Biological Recognition of Advanced End Product of the Maillard Reaction

[1]  V. Monnier,et al.  Aging of proteins: immunological detection of a glucose-derived pyrrole formed during maillard reaction in vivo. , 1989, The Journal of biological chemistry.

[2]  Y. Morino,et al.  Evidence against in vivo presence of 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole, a major fluorescent advanced end product generated by nonenzymatic glycosylation. , 1988, The Journal of biological chemistry.

[3]  Y. Morino,et al.  Endocytic uptake of nonenzymatically glycosylated proteins is mediated by a scavenger receptor for aldehyde-modified proteins. , 1988, The Journal of biological chemistry.

[4]  V. Monnier,et al.  Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole. , 1988, The Journal of biological chemistry.

[5]  Y. Morino,et al.  Receptor-mediated endocytosis of aldehyde-modified proteins by sinusoidal liver cells , 1987 .

[6]  Y Morino,et al.  Scavenger receptor for aldehyde-modified proteins. , 1986, The Journal of biological chemistry.

[7]  A. Cerami,et al.  High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[8]  R. Bucala,et al.  Detection of an advanced glycosylation product bound to protein in situ. , 1985, The Journal of biological chemistry.

[9]  Y Morino,et al.  Purification of a receptor for formaldehyde-treated serum albumin from rat liver. , 1985, The Journal of biological chemistry.

[10]  H. Maeda,et al.  Scavenger function of sinusoidal liver cells. Acetylated low-density lipoprotein is endocytosed via a route distinct from formaldehyde-treated serum albumin. , 1985, The Journal of biological chemistry.

[11]  Y Morino,et al.  Characterization of a membrane-associated receptor from rat sinusoidal liver cells that binds formaldehyde-treated serum albumin. , 1985, The Journal of biological chemistry.

[12]  A. Cerami,et al.  Nonenzymatic glycosylation and the pathogenesis of diabetic complications. , 1984, Annals of internal medicine.

[13]  S. Pongor,et al.  Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[14]  J. Witztum,et al.  Glucosylation of Low-Density Lipoproteins to an Extent Comparable to That Seen in Diabetes Slows Their Catabolism , 1984, Diabetes.

[15]  T. V. van Berkel,et al.  In vivo and in vitro uptake and degradation of acetylated low density lipoprotein by rat liver endothelial, Kupffer, and parenchymal cells. , 1983, The Journal of biological chemistry.

[16]  P. Higgins,et al.  Kinetic analysis of the nonenzymatic glycosylation of hemoglobin. , 1981, The Journal of biological chemistry.

[17]  M. Bitensky,et al.  Micropinocytic ingestion of glycosylated albumin by isolated microvessels: possible role in pathogenesis of diabetic microangiopathy. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[18]  T. Berg,et al.  Uptake and degdradation of formaldehyde-treated 125I-labeled human serum albumin in rat liver cells in vivo and in vitro , 1977 .

[19]  J. L. Mego,et al.  THE UPTAKE AND DEGRADATION OF INJECTED LABELED PROTEINS BY MOUSE-LIVER PARTICLES. , 1965, Biochimica et biophysica acta.

[20]  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.

[21]  M. Brown,et al.  Lipoprotein metabolism in the macrophage: implications for cholesterol deposition in atherosclerosis. , 1983, Annual review of biochemistry.