{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T20:34:15Z","timestamp":1786739655035,"version":"build-2736575974"},"reference-count":159,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"9","content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2023,9]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    In the last decades, the role of the prion protein (PrP) in neurodegenerative diseases has been intensively investigated, initially in prion diseases of humans (e.g., Creutzfeldt-Jakob disease) and animals (e.g., scrapie in sheep, chronic wasting disease in deer and elk, or \u201cmad cow disease\u201d in cattle). Templated misfolding of physiological cellular prion protein (PrP\n                    <jats:sup>C<\/jats:sup>\n                    ) into an aggregation-prone isoform (termed PrP \u201cScrapie\u201d (PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    )), self-replication and spreading of the latter inside the brain and to peripheral tissues, and the associated formation of infectious proteopathic seeds (termed \u201cprions\u201d) are among the essential pathogenic mechanisms underlying this group of fatal and transmissible spongiform encephalopathies. Later, key roles of the correctly folded PrP\n                    <jats:sup>C<\/jats:sup>\n                    were identified in more common human brain diseases (such as Alzheimer\u2019s disease or Parkinson\u2019s disease) associated with the misfolding and\/or accumulation of other proteins (such as amyloid-\u03b2, tau or \u03b1-synuclein, respectively). PrP\n                    <jats:sup>C<\/jats:sup>\n                    has also been linked with neuroprotective and regenerative functions, for instance in hypoxic\/ischemic conditions such as stroke. However, despite a mixed \u201cbouquet\u201d of suggested functions, our understanding of pathological and, especially, physiological roles played by PrP\n                    <jats:sup>C<\/jats:sup>\n                    in the brain and beyond is certainly incomplete. Interactions with various other proteins at the cell surface or within intracellular compartments may account for the functional diversity linked with PrP\n                    <jats:sup>C<\/jats:sup>\n                    . Moreover, conserved endogenous proteolytic processing of PrP\n                    <jats:sup>C<\/jats:sup>\n                    generates several defined PrP\n                    <jats:sup>C<\/jats:sup>\n                    fragments, possibly holding intrinsic functions in physiological and pathological conditions, thus making the \u201ctrue and complete biology\u201d of this protein more complicated to be elucidated. Here, we focus on one of those released PrP\n                    <jats:sup>C<\/jats:sup>\n                    fragments, namely shed PrP (sPrP), generated by a membrane-proximate ADAM10-mediated cleavage event at the cell surface. Similar to other soluble PrP\n                    <jats:sup>C<\/jats:sup>\n                    fragments (such as the N1 fragment representing PrP\u2019s released N-terminal tail upon the major \u03b1-cleavage event) or experimentally employed recombinant PrP, sPrP is being suggested to act neuroprotective in Alzheimer\u2019s disease and other protein misfolding diseases. Several lines of evidence on extracellular PrP\n                    <jats:sup>C<\/jats:sup>\n                    (fragments) suggest that induction of PrP\n                    <jats:sup>C<\/jats:sup>\n                    release could be a future therapeutic option in various brain disorders. Our recent identification of a substrate-specific approach to stimulate the shedding by ADAM10, based on ligands binding to cell surface PrP\n                    <jats:sup>C<\/jats:sup>\n                    , may further set the stage for research into this direction.\n                  <\/jats:p>","DOI":"10.4103\/1673-5374.366496","type":"journal-article","created":{"date-parts":[[2026,5,25]],"date-time":"2026-05-25T17:05:05Z","timestamp":1779728705000},"page":"1869-1875","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":1,"title":["Inducing prion protein shedding as a neuroprotective and regenerative approach in pathological conditions of the brain: from theory to facts"],"prefix":"10.4103","volume":"18","author":[{"given":"Andreu","family":"Matamoros-Angles","sequence":"first","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Behnam","family":"Mohammadi","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feizhi","family":"Song","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohsin","family":"Shafiq","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Santra","family":"Brenna","sequence":"additional","affiliation":[{"name":"Department of Neurology, Experimental Research in Stroke and Inflammation (ERSI), University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berta","family":"Puig","sequence":"additional","affiliation":[{"name":"Department of Neurology, Experimental Research in Stroke and Inflammation (ERSI), University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Glatzel","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9439-6533","authenticated-orcid":false,"given":"Hermann C.","family":"Altmeppen","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","published-online":{"date-parts":[[2023,1,5]]},"reference":[{"key":"R1-20260525","doi-asserted-by":"crossref","first-page":"e1008139","DOI":"10.1371\/journal.ppat.1008139","article-title":"Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion","volume":"15","author":"Abskharon","year":"2019","journal-title":"PLoS Pathog"},{"key":"R2-20260525","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1097\/01.jnen.0000228137.10531.72","article-title":"Immunohistochemical expression of prion protein (PrPC) in the human forebrain during development","volume":"65","author":"Adle-Biassette","year":"2006","journal-title":"J Neuropathol Exp Neurol"},{"key":"R3-20260525","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s00401-019-02085-x","article-title":"Shortening heparan sulfate chains prolongs survival and reduces parenchymal plaques in prion disease caused by mobile, ADAM10-cleaved prions","volume":"139","author":"Aguilar-Calvo","year":"2020","journal-title":"Acta Neuropathol"},{"key":"R4-20260525","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1172\/JCI200113919","article-title":"Peripheral prion