenberry EF Glycation induces expansion of the molecular packing of collagen J Mol Biol 1988, 203(2):495-505 10.1016/0022-2836(88)90015-0 3143838
    • (1988) J Mol Biol , vol.203 , Issue.2 , pp. 495-505
    • Tanaka, S.1    Avigad, G.2    Brodsky, B.3    Eikenberry, E.F.4
  • 15
    • 38049144209 scopus 로고    scopus 로고
    • Glycated fetal calf serum affects the viability of an insulin-secreting cell line in vitro
    • 10.1016/j.metabol.2007.08.020 18191044
    • Luciano Viviani G Puddu A Sacchi G Garuti A Storace D Durante A Monacelli F Odetti P Glycated fetal calf serum affects the viability of an insulin-secreting cell line in vitro Metabolism 2008, 57(2):163-169 10.1016/j.metabol.2007.08.020 18191044
    • (2008) Metabolism , vol.57 , Issue.2 , pp. 163-169
    • Luciano Viviani, G.1    Puddu, A.2    Sacchi, G.3    Garuti, A.4    Storace, D.5    Durante, A.6    Monacelli, F.7    Odetti, P.8
  • 17
    • 40949155274 scopus 로고    scopus 로고
    • Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: Inhibition by pyridoxamine
    • 10.1016/j.freeradbiomed.2007.09.016 18374270
    • Chetyrkin SV Mathis ME Ham AJ Hachey DL Hudson BG Voziyan PA Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: Inhibition by pyridoxamine Free Radic Biol Med 2008, 44(7):1276-1285 10.1016/j.freeradbiomed.2007.09.016 18374270
    • (2008) Free Radic Biol Med , vol.44 , Issue.7 , pp. 1276-1285
    • Chetyrkin, S.V.1    Mathis, M.E.2    Ham, A.J.3    Hachey, D.L.4    Hudson, B.G.5    Voziyan, P.A.6
  • 18
    • 0141643308 scopus 로고    scopus 로고
    • Paradoxical impact of antioxidants on post-Amadori glycoxidation: Counterintuitive increase in the yields of pentosidine and Nepsilon-carboxymethyllysine using a novel multifunctional pyridoxamine derivative
    • 10.1074/jbc.M305099200 12878609
    • Culbertson SM Vassilenko EI Morrison LD Ingold KU Paradoxical impact of antioxidants on post-Amadori glycoxidation: Counterintuitive increase in the yields of pentosidine and Nepsilon-carboxymethyllysine using a novel multifunctional pyridoxamine derivative J Biol Chem 2003, 278(40):38384-38394 10.1074/jbc.M305099200 12878609
    • (2003) J Biol Chem , vol.278 , Issue.40 , pp. 38384-38394
    • Culbertson, S.M.1    Vassilenko, E.I.2    Morrison, L.D.3    Ingold, K.U.4
  • 20
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • 10.1007/s00109-003-0464-5 12942175
    • Stefani M Dobson CM Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution J Mol Med 2003, 81(11):678-699 10.1007/s00109-003-0464-5 12942175
    • (2003) J Mol Med , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 21
    • 43649097136 scopus 로고    scopus 로고
    • Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology
    • 18374666
    • Sanghera N Wall M Venien-Bryan C Pinheiro TJ Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology Biochim Biophys Acta 2008 1784, 6:873-881 18374666
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 873-881
    • Sanghera, N.1    Wall, M.2    Venien-Bryan, C.3    Pinheiro, T.J.4
  • 22
    • 27844432224 scopus 로고    scopus 로고
    • Protein aggregation, metals and oxidative stress in neurodegenerative diseases
    • 16246050
    • Tabner BJ El-Agnaf OM German MJ Fullwood NJ Allsop D Protein aggregation, metals and oxidative stress in neurodegenerative diseases Biochem Soc Trans 2005, 33(Pt 5):1082-1086 16246050
    • (2005) Biochem Soc Trans , vol.33 , Issue.PART 5 , pp. 1082-1086
    • Tabner, B.J.1    El-Agnaf, O.M.2    German, M.J.3    Fullwood, N.J.4    Allsop, D.5
  • 24
