A Revised Picture of the Cu(II)?α-Synuclein Complex: The Role of N?Terminal Acetylation

Gina M. Moriarty; Conceic?a?o A. S. A. Minetti; David P. Remeta; Jean Baum

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A Revised Picture of the Cu(II)?α-Synuclein Complex: The Role of N?Terminal Acetylation

机译：Cu（II）？α-突触核蛋白复合物的修订图片：N？末端乙酰化的作用

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α-Synuclein (αS) is an amyloidogenic intrinsically disordered protein implicated in Parkinson’s disease, for which copper-mediated pathways of neurodegeneration have been suggested. We have employed nuclear magnetic resonance, circular dichroism, electrospray ionization mass spectrometry, and thioflavin T fluorescence to characterize interactions of Cu~(2+) with the physiological acetylated form (Ac-αS). Significantly, Nterminal acetylation abolishes Cu~(2+) binding at the highaffinity M1-D2 site present in the nonacetylated protein and maintains Cu~(2+) interactions around H50/D121. Fibrillation enhancement observed at an equimolar Cu~(2+) stoichiometry with the nonacetylated model does not occur with Ac-αS. These findings open new avenues of investigation into Cu~(2+)-mediated neurodegenerative pathology suggested in vivo.

机译：α-突触核蛋白（αS）是一种与淀粉样蛋白有关的内在失调蛋白，与帕金森氏病有关，已经提出了铜介导的神经变性途径。我们已经利用核磁共振，圆二色性，电喷雾电离质谱和硫黄素T荧光来表征Cu〜（2+）与生理乙酰化形式（Ac-αS）的相互作用。明显地，N末端乙酰化消除了非乙酰化蛋白质中存在的高亲和力M1-D2位点处的Cu〜（2+）结合，并维持了H50 / D121周围的Cu〜（2+）相互作用。 Ac-αS不会在等摩尔的Cu〜（2+）化学计量比下以非乙酰化模型观察到的原纤化增强。这些发现为体内暗示的Cu〜（2+）介导的神经退行性病变研究开辟了新途径。

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《Biochemistry》 |2014年第17期|共3页
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Gina M. Moriarty; Conceic?a?o A. S. A. Minetti; David P. Remeta; Jean Baum;
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Revised; Cu(II)?α-Synuclein Complex; N?Terminal Acetylation;

机译：修订版;Cu（II）？α-突触核蛋白复合物;N？末端乙酰化;

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1. A Revised Picture of the Cu(II)?α-Synuclein Complex: The Role of N?Terminal Acetylation [J] . Gina M. Moriarty, Conceic?a?o A. S. A. Minetti, David P. Remeta, Biochemistry . 2014,第17期

机译：Cu（II）？α-突触核蛋白复合物的修订图片：N？末端乙酰化的作用
2. Copper(II) melonates Cu _3[C _6N _7(NCN) _3] _2·8H _2O and [Cu(C _2H _8N _2) _2] _3[C _6N _7(NCN) _3] _2·4H _2O- using the terminal cyano group of the[C _6N _7(NCN) _3] ~(3-) ion for complexation [J] . Clauss C., Schmidt H., Schwarzer A., Zeitschrift fur Anorganische und Allgemeine Chemie . 2011,第14a15期

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3. A new heterobinuclear (FeCuII)-Cu-III complex with a single terminal Fe-III-O(phenolate) bond. Relevance to purple acid phosphatases and nucleases [J] . Lanznaster M, Neves A, Bortoluzzi AJ, Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry . 2005,第4期

机译：具有单末端Fe-III-O（酚盐）键的新型异双核（FeCuII）-Cu-III配合物。与紫色酸性磷酸酶和核酸酶的相关性
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机译：Cu屏障CMP期间FA / O II络合剂和钻头对凹陷和腐蚀减少的作用
5. Investigation into the Role of N-Terminal Acetylation of ESAT-6 in Pathogenesis of Mycobacterium Tuberculosis [D] . Aguilera, Javier A. 2017

机译：ESAT-6 N末端乙酰化在结核分枝杆菌发病机理中的作用研究
6. Complex of EGCG with Cu(II) Suppresses Amyloid Aggregation and Cu(II)-Induced Cytotoxicity of α-Synuclein [O] . Yilong Teng, Juan Zhao, Lulu Ding, 2019

机译：EGCG与铜（II）的复合物抑制淀粉样蛋白聚集和铜（II）诱导的α-突触核蛋白的细胞毒性。
7. Role of Parkinson’s Disease-Linked Mutations and N-Terminal Acetylation on the Oligomerization of α-Synuclein Induced by 3,4-Dihydroxyphenylacetaldehyde [O] . Vanderlei de Araújo Lima, Lucas Alex do Nascimento, David Eliezer, 2018

机译：帕金森病脉动突变和N-末端乙酰化对3,4-二羟基苯基乙醛诱导的α-突触核蛋白的寡聚化的作用

A Revised Picture of the Cu(II)?α-Synuclein Complex: The Role of N?Terminal Acetylation

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