Immunomodulation of the human prion peptide 106-126 aggregation

Biochemical and Biophysical Research Communications

Volumn 280, Issue 1, 2001, Pages 115-120

  Hanan, E ^a   Goren, O ^a   Eshkenazy, M ^a   Solomon, B ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

Aggregation; Immunomodulation; Monoclonal antibody; Neurotoxicity; Prion peptide

Indexed keywords

AMYLOID; PRION PROTEIN;

ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; IMMUNOMODULATION; LIGAND BINDING; MOUSE; NEUROTOXICITY; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; RAT;

EID: 0034805840     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.4097     Document Type: Article

References (35)

1. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
2. Conversion of alpha-helices into betasheets features in the formation of the scrapie prion proteins
3. Separation and properties of cellular and scrapie prion proteins
4. Molecular characteristics of a protease-resistant, amyloidogenic, and neurotoxic peptide homologous to residues 106-126 of the prion protein
5. Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro
6. Neurotoxicity of a prion protein fragment
7. Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
8. Antibody binding defines a structure for an epitope that participates in the PrPC→PrPSc conformational change
9. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
10. N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies
11. Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state
12. Temperature-dependent X-ray diffraction as a probe of prote Nature 1989 Oct 5;341(6241): 462-4 in structural dynamics
13. Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase
14. Molecular dynamics simulations in biology
15. Antibody assisted protein refolding
16. Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured carboxypeptidase A
17. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide
18. Disaggregation of Alzheimer beta-amyloid by site-directed mAb
19. Continuous cultures of fused cells secreting antibody of predefined specificity
20. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
21. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
22. Re-examination and farther development of a precise and rapid dye method for measuring cell growth/cell kill
23. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
24. Eight prion strains have PrP(Sc) molecules with different conformations
25. Computer graphics in drug design: Molecular modeling of thyroid hormone-prealbumin interactions
26. Inhibiting transthyretin amyloid fibril formation via protein stabilization
27. Mouse cortical cells lacking cellular PrP survive in culture with aneurotoxic PrP fragment
28. Different requirements for the neurotoxicity of fragments of PrP and β-amyloid
29. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
30. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
31. Structure of the recombinant full-length hamster prion protein PrP(29-231): The N-terminus is highly flexible
32. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
33. NMR solution structure of the human prion protein
34. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform