Advanced glycation end product ligands for the receptor for advanced glycation end products: biochemical characterization and formation kinetics.

[1]  H. Vlassara,et al.  Diabetes and advanced glycation endproducts , 2002, Journal of internal medicine.

[2]  G. Münch,et al.  Protein „AGEing”– cytotoxicity of a glycated protein increases with its degree of AGE-modification , 2001, Zeitschrift für Gerontologie und Geriatrie.

[3]  J. Baynes,et al.  Effect of advanced glycation end products on oxidative stress in endothelial cells in culture: a warning on the use of cells studied in serum-free media , 2001, Diabetologia.

[4]  M. Zeier,et al.  Advanced glycation endproducts (AGEs) as uremic toxins. , 2001, Die Nahrung.

[5]  A. Schmidt,et al.  RAGE: A New Target for the Prevention and Treatment of the Vascular and Inflammatory Complications of Diabetes , 2000, Trends in Endocrinology & Metabolism.

[6]  J. Bijlsma,et al.  Age-related accumulation of Maillard reaction products in human articular cartilage collagen. , 2000, The Biochemical journal.

[7]  K. Otero,et al.  Regulation of endothelial nitric oxide synthase expression by albumin-derived advanced glycosylation end products. , 2000, Circulation research.

[8]  T. Kislinger,et al.  N ε-(Carboxymethyl)Lysine Adducts of Proteins Are Ligands for Receptor for Advanced Glycation End Products That Activate Cell Signaling Pathways and Modulate Gene Expression* , 1999, The Journal of Biological Chemistry.

[9]  M. Neurath,et al.  RAGE Mediates a Novel Proinflammatory Axis A Central Cell Surface Receptor for S100/Calgranulin Polypeptides , 1999, Cell.

[10]  R. Khalifah,et al.  Amadorins: novel post-Amadori inhibitors of advanced glycation reactions. , 1999, Biochemical and biophysical research communications.

[11]  K. Tatsumi,et al.  2‐Isopropylidenehydrazono‐4‐oxo‐thiazolidin‐5‐ylacetanilide (OPB‐9195) treatment inhibits the development of intimal thickening after balloon injury of rat carotid artery: role of glycoxidation and lipoxidation reactions in vascular tissue damage , 1999, FEBS letters.

[12]  Paul J Thornalley.  Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. , 1998, Cellular and molecular biology.

[13]  Douglas R. McDonald,et al.  β-Amyloid Fibrils Activate Parallel Mitogen-Activated Protein Kinase Pathways in Microglia and THP1 Monocytes , 1998, The Journal of Neuroscience.

[14]  P. Guillausseau,et al.  Diabetes, advanced glycation endproducts and vascular disease , 1998, Vascular medicine.

[15]  E. Niki,et al.  Protein-bound acrolein: potential markers for oxidative stress. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[16]  R. Ziegler,et al.  AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept. , 1998, Cardiovascular research.

[17]  M. Fujishima,et al.  Advanced glycosylation end products induced tissue factor expression in human monocyte-like U937 cells and increased tissue factor expression in monocytes from diabetic patients. , 1998, Atherosclerosis.

[18]  V. Ollivier,et al.  Effect of advanced glycation end product-modified albumin on tissue factor expression by monocytes. Role of oxidant stress and protein tyrosine kinase activation. , 1997, Arteriosclerosis, thrombosis, and vascular biology.

[19]  A. Booth,et al.  In Vitro Kinetic Studies of Formation of Antigenic Advanced Glycation End Products (AGEs) , 1997, The Journal of Biological Chemistry.

[20]  J. Wautier,et al.  Advanced glycation end products, oxidant stress and vascular lesions , 1997, European journal of clinical investigation.

[21]  E. Schleicher,et al.  Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging. , 1997, The Journal of clinical investigation.

[22]  R. Bank,et al.  Amino acid analysis by reverse-phase high-performance liquid chromatography: improved derivatization and detection conditions with 9-fluorenylmethyl chloroformate. , 1996, Analytical biochemistry.

[23]  T. Miyata,et al.  The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. , 1996, The Journal of clinical investigation.

[24]  H. Sano,et al.  N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. , 1996, Biochemistry.

[25]  J. Mott,et al.  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. , 1996, Biochemistry.

[26]  J. Chen,et al.  The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin , 1995, The Journal of Biological Chemistry.

[27]  A. Schmidt,et al.  The dark side of glucose , 1995, Nature Medicine.

[28]  J. Baynes,et al.  N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. , 1995, Biochemistry.

[29]  Paul J Thornalley,et al.  Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins , 1995, Journal of protein chemistry.

[30]  F. Numano,et al.  The Effect of Glucose and Advanced Glycosylation End Products on IL‐6 Production by Human Monocytes , 1994, Annals of the New York Academy of Sciences.

[31]  K. Kuwabara,et al.  Receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to circulating AGE proteins. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[32]  Y. Zou,et al.  Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. , 1994, The Journal of biological chemistry.

[33]  Y. Zou,et al.  Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues. , 1993, The American journal of pathology.

[34]  M. Freeman,et al.  The collagenous domains of macrophage scavenger receptors and complement component C1q mediate their similar, but not identical, binding specificities for polyanionic ligands. , 1993, The Journal of biological chemistry.

[35]  K. O. Elliston,et al.  Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. , 1992, The Journal of biological chemistry.

[36]  Z. Makita,et al.  Radioreceptor Assay for Advanced Glycosylation End Products , 1991, Diabetes.

[37]  V. Monnier,et al.  Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. , 1991, The Journal of biological chemistry.

[38]  T. Lyons,et al.  Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)hydroxylysine in human skin collagen. , 1991, Biochemistry.

[39]  K. Manogue,et al.  Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. , 1988, Science.

[40]  V. Monnier,et al.  Accelerated age-related browning of human collagen in diabetes mellitus. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[41]  G. Means,et al.  Nonenzymatic Glycosylation of Proteins: Structure and Function Changes , 1982, Diabetes.

[42]  P. Higgins,et al.  Reaction of monosaccharides with proteins: possible evolutionary significance. , 1981, Science.