Peripheral Administration of a Humanized Anti-PrP Antibody Blocks Alzheimer's Disease Aβ Synaptotoxicity

A synaptic model of memory: long-term potentiation in the hippocampus

Bliss, T. V. P., & Collingridge, G. L. (1993) · Nature · doi:10.1038/361031a0 · Cited by 11,566 · see citing works

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works

Replacing the complementarity-determining regions in a human antibody with those from a mouse

Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S., & Winter, G. (1986) · Nature · doi:10.1038/321522a0 · Cited by 1,406 · see citing works

Prion Diseases of Humans and Animals: Their Causes and Molecular Basis

Collinge, J. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.519 · Cited by 1,344 · see citing works

Physiology of the prion protein

Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617 · see citing works

Monoclonal antibodies inhibit prion replication and delay the development of prion disease

White, A. R., Enever, P., Tayebi, M., Mushens, R., Linehan, J., Brandner, S., Anstee, D. J., Collinge, J., & Hawke, S. H. (2003) · Nature · doi:10.1038/nature01457 · Cited by 490 · see citing works

Cross-Linking Cellular Prion Protein Triggers Neuronal Apoptosis in Vivo

Solforosi, L., Criado, J. R., McGavern, D. B., Wirz, S. A., Sánchez-Alavez, M., Sugama, S., DeGiorgio, L. A., Volpe, B. T., Wiseman, E., Abalos, G. C., et al. (2004) · Science · doi:10.1126/science.1094273 · Cited by 367 · see citing works

Amyloid β Protein Dimer-Containing Human CSF Disrupts Synaptic Plasticity: Prevention by Systemic Passive Immunization

Klyubin, I., Betts, V., Welzel, A. T., Blennow, K., Zetterberg, H., Wallin, A., Lemere, C. A., Cullen, W. K., Peng, Y., Wisniewski, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5161-07.2008 · Cited by 321 · see citing works

Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites

Freir, D. B., Nicoll, A. J., Klyubin, I. V., Panico, S., Donald, J. M. M., Risse, E., Asante, E. A., Farrow, M. A., Sessions, R. B., Saibil, H. R., et al. (2011) · Nature Communications · doi:10.1038/ncomms1341 · Cited by 290 · see citing works

Human prion proteins expressed in Escherichia coli and purified by high‐affinity column refolding

Zahn, R., von Schroetter, C., & Wüthrich, K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01330-6 · Cited by 253 · see citing works

A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody

Angal, S., King, D. J., Bodmer, M., Turner, A. V., Lawson, A. D. G., Roberts, G., Pedley, B. R., & Adair, J. R. (1993) · Molecular Immunology · doi:10.1016/0161-5890(93)90432-b · Cited by 245 · see citing works

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP<i>In Vivo</i>Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237 · see citing works

The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein

Sonati, T., Reimann, R., Falsig, J., Baral, P. K., O’Connor, T., Hornemann, S., Yaganoglu, S., Li, B., Herrmann, U., Wieland, B., et al. (2013) · Nature · doi:10.1038/nature12402 · Cited by 205 · see citing works

The POM Monoclonals: A Comprehensive Set of Antibodies to Non-Overlapping Prion Protein Epitopes

Polymenidou, M., Moos, R., Scott, M., Sigurdson, C. J., Shi, Y., Yajima, B., Hafner‐Bratkovič, I., Jerala, R., Hornemann, S., Kurt Wüthrich, A., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003872 · Cited by 181 · see citing works

Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an alzheimer's disease model mouse

Chung, E., Ji, Y., Sun, Y., Kascsak, R. J., Kascsak, R. B., Mehta, P. D., Strittmatter, S. M., & Wısnıewskı, T. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-130 · Cited by 168 · see citing works

Crystal structure of human prion protein bound to a therapeutic antibody

Antonyuk, S. V., Trevitt, C. R., Strange, R. W., Jackson, G. S., Sangar, D., Batchelor, M., Cooper, S., Fraser, C., Jones, S., Georgiou, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809170106 · Cited by 124 · see citing works