pursuit","volume":"108","author":"Aguzzi","year":"2001","journal-title":"J Clin Invest"},{"key":"R5-20260525","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.jneuroim.2009.01.025","article-title":"Curative properties of antibodies against prion protein:a comparative in vitro study of monovalent fragments and divalent antibodies","volume":"209","author":"Alexandrenne","year":"2009","journal-title":"J Neuroimmunol"},{"key":"R6-20260525","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1750-1326-6-36","article-title":"Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo","volume":"6","author":"Altmeppen","year":"2011","journal-title":"Mol Neurodegener"},{"key":"R7-20260525","doi-asserted-by":"crossref","first-page":"4338","DOI":"10.1111\/febs.12196","article-title":"Roles of endoproteolytic \u03b1-cleavage and shedding of the prion protein in neurodegeneration","volume":"280","author":"Altmeppen","year":"2013","journal-title":"FEBS J"},{"key":"R8-20260525","doi-asserted-by":"crossref","first-page":"e04260","DOI":"10.7554\/eLife.04260","article-title":"The sheddase ADAM10 is a potent modulator of prion disease","volume":"4","author":"Altmeppen","year":"2015","journal-title":"Elife"},{"key":"R9-20260525","doi-asserted-by":"crossref","first-page":"3878","DOI":"10.1242\/jcs.183137","article-title":"Characterization of prion protein function by focal neurite stimulation","volume":"129","author":"Amin","year":"2016","journal-title":"J Cell Sci"},{"key":"R10-20260525","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/1756-6606-6-47","article-title":"Exosomes neutralize synaptic-plasticity-disrupting activity of Abeta assemblies in vivo","volume":"6","author":"An","year":"2013","journal-title":"Mol Brain"},{"key":"R11-20260525","doi-asserted-by":"crossref","first-page":"e1007335","DOI":"10.1371\/journal.ppat.1007335","article-title":"A bispecific immunotweezer prevents soluble PrP oligomers and abolishes prion toxicity","volume":"14","author":"Bardelli","year":"2018","journal-title":"PLOS Pathog"},{"key":"R12-20260525","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.nbd.2004.05.005","article-title":"GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice","volume":"16","author":"Barmada","year":"2004","journal-title":"Neurobiol Dis"},{"key":"R13-20260525","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1111\/j.1471-4159.2011.07613.x","article-title":"The prion protein unstructured N-terminal region is a broad-spectrum molecular sensor with diverse and contrasting potential functions","volume":"120","author":"Beland","year":"2012","journal-title":"J Neurochem"},{"key":"R14-20260525","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.neurobiolaging.2014.02.001","article-title":"Abeta induces its own prion protein N-terminal fragment (PrPN1)-mediated neutralization in amorphous aggregates","volume":"35","author":"Beland","year":"2014","journal-title":"Neurobiol Aging"},{"key":"R15-20260525","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1186\/1297-9716-43-87","article-title":"Healthy goats naturally devoid of prion protein","volume":"43","author":"Benestad","year":"2012","journal-title":"Vet Res"},{"key":"R16-20260525","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1111\/jnc.14281","article-title":"Mechanisms of neuroprotection against ischemic insult by stress-inducible phosphoprotein-1\/prion protein complex","volume":"145","author":"Beraldo","year":"2018","journal-title":"J Neurochem"},{"key":"R17-20260525","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/379339a0","article-title":"Normal host prion protein necessary for scrapie-induced neurotoxicity","volume":"379","author":"Brandner","year":"1996","journal-title":"Nature"},{"key":"R18-20260525","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/nn.2483","article-title":"Axonal prion protein is required for peripheral myelin maintenance","volume":"13","author":"Bremer","year":"2010","journal-title":"Nat Neurosci"},{"key":"R19-20260525","doi-asserted-by":"crossref","first-page":"1809065","DOI":"10.1080\/20013078.2020.1809065","article-title":"Characterization of brain-derived extracellular vesicles reveals changes in cellular origin after stroke and enrichment of the prion protein with a potential role in cellular uptake","volume":"9","author":"Brenna","year":"2020","journal-title":"J Extracell Vesicles"},{"key":"R20-20260525","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1038\/37783","article-title":"The cellular prion protein binds copper in vivo","volume":"390","author":"Brown","year":"1997","journal-title":"Nature"},{"key":"R21-20260525","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1007\/BF03403528","article-title":"High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene","volume":"1","author":"B\u00fceler","year":"1994","journal-title":"Mol Med"},{"key":"R22-20260525","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1038\/s41374-019-0282-1","article-title":"Role of prion protein glycosylation in replication of human prions by protein misfolding cyclic amplification","volume":"99","author":"Camacho","year":"2019","journal-title":"Lab Invest"},{"key":"R23-20260525","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1016\/j.bpj.2021.02.007","article-title":"Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction","volume":"120","author":"Cao","year":"2021","journal-title":"Biophys J"},{"key":"R24-20260525","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1016\/j.bpj.2015.06.065","article-title":"Prion protein - antibody complexes characterized by chromatography-coupled small-angle X-ray scattering","volume":"109","author":"Carter","year":"2015","journal-title":"Biophys J"},{"key":"R25-20260525","doi-asserted-by":"crossref","first-page":"3041","DOI":"10.1091\/mbc.e11-04-0321","article-title":"Neuroprotective role of PrPC against kainate-induced epileptic seizures and cell death depends on the modulation of JNK3 activation by GluR6\/7-PSD-95 binding","volume":"22","author":"Carulla","year":"2011","journal-title":"Mol Biol Cell"},{"key":"R26-20260525","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1111\/jnc.14044","article-title":"Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding","volume":"142","author":"Cheng","year":"2017","journal-title":"J Neurochem"},{"key":"R27-20260525","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1126\/science.1110837","article-title":"Anchorless prion