Source of funding :\u00a0<\/strong>National Council of Scientific Research in Higher Education \u2013 CNCSIS, UEFSCDI.<\/p>\n Project Code: <\/strong>PN-II-RU-TE-2011-3-0038.<\/p>\n Number of contract :<\/strong> 112 \/ 31.10.2011<\/p>\n Project title :\u00a0<\/strong>New Mass-Spectrometric-based Approaches to Elucidation of Oxidative Modifications in Proteins<\/p>\n Scientific context and motivation. The nitration of tyrosine residues in protein represents an important post-translational modification during development, oxidative stress, and biological aging; however it is difficult to be detected specifically. Nitration is a covalent modification in proteins resulting from the addition of a nitro group onto one of the two equivalent aromatic carbons adjacent to the hydroxyl group of a tyrosine residue. This modification leads to changes in protein structure and function. Only a selective number of proteins are modified by nitration in vivo, and the selectivity may be influenced by a combination of several factors such as (1), the proteins are in close proximity to the site of generation of nitrating agents; (2), the chemical selectivity of the nitrating reagent; (3), the relative abundance of the target proteins; (4), the proteins contain tyrosine residues in a specific primary sequence or in a specific environment and (5), the repair of nitrated proteins by a putative enzyme called denitrase [1].<\/p>\n Read more<\/a><\/p>\n <\/p>\n The scientific objectives of the proposed project comprised two major parts:<\/p>\n I. Affinity-mass spectrometric based approaches to the identification of tyrosine nitration in sputum samples of patients and purified proteins.<\/p>\n Since the identification of nitration sites in cellular proteins have been identified only in a few cases, and structural details have not been characterised in the literature, the application of the new developed affinity-mass spectrometry will provide important results which can be used further in claryfing and understanding the molecular basis of pathophysiological biochemistry. New nitrated target proteins and new nitration sites will be identified and their specific and selective properties will be evaluated.<\/p>\n Read more<\/a><\/p>\n <\/p>\n Noi abordari mass-spectrometrice pentru elucidarea modificarilor oxidative \u00een protein\u201d<\/b><\/i><\/p>\n \u00cen concordan\u0163\u0103 cu obiectivele proiectului stabilite ini\u0163ial o mare majoritate a acestora au fost realizate pana in prezent.<\/p>\n In prima etapa a proiectului <\/i>(Etapa I)<\/strong> s-a realizat perioada de documentare \u0219i pregatire a literaturii pentru a fi pus\u0103 la dispozi\u0163ia studen\u0163ilor ce au fost coopta\u0163i \u00een echip\u0103. Am preg\u0103tit materiale de studiu ale unor technici relativ nou introduse \u00een laboratoarele biochimice si cele de chimie analitic\u0103, pe care le folosim \u00een cadrul proiectului.<\/p>\n Aceste technici analitice constituie baza unei strategii de cercetare numit\u0103 proteomica. Proteomica reprezint<\/span>\u0103 un domeniu nou de cercetare folosit cu succes \u00een identificarea proteinelor din probe complexe, <\/span>determin\u00e2nd structura, modificarile lor post-translationale cat si relatiile dintre proteine si liganzi. Proteomica folose\u015fte tehnologii ce pot analiza cu succes sute de proteine \u00eentr-un singur experiment. <\/span><\/p>\n Read more<\/a><\/p>\n <\/p>\n Dissemination of results<\/b><\/p>\n Publications in which the financial support of the project was acknowledged:<\/b><\/i><\/p>\n Research \u00a0articles:<\/em><\/strong><\/p>\n Book chapters:<\/em><\/strong><\/p>\nProject description<\/h1>\n
Objectives<\/h1>\n
Scientific reports<\/h1>\n
Dissemination of results<\/h1>\n
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