Multiple folding pathways for heterologously expressed human prion protein

Jackson, G. S., Hill, A. F., Joseph, C., Hosszu, L. L. P., Power, A., Waltho, J. P., Clarke, A. R., & Collinge, J. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00038-2 · Cited by 112 · see citing works

Amyloid-β-induced Synapse Damage Is Mediated via Cross-linkage of Cellular Prion Proteins

Bate, C., & Williams, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248724 · Cited by 89 · see citing works

Altered blood-brain barrier permeability and its effect on the distribution of Evans blue and sodium fluorescein in the rat brain applied by intracarotid injection.

Kozler, P., & Pokorny, J. (2003) · Physiological Research · doi:10.33549/physiolres.930289 · Cited by 87 · see citing works

PrP glycoforms are associated in a strain-specific ratio in native PrPSc

Khalili-Shirazi, A., Summers, L. E., Linehan, J. M., Mallinson, G., Anstee, D. J., Hawke, S. H., Jackson, G. S., & Collinge, J. (2005) · Journal of General Virology · doi:10.1099/vir.0.80375-0 · Cited by 70 · see citing works

PrP Antibodies Do Not Trigger Mouse Hippocampal Neuron Apoptosis

Klöhn, P., Farmer, M., Linehan, J. M., O'Malley, C., de Marco, M. F., Taylor, W., Farrow, M. A., Khalili-Shirazi, A., Brandner, S., & Collinge, J. (2012) · Science · doi:10.1126/science.1215579 · Cited by 69 · see citing works

The prion protein unstructured N‐terminal region is a broad‐spectrum molecular sensor with diverse and contrasting potential functions

Béland, M., & Roucou, X. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07613.x · Cited by 65 · see citing works

Immunotherapy in prion disease

Roettger, Y., Du, Y., Bacher, M., Zerr, I., Dodel, R. C., & Bach, J. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.258 · Cited by 44 · see citing works

Preventing Prion Pathogenicity by Targeting the Cellular Prion Protein

Nicoll, A. J., & Collinge, J. (2009) · Infectious Disorders - Drug Targets · doi:10.2174/1871526510909010048 · Cited by 36 · see citing works

Therapeutic effect of peripheral administration of an anti‐prion protein antibody on mice infected with prions

Ohsawa, N., Song, C., Suzuki, A., Furuoka, H., Hasebe, R., & Horiuchi, M. (2013) · Microbiology and Immunology · doi:10.1111/1348-0421.12037 · Cited by 25 · see citing works

Humanising Antibodies by CDR Grafting

Williams, D. G., Matthews, D. J., & Jones, T. (2010) · Springer eBooks · doi:10.1007/978-3-642-01144-3_21 · Cited by 21 · see citing works

Humanising Antibodies by CDR Grafting

O’Brien, S., & Jones, T. (2001) · Springer eBooks · doi:10.1007/978-3-662-04605-0_40 · Cited by 9 · see citing works

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works

Large Soluble Oligomers of Amyloid β-Protein from Alzheimer Brain Are Far Less Neuroactive Than the Smaller Oligomers to Which They Dissociate

Yang, T., Li, S., Xu, H., Walsh, D. M., & Selkoe, D. J. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1698-16.2016 · Cited by 347 · see citing works

A mechanistic hypothesis for the impairment of synaptic plasticity by soluble Aβ oligomers from Alzheimer’s brain

Li, S., & Selkoe, D. J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15007 · Cited by 264 · see citing works

Mammalian prions and their wider relevance in neurodegenerative diseases

Collinge, J. (2016) · Nature · doi:10.1038/nature20415 · Cited by 231 · see citing works

Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer’s disease

Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 140 · see citing works

Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models

Kostylev, M. A., Kaufman, A. C., Nygaard, H. B., Patel, P., Haas, L. T., Gunther, E. C., Vortmeyer, A., & Strittmatter, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643577 · Cited by 133 · see citing works

Prion protein monoclonal antibody (PRN100) therapy for Creutzfeldt–Jakob disease: evaluation of a first-in-human treatment programme