protein results in infectious amyloid disease without clinical scrapie","volume":"308","author":"Chesebro","year":"2005","journal-title":"Science"},{"key":"R28-20260525","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1186\/1471-2202-11-130","article-title":"Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an Alzheimer's disease model mouse","volume":"11","author":"Chung","year":"2010","journal-title":"BMC Neurosci"},{"key":"R29-20260525","first-page":"1375","article-title":"Cellular prion protein ablation impairs behavior as a function of age","volume":"14","author":"Coitinho","year":"2003","journal-title":"Neuroreport"},{"key":"R30-20260525","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1007\/s00401-019-02114-9","article-title":"PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins","volume":"139","author":"Corbett","year":"2020","journal-title":"Acta Neuropathol"},{"key":"R31-20260525","doi-asserted-by":"crossref","first-page":"7758","DOI":"10.1007\/s12035-018-0944-9","article-title":"Interaction of peptide aptamers with prion protein central domain promotes \u03b1-cleavage of PrP C","volume":"55","author":"Corda","year":"2018","journal-title":"Mol Neurobiol"},{"key":"R32-20260525","doi-asserted-by":"crossref","first-page":"e12114","DOI":"10.1002\/jev2.12114","article-title":"Astrocytes-derived extracellular vesicles in motion at the neuron surface:involvement of the prion protein","volume":"10","author":"D'Arrigo","year":"2021","journal-title":"J Extracell vesicles"},{"key":"R33-20260525","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1080\/19336896.2017.1423186","article-title":"The role of the prion protein in the internalization of alpha-synuclein amyloids","volume":"12","author":"De","year":"2018","journal-title":"Prion"},{"key":"R34-20260525","doi-asserted-by":"crossref","first-page":"4640","DOI":"10.3390\/ijms20184640","article-title":"The link of the prion protein with Ca2+metabolism and ROS production, and the possible implication in A\u03b2toxicity","volume":"20","author":"De","year":"2019","journal-title":"Int J Mol Sci"},{"key":"R35-20260525","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1111\/j.1471-4159.2009.05892.x","article-title":"Characterization of cell-surface prion protein relative to its recombinant analogue:insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein","volume":"109","author":"Demarco","year":"2009","journal-title":"J Neurochem"},{"key":"R36-20260525","doi-asserted-by":"crossref","first-page":"15987","DOI":"10.1073\/pnas.1409354111","article-title":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10","volume":"111","author":"Deng","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R37-20260525","doi-asserted-by":"crossref","first-page":"e2024","DOI":"10.1038\/cddis.2015.365","article-title":"Cellular prion protein promotes post-ischemic neuronal survival, angioneurogenesis and enhances neural progenitor cell homing via proteasome inhibition","volume":"6","author":"Doeppner","year":"2015","journal-title":"Cell Death Dis"},{"key":"R38-20260525","doi-asserted-by":"crossref","first-page":"9295","DOI":"10.1073\/pnas.151242598","article-title":"Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody","volume":"98","author":"Enari","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R39-20260525","doi-asserted-by":"crossref","first-page":"3323","DOI":"10.1093\/brain\/awq217","article-title":"Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer's disease","volume":"133","author":"Epis","year":"2010","journal-title":"Brain"},{"key":"R40-20260525","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1111\/jnc.13514","article-title":"Exosomal cellular prion protein drives fibrillization of amyloid beta and counteracts amyloid beta-mediated neurotoxicity","volume":"137","author":"Falker","year":"2016","journal-title":"J Neurochem"},{"key":"R41-20260525","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1038\/nn.4648","article-title":"Alpha-synuclein interacts with PrPC to induce cognitive impairment through mGluR5 and NMDAR2B","volume":"20","author":"Ferreira","year":"2017","journal-title":"Nat Neurosci"},{"key":"R42-20260525","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1002\/j.1460-2075.1996.tb00467.x","article-title":"Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie","volume":"15","author":"Fischer","year":"1996","journal-title":"EMBO J"},{"key":"R43-20260525","doi-asserted-by":"crossref","first-page":"7857","DOI":"10.1074\/jbc.M112.423954","article-title":"An N-terminal fragment of the prion protein binds to amyloid-beta oligomers and inhibits their neurotoxicity in vivo","volume":"288","author":"Fluharty","year":"2013","journal-title":"J Biol Chem"},{"key":"R44-20260525","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/ncomms1341","article-title":"Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites","volume":"2","author":"Freir","year":"2011","journal-title":"Nat Commun"},{"key":"R45-20260525","doi-asserted-by":"crossref","first-page":"e9","DOI":"10.1038\/mtna.2011.6","article-title":"Intracerebral infusion of antisense oligonucleotides into prion-infected mice","volume":"1","author":"Friberg","year":"2012","journal-title":"Mol Ther Nucleic Acids"},{"key":"R46-20260525","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/s41594-022-00814-7","article-title":"2022) A conformational switch controlling the toxicity of the prion protein","volume":"29","author":"Frontzek","journal-title":"Nat Struct Mol Biol"},{"key":"R47-20260525","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1089\/ars.2014.6032","article-title":"Prion protein and copper cooperatively protect neurons by modulating NMDA receptor through S-nitrosylation","volume":"22","author":"Gasperini","year":"2015","journal-title":"Antioxid Redox Signal"},{"key":"R48-20260525","doi-asserted-by":"crossref","first-page":"18524","DOI":"10.1074\/jbc.M210723200","article-title":"Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells","volume":"278","author":"Gilch","year":"2003","journal-title":"J Biol Chem"},{"key":"R49-20260525","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1007\/s00401-019-02053-5","article-title":"A\u03b2-induced acceleration of Alzheimer-related \u03c4-pathology spreading and its association with prion protein","volume":"138","author":"Gomes","year":"2019","journal-title":"Acta Neuropathol"},{"key":"R50-20260525","doi-asserted-by":"crossref","first-page":"101642","DOI":"10.1016\/j.jbc.2022.101642","article-title":"Cellular prion protein in human plasma-derived extracellular vesicles promotes neurite outgrowth via the NMDA receptor-LRP1 receptor system","volume":"298","author":"Gonias","year":"2022","journal-title":"J Biol Chem"},{"key":"R51-20260525","doi-asserted-by":"crossref","first-page":"33489","DOI":"10.1074\/jbc.M111.278556","article-title":"Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein","volume":"286","author":"Griffiths","year":"2011","journal-title":"J Biol Chem"},{"key":"R52-20260525","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1002\/glia.22963","article-title":"Improvement of neuronal cell survival by astrocyte-derived exosomes under hypoxic and ischemic conditions depends on prion protein","volume":"64","author":"Guitart","year":"2016","journal-title":"Glia"},{"key":"R53-20260525","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1242\/jcs.043604","article-title":"Dominant roles of the polybasic proline motif and copper in the PrP23-89-mediated stress protection response","volume":"122","author":"Haigh","year":"2009","journal-title":"J Cell Sci"},{"key":"R54-20260525","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/s00401-022-02461-0","article-title":"Cryo-EM structures of prion protein filaments from Gerstmann-Str\u00e4ussler-Scheinker disease","volume":"144","author":"Hallinan","year":"2022","journal-title":"Acta Neuropathol"},{"key":"R55-20260525","doi-asserted-by":"crossref","first-page":"17041","DOI":"10.1074\/jbc.M114.610204","article-title":"Inside-out regulation of ectodomain cleavage of cluster-of-differentiation-44 (CD44) and of neuregulin-1 requires substrate dimerization","volume":"290","author":"Hartmann","year":"2015","journal-title":"J Biol Chem"},{"key":"R56-20260525","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1126\/science.1063093","article-title":"Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies","volume":"294","author":"Heppner","year":"2001","journal-title":"Science"},{"key":"R57-20260525","doi-asserted-by":"crossref","first-page":"e1004808","DOI":"10.1371\/journal.ppat.1004808","article-title":"Correction:prion infections and anti-PrP antibodies trigger converging neurotoxic pathways","volume":"11","author":"Herrmann","year":"2015","journal-title":"PLoS Pathog"},{"key":"R58-20260525","doi-asserted-by":"crossref","first-page":"101911","DOI":"10.1016\/j.jbc.2022.101911","article-title":"The transmembrane domain of the amyloid precursor protein is required for antiamyloidogenic processing by \u03b1-secretase ADAM10","volume":"298","author":"Hitschler","year":"2022","journal-title":"J Biol Chem"},{"key":"R59-20260525","doi-asserted-by":"crossref","first-page":"e108375","DOI":"10.15252\/embj.2021108375","article-title":"Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites","volume":"40","author":"Hoffmann","year":"2021","journal-title":"EMBO J"},{"key":"R60-20260525","doi-asserted-by":"crossref","first-page":"4005","DOI":"10.1038\/s41467-022-30458-6","article-title":"Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains","volume":"13","author":"Hoyt","year":"2022","journal-title":"Nat Commun"},{"key":"R61-20260525","doi-asserted-by":"crossref","first-page":"1932","DOI":"10.1016\/j.celrep.2018.04.040","article-title":"Extracellular forms of A\u03b2and Tau from iPSC models of Alzheimer's disease disrupt synaptic plasticity","volume":"23","author":"Hu","year":"2018","journal-title":"Cell Rep"},{"key":"R62-20260525","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.cell.2005.08.014","article-title":"Adam meets Eph:an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans","volume":"123","author":"Janes","year":"2005","journal-title":"Cell"},{"key":"R63-20260525","doi-asserted-by":"crossref","first-page":"4833","DOI":"10.1523\/JNEUROSCI.5221-09.2010","article-title":"The disintegrin\/metalloproteinase ADAM10 is essential for the establishment of the brain cortex","volume":"30","author":"Jorissen","year":"2010","journal-title":"J Neurosci"},{"key":"R64-20260525","doi-asserted-by":"crossref","first-page":"e51305","DOI":"10.1371\/journal.pone.0051305","article-title":"Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development","volume":"7","author":"Kaiser","year":"2012","journal-title":"PLoS One"},{"key":"R65-20260525","doi-asserted-by":"crossref","first-page":"e1009628","DOI":"10.1371\/journal.ppat.1009628","article-title":"The ultrastructure of infectious L-type bovine spongiform encephalopathy prions constrains molecular models","volume":"17","author":"Kamali-Jamil","year":"2021","journal-title":"PLoS Pathog"},{"key":"R66-20260525","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1083\/jcb.200711002","article-title":"Prion protein attenuates excitotoxicity by inhibiting NMDA receptors","volume":"181","author":"Khosravani","year":"2008","journal-title":"J Cell Biol"},{"key":"R67-20260525","doi-asserted-by":"crossref","first-page":"6140","DOI":"10.1523\/JNEUROSCI.3526-13.2014","article-title":"Peripheral administration of a humanized anti-PrP antibody blocks Alzheimer's disease Abeta synaptotoxicity","volume":"34","author":"Klyubin","year":"2014","journal-title":"J Neurosci"},{"key":"R68-20260525","doi-asserted-by":"crossref","first-page":"12822","DOI":"10.1074\/jbc.RA120.012601","article-title":"The tetraspanin Tspan15 is an essential subunit of an ADAM10 scissor complex","volume":"295","author":"Koo","year":"2020","journal-title":"J Biol Chem"},{"key":"R69-20260525","doi-asserted-by":"crossref","first-page":"17415","DOI":"10.1074\/jbc.M115.643577","article-title":"Prion-protein-interacting amyloid-beta oligomers of high molecular weight are tightly correlated with memory impairment in multiple Alzheimer mouse models","volume":"290","author":"Kostylev","year":"2015","journal-title":"J Biol Chem"},{"key":"R70-20260525","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.3390\/ijms23031232","article-title":"Prion protein:the molecule of many forms and faces","volume":"23","author":"Kova\u010d","year":"2022","journal-title":"Int J Mol Sci"},{"key":"R71-20260525","doi-asserted-by":"crossref","first-page":"4540","DOI":"10.1016\/j.molcel.2021.08.011","article-title":"High-resolution structure and strain comparison of infectious mammalian prions","volume":"81","author":"Kraus","year":"2021","journal-title":"Mol