133125-17-4Relevant articles and documents
Synthesis of desmosine-containing cyclic peptide for the possible elucidation of elastin crosslinking structure
Ogawa, Keita,Hayashi, Takahiro,Lin, Yong Y.,Usuki, Toyonobu
, p. 3838 - 3847 (2017)
Elastin is a vital extracellular matrix protein, which is known for providing elasticity in numerous tissues. It is formed by the self-assembly and subsequent crosslinking of elastin precursor, tropoelastin. Two tetrafunctional, pyridinium-based amino acids desmosine and isodesmosine are exclusively found in elastin and play an important role as crosslinkers. Structural elucidation of elastin has eluded scientists to date, owing to the highly cross-linked structure and insoluble nature. Therefore, in this study, we aimed to synthesize a desmosine-containing cyclic peptide as a partial elastin mimic, in order to eventually facilitate the elucidation of the crosslinking pattern of elastin by mass spectrometric analysis.
The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism
Dreyfus, Cyril,Larrouy, Manuel,Cavelier, Florine,Martinez, Jean,Pignol, David,Arnoux, Pascal
supporting information; experimental part, p. 5825 - 5827 (2011/06/23)
We determined the three-dimensional structure of a complex between an archaeal nicotianamine synthase homologue and a chemically synthesised reaction intermediate. This structure suggests that the enzymes cavity allows both an ordered substrate binding an
PYRIMIDINE DERIVATIVES USEFUL AS DHFR INHIBITORS
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Page/Page column 24; 26, (2010/11/29)
Compounds of formula (I) or (II) are dihydrofolatereductase inhibitors, useful for the treatment of, for example, cell proliferative diseases: wherein A and D are independently -CHR6- or -NR6; E and G are independently =CR6/sub