تقوی, فرشته and حبیبی رضایی, مهران and امانی, مجتبی and صبوری, علی اکبر and موسوی موحدی, علی اکبر (1396) نقش گلیکاسیون در توده ای شدن پروتئین. International journal of biological macromolecules ــ 100 . pp. 67-74. شاپا 8130-0141
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Official URL: http://www.sciencedirect.com/science/journal/01418...
Title
The status of glycation in protein aggregation
English Abstract
Protein crucial function and flexibility directly depend on its whole structure which is determined by the native distribution of structural elements. Any disturbances in a protein architecture leads to many kind of abnormalities and intra- or extracellular accumulation of misfolded proteins which are the basis of conformational diseases. Glycation is one of the most important unwanted post-translational modi- fications (PTM) which modifies protein three dimensional decoration and triggers its abnormalities. In current review, we take a look at the brief history of protein glycation, its mechanism and kinetics, glycation consequences and toxic products and its involvement in protein chemical modification, aggregation amyloids and fibril formation and different mechanisms nduced by such alterations
| Item Type: | Article |
|---|---|
| زبان سند : | انگلیسی |
| نویسنده اول : | فرشته تقوی |
| نویسنده : | مهران حبیبی رضایی |
| نویسنده : | مجتبی امانی |
| نویسنده : | علی اکبر صبوری |
| نویسنده مسئول : | علی اکبر موسوی موحدی |
| Additional Information: | Impact Factor (2015) 3.138 Indexed in: ISI,Pubmed/Medline/Index Medicus, Scopus, Elsevier BIOBASE, Current Contents, EMBASE, FSTA, Polymer Contents, EMBiology, *Review |
| کلیدواژه ها (انگلیسی): | Glycation ,Oxidative stress, Aggregation, Amyloid, Non amyloid |
| Subjects: | QU Biochemistry |
| Divisions: | Faculty of Medicine > Department of Basic Sciences > Department of Biochemistry |
| ID Code: | 8759 |
| Deposited By: | Dr Mojtaba Amani |
| Deposited On: | 02 Mar 1396 09:16 |
| Last Modified: | 02 Mar 1396 09:24 |
Available Versions of this Item
- نقش گلیکاسیون در توده ای شدن پروتئین. (deposited 02 Mar 1396 09:16) [Currently Displayed]
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