Cell"},{"key":"R72-20260525","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1038\/nature19312","article-title":"The prion protein is an agonistic ligand of the G protein-coupled receptor Adgrg6","volume":"536","author":"K\u00fcffer","year":"2016","journal-title":"Nature"},{"key":"R73-20260525","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1038\/emboj.2010.167","article-title":"ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons","volume":"29","author":"Kuhn","year":"2010","journal-title":"EMBO J"},{"key":"R74-20260525","doi-asserted-by":"crossref","first-page":"e13056","DOI":"10.1111\/bpa.13056","article-title":"Glial activation in prion diseases is selectively triggered by neuronal PrPSc","volume":"32","author":"Lakkaraju","year":"2022","journal-title":"Brain Pathol"},{"key":"R75-20260525","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1038\/nature07761","article-title":"Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers","volume":"457","author":"Laur\u00e9n","year":"2009","journal-title":"Nature"},{"key":"R76-20260525","doi-asserted-by":"crossref","first-page":"198","DOI":"10.4161\/pri.1.3.4870","article-title":"Toxic effects of intracerebral PrP antibody administration during the course of BSE infection in mice","volume":"1","author":"Lefebvre-Roque","year":"2007","journal-title":"Prion"},{"key":"R77-20260525","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1080\/19336896.2020.1854034","article-title":"On the role of the cellular prion protein in the uptake and signaling of pathological aggregates in neurodegenerative diseases","volume":"14","author":"Legname","year":"2020","journal-title":"Prion"},{"key":"R78-20260525","doi-asserted-by":"crossref","first-page":"e88797","DOI":"10.1371\/journal.pone.0088797","article-title":"Systemic delivery of siRNA down regulates brain prion protein and ameliorates neuropathology in prion disorder","volume":"9","author":"Lehmann","year":"2014","journal-title":"PLoS One"},{"key":"R79-20260525","first-page":"218","article-title":"Protein-protein interactions in the tetraspanin web","volume":"20","author":"Levy","year":"2005","journal-title":"Physiology (Bethesda)"},{"key":"R80-20260525","doi-asserted-by":"crossref","first-page":"2128","DOI":"10.1016\/j.bbamcr.2017.06.022","article-title":"Diverse functions of the prion protein \u2013Does proteolytic processing hold the key?","volume":"1864","author":"Linsenmeier","year":"2017","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"R81-20260525","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/s13024-018-0248-6","article-title":"Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein","volume":"13","author":"Linsenmeier","year":"2018","journal-title":"Mol Neurodegener"},{"key":"R82-20260525","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1126\/sciadv.abj1826","article-title":"Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies","volume":"7","author":"Linsenmeier","year":"2021","journal-title":"Sci Adv"},{"key":"R83-20260525","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.str.2021.10.007","article-title":"Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site","volume":"30","author":"Lipper","year":"2022","journal-title":"Structure"},{"key":"R84-20260525","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1750-1326-4-17","article-title":"LRP1 shedding in human brain:roles of ADAM10 and ADAM17","volume":"4","author":"Liu","year":"2009","journal-title":"Mol Neurodegener"},{"key":"R85-20260525","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1096\/fj.11-185579","article-title":"Neuritogenesis:the prion protein controls beta1 integrin signaling activity","volume":"26","author":"Loubet","year":"2011","journal-title":"FASEB J"},{"key":"R86-20260525","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.brainres.2006.04.056","article-title":"Role of cellular prion protein on LTP expression in aged mice","volume":"1097","author":"Maglio","year":"2006","journal-title":"Brain Res"},{"key":"R87-20260525","doi-asserted-by":"crossref","first-page":"e55","DOI":"10.1371\/journal.pbio.1000055","article-title":"Regulation of embryonic cell adhesion by the prion protein","volume":"7","author":"M\u00e1laga-Trillo","year":"2009","journal-title":"PLoS Biol"},{"key":"R88-20260525","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.1090187","article-title":"Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis","volume":"302","author":"Mallucci","year":"2003","journal-title":"Science"},{"key":"R89-20260525","doi-asserted-by":"crossref","first-page":"14178","DOI":"10.1074\/jbc.RA120.013779","article-title":"A soluble derivative of PrPC activates cell-signaling and regulates cell physiology through LRP1 and the NMDA receptor","volume":"295","author":"Mantuano","year":"2020","journal-title":"J Biol Chem"},{"key":"R90-20260525","doi-asserted-by":"crossref","first-page":"85","DOI":"10.4049\/jimmunol.2100412","article-title":"A soluble PrPC derivative and membrane-anchored PrPC in extracellular vesicles attenuate innate immunity by engaging the NMDA-R\/LRP1 receptor complex","volume":"208","author":"Mantuano","year":"2022","journal-title":"J Immunol"},{"key":"R91-20260525","doi-asserted-by":"crossref","first-page":"345","DOI":"10.3390\/ijms20020345","article-title":"Cellular and molecular mechanisms mediated by recPrP C involved in the neuronal differentiation process of mesenchymal stem cells","volume":"20","author":"Martellucci","year":"2019","journal-title":"Int J Mol Sci"},{"key":"R92-20260525","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s12915-021-01203-0","article-title":"Analysis of co-isogenic prion protein deficient mice reveals behavioral deficits, learning impairment, and enhanced hippocampal excitability","volume":"20","author":"Matamoros-Angles","year":"2022","journal-title":"BMC Biol"},{"key":"R93-20260525","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0002-9440(10)63291-9","article-title":"Prion protein accumulation and neuroprotection in hypoxic brain damage","volume":"165","author":"Mclennan","year":"2004","journal-title":"Am J Pathol"},{"key":"R94-20260525","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S1474-4422(22)00082-5","article-title":"Prion protein monoclonal antibody (PRN100) therapy for Creutzfeldt\u2013Jakob disease:evaluation of a first-in-human treatment programme","volume":"21","author":"Mead","year":"2022","journal-title":"Lancet