1-8 of 8
Keywords: Aggregation
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Journal Articles
J Cell Sci (2011) 124 (11): 1891–1902.
Published: 1 June 2011
... insoluble aggregates. In some cases, protein aggregation leads to the development of human neurodegenerative maladies, including Alzheimer's and prion diseases. Aggregates of misfolded prion protein (PrP), which appear in cells after exposure to the drug cyclosporin A (CsA), and disease-linked PrP mutants...
Includes: Supplementary data
Journal Articles
J Cell Sci (2009) 122 (18): 3262–3271.
Published: 15 September 2009
... of these proteins containing the expanded polyQ tract are thought to initiate aggregation and represent the toxic species. Although it is not clear how these toxic fragments are generated, in vitro data suggest that proteasomes are unable to digest polyQ tracts. To examine whether the resulting polyQ peptides could...
Includes: Supplementary data
Journal Articles
Journal Articles
J Cell Sci (2004) 117 (24): 5887–5895.
Published: 15 November 2004
... that PSGL-1 binds to the C-terminal (G3 domain) of the extracellular proteoglycan PG-M/versican. Cells transfected with PSGL-1 or a shorter form containing the binding site, or cells expressing endogenous PSGL-1 aggregate in the presence of versican or G3 product. The aggregation appears to be induced by G3...
Journal Articles
J Cell Sci (2004) 117 (23): 5681–5686.
Published: 1 November 2004
...Takashi Hamazaki; Masahiro Oka; Shinya Yamanaka; Naohiro Terada When embryonic stem cells are allowed to aggregate, the outer layer of the aggregated spheres (referred to as embryoid bodies) differentiates into primitive endoderm. This initial specification of cell lineage facilitates further...
Journal Articles
J Cell Sci (2004) 117 (21): 5133–5143.
Published: 1 October 2004
... to aggregate and these enlarged yolk platelets fill the cytoplasm of cpl-1 mutant embryos. Coincident with this aggregation is loss of fluorescence from a yolk green fluorescent protein (YP170::GFP). This suggests that loss of CPL-1 activity leads to aberrant processing and/or conformational changes in yolk...
Journal Articles
J Cell Sci (2004) 117 (7): 1017–1024.
Published: 1 March 2004
... familial autosomal dominant Parkinson's disease. One explanation for the formation of perikaryal and neuritic aggregates of α-synuclein, which is a presynaptic protein, is that the mutations disrupt α-synuclein transport and lead to its proximal accumulation. We found that mutant forms of α-synuclein...
Journal Articles