ライフサイエンスコーパス: aggregate form of

1 tious agent that consists of a misfolded and aggregated form of a sialoglycoprotein called prion prot

2 tes that recognize and sort both soluble and aggregated forms of aberrant or misfolded proteins.

3 Small molecules that bind to aggregated forms of Abeta peptides show promise as poten

4 interest because the accumulation of toxic, aggregated forms of Abeta, from small oligomers to very

5 smin, which degrades both aggregated and non-aggregated forms of Abeta.

6 ue to the interactions of the chaperone with aggregated forms of Abeta42 rather than the monomeric fo

7 Reagents that can interact with specific aggregate forms of alpha-synuclein would be very useful

8 The aggregated form of alpha-syn is well known for its role

9 rons in vivo, although the precise role each aggregated form of alpha-synuclein plays in neurotoxicit

10 aggregation than the cytosolic protein, and aggregated forms of alpha-syn are also secreted from cel

11 Aggregated forms of alpha-synuclein constitute the major

12 Spatz disease, implicating a crucial role of aggregated forms of alpha-synuclein in the pathogenesis.

13 ence of "Lewy body" inclusions enriched with aggregated forms of alpha-synuclein, a presynaptic prote

14 e nuclei for the formation of multimeric and aggregated forms of alpha-synuclein.

15 Soluble oligomeric and aggregated forms of amyloid beta peptides, especially am

16 Microglia are activated by aggregated forms of amyloid-beta protein (Abeta), usuall

17 attributed to the transformation of the non-aggregated form of AuNPs to its aggregated form upon bin

18 owed strong binding to various fragmented or aggregated forms of CII in Western blots, as well as str

19 Properties of the monomeric as well as J-aggregated forms of dithio- and diamino-B-isoindigo were

20 equilibrium ratio of the monomers versus the aggregated forms of Eps15.

21 protected against toxicity resulting from an aggregating form of green fluorescent protein (GFP) in a

22 Here we report the novel finding that aggregated forms of huPrP and Abeta42 are co-purified fr

23 marked by their common pathologic feature of aggregates formed of hyperphosphorylated tau protein, wh

24 sequestration of the poly-ubiquitinated and aggregated form of mutant TDP-43, which correlated with

25 with age-related accumulation of soluble and aggregated forms of N-terminal mutant htt fragments, sug

26 polypeptides, and the physical properties of aggregated forms of polyglutamine in the cell.

27 ficulties in detecting and quantifying small aggregated forms of polyQ, and because all possible stru

28 physico-chemical properties of the different aggregated forms of proteins, and of their interactions

29 Scrapie prion protein is a misfolded and aggregated form of PrP(C) responsible for prion-induced

30 f the yeast prion [PSI+], a self-replicating aggregated form of Sup35p, requires Hsp104.

31 Transgenic nematodes expressing a pro-aggregate form of tau displayed altered mitochondrial co

32 Both soluble and aggregated forms of tau are thought to have neurotoxic p

33 Misfolded and aggregated forms of tau produce pathological structures

34 ressive accumulation of hyperphosphorylated, aggregated forms of tau.

35 ows very high selectivity toward the amyloid-aggregated form of the protein as compared to its native

36 tion of neuritic amyloid plaques composed of aggregated forms of the beta-amyloid peptide (Abeta).

37 eurodegenerative disorders that present with aggregated forms of the cellular prion protein (PrPC), w

38 rate of thermal energy dissipation from the aggregated forms of the complex and, possibly, thermal e

39 pathology that includes the accumulation of aggregated forms of the mutant protein.

40 unusual properties, such as specificity for aggregated forms of the peptide, the ability to distingu

41 residues 101-117 affect the conformation of aggregated forms of the peptides.

42 Misfolded and aggregated forms of the prion protein (PrP(Sc)) have bee

43 important marker of pathologically relevant, aggregated forms of the protein in several important hum

44 Cellular accumulation of aggregated forms of the protein tau is a defining featur

45 At the dispersed phase, the aggregated form of TPE-mercury ions recovers planarity b

46 utations in the sod1 gene, and misfolded and aggregated forms of wild-type SOD1 are found in both spo

47 ence for the hallmarks of amyloid fibrils in aggregated forms of WT and mutant myocilin localized to