Neurol"},{"key":"R95-20260525","doi-asserted-by":"crossref","first-page":"10615","DOI":"10.1093\/nar\/gkaa616","article-title":"Prion protein lowering is a disease-modifying therapy across prion disease stages, strains and endpoints","volume":"48","author":"Minikel","year":"2020","journal-title":"Nucleic Acids Res"},{"key":"R96-20260525","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1111\/j.1750-3639.2007.00061.x","article-title":"The role of the octarepeat region in neuroprotective function of the cellular prion protein","volume":"17","author":"Mitteregger","year":"2007","journal-title":"Brain Pathol"},{"key":"R97-20260525","article-title":"Anchorless risk or released benefit?An updated view on the ADAM10-mediated shedding of the prion protein","author":"Mohammadi","year":"2022","journal-title":"Cell Tissue Res"},{"key":"R98-20260525","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1074\/jbc.M308578200","article-title":"The cellular prion protein PrPc is expressed in human enterocytes in cell-cell junctional domains","volume":"279","author":"Morel","year":"2004","journal-title":"J Biol Chem"},{"key":"R99-20260525","doi-asserted-by":"crossref","first-page":"101478","DOI":"10.1016\/j.jbc.2021.101478","article-title":"Aptamers targeting amyloidogenic proteins and their emerging role in neurodegenerative diseases","volume":"298","author":"Murakami","year":"2022","journal-title":"J Biol Chem"},{"key":"R100-20260525","doi-asserted-by":"crossref","first-page":"e1009511","DOI":"10.1371\/journal.ppat.1009511","article-title":"Correction:site-specific analysis of N-glycans from different sheep prion strains","volume":"17","author":"Naki\u0107","year":"2021","journal-title":"PLoS Pathog"},{"key":"R101-20260525","doi-asserted-by":"crossref","first-page":"166209","DOI":"10.1016\/j.bbadis.2021.166209","article-title":"Neurotoxicity of oligomers of phosphorylated Tau protein carrying tauopathy-associated mutation is inhibited by prion protein","volume":"1867","author":"Nieznanska","year":"2021","journal-title":"Biochim Biophys acta Mol basis Dis"},{"key":"R102-20260525","doi-asserted-by":"crossref","first-page":"10595","DOI":"10.1523\/JNEUROSCI.1700-18.2018","article-title":"Cellular prion protein mediates the disruption of hippocampal synaptic plasticity by soluble Tau in vivo","volume":"38","author":"Ondrejcak","year":"2018","journal-title":"J Neurosci"},{"key":"R103-20260525","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1242\/jcs.021816","article-title":"LRP1 controls biosynthetic and endocytic trafficking of neuronal prion protein","volume":"121","author":"Parkyn","year":"2008","journal-title":"J Cell Sci"},{"key":"R104-20260525","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1080\/19336896.2020.1714373","article-title":"The cellular prion protein promotes neuronal regeneration after acute nasotoxic injury","volume":"14","author":"Parrie","year":"2020","journal-title":"Prion"},{"key":"R105-20260525","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/35089090","article-title":"Antibodies inhibit prion propagation and clear cell cultures of prion infectivity","volume":"412","author":"Peretz","year":"2001","journal-title":"Nature"},{"key":"R106-20260525","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1111\/j.1471-4159.2004.02356.x","article-title":"Anti-PrP antibodies block PrPSc replication in prion-infected cell cultures by accelerating PrPC degradation","volume":"89","author":"Perrier","year":"2004","journal-title":"J Neurochem"},{"key":"R107-20260525","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX:structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci"},{"key":"R108-20260525","doi-asserted-by":"crossref","first-page":"e3872","DOI":"10.1371\/journal.pone.0003872","article-title":"The POM monoclonals:a comprehensive set of antibodies to non-overlapping prion protein epitopes","volume":"3","author":"Polymenidou","year":"2008","journal-title":"PLoS One"},{"key":"R109-20260525","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/ana.410120102","article-title":"Kuru with incubation periods exceeding two decades","volume":"12","author":"Prusiner","year":"1982","journal-title":"Ann Neurol"},{"key":"R110-20260525","doi-asserted-by":"crossref","first-page":"e24624","DOI":"10.1371\/journal.pone.0024624","article-title":"N-glycans and glycosylphosphatidylinositol-anchor act on polarized sorting of mouse PrP(C) in Madin-Darby canine kidney cells","volume":"6","author":"Puig","year":"2011","journal-title":"PLoS One"},{"key":"R111-20260525","doi-asserted-by":"crossref","first-page":"e1007520","DOI":"10.1371\/journal.ppat.1007520","article-title":"GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice","volume":"15","author":"Puig","year":"2019","journal-title":"PLoS Pathog"},{"key":"R112-20260525","doi-asserted-by":"crossref","first-page":"e11085","DOI":"10.1371\/journal.pone.0011085","article-title":"Liposome-siRNA-peptide complexes cross the blood-brain barrier and significantly decrease PrP on neuronal cells and PrP in infected cell cultures","volume":"5","author":"Pulford","year":"2010","journal-title":"PLoS One"},{"key":"R113-20260525","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1080\/19336896.2017.1336274","article-title":"Ultrastructure and pathology of prion protein amyloid accumulation and cellular damage in extraneural tissues of scrapie-infected transgenic mice expressing anchorless prion protein","volume":"11","author":"Race","year":"2017","journal-title":"Prion"},{"key":"R114-20260525","doi-asserted-by":"crossref","first-page":"e131175","DOI":"10.1172\/jci.insight.131175","article-title":"Antisense oligonucleotides extend survival of prion-infected mice","volume":"5","author":"Raymond","year":"2019","journal-title":"JCI Insight"},{"key":"R115-20260525","doi-asserted-by":"crossref","first-page":"9493","DOI":"10.1038\/s41598-022-13455-z","article-title":"A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody","volume":"12","author":"Reilly","year":"2022","journal-title":"Sci Rep"},{"key":"R116-20260525","doi-asserted-by":"crossref","first-page":"e1005401","DOI":"10.1371\/journal.ppat.1005401","article-title":"Differential toxicity of antibodies to the prion protein","volume":"12","author":"Reimann","year":"2016","journal-title":"PLoS Pathog"},{"key":"R117-20260525","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1038\/emboj.2011.86","article-title":"The cellular prion protein mediates neurotoxic