Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin. [electronic resource]
Producer: 20040126Description: 1456-70 p. digitalISSN:- 0022-3042
- 14-3-3 Proteins
- Animals
- Blotting, Western -- methods
- Calcineurin -- metabolism
- Carbocyanines -- metabolism
- Choline O-Acetyltransferase -- metabolism
- Copper Sulfate -- pharmacology
- Cyclophilin A -- metabolism
- Cysteine -- analogs & derivatives
- Dose-Response Relationship, Drug
- Epitopes -- chemistry
- Humans
- In Vitro Techniques
- Membrane Glycoproteins -- metabolism
- Membrane Proteins -- metabolism
- Mercaptoethanol -- pharmacology
- Nerve Tissue Proteins -- metabolism
- Neurons -- cytology
- Nitrosation -- drug effects
- Oxidation-Reduction -- drug effects
- Peroxynitrous Acid -- pharmacology
- Prions -- chemistry
- Protein Binding
- Pyruvic Acid -- pharmacology
- Qa-SNARE Proteins
- R-SNARE Proteins
- Recombinant Proteins -- metabolism
- S-Nitrosothiols -- metabolism
- Sheep
- Synapsins -- metabolism
- Synaptic Vesicles -- drug effects
- Synaptosomes -- drug effects
- Tacrolimus Binding Proteins -- metabolism
- Thioredoxins -- metabolism
- Time Factors
- Torpedo
- Tyrosine -- analogs & derivatives
- Tyrosine 3-Monooxygenase -- metabolism
No physical items for this record
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
There are no comments on this title.
Log in to your account to post a comment.