LEADER 04616nam 22006735 450 001 9910253921003321 005 20200701211746.0 010 $a981-10-3707-8 024 7 $a10.1007/978-981-10-3707-8 035 $a(CKB)3710000001364744 035 $a(DE-He213)978-981-10-3707-8 035 $a(MiAaPQ)EBC4860941 035 $a(PPN)201469979 035 $a(EXLCZ)993710000001364744 100 $a20170516d2017 u| 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aCellular Osmolytes $eFrom Chaperoning Protein Folding to Clinical Perspectives /$fedited by Laishram Rajendrakumar Singh, Tanveer Ali Dar 205 $a1st ed. 2017. 210 1$aSingapore :$cSpringer Singapore :$cImprint: Springer,$d2017. 215 $a1 online resource (VII, 249 p. 36 illus., 16 illus. in color.) 311 $a981-10-3706-X 320 $aIncludes bibliographical references at the end of each chapters. 327 $aPolyols as exceptional Protein stabilizers -- Osmolyte mixtures versus individuals in protein folding and aggregation -- Molecular insights of Osmolyte-protein Interaction -- MDS simulation studies on osmolyte protein interactions -- Osmolytes as protein aggregation Modifiers -- Osmolytes as Nano-probes of conformational changes -- Inhibition of Protein fibrillation by Chemical chaperones: a Therapeutic strategy -- Osmolyte in Infectious Diseases -- Possible strategies for the therapeutic intervention of osmolyte in Cancer -- Antioxidant osmolytes -- Advances on the in vivo studies of the effect of osmolyte on various pathophysiological conditions -- TMAO in alpha Synuclein aggregation -- Osmolytes: from cell physiology to Disease Prevention -- Osmolytes in Cell-volume Regulation -- Role of Osmolytes in counteracting the deleterious effects of denaturant/pressure. 330 $aThis book provides essential insights into improving protein folding/stability, which is a result of the balance between the intra-molecular interactions of protein functional groups and their interactions with the solvent environment. Even a subtle change in the composition of the solvent environment will alter the fidelity of the protein folding process, and hostile environmental stresses represent one of the basic causes of challenges in protein folding or misfolding. Among the strategies employed in a wide range of species and cell types to circumvent the hostile environmental conditions is the elaboration of small organic molecules called osmolytes, and recent advances have revealed that certain specific osmolytes might be key biomarkers of cancer, infectious diseases and are useful in heterologous protein expression and vaccine flocculation. As such a large pool of data has been collected regarding their potential for therapeutic intervention in neurodegenerative diseases and other metabolic disorders caused by protein aggregation or proteiostasis failure. 606 $aBiomedical engineering 606 $aCell physiology 606 $aProteins  606 $aCancer research 606 $aBiochemistry 606 $aPlant biochemistry 606 $aBiomedical Engineering/Biotechnology$3https://scigraph.springernature.com/ontologies/product-market-codes/B24000 606 $aCell Physiology$3https://scigraph.springernature.com/ontologies/product-market-codes/L33010 606 $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060 606 $aCancer Research$3https://scigraph.springernature.com/ontologies/product-market-codes/B11001 606 $aAnimal Biochemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/L14013 606 $aPlant Biochemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/L14021 615 0$aBiomedical engineering. 615 0$aCell physiology. 615 0$aProteins . 615 0$aCancer research. 615 0$aBiochemistry. 615 0$aPlant biochemistry. 615 14$aBiomedical Engineering/Biotechnology. 615 24$aCell Physiology. 615 24$aProtein-Ligand Interactions. 615 24$aCancer Research. 615 24$aAnimal Biochemistry. 615 24$aPlant Biochemistry. 676 $a610.28 702 $aRajendrakumar Singh$b Laishram$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aDar$b Tanveer Ali$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910253921003321 996 $aCellular Osmolytes$92215775 997 $aUNINA