Heat Shock Proteins in Neural Cells

Β· Springer Science & Business Media
5.0
αž€αžΆαžšαžœαžΆαž™αžαž˜αŸ’αž›αŸƒ 1
αžŸαŸ€αžœαž—αŸ…β€‹αž’αŸαž‘αž·αž…αžαŸ’αžšαžΌαž“αž·αž…
115
αž‘αŸ†αž–αŸαžš
αž€αžΆαžšαžœαžΆαž™αžαž˜αŸ’αž›αŸƒ αž“αž·αž„αž˜αžαž·αžœαžΆαž™αžαž˜αŸ’αž›αŸƒαž˜αž·αž“αžαŸ’αžšαžΌαžœαž”αžΆαž“αž•αŸ’αž‘αŸ€αž„αž•αŸ’αž‘αžΆαžαŸ‹αž‘αŸ αžŸαŸ’αžœαŸ‚αž„αž™αž›αŸ‹αž”αž“αŸ’αžαŸ‚αž˜

αž’αŸ†αž–αžΈαžŸαŸ€αžœαž—αŸ…β€‹αž’αŸαž‘αž·αž…αžαŸ’αžšαžΌαž“αž·αž€αž“αŸαŸ‡

Eat shock proteins (HSPs), also called stress proteins, are not only induced in response to elevated temperatures, but also as a result of various stress situations, including environmental strains, viral H infection, ischemia, anoxia and oxidative stress. These stress situations trigger cellular defence mechanisms that act as an emergency system capable of combatting the toxic consequences due to the accumulation of misfolded proteins. Heat shock proteins are involved in many physiological processes, including development and differentiation, organisation of the cytoarchi tecture by binding to cytoskeletal elements and regulation of the balance between cell death and survival. Many heat shock proteins work as molecular chaperones. In this role, they contribute to in vivo protein folding and prevent nonproductive interactions with other proteins and cellular c- ponents. In recent years it has been found that the chaperone system and the proteolytic machinery work closely together, and that proteasomal - hibition causes the upregulation of stress proteins. Impairment of the proteasomal machinery and chaperone functions lead to protein damage, which contributes to neurodegenerative disorders and to the aging process.

αž€αžΆαžšαžŠαžΆαž€αŸ‹αž•αŸ’αž€αžΆαž™ αž“αž·αž„αž˜αžαž·αžœαžΆαž™αžαž˜αŸ’αž›αŸƒ

5.0
αž€αžΆαžšαžœαžΆαž™αžαž˜αŸ’αž›αŸƒ 1

αžœαžΆαž™αžαž˜αŸ’αž›αŸƒαžŸαŸ€αžœαž—αŸ…β€‹αž’αŸαž‘αž·αž…αžαŸ’αžšαžΌαž“αž·αž€αž“αŸαŸ‡

αž”αŸ’αžšαžΆαž”αŸ‹αž™αžΎαž„αž’αŸ†αž–αžΈαž€αžΆαžšαž™αž›αŸ‹αžƒαžΎαž‰αžšαž”αžŸαŸ‹αž’αŸ’αž“αž€αŸ”