Mead, S., Khalili-Shirazi, A., Potter, C., Mok, T., Nihat, A., Hyare, H., Canning, S., Schmidt, C., Campbell, T., Darwent, L., et al. (2022) · The Lancet Neurology · doi:10.1016/s1474-4422(22)00082-5 · Cited by 116 · see citing works

Binding Sites for Amyloid-β Oligomers and Synaptic ToxicityPreprint

Smith, L. M., & Strittmatter, S. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024075 · Cited by 108 · see citing works

Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble TauIn Vivo

Ondrejčák, T., Klyubin, I. V., Corbett, G. T., Fraser, G. M., Hong, W., Mably, A. J., Gardener, M. J., Hammersley, J., Perkinton, M. S., Billinton, A., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1700-18.2018 · Cited by 102 · see citing works

The function of the cellular prion protein in health and disease

Watts, J. C., Bourkas, M. E. C., & Arshad, H. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1790-y · Cited by 97 · see citing works

Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers

Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92 · see citing works

Neural Glycosylphosphatidylinositol-Anchored Proteins in Synaptic Specification

Um, J. W., & Ko, J. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.06.007 · Cited by 92 · see citing works

Cellular prion protein as a receptor for amyloid-β oligomers in Alzheimer's disease

Salazar, S. V., & Strittmatter, S. M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.062 · Cited by 90 · see citing works

Prion Protein as a Toxic Acceptor of Amyloid-β Oligomers

Purro, S. A., Nicoll, A. J., & Collinge, J. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.020 · Cited by 80 · see citing works

Neurofilament light chain and tau concentrations are markedly increased in the serum of patients with sporadic Creutzfeldt-Jakob disease, and tau correlates with rate of disease progression

Thompson, A. G. B., Luk, C. Y., Heslegrave, A., Zetterberg, H., Mead, S., Collinge, J., & Jackson, G. S. (2018) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-317793 · Cited by 84 · see citing works

Formyl peptide receptor 2, as an important target for ligands triggering the inflammatory response regulation: a link to brain pathology

Tylek, K., Trojan, E., Regulska, M., Lacivita, E., Leopoldo, M., & Basta‐Kaim, A. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00271-x · Cited by 83 · see citing works

An Insight into Cellular and Molecular Mechanisms Underlying the Pathogenesis of Neurodegeneration in Alzheimer’s Disease

Ratan, Y., Rajput, A., Maleysm, S., Pareek, A., Jain, V. K., Pareek, A., Kaur, R., & Singh, G. (2023) · Biomedicines · doi:10.3390/biomedicines11051398 · Cited by 87 · see citing works

The N-terminus of the prion protein is a toxic effector regulated by the C-terminus

Wu, B., McDonald, A. J., Markham, K., Rich, C. B., McHugh, K. P., Tatzelt, J., Colby, D. W., Millhauser, G. L., & Harris, D. A. (2017) · eLife · doi:10.7554/elife.23473 · Cited by 77 · see citing works

Ginsenoside Rg1 and Acori Graminei Rhizoma Attenuates Neuron Cell Apoptosis by Promoting the Expression of miR-873-5p in Alzheimer’s Disease

Shi, R., Zhang, S., Cheng, G., Yang, X., Zhao, N., & Chen, C. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2567-y · Cited by 56 · see citing works

Conditional Deletion of Prnp Rescues Behavioral and Synaptic Deficits after Disease Onset in Transgenic Alzheimer's Disease

Salazar, S. V., Gallardo, C., Kaufman, A. C., Herber, C. S., Haas, L. T., Robinson, S., Manson, J. C., Lee, M. K., & Strittmatter, S. M. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0722-17.2017 · Cited by 52 · see citing works

The Binding Receptors of Aβ: an Alternative Therapeutic Target for Alzheimer’s Disease

Xia, M., Cheng, X., Yi, R., Gao, D., & Xiong, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8994-0 · Cited by 53 · see citing works

