Antibody binding increases the flexibility of the prion protein
Tài liệu tham khảo
Aguzzi, 2009, Prions: protein aggregation and infectious diseases, Physiol. Rev., 89, 1105, 10.1152/physrev.00006.2009
Kretzschmar, 1986, Scrapie prion proteins are synthesized in neurons, Am. J. Pathol., 122, 1
Zahn, 2000, Nmr solution structure of the human prion protein, Proc. Nat. Acad. Sci., 97, 145, 10.1073/pnas.97.1.145
Riek, 1996, Nmr structure of the mouse prion protein domain prp(121?231), Nature, 382, 180, 10.1038/382180a0
Zweckstetter, 2017, Elucidating the structure of an infectious protein, PLoS Pathog., 13, 1, 10.1371/journal.ppat.1006229
Aguzzi, 2018, Toward therapy of human prion diseases, Annu. Rev. Pharmacol. Toxicol., 58, 331, 10.1146/annurev-pharmtox-010617-052745
Polymenidou, 2008, The pom monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes, PLoS One, 3, 1, 10.1371/journal.pone.0003872
Sonati, 2013, The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein, Nature, 501, 102, 10.1038/nature12402
Bardelli, 2018, A bispecific immunotweezer prevents soluble prp oligomers and abolishes prion toxicity, PLoS Path., 14, 1, 10.1371/journal.ppat.1007335
Kurt, 2014, Prion transmission prevented by modifying the β2–α2 loop structure of host prpc, J. Neurosci., 34, 1022, 10.1523/JNEUROSCI.4636-13.2014
Huang, 2015, The roles of the conserved tyrosine in the β2-α2 loop of the prion protein, Prion, 9, 412, 10.1080/19336896.2015.1115944
Huang, 2015, Evolutionary conserved tyr169 stabilizes the β2–α2 loop of the prion protein, J. Am. Chem. Soc., 137, 2948, 10.1021/ja511568m
Caldarulo, 2017, Prion protein β2–α2 loop conformational landscape, Proc. Nat. Acad. Sci., 114, 9617, 10.1073/pnas.1712155114
Zhou, 2019, ph-induced misfolding mechanism of prion protein: insights from microsecond-accelerated molecular dynamics simulations, ACS Chem. Neurosci., 10, 2718, 10.1021/acschemneuro.8b00582
Chen, 2014, Structural and dynamic properties of the human prion protein, Biophys. J., 106, 1152, 10.1016/j.bpj.2013.12.053
De Simone, 2007, Structural and hydration properties of the partially unfolded states of the prion protein, Biophys. J., 93, 1284, 10.1529/biophysj.107.108613
Eghiaian, 2007, Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage, Proc. Nat. Acad. Sci., 104, 7414, 10.1073/pnas.0607745104
Kuwata, 2004, Slow conformational dynamics in the hamster prion protein, Biochem., 43, 4439, 10.1021/bi036123o
Viles, 2001, Local structural plasticity of the prion protein. Analysis of nmr relaxation dynamics, Biochem., 40, 2743, 10.1021/bi002898a
Camilloni, 2012, Energy landscape of the prion protein helix 1 probed by metadynamics and nmr, Biophys. J., 102, 158, 10.1016/j.bpj.2011.12.003
Frontzek, 2021, A conformational switch controlling the toxicity of the prion protein, bioRxiv
Ilie, 2022, Antibody binding modulates the dynamics of the membrane-bound prion protein, Biophys. J., 121, 1, 10.1016/j.bpj.2022.06.007
Baral, 2012, Structural studies on the folded domain of the human prion protein bound to the fab fragment of the antibody pom1, Acta Crystallogr D, 68, 1501, 10.1107/S0907444912037328
Baral, 2018, Structural characterization of pom6 fab and mouse prion protein complex identifies key regions for prions conformational conversion, FEBS J., 285, 1701, 10.1111/febs.14438
Gossert, 2005, Prion protein nmr structures of elk and of mouse/elk hybrids, Proc. Nat. Acad. Sci., 102, 646, 10.1073/pnas.0409008102
Berendsen, 1995, Gromacs: a message-passing parallel molecular dynamics implementation, Comput. Phys. Commun., 91, 43, 10.1016/0010-4655(95)00042-E
Hess, 2008, Gromacs 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation, J. Chem. Theor. Comp., 4, 435, 10.1021/ct700301q
Huang, 2016, Charmm36m: an improved force field for folded and intrinsically disordered proteins, Nat. Methods, 14, 71, 10.1038/nmeth.4067
Jorgensen, 1983, Comparison of simple potential functions for simulating liquid water, J. Chem. Phys., 79, 926, 10.1063/1.445869
Bussi, 2007, Canonical sampling through velocity rescaling, J. Chem. Phys., 126, 10.1063/1.2408420
Berendsen, 1984, Molecular dynamics with coupling to an external bath, J. Chem. Phys., 81, 3684, 10.1063/1.448118
Darden, 1993, Particle mesh ewald: an nlog(n) method for ewald sums in large systems, J. Chem. Phys., 98, 10089, 10.1063/1.464397
Hess, 1997, Lincs: a linear constraint solver for molecular simulations, J. Comp. Chem., 18, 1463, 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
Blochliger, 2013, A scalable algorithm to order and annotate continuous observations reveals the metastable states visited by dynamical systems, Comput. Phys. Commun., 184, 2446, 10.1016/j.cpc.2013.06.009
Cocina, 2020, Sapphire-based clustering, J. Chem. Theor. Comp., 16, 6383, 10.1021/acs.jctc.0c00604
Baral, 2014, Structural basis of prion inhibition by phenothiazine compounds, Structure, 22, 291, 10.1016/j.str.2013.11.009
Chiesa, 2015, The elusive role of the prion protein and the mechanism of toxicity in prion disease, PLoS Path., 11, 1, 10.1371/journal.ppat.1004745
Westergard, 2007, The cellular prion protein (prp): its physiological function and role in disease, Biochim. et Biophys. Acta - Mol. Basis Dis., 1772, 629, 10.1016/j.bbadis.2007.02.011
Moreno, 2012, Sustained translational repression by eif2α—p mediates prion neurodegeneration, Nature, 485, 507, 10.1038/nature11058
Dametto, 2015, Neurodegeneration and unfolded-protein response in mice expressing a membrane-tethered flexible tail of prp, PLoS One, 10, 1, 10.1371/journal.pone.0117412
Beland, 2012, The prion protein unstructured n-terminal region is a broad-spectrum molecular sensor with diverse and contrasting potential functions, J. Neurochem., 120, 853, 10.1111/j.1471-4159.2011.07613.x
Wu, 2017, The n-terminus of the prion protein is a toxic effector regulated by the c-terminus, eLife, 6, 10.7554/eLife.23473
Frontzek, 2017
Falsig, 2012, Prion pathogenesis is faithfully reproduced in cerebellar organotypic slice cultures, PLoS Pathog., 8, 1, 10.1371/journal.ppat.1002985