The recently discovered HspB8-Bag3 complex participates in protein quality control through a mechanism that requires the activation of the eIF2alpha signaling pathway and that leads to protein synthesis inhibition and autophagy stimulation. Both processes help to protect the cells against the accumulation of aggregate-prone proteins, which may be relevant in many protein-conformational neurodegenerative disorders. Besides, this activity of HspB8-Bag3 may have important implications during viral infection
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The mammalian family of small heat shock proteins (sHSP/HSPB) consists of ten members (HSPB1-HSPB10)...
The recently discovered HspB8-Bag3 complex participates in protein quality control through a mechani...
The recently discovered HspB8-Bag3 complex participates in protein quality control through a mechani...
Aggregation of mutated proteins is a hallmark of many neurodegenerative disorders, including Hunting...
Aggregation of mutated proteins is a hallmark of many neurodegenerative disorders, including Hunting...
Proper protein folding is crucial for protein stability and function; when folding fails, due to str...
Eukaryotic cells use autophagy and the ubiquitin\u2013proteasome system as their major protein degra...
Proper protein folding is crucial for protein stability and function; when folding fails, due to str...
Protein quality control involves molecular chaperones that recognize misfolded proteins thereby prev...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
During cell life, proteins often misfold, depending on particular mutations or environmental changes...
AIMS:HSPB8 is a small heat shock protein that forms a complex with the co-chaperone BAG3. Overexpres...
Mutations in HspB8, a member of the B group of heat shock proteins (Hsp), have been associated with ...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The mammalian family of small heat shock proteins (sHSP/HSPB) consists of ten members (HSPB1-HSPB10)...
The recently discovered HspB8-Bag3 complex participates in protein quality control through a mechani...
The recently discovered HspB8-Bag3 complex participates in protein quality control through a mechani...
Aggregation of mutated proteins is a hallmark of many neurodegenerative disorders, including Hunting...
Aggregation of mutated proteins is a hallmark of many neurodegenerative disorders, including Hunting...
Proper protein folding is crucial for protein stability and function; when folding fails, due to str...
Eukaryotic cells use autophagy and the ubiquitin\u2013proteasome system as their major protein degra...
Proper protein folding is crucial for protein stability and function; when folding fails, due to str...
Protein quality control involves molecular chaperones that recognize misfolded proteins thereby prev...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
During cell life, proteins often misfold, depending on particular mutations or environmental changes...
AIMS:HSPB8 is a small heat shock protein that forms a complex with the co-chaperone BAG3. Overexpres...
Mutations in HspB8, a member of the B group of heat shock proteins (Hsp), have been associated with ...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The accumulation of misfolded, mutant proteins is a common basis for many adult onset neurodegenerat...
The mammalian family of small heat shock proteins (sHSP/HSPB) consists of ten members (HSPB1-HSPB10)...