signalling of \u03b2-sheet-rich conformers independent of prion replication","volume":"30","author":"Resenberger","year":"2011","journal-title":"EMBO J"},{"key":"R118-20260525","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/s42003-020-1085-z","article-title":"Clustering of human prion protein and \u03b1-synuclein oligomers requires the prion protein N-terminus","volume":"3","author":"R\u00f6sener","year":"2020","journal-title":"Commun Biol"},{"key":"R119-20260525","doi-asserted-by":"crossref","first-page":"13044","DOI":"10.1073\/pnas.96.23.13044","article-title":"Glycosylation differences between the normal and pathogenic prion protein isoforms","volume":"96","author":"Rudd","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R120-20260525","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1681\/ASN.2020081213","article-title":"ADAM10-mediated ectodomain shedding is an essential driver of podocyte damage","volume":"32","author":"Sachs","year":"2021","journal-title":"J Am Soc Nephrol"},{"key":"R121-20260525","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pneurobio.2015.10.003","article-title":"The alpha secretase ADAM10:a metalloprotease with multiple functions in the brain","volume":"135","author":"Saftig","year":"2015","journal-title":"Prog Neurobiol"},{"key":"R122-20260525","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1042\/BST20160296","article-title":"Regulation of the trafficking and the function of the metalloprotease ADAM10 by tetraspanins","volume":"45","author":"Saint-Pol","year":"2017","journal-title":"Biochem Soc Trans"},{"key":"R123-20260525","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nature09768","article-title":"Prion propagation and toxicity in vivo occur in two distinct mechanistic phases","volume":"470","author":"Sandberg","year":"2011","journal-title":"Nature"},{"key":"R124-20260525","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1083\/jcb.200409127","article-title":"Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth","volume":"169","author":"Santuccione","year":"2005","journal-title":"J Cell Biol"},{"key":"R125-20260525","doi-asserted-by":"crossref","first-page":"26335","DOI":"10.1074\/jbc.M110.106435","article-title":"A disintegrin and metalloproteinase-10 (ADAM-10) mediates DN30 antibody-induced shedding of the met surface receptor","volume":"285","author":"Schelter","year":"2010","journal-title":"J Biol Chem"},{"key":"R126-20260525","doi-asserted-by":"crossref","first-page":"4408","DOI":"10.1016\/j.jmb.2020.05.020","article-title":"Both N-terminal and C-terminal histidine residues of the prion protein are essential for copper coordination and neuroprotective self-regulation","volume":"432","author":"Schilling","year":"2020","journal-title":"J Mol Biol"},{"key":"R127-20260525","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1006\/jmbi.2000.5183","article-title":"Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein","volume":"314","author":"Schmitt-Ulms","year":"2001","journal-title":"J Mol Biol"},{"key":"R128-20260525","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1007\/s12035-014-8655-3","article-title":"Loss of prion protein leads to age-dependent behavioral abnormalities and changes in cytoskeletal protein expression","volume":"50","author":"Schmitz","year":"2014","journal-title":"Mol Neurobiol"},{"key":"R129-20260525","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.nbd.2016.03.001","article-title":"Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by A\u03b2oligomers:implications for novel therapeutic strategy in Alzheimer's disease","volume":"91","author":"Scott-McKean","year":"2016","journal-title":"Neurobiol Dis"},{"key":"R130-20260525","doi-asserted-by":"crossref","first-page":"1638","DOI":"10.1016\/j.cell.2017.11.014","article-title":"Structural basis for regulated proteolysis by the \u03b1-secretase ADAM10","volume":"171","author":"Seegar","year":"2017","journal-title":"Cell"},{"key":"R131-20260525","doi-asserted-by":"crossref","first-page":"3251","DOI":"10.1007\/s00018-018-2791-2","article-title":"In vivo regulation of the A disintegrin and metalloproteinase 10 (ADAM10) by the tetraspanin 15","volume":"75","author":"Seipold","year":"2018","journal-title":"Cell Mol Life Sci"},{"key":"R132-20260525","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1172\/JCI131564","article-title":"Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease","volume":"130","author":"Sevillano","year":"2020","journal-title":"J Clin Invest"},{"key":"R133-20260525","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/s12987-016-0038-x","article-title":"Inhibition of ADAM10 promotes the clearance of A\u03b2across the BBB by reducing LRP1 ectodomain shedding","volume":"13","author":"Shackleton","year":"2016","journal-title":"Fluids Barriers CNS"},{"key":"R134-20260525","doi-asserted-by":"crossref","first-page":"123","DOI":"10.4049\/jimmunol.167.1.123","article-title":"Antibody-induced shedding of CD44 from adherent cells is linked to the assembly of the cytoskeleton","volume":"167","author":"Shi","year":"2001","journal-title":"J Immunol"},{"key":"R135-20260525","doi-asserted-by":"crossref","first-page":"8967","DOI":"10.1523\/JNEUROSCI.1115-05.2005","article-title":"Overexpression of PrPC by adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model","volume":"25","author":"Shyu","year":"2005","journal-title":"J Neurosci"},{"key":"R136-20260525","doi-asserted-by":"crossref","first-page":"21857","DOI":"10.1074\/jbc.M116.743435","article-title":"The N terminus of the prion protein mediates functional interactions with the neuronal cell adhesion molecule (NCAM) fibronectin domain","volume":"291","author":"Slapsak","year":"2016","journal-title":"J Biol Chem"},{"key":"R137-20260525","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1126\/science.1094273","article-title":"Cross-linking cellular prion protein triggers neuronal apoptosis in vivo","volume":"303","author":"Solforosi","year":"2004","journal-title":"Science"},{"key":"R138-20260525","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/nature12402","article-title":"The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein","volume":"501","author":"Sonati","year":"2013","journal-title":"Nature"},{"key":"R139-20260525","doi-asserted-by":"crossref","first-page":"e1007864","DOI":"10.1371\/journal.ppat.1007864","article-title":"Full atomistic model of prion structure and