αž’αžΆαž“β€‹αž–αŸαžαŸŒαž˜αžΆαž“

αž‘αžΌαžšαžŸαž–αŸ’αž‘αž†αŸ’αž›αžΆαžαžœαŸƒ αž“αž·αž„β€‹αžαŸαž”αŸ’αž›αŸαž
αžŠαŸ†αž‘αžΎαž„αž€αž˜αŸ’αž˜αžœαž·αž’αžΈ Google Play Books αžŸαž˜αŸ’αžšαžΆαž”αŸ‹ Android αž“αž·αž„ iPad/iPhone αŸ” αžœαžΆβ€‹αž’αŸ’αžœαžΎαžŸαž˜αž€αžΆαž›αž€αž˜αŸ’αž˜β€‹αžŠαŸ„αž™αžŸαŸ’αžœαŸαž™αž”αŸ’αžšαžœαžαŸ’αžαž·αž‡αžΆαž˜αž½αž™β€‹αž‚αžŽαž“αžΈβ€‹αžšαž”αžŸαŸ‹αž’αŸ’αž“αž€β€‹ αž“αž·αž„β€‹αž’αž“αž»αž‰αŸ’αž‰αžΆαžαž±αŸ’αž™β€‹αž’αŸ’αž“αž€αž’αžΆαž“αž–αŸαž›β€‹αž˜αžΆαž“αž’αŸŠαžΈαž“αž’αžΊαžŽαž·αž αž¬αž‚αŸ’αž˜αžΆαž“β€‹αž’αŸŠαžΈαž“αž’αžΊαžŽαž·αžβ€‹αž“αŸ…αž‚αŸ’αžšαž”αŸ‹αž‘αžΈαž€αž“αŸ’αž›αŸ‚αž„αŸ”
αž€αž»αŸ†αž–αŸ’αž™αžΌαž‘αŸαžšβ€‹αž™αž½αžšαžŠαŸƒ αž“αž·αž„αž€αž»αŸ†αž–αŸ’αž™αžΌαž‘αŸαžš
αž’αŸ’αž“αž€αž’αžΆαž…αžŸαŸ’αžŠαžΆαž”αŸ‹αžŸαŸ€αžœαž—αŸ…αž‡αžΆαžŸαŸ†αž‘αŸαž„αžŠαŸ‚αž›αž”αžΆαž“αž‘αž·αž‰αž“αŸ…αž€αŸ’αž“αž»αž„ Google Play αžŠαŸ„αž™αž”αŸ’αžšαžΎαž€αž˜αŸ’αž˜αžœαž·αž’αžΈαžšαž»αž€αžšαž€αžαžΆαž˜αž’αŸŠαžΈαž“αž’αžΊαžŽαž·αžαž€αŸ’αž“αž»αž„αž€αž»αŸ†αž–αŸ’αž™αžΌαž‘αŸαžšαžšαž”αžŸαŸ‹αž’αŸ’αž“αž€αŸ”
eReaders αž“αž·αž„β€‹αž§αž”αž€αžšαžŽαŸβ€‹αž•αŸ’αžŸαŸαž„β€‹αž‘αŸ€αž
αžŠαžΎαž˜αŸ’αž”αžΈαž’αžΆαž“αž“αŸ…αž›αžΎβ€‹αž§αž”αž€αžšαžŽαŸ e-ink αžŠαžΌαž…αž‡αžΆβ€‹αž§αž”αž€αžšαžŽαŸαž’αžΆαž“β€‹αžŸαŸ€αžœαž—αŸ…αž’αŸαž‘αž·αž…αžαŸ’αžšαžΌαž“αž·αž€ Kobo αž’αŸ’αž“αž€αž“αžΉαž„αžαŸ’αžšαžΌαžœβ€‹αž‘αžΆαž‰αž™αž€β€‹αž―αž€αžŸαžΆαžš αž αžΎαž™β€‹αž•αŸ’αž‘αŸαžšαžœαžΆαž‘αŸ…β€‹αž§αž”αž€αžšαžŽαŸβ€‹αžšαž”αžŸαŸ‹αž’αŸ’αž“αž€αŸ” αžŸαžΌαž˜αž’αž“αž»αžœαžαŸ’αžαžαžΆαž˜β€‹αž€αžΆαžšαžŽαŸ‚αž“αžΆαŸ†αž›αž˜αŸ’αž’αž·αžαžšαž”αžŸαŸ‹αž˜αž‡αŸ’αžˆαž˜αžŽαŸ’αžŒαž›αž‡αŸ†αž“αž½αž™ αžŠαžΎαž˜αŸ’αž”αžΈαž•αŸ’αž‘αŸαžšαž―αž€αžŸαžΆαžšβ€‹αž‘αŸ…αž§αž”αž€αžšαžŽαŸαž’αžΆαž“αžŸαŸ€αžœαž—αŸ…β€‹αž’αŸαž‘αž·αž…αžαŸ’αžšαžΌαž“αž·αž€αžŠαŸ‚αž›αžŸαŸ’αž‚αžΆαž›αŸ‹αŸ”