نتایج جستجو برای: isomerases
تعداد نتایج: 1906 فیلتر نتایج به سال:
نیتریل¬اکسایدها یکی از مهمترین حدواسط¬ها در شیمی آلی هستند. بیشتر نیتریل اکسایدها (rcno) نیمه عمر کوتاهی دارند، فعال بوده و جداسازی آنها به صورت خالص ممکن نیست. ترکیب¬های اولفینی و استیلنی¬ واکنش¬گرهای مفیدی برای به دام انداختن آن¬ها می¬باشند. نیتریل¬اکسایدها حلقه¬زایی ]2+3[ را با اولفین¬ها و استیلنی¬ها انجام می¬دهند که به ترتیب ایزوکسازولین¬ها و ایزوکسازول¬ها به¬دست می¬آیند. در این تحقیق تر...
Diffuse gliomas are the most common type of primary brain and central nervous system (CNS) tumors. Protein disulfide isomerases (PDIs) such as P4HB and PDIA3 act as molecular chaperones for reconstructing misfolded proteins, and are involved in endoplasmic reticulum stress and the unfolded protein response. The present study focused on the role of P4HB and PDIA3 in diffuse gliomas. Analysis of ...
Peptide bond isomerases are involved in important physiological processes that can be targeted in order to treat neurodegenerative disease, cancer, diseases of the immune system, allergies, and many others. The folding helper enzyme class of Peptidyl-Prolyl-cis/trans Isomerases (PPIases) contains the three enzyme families of cyclophilins (Cyps), FK506 binding proteins (FKBPs), and parvulins (Pa...
Prolyl isomerases are divided into three groups, the FKBP family, Cyclophilin and the Parvulin family (Pin1 and Par14). Among these isomerases, Pin1 is a unique prolyl isomerase binding to the motif including pSer/pThr-Pro that is phosphorylated by kinases. Once bound, Pin1 modulates the enzymatic activity, protein stability or subcellular localization of target proteins by changing the cis- an...
Prolyl isomerases are defined by a catalytic domain that facilitates the cis-trans interconversion of proline residues. In most cases, additional domains in these enzymes add important biological function, including recruitment to a set of protein substrates. Here, we report that the N-terminal basic tilted helix bundle (BTHB) domain of the human prolyl isomerase FKBP25 confers specific binding...
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