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pro vyhledávání: '"Rodgers KJ"'
β-N-methylamino L-alanine (BMAA) is a neurotoxin linked to high incidences of neurodegenerative disease. The toxin, along with two of its common isomers, 2,4-diaminobuytric acid (2,4-DAB) and N-(2-aminoethyl)glycine (AEG), is produced by multiple ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______363::e3c35fa4aacf0790b6f07127e77a7477
https://hdl.handle.net/10453/164151
https://hdl.handle.net/10453/164151
In the original publication, there was a mistake in Table 2 as published [...].
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https://explore.openaire.eu/search/publication?articleId=od_______363::7f142b018947d79c1585eff9b20a5f93
https://hdl.handle.net/10453/160404
https://hdl.handle.net/10453/160404
Proteinopathies are diseases caused by factors that affect proteoform conformation. As such, a prevalent hypothesis is that the misincorporation of noncanonical amino acids into a proteoform results in detrimental structures. However, this hypothesis
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https://explore.openaire.eu/search/publication?articleId=od_______363::f6a0c0c63ba61878e68c50be19b26e2e
https://hdl.handle.net/10453/146553
https://hdl.handle.net/10453/146553
© 2018 The emerging toxin β-methylamino-L-alanine (BMAA) has been linked to the development of a number of neurodegenerative diseases in humans including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and Parkinson's disease. BMAA has be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______363::40e4b22b6002e58e389046ecc5626481
https://hdl.handle.net/10453/128585
https://hdl.handle.net/10453/128585
BACKGROUND AND AIMS: Apolipoprotein (apo) A-IV, the third most abundant HDL-associated protein, is atheroprotective and shares similar properties as apoA-I. We have reported previously that apoA-I, the most abundant apolipoprotein in HDL, inhibits pl
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https://explore.openaire.eu/search/publication?articleId=od_______363::8c91d18285bec9545f44ddbd8a1f33d3
https://hdl.handle.net/10453/154401
https://hdl.handle.net/10453/154401
© 2015 Published by Elsevier Ltd. β-methylamino-l-alanine (BMAA), a non-protein amino acid synthesised by cyanobacteria, has been linked to a complex neurological disorder on Guam and more recently to other cases of sporadic ALS (sALS), however the
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https://explore.openaire.eu/search/publication?articleId=od_______363::f15abf1cf383317f548548f3b9f20d7a
https://hdl.handle.net/10453/40966
https://hdl.handle.net/10453/40966
Levodopa (l-dopa), a close structural analogue of the protein amino acid l-tyrosine, can substitute for l-tyrosine in protein synthesis and be mistakenly incorporated into newly synthesised proteins in vitro. We show that l- dopa-containing proteins
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https://explore.openaire.eu/search/publication?articleId=od_______363::e3555d4647751a0cca2dbfcee3db5c3b
https://hdl.handle.net/10453/18612
https://hdl.handle.net/10453/18612
Proteins are major biological targets for oxidative damage within cells because of their high abundance and rapid rates of reaction with radicals and singlet oxygen. These reactions generate high yields of hydroperoxides. The turnover of both native
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https://explore.openaire.eu/search/publication?articleId=od_______363::46b2d4cc2f58e6e7299f3a0fc67b7148
https://hdl.handle.net/10453/14645
https://hdl.handle.net/10453/14645
Hyperglycaemia, triose phosphate decomposition and oxidation reactions generate reactive aldehydes in vivo. These compounds react non-enzymatically with protein side chains and N-terminal amino groups to give adducts and cross-links, and hence modifi
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https://explore.openaire.eu/search/publication?articleId=od_______363::e5d6f04a8be7ce072067a10172866334
https://hdl.handle.net/10453/14810
https://hdl.handle.net/10453/14810
Autor:
Rodgers, KJ, Watkins, DJ, Miller, AL, Chan, PY, Karanam, S, Brissette, WH, Long, CJ, Jackson, CL
Objective - Lysosomal proteinases have been implicated in a number of pathologies associated with extracellular matrix breakdown. Therefore, we investigated the possibility that the lysosomal proteinase cathepsin S may be involved in atherosclerotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______363::b82ff003f979f4a20d4cf99d8b5a49c1
https://hdl.handle.net/10453/16872
https://hdl.handle.net/10453/16872