    • 0031001305 scopus 로고    scopus 로고
    • Glucose modification of human serum albumin: A structural study
    • 10.1016/S0891-5849(96)00557-6 9098096
    • Coussons PJ Jacoby J McKay A Kelly SM Price NC Hunt JV Glucose modification of human serum albumin: A structural study Free Radic Biol Med 1997, 22(7):1217-1227 10.1016/S0891-5849(96)00557-6 9098096
    • (1997) Free Radic Biol Med , vol.22 , Issue.7 , pp. 1217-1227
    • Coussons, P.J.1    Jacoby, J.2    McKay, A.3    Kelly, S.M.4    Price, N.C.5    Hunt, J.V.6
  • 25
    • 28444462161 scopus 로고    scopus 로고
    • The effect of non-enzymatic glycation on the unfolding of human serum albumin
    • 10.1016/j.abb.2005.10.019 16309624
    • Mendez DL Jensen RA McElroy LA Pena JM Esquerra RM The effect of non-enzymatic glycation on the unfolding of human serum albumin Arch Biochem Biophys 2005, 444(2):92-99 10.1016/j.abb.2005.10.019 16309624
    • (2005) Arch Biochem Biophys , vol.444 , Issue.2 , pp. 92-99
    • Mendez, D.L.1    Jensen, R.A.2    McElroy, L.A.3    Pena, J.M.4    Esquerra, R.M.5
  • 26
    • 4544312032 scopus 로고    scopus 로고
    • Lasting blood-brain barrier disruption induces epileptic focus in the rat somatosensory cortex
    • 10.1523/JNEUROSCI.1751-04.2004 15356194
    • Seiffert E Dreier JP Ivens S Bechmann I Tomkins O Heinemann U Friedman A Lasting blood-brain barrier disruption induces epileptic focus in the rat somatosensory cortex J Neurosci 2004, 24(36):7829-7836 10.1523/ JNEUROSCI.1751-04.2004 15356194
    • (2004) J Neurosci , vol.24 , Issue.36 , pp. 7829-7836
    • Seiffert, E.1    Dreier, J.P.2    Ivens, S.3    Bechmann, I.4    Tomkins, O.5    Heinemann, U.6    Friedman, A.7
  • 27
    • 33846623307 scopus 로고    scopus 로고
    • TGF-beta receptor-mediated albumin uptake into astrocytes is involved in neocortical epileptogenesis
    • 10.1093/brain/awl317 17121744
    • Ivens S Kaufer D Flores LP Bechmann I Zumsteg D Tomkins O Seiffert E Heinemann U Friedman A TGF-beta receptor-mediated albumin uptake into astrocytes is involved in neocortical epileptogenesis Brain 2007, 130(Pt 2):535-547 10.1093/brain/awl317 17121744
    • (2007) Brain , vol.130 , Issue.PART 2 , pp. 535-547
    • Ivens, S.1    Kaufer, D.2    Flores, L.P.3    Bechmann, I.4    Zumsteg, D.5    Tomkins, O.6    Seiffert, E.7    Heinemann, U.8    Friedman, A.9
  • 28
    • 0000774327 scopus 로고    scopus 로고
    • Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction
    • 10.1021/jf9605005
    • Moreaux V Birlouez-Aragon I Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction J Agric Food Chem 1997, 45:1905-1910 10.1021/jf9605005
    • (1997) J Agric Food Chem , vol.45 , pp. 1905-1910
    • Moreaux, V.1    Birlouez-Aragon, I.2
  • 29
    • 21644438624 scopus 로고    scopus 로고
    • Fluorescence, browning index, and color in infant formulas during storage
    • 10.1021/jf0403585 15941335
    • Ferrer E Alegria A Farre R Clemente G Calvo C Fluorescence, browning index, and color in infant formulas during storage J Agric Food Chem 2005, 53(12):4911-4917 10.1021/jf0403585 15941335
    • (2005) J Agric Food Chem , vol.53 , Issue.12 , pp. 4911-4917
    • Ferrer, E.1    Alegria, A.2    Farre, R.3    Clemente, G.4    Calvo, C.5
  • 30
    • 25844445919 scopus 로고    scopus 로고
    • A critical evaluation of fluorescence as a potential marker for the Maillard reaction
    • 10.1016/j.foodchem.2005.01.027
    • Matiacevich SB Buera MP A critical evaluation of fluorescence as a potential marker for the Maillard reaction Food Chem 2006, 95:423-430 10.1016/j.foodchem.2005.01.027