Proteolytic shedding of the prion protein via activation of metallopeptidase ADAM10 reduces cellular binding and toxicity of amyloid-β oligomers

Jarosz-Griffiths, H., Corbett, N. J., Rowland, H. A., Fisher, K., Jones, A. C., Baron, J., Howell, G. J., Cowley, S. A., Chintawar, S., Cader, M. Z., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005364 · Cited by 44 · see citing works

Clinical Trial Simulations Based on Genetic Stratification and the Natural History of a Functional Outcome Measure in Creutzfeldt-Jakob Disease

Mead, S., Burnell, M., Lowe, J., Thompson, A. G. B., Lukić, A., Porter, M., Carswell, C. J., Kaski, D. N., Kenny, J., Mok, T. H., et al. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2015.4885 · Cited by 43 · see citing works

Recent advancements toward therapeutic vaccines against Alzheimer’s disease

Herline, K., Drummond, E., & Wısnıewskı, T. (2018) · Expert Review of Vaccines · doi:10.1080/14760584.2018.1500905 · Cited by 44 · see citing works

Identification of a Compound That Disrupts Binding of Amyloid-β to the Prion Protein Using a Novel Fluorescence-based Assay

Risse, E., Nicoll, A. J., Taylor, W. A., Wright, D., Badoni, M., Yang, X., Farrow, M. A., & Collinge, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.637124 · Cited by 40 · see citing works

Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation

Bove‐Fenderson, E., Urano, R., Straub, J. E., & Harris, D. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.789990 · Cited by 41 · see citing works

Cellular prion protein (PrPC) in the development of Merlin-deficient tumours

Provenzano, L., Ryan, Y., Hilton, D. A., Rimmer, J. L., Dave, F., Maze, E. A., Adams, C., Rigby-Jones, R., Ammoun, S., & Hanemann, C. O. (2017) · Oncogene · doi:10.1038/onc.2017.200 · Cited by 36 · see citing works

Prion neurotoxicity

Le, N. T. T., Wu, B., & Harris, D. A. (2018) · Brain Pathology · doi:10.1111/bpa.12694 · Cited by 35 · see citing works

Rescue of Transgenic Alzheimer’s Pathophysiology by Polymeric Cellular Prion Protein Antagonists

Gunther, E. C., Smith, L. M., Kostylev, M. A., Cox, T. O., Kaufman, A. C., Lee, S., Folta‐Stogniew, E. J., Maynard, G. D., Um, J. W., Stagi, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.021 · Cited by 34 · see citing works

Human prion diseases and the prion protein – what is the current state of knowledge?

Nafe, R., Arendt, C. T., & Hattingen, E. (2023) · Translational Neuroscience · doi:10.1515/tnsci-2022-0315 · Cited by 35 · see citing works

New Alzheimer’s disease model mouse specialized for analyzing the function and toxicity of intraneuronal Amyloid β oligomers

Ochiishi, T., Kaku, M., Kiyosue, K., Doi, M., Urabe, T., Hattori, N., Shimura, H., & Ebihara, T. (2019) · Scientific Reports · doi:10.1038/s41598-019-53415-8 · Cited by 34 · see citing works

Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies

Linsenmeier, L., Mohammadi, B., Shafiq, M., Frontzek, K., Bär, J., Shrivastava, A. N., Daμμe, M., Song, F., Schwarz, A., Vela, S. D., et al. (2021) · Science Advances · doi:10.1126/sciadv.abj1826 · Cited by 33 · see citing works

Prospects for safe and effective vaccines against prion diseases

Mabbott, N. A. (2014) · Expert Review of Vaccines · doi:10.1586/14760584.2015.965691 · Cited by 33 · see citing works

Neuronal transcriptome, tau and synapse loss in Alzheimer’s knock-in mice require prion protein

Stoner, A. J., Fu, L., Nicholson, L., Zheng, C., Toyonaga, T., Spurrier, J. M., Laird, W., Cai, Z., & Strittmatter, S. M. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01345-z · Cited by 33 · see citing works

