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provides coniferyl ferulate(CAS#:33783-80-1) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Protein aggregation is linked to a growing list of diseases, but it is also an intrinsic property of polypeptides, because the formation of functional globular proteins comes at the expense of an inherent aggregation propensity. Certain proteins can access aggregation-prone states from native-like conformations without the need to cross the energy barrier for unfolding. This is the case of transthyretin (TTR), a homotetrameric protein whose dissociation into its monomers initiates the aggregation cascade. Domains with structural homology to TTR exist in a number of proteins, including the M14B subfamily carboxypeptidases. We show here that the monomeric transthyretin-like domain of human carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the population of folded but aggregation-prone states being controlled by the conformational stability of the domain. We thus confirm that the TTR fold keeps a generic residual aggregation propensity upon folding, resulting from the presence of preformed amyloidogenic β-strands in the native state. These structural elements should serve for functional/structural purposes, because they have not been purged out by evolution, but at the same time they put proteins like carboxypeptidase D at risk of aggregation in biological environments and thus can potentially lead to deposition diseases.
Amyloid, Carboxypeptidase, Protein Aggregation, Protein Misfolding, Protein Stability, Transthyretin
Amyloid Formation by Human Carboxypeptidase D Transthyretin-like Domain under Physiological Conditions*
Javier Garcia-Pardo,‡§,1 Ricardo GraNa-Montes,‡§,2 Marc Fernandez-Mendez,‡§ Angels Ruyra,‡,3 Nerea Roher,‡¶,4 Francesc X. Aviles,‡§ Julia Lorenzo,‡§,5 and Salvador Ventura‡§,6
2014 Dec 5
Rationale: Puberty may influence lung function, but the precise role of pubertal height growth in lung development is unclear.
Objectives: To examine associations of timing of puberty and peak velocity of pubertal height growth with lung function in adolescence and early adulthood.
Methods: Longitudinal analyses of repeat height measurements from age 5 to 20 years for a British birth cohort with 4,772 males and 4,849 females were conducted to characterize height growth trajectories and to derive pubertal age and peak height velocity using the validated SITAR (SuperImposition by Translation and Rotation) model. Association of these estimates with prebronchodilator and post-bronchodilator spirometry measures: FEV1; FVC; FEV1/FVC; FEF25-75% at age 15 and 24 years were investigated using multivariable regression models adjusted for lung function at age 8 years, height and age at time of outcome measurements, and potential confounders.
Measurements and Main Results: Later pubertal age and greater peak velocity were associated with higher FEV1 and FVC at 24 years in both sexes. A 1-year increase in pubertal age was associated with a 263-ml higher FVC (95% confidence interval [CI], 167-360 ml) for males (n = 567) and 100-ml (95% CI, 50-150 ml) higher FVC for females (n = 990). A 1-cm/yr increase in peak velocity was associated with 145-ml (95% CI, 56-234 ml) and 50-ml (95% CI, 2-99 ml) increases in FVC for males and females, respectively. No associations were found with FEV1/FVC.
Conclusions: Later onset and greater peak velocity of height growth in puberty are associated with increased FEV1 and FVC in young adults but there was no evidence of dysanapsis of pubertal lung growth.
Avon Longitudinal Study of Parents and Children, SuperImposition by Translation and Rotation, pubertal age, velocity of pubertal height growth, maximal lung function
Association of Height Growth in Puberty with Lung Function. A Longitudinal Study
Osama Mahmoud,corresponding author1,2 Raquel Granell,1 Kate Tilling,1 Cosetta Minelli,3 Judith Garcia-Aymerich,4,5,6 John W. Holloway,7 Adnan Custovic,8 Deborah Jarvis,3 Jonathan Sterne,1 and John Henderson1
2018 Dec 15
Novel 18β-glycyrrhetinic acid derivatives possessing a carbamate moiety and structurally similar ester derivatives were developed and evaluated for their efficacy as antitumor inhibitors. In the cellular assays, most of the N-substituted carbamate derivatives at the C3-position exhibited potent activities. The results of SAR investigation revealed that the introduction of the morpholine group at the C30-COOH led to a significant loss of the inhibitory potency. Among the ester derivatives, the ester group at C3-position also determined a noticeable reduction in the efficacy. Compound 3j exhibited the most prominent antiproliferative activity against six human cancer cells (A549, HT29, HepG2, MCF-7, PC-3, and Karpas299). Furthermore, compound 3j exerted a moderate inhibiting effect on the ALK. The results of molecular docking analyses suggested that it could bind well to the active site of the receptor ALK, which was consistent with the biological data. These results might inspire further structural optimization of 18β-glycyrrhetinic acid aiming at the development of potent antitumor agents. The structures 4d, 4g, 4h, 4j, and 4n were studied by X-ray crystallographic analyses.
18β-glycyrrhetinic acid, carbamate moiety, antitumor inhibitors
Exploring New Structural Features of the 18β-Glycyrrhetinic Acid Scaffold for the Inhibition of Anaplastic Lymphoma Kinase
Dong Cai,1 ZhiHua Zhang,2 Yu Chen,3 YanYan Zhang,4 YuQi Sun,4,* and YiXia Gong1,*