    • (2006) Food Chem , vol.95 , pp. 423-430
    • Matiacevich, S.B.1    Buera, M.P.2
  • 31
    • 35748980603 scopus 로고    scopus 로고
    • Application of fluorescence spectroscopy for monitoring changes in nonfat dry milk during storage
    • 17183072
    • Liu X Metzger LE Application of fluorescence spectroscopy for monitoring changes in nonfat dry milk during storage J Dairy Sci 2007, 90(1):24-37 17183072
    • (2007) J Dairy Sci , vol.90 , Issue.1 , pp. 24-37
    • Liu, X.1    Metzger, L.E.2
  • 32
    • 0029665694 scopus 로고    scopus 로고
    • N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
    • 10.1021/bi9530550 8672512
    • Ikeda K Higashi T Sano H Jinnouchi Y Yoshida M Araki T Ueda S Horiuchi S N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction Biochemistry 1996, 35(24):8075-8083 10.1021/bi9530550 8672512
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 8075-8083
    • Ikeda, K.1    Higashi, T.2    Sano, H.3    Jinnouchi, Y.4    Yoshida, M.5    Araki, T.6    Ueda, S.7    Horiuchi, S.8
  • 34
    • 0034306109 scopus 로고    scopus 로고
    • Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase
    • 1221354 10998366 10.1042/0264-6021:3510233
    • Chen YH He RQ Liu Y Xue ZG Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase Biochem J 2000, 351(Pt 1):233-240 1221354 10998366 10.1042/ 0264-6021:3510233
    • (2000) Biochem J , vol.351 , Issue.PART 1 , pp. 233-240
    • Chen, Y.H.1    He, R.Q.2    Liu, Y.3    Xue, Z.G.4
  • 35
    • 0028807743 scopus 로고
    • Inactivation and conformation changes of the glycated and non-glycated D-glyceraldehyde-3-phosphate dehydrogenase during guanidine-HCl denaturation
    • 7492598
    • He RQ Li YG Wu XQ Li L Inactivation and conformation changes of the glycated and non-glycated D-glyceraldehyde-3-phosphate dehydrogenase during guanidine-HCl denaturation Biochim Biophys Acta 1995, 1253(1):47-56 7492598
    • (1995) Biochim Biophys Acta , vol.1253 , Issue.1 , pp. 47-56
    • He, R.Q.1    Li, Y.G.2    Wu, X.Q.3    Li, L.4
  • 36
    • 0024644046 scopus 로고
    • Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding
    • 10.1007/BF01115995 2765662
    • Swamy MJ Surolia A Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding Biosci Rep 1989, 9(2):189-198 10.1007/BF01115995 2765662
    • (1989) Biosci Rep , vol.9 , Issue.2 , pp. 189-198
    • Swamy, M.J.1    Surolia, A.2
  • 37
    • 33845482913 scopus 로고    scopus 로고
    • Characterization of LPS and interferon-gamma triggered activation-induced cell death in N9 and primary microglial cells: Induction of the mitochondrial gateway by nitric oxide
    • 10.1038/sj.cdd.4401989 16778833
    • Mayo L Stein R Characterization of LPS and interferon-gamma triggered activation-induced cell death in N9 and primary microglial cells: induction of the mitochondrial gateway by nitric oxide Cell Death Differ 2007, 14(1):183-186 10.1038/sj.cdd.4401989 16778833
    • (2007) Cell Death Differ , vol.14 , Issue.1 , pp. 183-186
    • Mayo, L.1    Stein, R.2
  • 38
    • 0033950664 scopus 로고    scopus 로고
    • A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1)
    • 10.1016/S0009-8981(99)00246-6 10699430
    • Peskin AV Winterbourn CC A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1) Clin Chim Acta 2000, 293(1-2):157-166 10.1016/S0009-8981(99)00246-6 10699430
    • (2000) Clin Chim Acta , vol.293 , Issue.1-2 , pp. 157-166
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 39
