کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298941 | 1537049 | 2010 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Nitration of tyrosine 74 prevents human cytochrome c to play a key role in apoptosis signaling by blocking caspase-9 activation
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کلمات کلیدی
DSFreactive nitrogen/oxygen speciesphenylmethanesulphonylfluorideRNOSH2DCFAc-LEHD-AFCRMSFPMSFRMSDDTTHEPESEDC1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride - 1-اتیل-3- (3-دی متیل آمینوپروپیل) کاربیدیدید هیدروکلرایدBSA - BSAbovine serum albumin - آلبومین سرم گاوpost-translational modification - اصلاح post-translationalAlkaline transition - انتقال قلیاییApoptosis - خزان یاختهایMolecular dynamics - دینامیک ملکولی یا پویایی مولکولیdithiothreitol - دیتیوتریتولcircular dichroism - رنگ تابی دورانیRoot Mean Square Fluctuations - ریشه میانگین نوسانات میدانcytochrome c - سیتوکروم سیperoxidase activity - فعالیت پراکسیدازDifferential scanning fluorimetry - فلوریمتری اسکن دیفرانسیلroot mean square deviation - میانگین انحراف مربع ریشهTyrosine nitration - نیتراسیون تیروزین
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Nitration of tyrosine 74 prevents human cytochrome c to play a key role in apoptosis signaling by blocking caspase-9 activation Nitration of tyrosine 74 prevents human cytochrome c to play a key role in apoptosis signaling by blocking caspase-9 activation](/preview/png/8298941.png)
چکیده انگلیسی
Tyrosine nitration is one of the most common post-transcriptional modifications of proteins, so affecting their structure and function. Human cytochrome c, with five tyrosine residues, is an excellent case study as it is a well-known protein playing a double physiological role in different cell compartments. On one hand, it acts as electron carrier within the mitochondrial respiratory electron transport chain, and on the other hand, it serves as a cytoplasmic apoptosis-triggering agent. In a previous paper, we reported the effect of nitration on physicochemical and kinetic features of monotyrosine cytochrome c mutants. Here, we analyse the nitration-induced changes in secondary structure, thermal stability, haem environment, alkaline transition and molecular dynamics of three of such monotyrosine mutants - the so-called h-Y67, h-Y74 and h-Y97 - which have four tyrosines replaced by phenylalanines and just keep the tyrosine residue giving its number to the mutant. The resulting data, along with the functional analyses of the three mutants, indicate that it is the specific nitration of solvent-exposed Tyr74 which enhances the peroxidase activity and blocks the ability of Cc to activate caspase-9, thereby preventing the apoptosis signaling pathway.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 981-993
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 981-993
نویسندگان
José M. GarcÃa-Heredia, Irene DÃaz-Moreno, Pedro M. Nieto, Mar Orzáez, Stella Kocanis, Miguel Teixeira, Enrique Pérez-Payá, Antonio DÃaz-Quintana, Miguel A. De la Rosa,