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Structural characterization of codon 129 polymorphism in prion peptide segments (PrP127-132) using the Markov State Models.
J Mol Graph Model
March 2025
Department of Chemistry, Faculty of Science and Technology, University of Nairobi, P.O. Box 30197-00100, Nairobi, Kenya.
The human prion protein gene (PRNP) consists of two common alleles that encode either methionine or valine residues at codon 129. Polymorphism at codon 129 of the prion protein (PRNP) gene is closely associated with genetic variations and susceptibility to specific variants of prion diseases. The presence of these different alleles, known as the PRNP codon 129 polymorphism, plays a significant role in disease susceptibility and progression.
View Article and Find Full Text PDFPleiotropic Function of Cellular Prion Protein: Encompassing Endoplasmic-Reticulum Stress, Cell Proliferation in Vascular Smooth Muscle Cells.
J Cell Biochem
January 2025
Division of Cell Biology and Physiology, CSIR-Indian Institute of Chemical Biology, Kolkata, India.
Cellular prion protein (PRNP) has been implicated in various physiological processes in different cell types, for decades. Little has been known how PRNP functions in multiple, yet related processes within a particular system. In our current study, with the aid of high-throughput RNA-sequencing technique, we have presented an overall transcriptome profile of rat vascular smooth muscle cells (VSMCs) with Prnp knockdown.
View Article and Find Full Text PDFSubstantia nigra alterations in mice modeling Parkinson's disease.
Vavilovskii Zhurnal Genet Selektsii
November 2024
Institute of Cytology and Genetics of the Siberian Branch of the Russian Academy of Sciences, Novosibirsk, Russia.
Parkinson's disease (PD) is an age-related neurodegenerative pathology of the central nervous system. The well-known abnormalities characteristic of PD are dysfunctions in the nigrostriatal system including the substantia nigra of the midbrain and the striatum. Moreover, in PD persons, alpha-synucleinopathy is associated with abnormalities in the dopaminergic brain system.
View Article and Find Full Text PDFA novel ER stress regulator ARL6IP5 induces reticulophagy to ameliorate the prion burden.
Autophagy
October 2024
Molecular Sciences Lab, National Institute of Immunology, New Delhi, India.
Prion disease is a fatal and infectious neurodegenerative disorder caused by the trans-conformation conversion of PRNP/PrP to PRNP/PrP. Accumulated PRNP/PrP-induced ER stress causes chronic unfolded protein response (UPR) activation, which is one of the fundamental steps in prion disease progression. However, the role of various ER-resident proteins in prion-induced ER stress is elusive.
View Article and Find Full Text PDFCopper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein.
Phys Chem Chem Phys
October 2024
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Transmissible spongiform encephalopathies (or prion diseases) such as Creutzfeldt-Jacob disease, mad cow disease, and scrapie are characterized by accumulation in the brain of misfolded prion protein aggregates (PrP) that have properties of amyloid fibrils. Given that transition metal ions, such as copper and zinc, appear to be important for physiological functions of cellular PrP (PrP) as well as for prion disease pathogenesis, exploring their role in the protein aggregation process is of considerable interest. Copper(II) in particular is well-known to bind to the four tandem octapeptide repeats (PHGGGWGQ) located in the N-terminal region of PrP (human PrP amino acids 60-91), as well as to additional histidine binding sites outside the octarepeat region with distinct binding modes depending on Cu concentration.
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