ArticleBiophysical journal2015
Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Inducing prion protein shedding as a neuroprotective and regenerative approach in pathological conditions of the brain: from theory to facts.Neural regeneration research · 2023Review
- Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies.Science advances · 2021Article
- Integrating an Enhanced Sampling Method and Small-Angle X-Ray Scattering to Study Intrinsically Disordered Proteins.Frontiers in molecular biosciences · 2021Article
- Antibody Fragments as Tools for Elucidating Structure-Toxicity Relationships and for Diagnostic/Therapeutic Targeting of Neurotoxic Amyloid Oligomers.International journal of molecular sciences · 2020Review
- Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain.Biophysical journal · 2020Article
- Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes.Structure (London, England : 1993) · 2019Article
- Review
- Glutamine Side ChainJournal of the American Chemical Society · 2019Article
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
- Dissociation of the Dimer of the Intrinsically Disordered Domain of RNase Y upon Antibody Binding.Biophysical journal · 2018Article
- Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.Structure (London, England : 1993) · 2018Article
- Modeling Structure and Dynamics of Protein Complexes with SAXS Profiles.Methods in molecular biology (Clifton, N.J.) · 2018Article
- 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.Acta crystallographica. Section D, Structural biology · 2017Article
- Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Scientific reports · 2017Article
- Critical Role of Interdomain Interactions in the Conformational Change and Catalytic Mechanism of Endoplasmic Reticulum Aminopeptidase 1.Biochemistry · 2017Article
- A retrospective study of transfusion practices in a Tertiary Care Institute.Indian journal of anaesthesia · 2017Article
- Article
- Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1).The Journal of biological chemistry · 2016Article
- Assembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85α Homodimer.The Journal of biological chemistry · 2015Article
- From integrative structural biology to cell biology.The Journal of biological chemistryReview
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9 authors.
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Abstract
Aberrant self-assembly, induced by structural misfolding of the prion proteins, leads to a number of neurodegenerative disorders. In particular, misfolding of the mostly α-helical cellular prion protein (PrP(C)) into a β-sheet-rich disease-causing isoform (PrP(Sc)) is the key molecular event in the formation of PrP(Sc) aggregates. The molecular mechanisms underlying the PrP(C)-to-PrP(Sc) conversion and subsequent aggregation remain to be elucidated. However, in persistently prion-infected cell-culture models, it was shown that treatment with monoclonal antibodies against defined regions of the prion protein (PrP) led to the clearing of PrP(Sc) in cultured cells. To gain more insight into this process, we characterized PrP-antibody complexes in solution using a fast protein liquid chromatography coupled with small-angle x-ray scattering (FPLC-SAXS) procedure. High-quality SAXS data were collected for full-length recombinant mouse PrP [denoted recPrP(23-230)] and N-terminally truncated recPrP(89-230), as well as their complexes with each of two Fab fragments (HuM-P and HuM-R1), which recognize N- and C-terminal epitopes of PrP, respectively. In-line measurements by fast protein liquid chromatography coupled with SAXS minimized data artifacts caused by a non-monodispersed sample, allowing structural analysis of PrP alone and in complex with Fab antibodies. The resulting structural models suggest two mechanisms for how these Fabs may prevent the conversion of PrP(C) into PrP(Sc).
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