Targeting glutamatergic and cellular prion protein mechanisms of amyloid β-mediated persistent synaptic plasticity disruption: Longitudinal studies

Zhang, D., Qi, Y., Klyubin, I. V., Ondrejčák, T., Sarell, C. J., Cuello, A. C., Collinge, J., & Rowan, M. J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.03.036 · Cited by 31 · see citing works

Anti‐PrPC antibody rescues cognition and synapses in transgenic alzheimer mice

Cox, T. O., Gunther, E. C., Brody, A. H., Chiasseu, M., Stoner, A. J., Smith, L. M., Haas, L. T., Hammersley, J., Rees, G., Dosanjh, B., et al. (2019) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.730 · Cited by 30 · see citing works

Immunotherapy against Prion Disease

Ma, Y., & Ma, J. (2020) · Pathogens · doi:10.3390/pathogens9030216 · Cited by 30 · see citing works

Recombinant prion protein vaccination of transgenic elk PrP mice and reindeer overcomes self-tolerance and protects mice against chronic wasting disease

Abdelaziz, D. H., Thapa, S., Brandon, J., Maybee, J., Vankuppeveld, L., McCorkell, R. B., & Schätzl, H. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004810 · Cited by 24 · see citing works

Protective anti‐prion antibodies in human immunoglobulin repertoires

Senatore, A., Frontzek, K., Emmenegger, M., Chincisan, A., Losa, M., Reimann, R., Horny, G., Guo, J., Fels, S., Sorce, S., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012739 · Cited by 23 · see citing works

Spontaneous generation of prions and transmissible PrP amyloid in a humanised transgenic mouse model of A117V GSS

Asante, E. A., Linehan, J. M., Tomlinson, A., Jakubcova, T., Hamdan, S., Grimshaw, A., Smidak, M., Jeelani, A., Nihat, A., Mead, S., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000725 · Cited by 21 · see citing works

Copper- and Zinc-Promoted Interdomain Structure in the Prion Protein: A Mechanism for Autoinhibition of the Neurotoxic N-Terminus

Evans, E. G. B., & Millhauser, G. L. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.06.005 · Cited by 20 · see citing works

To develop with or without the prion protein

Halliez, S., Passet, B., Martin‐Lannerée, S., Hernandez-Rapp, J., Laude, H., Mouillet‐Richard, S., Vilotte, J.-L., & Béringue, V. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00058 · Cited by 20 · see citing works

Prion Protein-Specific Antibodies-Development, Modes of Action and Therapeutics Application

Roviš, T. L., & Legname, G. (2014) · Viruses · doi:10.3390/v6103719 · Cited by 19 · see citing works

MicroRNAs mediate the anti-tumor and protective effects of ginsenosides

Ashrafizadeh, M., Ahmadi, Z., Mohammadinejad, R., Farkhondeh, T., & Samarghandian, S. (2019) · Nutrition and Cancer · doi:10.1080/01635581.2019.1675722 · Cited by 18 · see citing works

A review of drug therapy for sporadic fatal insomnia

Damavandi, P. T., Dove, M. T., & Pickersgill, R. W. (2017) · Prion · doi:10.1080/19336896.2017.1368937 · Cited by 18 · see citing works

Anchorless risk or released benefit? An updated view on the ADAM10-mediated shedding of the prion protein

Mohammadi, B., Song, F., Matamoros‐Angles, A., Shafiq, M., Daμμe, M., Puig, B., Glatzel, M., & Altmeppen, H. C. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03582-4 · Cited by 15 · see citing works

A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody

Reilly, M., Benilova, I., Khalili-Shirazi, A., Schmidt, C., Ahmed, P., Yip, D. C.-M., Jat, P., & Collinge, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-13455-z · Cited by 14 · see citing works

The future for treating Creutzfeldt–Jakob disease

Vetrugno, V., Puopolo, M., Cardone, F., Capozzoli, F., Ladogana, A., & Pocchiari, M. (2014) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2015.994605 · Cited by 13 · see citing works

Prion Diseases

Whitechurch, B. C., Welton, J. M., Collins, S. J., & Lawson, V. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-57193-5_13 · Cited by 13 · see citing works

