Protein Folding and Misfolding, Endoplasmic Reticulum Stress in XXXX : in Trace of Novel Drug Targets.

@entity8095 @entity209 @entity73 @entity179 @entity195 @entity141 @entity2414
UNASSIGNED: @entity195 ( @entity195 ) is characterized by severe @entity73 and @entity2414 . @entity195 is classified both into the "protein conformational" and the "endoplasmic reticulum-mitochondria stress" disorders. @entity195 is a very complex, multifactorial disease of heterogeneous genetic and environmental background. The amyloid hypothesis of @entity195 cannot fully explain the various clinical forms of the disease. Protein folding and misfolding in the endoplasmic reticulum (ER), and accumulation of several misfolded proteins (b-amyloid, Tau, @entity8095 , etc.) in ER and mitochondria (MT) may play a key role in the development of @entity195 . Functional degradation of the synapse and the synapse holding neurites represents the first step in the pathogenesis of @entity179 . MT and ER are tightly coupled both physically and functionally with a special lipid raft called mitochondria-associated ER-membrane (MAM). MAM is crucial for @entity141 signalling and metabolic regulation of the cell. In turn, the impairment of ER-MT interplay is a common mechanism of different @entity179 . In this review, we discuss recent findings focusing on the protein conformational and @entity209 , and the role of MAM and ER-MT crosstalk in @entity179 .
