ArticleBiophysical journal2010
Influence of pH on the human prion protein: insights into the early steps of misfolding.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 84 citations in OpenAlex.
- Physiological responses to mask-associated COFrontiers in public health · 2026Review
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Essential Components of Synthetic Infectious Prion Formation De Novo.Biomolecules · 2022Review
- The role of α-sheet structure in amyloidogenesis: characterization and implications.Open biology · 2022Review
- Antibody binding modulates the dynamics of the membrane-bound prion protein.Biophysical journal · 2022Article
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization.Protein science : a publication of the Protein Society · 2021Article
- A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020Review
- Unique Structural Features of Mule Deer Prion Protein Provide Insights into Chronic Wasting Disease.ACS omega · 2019Article
- Cryo-LESA Mass Spectrometry-a Step Towards Truly Native Surface Sampling of Proteins.Journal of the American Society for Mass Spectrometry · 2019Article
- Effects of pH and aggregation in the human prion conversion into scrapie form: a study using molecular dynamics with excited normal modes.European biophysics journal : EBJ · 2018Article
- Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Journal of neurochemistry · 2017Article
- Interplay of buried histidine protonation and protein stability in prion misfolding.Scientific reports · 2017Article
- The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.Protein science : a publication of the Protein Society · 2016Article
- Article
- Insight into Early-Stage Unfolding of GPI-Anchored Human Prion Protein.Biophysical journal · 2015Article
- Copper-induced structural propensities of the amyloidogenic region of human prion protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Structural and dynamic properties of the human prion protein.Biophysical journal · 2014Article
- Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH.Biomolecules · 2014Article
- The role of Cys179-Cys214 disulfide bond in the stability and folding of prion protein: insights from molecular dynamics simulations.Journal of molecular modeling · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. Conversion from the normal cellular form (PrP(C)) or recombinant PrP (recPrP) to a misfolded form is pH-sensitive, in that misfolding and aggregation occur more readily at lower pH. To gain more insight into the influence of pH on the dynamics of PrP and its potential to misfold, we performed extensive molecular-dynamics simulations of the recombinant PrP protein (residues 90-230) in water at three different pH regimes: neutral (or cytoplasmic) pH (∼7.4), middle (or endosomal) pH (∼5), and low pH (<4). We present five different simulations of 50 ns each for each pH regime, amounting to a total of 750 ns of simulation time. A detailed analysis and comparison with experiment validate the simulations and lead to new insights into the mechanism of pH-induced misfolding. The mobility of the globular domain increases with decreasing pH, through displacement of the first helix and instability of the hydrophobic core. At middle pH, conversion to a misfolded (PrP(Sc)-like) conformation is observed. The observed changes in conformation and stability are consistent with experimental data and thus provide a molecular basis for the initial steps in the misfolding process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.