Citation: Jr. Requena et Rl. Levine, Thioredoxin converts the Syrian hamster (29-231) recombinant prion proteinto an insoluble form, FREE RAD B, 30(2), 2001, pp. 141-147
Authors:
Requena, JR
Chao, CC
Levine, RL
Stadtman, ER
Citation: Jr. Requena et al., Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins, P NAS US, 98(1), 2001, pp. 69-74
Authors:
Pamplona, R
Portero-Otin, M
Riba, D
Requena, JR
Thorpe, SR
Lopez-Torres, M
Barja, G
Citation: R. Pamplona et al., Low fatty acid unsaturation: A mechanism for lowered lipoperoxidative modification of tissue proteins in mammalian species with long life spans, J GERONT A, 55(6), 2000, pp. B286-B291
Authors:
Pamplona, R
Portero-Otin, M
Ruiz, C
Bellmunt, MJ
Requena, JR
Thorpe, SR
Baynes, JW
Romero, M
Lopez-Torres, M
Barja, G
Citation: R. Pamplona et al., Thyroid status modulates glycoxidative and lipoxidative modification of tissue proteins, FREE RAD B, 27(7-8), 1999, pp. 901-910
Authors:
Pamplona, R
Portero-Otin, M
Requena, JR
Thorpe, SR
Herrero, A
Barja, G
Citation: R. Pamplona et al., A low degree of fatty acid unsaturation leads to lower lipid peroxidation and lipoxidation-derived protein modification in heart mitochondria of the longevous pigeon than in the short-lived rat, MECH AGE D, 106(3), 1999, pp. 283-296
Authors:
Anderson, MM
Requena, JR
Crowley, JR
Thorpe, SR
Heinecke, JW
Citation: Mm. Anderson et al., The myeloperoxidase system of human phagocytes generates N-epsilon-(carboxymethyl)lysine on proteins: a mechanism for producing advances glycation end products at sites of inflammation, J CLIN INV, 104(1), 1999, pp. 103-113
Citation: Jr. Requena et Er. Stadtman, Conversion of lysine to N-epsilon-(carboxymethyl)lysine increases susceptibility of proteins to metal-catalyzed oxidation, BIOC BIOP R, 264(1), 1999, pp. 207-211
Authors:
Fountain, WC
Requena, JR
Jenkins, AJ
Lyons, TJ
Smyth, B
Baynes, JW
Thorpe, SR
Citation: Wc. Fountain et al., Quantification of N-(glucitol)ethanolamine and N-(carboxymethyl)serine: Two products of nonenzymatic modification of aminophospholipids formed in vivo, ANALYT BIOC, 272(1), 1999, pp. 48-55