Site-specific cross-linking of collagen peptides by lysyl advanced glycation endproducts.
暂无分享,去创建一个
[1] Mark Woodward,et al. Oral glycotoxins are a modifiable cause of dementia and the metabolic syndrome in mice and humans , 2014, Proceedings of the National Academy of Sciences.
[2] M. Antonietti,et al. A sustainable route towards imidazolium building blocks based on biomass molecules. , 2013, Chemistry.
[3] G. Cooper,et al. Synthesis of monolysyl advanced glycation endproducts and their incorporation into collagen model peptides. , 2012, Organic letters.
[4] G. Striker,et al. AGE restriction in diabetes mellitus: a paradigm shift , 2011, Nature Reviews Endocrinology.
[5] H. Wennemers,et al. Functionalizable collagen model peptides. , 2010, Journal of the American Chemical Society.
[6] D. Tew,et al. Solid-phase synthesis of homodimeric peptides: preparation of covalently-linked dimers of amyloid beta peptide. , 2009, Chemical communications.
[7] J. Ames. Evidence against dietary advanced glycation endproducts being a risk to human health. , 2007, Molecular nutrition & food research.
[8] M. Linetsky,et al. Convenient synthesis of GOLD and MOLD and identification of their oxidation products in vitro and in vivo , 2007, Amino Acids.
[9] M. Bouxsein,et al. Contribution of the advanced glycation end product pentosidine and of maturation of type I collagen to compressive biomechanical properties of human lumbar vertebrae. , 2006, Bone.
[10] T. Kawakami,et al. Intact glycation end products containing carboxymethyl-lysine and glyoxal lysine dimer obtained from synthetic collagen model peptide. , 2004, Bioorganic & medicinal chemistry letters.
[11] J. Baynes,et al. The role of AGEs in aging: causation or correlation , 2001, Experimental Gerontology.
[12] R. Nagaraj,et al. Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes. , 1999, Archives of biochemistry and biophysics.
[13] J. Baynes,et al. Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia , 1998, FEBS letters.
[14] J. Baynes,et al. Characterization of an Imidazolium Salt Formed from Glyoxal and N.alpha.-Hippuryllysine: A Model for Maillard Reaction Crosslinks in Proteins , 1995 .
[15] A. Cerami,et al. Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. , 1988, The New England journal of medicine.
[16] G. Han,et al. 9-Fluorenylmethoxycarbonyl amino-protecting group , 1972 .
[17] J. Baynes,et al. Characterization of an imidazolium compound formed by reaction of methylglyoxal and N-hippuryllysine , 1995 .
[18] J. Myers,et al. Human proα1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons , 1984, Nature.
[19] F. O. Schmitt,et al. Action of proteolytic enzymes on tropocollagen and insoluble collagen. , 1966, Biochemistry.