    • 20444476724 scopus 로고    scopus 로고
    • Time window characteristics of cultured rat hippocampal neurons subjected to ischemia and reperfusion
    • 15896277
    • Xu Z Xu RX Liu BS Jiang XD Huang T Ding LS Yuan J Time window characteristics of cultured rat hippocampal neurons subjected to ischemia and reperfusion Chin J Traumatol 2005, 8(3):179-182 15896277
    • (2005) Chin J Traumatol , vol.8 , Issue.3 , pp. 179-182
    • Xu, Z.1    Xu, R.X.2    Liu, B.S.3    Jiang, X.D.4    Huang, T.5    Ding, L.S.6    Yuan, J.7
  • 41
    • 0035830924 scopus 로고    scopus 로고
    • Early glycation products produce pentosidine cross-links on native proteins. novel mechanism of pentosidine formation and propagation of glycation
    • 10.1074/jbc.M008626200 11076948
    • Chellan P Nagaraj RH Early glycation products produce pentosidine cross-links on native proteins. novel mechanism of pentosidine formation and propagation of glycation J Biol Chem 2001, 276(6):3895-3903 10.1074/ jbc.M008626200 11076948
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 3895-3903
    • Chellan, P.1    Nagaraj, R.H.2
  • 42
    • 0031054249 scopus 로고    scopus 로고
    • In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways
    • 10.1074/jbc.272.9.5430 9038143
    • Booth AA Khalifah RG Todd P Hudson BG In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways J Biol Chem 1997, 272(9):5430-5437 10.1074/jbc.272.9.5430 9038143
    • (1997) J Biol Chem , vol.272 , Issue.9 , pp. 5430-5437
    • Booth, A.A.1    Khalifah, R.G.2    Todd, P.3    Hudson, B.G.4
  • 43
    • 34948889385 scopus 로고    scopus 로고
    • Carbohydrates and Glycobiology
    • New York: Worth Publishers Elizabeth G
    • Nelson DL Cox MM Carbohydrates and Glycobiology Principle of Biochemistry New York: Worth Publishers Elizabeth G 2004 296-326
    • (2004) Principle of Biochemistry , pp. 296-326
    • Nelson, D.L.1    Cox, M.M.2
  • 44
    • 48649103658 scopus 로고    scopus 로고
    • A procedure for the rapid screening of Maillard reaction inhibitors
    • 10.1016/j.jprot.2007.10.002 18096239
    • Fatima S Jairajpuri DS Saleemuddin M A procedure for the rapid screening of Maillard reaction inhibitors J Biochem Biophys Methods 2008, 70(6):958-965 10.1016/j.jprot.2007.10.002 18096239
    • (2008) J Biochem Biophys Methods , vol.70 , Issue.6 , pp. 958-965
    • Fatima, S.1    Jairajpuri, D.S.2    Saleemuddin, M.3
  • 45
    • 0025773632 scopus 로고
    • Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure
    • 2019568
    • Horiuchi S Araki N Morino Y Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure J Biol Chem 1991, 266(12):7329-7332 2019568
    • (1991) J Biol Chem , vol.266 , Issue.12 , pp. 7329-7332
    • Horiuchi, S.1    Araki, N.2    Morino, Y.3
  • 46
    • 53049097848 scopus 로고    scopus 로고
    • Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins
    • 10.1016/j.jphotobiol.2008.06.011 18700180
    • Chakraborty A Basak S Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins J Photochem Photobiol B 2008, 93(1):36-43 10.1016/j.jphotobiol.2008.06.011 18700180
    • (2008) J Photochem Photobiol B , vol.93 , Issue.1 , pp. 36-43
    • Chakraborty, A.1    Basak, S.2
  • 47
    • 33846839522 scopus 로고    scopus 로고
    • Characterisation of salmon calcitonin in spray-dried powder for inhalation. Effect of chitosan
    • 10.1016/j.ijpharm.2006.10.030 17126507
    • Yang M Velaga S Yamamoto H Takeuchi H Kawashima Y Hovgaard L Weert van de M Frokjaer S Characterisation of salmon calcitonin in spray-dried powder for inhalation. Effect of chitosan Int J Pharm 2007, 331(2):176-181 10.1016/j.ijpharm.2006.10.030 17126507
