Modulation of neurodegeneration by molecular chaperones

By P. Muchowski, Jennifer L. Wacker. Nature Reviews Neuroscience, 2005

1,065 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

ER chaperones in mammalian development and human diseases (2007, background): “Alzheimer’s disease are pathologically characterized by the intracellular or extracellular accumulation of misfolded proteins or mutated gene products [51].”
Heat shock proteins (2011, background): “generative disease has been extensively reviewed.(3,10,12-14,26,27) See also table 2.”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “At the same time, off-pathway oligomers and protofibrils have been reported [ 10 ].”
Converging concepts of protein folding in vitro and in vivo (2009, background): “Interestingly, increasing the levels of molecular chaperones, most prominently members of the Hsp70 family, has been shown to inhibit the formation of such oligomers and to prevent the formation of amyloid aggregates for different disease protein”
A network dysfunction perspective on neurodegenerative diseases (2006, background): “Notably, the abnormal proteins that are suspected of causing neurodegenerative disorders impair the integrity or function of presynaptic terminals and postsynaptic specialization”