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2. Convergent generation of atypical prions in knockin mouse models of genetic prion disease

4. The molecular determinants of a universal prion acceptor.

7. Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease

8. α-Synuclein aggregation nucleates through liquid–liquid phase separation

11. Convergent generation of atypical prions in knock-in mouse models of genetic prion disease

13. The G51D SNCA mutation generates a slowly progressive alpha-synuclein strain in early-onset Parkinson's disease

14. α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties

15. Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification

16. Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids

17. Author response: Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids

20. Effect of Disease-Associated P123H and V70M Mutations on β-Synuclein Fibrillation

23. Liquid-liquid phase separation and liquid-to-solid transition mediate α-synuclein amyloid fibril containing hydrogel formation

24. Lipopolysaccharide from Gut Microbiota Modulates α-Synuclein Aggregation and Alters Its Biological Function

25. Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils

26. The Familial α-Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers

28. Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation

33. p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis

35. Complexation of NAC-Derived Peptide Ligands with the C-Terminus of α-Synuclein Accelerates Its Aggregation

36. Anti-prion drugs do not improve survival in knock-in models of inherited prion disease.

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