conversion","volume":"15","author":"Spagnolli","year":"2019","journal-title":"PLoS Pathog"},{"key":"R140-20260525","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0092-8674(87)90150-4","article-title":"Scrapie prion protein contains a phosphatidylinositol glycolipid","volume":"51","author":"Stahl","year":"1987","journal-title":"Cell"},{"key":"R141-20260525","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.1073\/pnas.0511290103","article-title":"Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis","volume":"103","author":"Steele","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R142-20260525","doi-asserted-by":"crossref","first-page":"83","DOI":"10.4161\/pri.1.2.4346","article-title":"The prion protein knockout mouse:a phenotype under challenge","volume":"1","author":"Steele","year":"2007","journal-title":"Prion"},{"key":"R143-20260525","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1042\/BJ20061736","article-title":"The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein","volume":"402","author":"Taylor","year":"2007","journal-title":"Biochem J"},{"key":"R144-20260525","doi-asserted-by":"crossref","first-page":"22590","DOI":"10.1074\/jbc.M109.032599","article-title":"Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein","volume":"284","author":"Taylor","year":"2009","journal-title":"J Biol Chem"},{"key":"R145-20260525","doi-asserted-by":"crossref","first-page":"4003","DOI":"10.1038\/s41467-022-31460-8","article-title":"The shape of things to come:structural insights into how prion proteins encipher heritable information","volume":"13","author":"Telling","year":"2022","journal-title":"Nat Commun"},{"key":"R146-20260525","doi-asserted-by":"crossref","first-page":"12580","DOI":"10.1073\/pnas.95.21.12580","article-title":"Doxycycline control of prion protein transgene expression modulates prion disease in mice","volume":"95","author":"Tremblay","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R147-20260525","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1080\/19336896.2017.1334748","article-title":"The cellular prion protein (PrPC) as neuronal receptor for alpha-synuclein","volume":"11","author":"Urrea","year":"2017","journal-title":"Prion"},{"key":"R148-20260525","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1007\/s12035-014-8793-7","article-title":"Role of PrP(C) expression in Tau protein levels and phosphorylation in Alzheimer's disease evolution","volume":"51","author":"Vergara","year":"2015","journal-title":"Mol Neurobiol"},{"key":"R149-20260525","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1111\/j.1528-1157.1999.tb01583.x","article-title":"Increased sensitivity to seizures in mice lacking cellular prion protein","volume":"40","author":"Walz","year":"1999","journal-title":"Epilepsia"},{"key":"R150-20260525","doi-asserted-by":"crossref","first-page":"35914","DOI":"10.1074\/jbc.M507327200","article-title":"Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress","volume":"280","author":"Watt","year":"2005","journal-title":"J Biol Chem"},{"key":"R151-20260525","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1161\/01.STR.0000217262.03192.d4","article-title":"Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury","volume":"37","author":"Weise","year":"2006","journal-title":"Stroke"},{"key":"R152-20260525","doi-asserted-by":"crossref","first-page":"10238","DOI":"10.1073\/pnas.0802759105","article-title":"Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease","volume":"105","author":"White","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R153-20260525","doi-asserted-by":"crossref","first-page":"498","DOI":"10.4161\/pri.22588","article-title":"Separate mechanisms act concurrently to shed and release the prion protein from the cell","volume":"6","author":"Wik","year":"2012","journal-title":"Prion"},{"key":"R154-20260525","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1034\/j.1600-0854.2003.00088.x","article-title":"Inhibition of complex glycosylation increases the formation of PrPsc","volume":"4","author":"Winklhofer","year":"2003","journal-title":"Traffic"},{"key":"R155-20260525","doi-asserted-by":"crossref","first-page":"e23473","DOI":"10.7554\/eLife.23473","article-title":"The N-terminus of the prion protein is a toxic effector regulated by the C-terminus","volume":"6","author":"Wu","year":"2017","journal-title":"Elife"},{"key":"R156-20260525","doi-asserted-by":"crossref","first-page":"8763","DOI":"10.1073\/pnas.1807439115","article-title":"N-glycan microheterogeneity regulates interactions of plasma proteins","volume":"115","author":"Wu","year":"2018","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R157-20260525","doi-asserted-by":"crossref","first-page":"13486","DOI":"10.1038\/s41598-018-31650-9","article-title":"Glycosylation significantly inhibits the aggregation of human prion protein and decreases its cytotoxicity","volume":"8","author":"Yi","year":"2018","journal-title":"Sci Rep"},{"key":"R158-20260525","doi-asserted-by":"crossref","first-page":"13090","DOI":"10.1074\/jbc.RA118.003319","article-title":"Prion protein stabilizes amyloid-\u03b2(A\u03b2) oligomers and enhances A\u03b2neurotoxicity in a Drosophila model of Alzheimer's disease","volume":"293","author":"Younan","year":"2018","journal-title":"J Biol Chem"},{"key":"R159-20260525","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1111\/j.1742-4658.2008.06346.x","article-title":"Branched N-glycans regulate the biological functions of integrins and cadherins","volume":"275","author":"Zhao","year":"2008","journal-title":"FEBS J"}],"container-title":["Neural Regeneration Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.ovid.com\/10.4103\/1673-5374.366496","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T19:30:57Z","timestamp":1786735857000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.ovid.com\/10.4103\/1673-5374.366496"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1,5]]},"references-count":159,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2023]]}},"URL":"https:\/\/doi.org\/10.4103\/1673-5374.366496","relation":{},"ISSN":["1673-5374","1876-7958"],"issn-type":[{"value":"1673-5374","type":"print"},{"value":"1876-7958","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,1,5]]},"assertion":[{"value":"2022-08-12","name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2022-11-30","name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}}]}}