Autophagy-ERK1/2-Involved Disinhibition of Hippocampal Neurons Contributes to the Pre-Synaptic Toxicity Induced by Aβ 42 Exposure

Yin, Y., Zhao, Y., Han, S., Zhang, N., Chen, H., & Wang, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170246 · Cited by 12 · see citing works

Decoding the function of the N-terminal tail of the cellular prion protein to inspire novel therapeutic avenues for neurodegenerative diseases

Iraci, N., Stincardini, C., Barreca, M. L., & Biasini, E. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.015 · Cited by 12 · see citing works

Prion Protein Signaling in the Nervous System—A Review and Perspective

Liebert, A. D., Bicknell, B. T., & Adams, R. D. (2014) · Signal Transduction Insights · doi:10.4137/sti.s12319 · Cited by 10 · see citing works

Turmeric effect on subcutaneous insulin-induced amyloid mass: anin vivostudy

Kheirbakhsh, R., Chinisaz, M., Amanpour, S., Amini, S., Khodayari, S., Khodayari, H., Dilmaghanian, A., Haddadi, M., & Ebrahim‐Habibi, A. (2016) · Drug and Chemical Toxicology · doi:10.3109/01480545.2016.1163575 · Cited by 10 · see citing works

Inducing prion protein shedding as a neuroprotective and regenerative approach in pathological conditions of the brain: from theory to facts

Matamoros‐Angles, A., Mohammadi, B., Song, F., Shafiq, M., Brenna, S., Puig, B., Glatzel, M., & Altmeppen, H. C. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.366496 · Cited by 9 · see citing works

α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model

So, R. W. L., Amano, G., Stuart, E., Amini, A. E., Aguzzi, A., Collingridge, G. L., & Watts, J. C. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012517 · Cited by 6 · see citing works

Common therapeutic strategies for prion and Alzheimer’s diseases

Elezgarai, S. R., & Biasini, E. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0190 · Cited by 7 · see citing works

Large Soluble Oligomers of Amyloid β-Protein from Alzheimer Brain Are Far Less Neuroactive Than the Smaller Oligomers to Which They Dissociate

Yang, T., Li, S., Xu, H., Walsh, D. M., & Selkoe, D. J. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1698-16.2017 · Cited by 7 · see citing works

Clinical trials

Mead, S., & Tagliavini, F. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63945-5.00024-6 · Cited by 7 · see citing works

Soluble Prion Peptide 107–120 Protects Neuroblastoma SH-SY5Y Cells against Oligomers Associated with Alzheimer’s Disease

Boroujeni, E. R., Hosseini, S. M., Fani, G., Cecchi, C., & Chiti, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197273 · Cited by 6 · see citing works

Prion Diseases

Mercer, R. C. C., McDonald, A. J., Bove‐Fenderson, E., Fang, C., Wu, B., & Harris, D. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00002-x · Cited by 5 · see citing works

Intrinsic Toxicity of Antibodies to the Globular Domain of the Prion Protein

Reimann, R., & Aguzzi, A. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.01.028 · Cited by 5 · see citing works

Treatment of microglia with Anti-PrP monoclonal antibodies induces neuronal apoptosis in vitro

Adhikari, U. K., Sakiz, E., Habiba, U., Mikhael, M., Senesi, M., David, M. A., Guillemin, G. J., Ooi, L., Karl, T., Collins, S. J., et al. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e08644 · Cited by 4 · see citing works

An inter-domain regulatory mechanism controls toxic activities of PrPC

McDonald, A. J., Wu, B., & Harris, D. A. (2017) · Prion · doi:10.1080/19336896.2017.1384894 · Cited by 4 · see citing works

Reply to: Intrinsic Toxicity of Antibodies to the Globular Domain of the Prion Protein

Purro, S. A., Mead, S., Khalili-Shirazi, A., Nicoll, A. J., & Collinge, J. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.04.002 · Cited by 4 · see citing works

