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Introduction
Current institution
Publications
Publications (7)
Background
Alzheimer’s disease (AD) is characterized by the aggregation of Tau protein and Amyloid-β peptides (Aβ 1-40 and Aβ 1-42). A loss of ribosomal population is also observed in the neurons in affected regions of AD. Our studies had demonstrated that in vitro aggregation of amyloid forming proteins, Aβ peptides and Tau protein variants (AFPs)...
Alzheimer’s disease (AD) is characterized by the appearance of neurofibrillary tangles comprising of the Tau protein and aggregation of amyloid‐β peptides (Aβ 1‐40 and Aβ 1‐42). A concomitant loss of the ribosomal population is also observed in AD‐affected neurons. Our studies demonstrate that, similarly to Tau protein aggregation, in vitro aggrega...
Ribosome hibernation is a prominent cellular strategy to modulate protein synthesis during starvation and the stationary phase of bacterial cell growth. Translational suppression involves the formation of either factor‐bound inactive 70S monomers or dimeric 100S hibernating ribosomal complexes, the biological significance of which is poorly underst...
The human tau is a microtubule-associated intrinsically unstructured protein that forms intraneuronal cytotoxic deposits in neurodegenerative diseases, like tauopathies. Recent studies indicate that in Alzheimer’s disease, ribosomal dysfunction might be a crucial event in the disease pathology. Our earlier studies had demonstrated that amorphous pr...
The ability of the ribosome to assist in folding of proteins both in vitro and in vivo is well documented. The interaction of the unfolded protein with the peptidyltransferase center (PTC) of the bacterial large ribosomal subunit is followed by release of the protein in a folding competent state and rapid dissociation of ribosome into its subunits....
An understanding of the mechanisms underlying protein aggregation and cytotoxicity of the protein aggregates is crucial in the prevention of several diseases in humans. Ribosome, the cellular protein synthesis machine is capable of acting as a protein folding modulator. The peptidyltransferase center residing in the domain V of large ribosomal subu...
Questions
Question (1)
I am looking for ways to predict localised secondary structure formation in my intrinsically disordered proteins when i expose them to different salt concentrations.Doing a CD would have helped but right now because of the lockdown (corona), that is not an option.