    • (2007) Int J Pharm , vol.331 , Issue.2 , pp. 176-181
    • Yang, M.1    Velaga, S.2    Yamamoto, H.3    Takeuchi, H.4    Kawashima, Y.5    Hovgaard, L.6    Weert, M.7    Frokjaer, S.8
  • 48
    • 0141543878 scopus 로고    scopus 로고
    • A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114
    • 10.1046/j.1471-4159.2003.01949.x 12950445
    • Crystal AS Giasson BI Crowe A Kung MP Zhuang ZP Trojanowski JQ Lee VM A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114 J Neurochem 2003, 86(6):1359-1368 10.1046/ j.1471-4159.2003.01949.x 12950445
    • (2003) J Neurochem , vol.86 , Issue.6 , pp. 1359-1368
    • Crystal, A.S.1    Giasson, B.I.2    Crowe, A.3    Kung, M.P.4    Zhuang, Z.P.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 49
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine kappa-casein: Reduction and conversion to fibrillar (amyloid) structures
    • 10.1023/A:1025020503769 12962326
    • Farrell HM Jr Cooke PH Wickham ED Piotrowski EG Hoagland PD Environmental influences on bovine kappa-casein: Reduction and conversion to fibrillar (amyloid) structures J Protein Chem 2003, 22(3):259-273 10.1023/A:1025020503769 12962326
    • (2003) J Protein Chem , vol.22 , Issue.3 , pp. 259-273
    • Farrell Jr., H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.G.4    Hoagland, P.D.5
  • 50
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
    • 126058 12065404 10.1093/emboj/cdf303
    • Bousset L Thomson NH Radford SE Melki R The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro EMBO J 2002, 21(12):2903-2911 126058 12065404 10.1093/emboj/ cdf303
    • (2002) EMBO J , vol.21 , Issue.12 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 51
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    • 10.1016/j.jmb.2005.06.043 16024042
    • Plakoutsi G Bemporad F Calamai M Taddei N Dobson CM Chiti F Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates J Mol Biol 2005, 351(4):910-922 10.1016/j.jmb.2005.06.043 16024042
    • (2005) J Mol Biol , vol.351 , Issue.4 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Calamai, M.3    Taddei, N.4    Dobson, C.M.5    Chiti, F.6
  • 52
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity
    • 10834945
    • Bhatia R Lin H Lal R Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity FASEB J 2000, 14(9):1233-1243 10834945
    • (2000) FASEB J , vol.14 , Issue.9 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 53
    • 39549101751 scopus 로고    scopus 로고
    • Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo
    • 1913207 17637844 10.1371/journal.pone.0000629
    • Nie CL Wei Y Chen X Liu YY Dui W Liu Y Davies MC Tendler SJ He RG Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo PLoS ONE 2007, 2(7):e629 1913207 17637844 10.1371/journal.pone.0000629
    • (2007) PLoS ONE , vol.2 , Issue.7
    • Nie, C.L.1    Wei, Y.2    Chen, X.3    Liu, Y.Y.4    Dui, W.5    Liu, Y.6    Davies, M.C.7    Tendler, S.J.8    He, R.G.9
  • 54
    • 33846994092 scopus 로고    scopus 로고
    • Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells
    • 1790706 17241479 10.1186/1471-2202-8-9
    • Nie CL Wang XS Liu Y Perrett S He RQ Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells BMC Neurosci 2007, 8:9 1790706 17241479 10.1186/1471-2202-8-9
    • (2007) BMC Neurosci , vol.8 , pp. 9
    • Nie, C.L.1    Wang, X.S.2    Liu, Y.3    Perrett, S.4    He, R.Q.5
  • 56
    • 0037036345 scopus 로고    scopus 로고
    • Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells
    • 10.1074/jbc.M202634200 11912219
    • Yamagishi S Inagaki Y Okamoto T Amano S Koga K Takeuchi M Makita Z Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells J Biol Chem 2002, 277(23):20309-20315 10.1074/jbc.M202634200 11912219
    • (2002) J Biol Chem , vol.277 , Issue.23 , pp. 20309-20315
    • Yamagishi, S.1    Inagaki, Y.2    Okamoto, T.3    Amano, S.4    Koga, K.5    Takeuchi, M.6    Makita, Z.7
  • 58
    • 84948354328 scopus 로고
    • A new method for the determination of sugars in cerebrospinal fluid (author's transl)
    • 604418
    • Seuffer R [A new method for the determination of sugars in cerebrospinal fluid (author's transl)] J Clin Chem Clin Biochem 1977, 15(12):663-668 604418
    • (1977) J Clin Chem Clin Biochem , vol.15 , Issue.12 , pp. 663-668
    • Seuffer, R.1
  • 59
    • 33745015720 scopus 로고    scopus 로고
    • Butyrylcholinesterase attenuates amyloid fibril formation in vitro
    • 1482631 16731619 10.1073/pnas.0602922103
    • Diamant S Podoly E Friedler A Ligumsky H Livnah O Soreq H Butyrylcholinesterase attenuates amyloid fibril formation in vitro Proc Natl Acad Sci USA 2006, 103(23):8628-8633 1482631 16731619 10.1073/ pnas.0602922103
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.23 , pp. 8628-8633
    • Diamant, S.1    Podoly, E.2    Friedler, A.3    Ligumsky, H.4    Livnah, O.5    Soreq, H.6
  • 60
    • 0022219133 scopus 로고
    • Use of protein-based standards in automated colorimetric determinations of fructosamine in serum
    • 4028402
    • 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(9):1550-1554 4028402
    • (1985) Clin Chem , vol.31 , Issue.9 , pp. 1550-1554
    • Baker, J.R.1    Metcalf, P.A.2    Johnson, R.N.3    Newman, D.4    Rietz, P.5
  • 61
    • 0030569357 scopus 로고    scopus 로고
    • Beta-amyloid induces apoptosis in human-derived neurotypic SH-SY5Y cells
    • 10.1016/S0006-8993(96)00733-0 8955513
    • Li YP Bushnell AF Lee CM Perlmutter LS Wong SK Beta-amyloid induces apoptosis in human-derived neurotypic SH-SY5Y cells Brain Res 1996, 738(2):196-204 10.1016/S0006-8993(96)00733-0 8955513
    • (1996) Brain Res , vol.738 , Issue.2 , pp. 196-204
    • Li, Y.P.1    Bushnell, A.F.2    Lee, C.M.3    Perlmutter, L.S.4    Wong, S.K.5
  • 62
    • 0025428079 scopus 로고
    • Use of lactate dehydrogenase release to assess changes in culture viability
    • 10.1007/BF00365494 1366664
    • Racher AJLD Griffiths JB Use of lactate dehydrogenase release to assess changes in culture viability Cytotechnology 1990, 3(3):301-307 10.1007/ BF00365494 1366664
    • (1990) Cytotechnology , vol.3 , Issue.3 , pp. 301-307
    • Racher, A.J.L.D.1    Griffiths, J.B.2
  • 63
    • 0026662769 scopus 로고
    • Lactate dehydrogenase (LDH) activity of the cultured eukaryotic cells as marker of the number of dead cells in the medium
    • [corrected] 10.1016/0168-1656(92)90158-6 1368802
    • Legrand C Bour JM Jacob C Capiaumont J Martial A Marc A Wudtke M Kretzmer G Demangel C Duval D et al Lactate dehydrogenase (LDH) activity of the cultured eukaryotic cells as marker of the number of dead cells in the medium [corrected] J Biotechnol 1992, 25(3):231-243 10.1016/ 0168-1656(92)90158-6 1368802
    • (1992) J Biotechnol , vol.25 , Issue.3 , pp. 231-243
    • Legrand, C.1    Bour, J.M.2    Jacob, C.3    Capiaumont, J.4    Martial, A.5    Marc, A.6    Wudtke, M.7    Kretzmer, G.8    Demangel, C.9    Duval, D.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.