Two mouse models of Alzheimer’s disease accumulate amyloid at different rates and have distinct Aβ oligomer profiles unaltered by ablation of cellular prion protein

Purro, S. A., Farmer, M., Noble, E., Sarell, C. J., Powell, M., Yip, D. C.-M., Giggins, L., Zakka, L., Thomas, D. X., Farrow, M. A., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0294465 · Cited by 3 · see citing works

Targeting Aβ Receptors to Modify Alzheimer’s Disease Progression

Haas, L. T., & Strittmatter, S. M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00008-3 · Cited by 2 · see citing works

Genome-wide screens identify core regulators of cell surface prion protein expression

Beauchemin, K. S., & Supattapone, S. (2026) · Scientific Reports · doi:10.1038/s41598-026-37137-2 · Cited by 2 · see citing works

Epitope-specific anti-PrP antibody toxicity: a comparative in-silico study of human and mouse prion proteins

Adhikari, U. K., & Tayebi, M. (2021) · Prion · doi:10.1080/19336896.2021.1964326 · Cited by 1 · see citing works

Neuronal Transcriptome Disruption, Tau Accumulation and Synapse Loss in Alzheimer’s Knock-in Mice Require Cellular Prion ProteinPreprint

Stoner, A. J., Fu, L., Nicholson, L., Zheng, C., Toyonaga, T., Spurrier, J. M., Laird, W., Cai, Z., & Strittmatter, S. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.15.528700 · Cited by 1 · see citing works

A New Approach to Alzheimer Disease

Dubovsky, S. L. (2014) · Journal watch · doi:10.1056/nejm-jw.na34645

Faculty Opinions recommendation of Conditional Deletion of Prnp Rescues Behavioral and Synaptic Deficits after Disease Onset in Transgenic Alzheimer's Disease.

Allinquant, B. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.729275349.793537672

Impact of cellular prion protein expression on disease progression and pathology in two mouse models of Alzheimer’s diseasePreprint

Purro, S. A., Farmer, M., Noble, E., Sarell, C. J., Powell, M., Yip, D. C.-M., Giggins, L., Zakka, L., Thomas, D. X., Farrow, M. A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.25.508690

α-Synuclein Strain Propagation is Independent of Cellular Prion Protein Expression in Transgenic MicePreprint

So, R. W. L., Stuart, E., Amini, A. E., Aguzzi, A., Collingridge, G. L., & Watts, J. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.27.587028

Additional file 1 of Neuronal transcriptome, tau and synapse loss in Alzheimer’s knock-in mice require prion protein

Stoner, A. J., Fu, L., Nicholson, L., Zheng, C., Toyonaga, T., Spurrier, J. M., Laird, W., Cai, Z., & Strittmatter, S. M. (2023) · Figshare · doi:10.6084/m9.figshare.24571848

Therapeutic strategies in prion disease: current evidence, translational challenges, and emerging directions

Zhu, Y.-X., Bradford, B. M., & Mabbott, N. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1924347

Peripheral administration of a humanized anti-PrP antibody blocks Alzheimer's disease Aß synaptotoxicity

ROWAN, M. (2014) · Arrow@dit (Dublin Institute of Technology)

Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites

Freir, D. B., Nicoll, A. J., Klyubin, I. V., Panico, S., Donald, J. M. M., Risse, E., Asante, E. A., Farrow, M. A., Sessions, R. B., Saibil, H. R., et al. (2011) · Nature Communications · doi:10.1038/ncomms1341 · Cited by 290 · see citing works

Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites

Freir, D., Nicoll, A., Klyubin, I., Panico, S., Mc Donald, J., Risse, E., Asante, E., Farrow, M., Sessions, R., Saibil, H. R., et al. (2011) · UCL Discovery (University College London) · Cited by 1 · see citing works

Interaction between prion protein and toxic amyloid ß assemblies can be therapeutically targeted at multiple sites.

Klyubin, I. V., & ROWAN, M. (2011) · Arrow@dit (Dublin Institute of Technology)

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP<i>In Vivo</i>Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237 · see citing works