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Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: an intriguing role for methionine 35.
Aβ(31–35) and Aβ(25–35) fragments of amyloid beta‐protein induce cellular death through apoptotic signals: Role of the redox state of methionine‐35
Functional Modulation by Lactate of Myoglobin
- B. Giardina, P. Ascenzi, M. Clementi, G. de Sanctis, M. Rizzi, M. Coletta
- BiologyThe Journal of Biological Chemistry
- 19 July 1996
The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH and lactate shows a different affinity for the deoxygenated and oxygenated form, behaving as a heterotropic modulator.
Synergistic modulation by chloride and organic phosphates of hemoglobin from bear (Ursus arctos).
DHA protects PC12 cells against oxidative stress and apoptotic signals through the activation of the NFE2L2/HO-1 axis.
- M. Clementi, G. Lazzarino, B. Sampaolese, A. Brancato, G. Tringali
- BiologyInternational journal of molecular medicine
- 1 June 2019
Evidence is provided suggesting that DHA is able to prevent H2O2‑induced oxidative damage to PC12 cells, which is attributed to its antioxidant and anti‑apoptotic effects via the regulation NFE2L2/HO‑1 signaling.
Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1–42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function
Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid β-protein fragment (31–35) on isolated brain mitochondria
Protective effect of rhubarb derivatives on amyloid beta (1–42) peptide-induced apoptosis in IMR-32 cells: A case of nutrigenomic
Functional and structural properties of the hemoglobin components from Italian sturgeon (Acipenser naccarii)
The structural and oxygen binding properties of Acipenser naccarii blood have been investigated and the functional properties seem to be related to the particular physiological needs dictated by the environmental characteristics.
A comparative study of the temperature dependence of the oxygen-binding properties of mammalian hemoglobins.
- M. Coletta, M. Clementi, P. Ascenzi, R. Petruzzelli, S. Condò, B. Giardina
- BiologyEuropean journal of biochemistry
- 1 March 1992
Different from HbA, the intrinsically less exothermic oxygen binding seems to be independent of the experimental conditions for ruminant Hb, underlying specific structural characteristics which might be responsible for this feature.