US 6890535B1
· Schenk
· 2005
[cited by applicant]
US 7306945B2
· Chilcote et al.
· 2007
[cited by applicant]
US 7358331B2
· Chilcote et al.
· 2008
[cited by applicant]
US 7727957B2
· Schenk et al.
· 2010
[cited by applicant]
US 7910333B2
· Chilcote et al.
· 2011
[cited by applicant]
US 7919088B2
· Schenk et al.
· 2011
[cited by applicant]
US 7977316B2
· Schenk
· 2011
[cited by applicant]
US 8092801B2
· Schenk et al.
· 2012
[cited by applicant]
US 8147833B2
· Schenk et al.
· 2012
[cited by applicant]
US 8506959B2
· Schenk et al.
· 2013
[cited by applicant]
US 8609820B2
· Saldanha et al.
· 2013
[cited by applicant]
US 8632776B2
· Nordström et al.
· 2014
[cited by applicant]
US 8673593B2
· Chilcote et al.
· 2014
[cited by applicant]
US 8741293B2
· Dodel et al.
· 2014
[cited by applicant]
US 8790644B2
· Saldanha et al.
· 2014
[cited by applicant]
US 8809506B2
· Lannfelt et al.
· 2014
[cited by applicant]
US 8940276B2
· Weihofen et al.
· 2015
[cited by applicant]
US 8968734B2
· Nordström et al.
· 2015
[cited by applicant]
US 9315569B2
· Lannfelt et al.
· 2016
[cited by applicant]
US 9493553B2
· Kaluza et al.
· 2016
[cited by applicant]
US 9605056B2
· Barbour et al.
· 2017
[cited by applicant]
US 9670274B2
· Kaluza et al.
· 2017
[cited by applicant]
US 9732148B2
· Ayalon et al.
· 2017
[cited by applicant]
US 9890209B2
· Kaluza et al.
· 2018
[cited by applicant]
US 9896504B2
· Weihofen et al.
· 2018
[cited by applicant]
US 20080014194A1
· Schenk et al.
· 2008
[cited by applicant]
US 20160060331A1
· Schenk et al.
· 2016
[cited by applicant]
US 20170320940A1
· Ayalon et al.
· 2017
[cited by applicant]
US 20170349651A1
· Schenk et al.
· 2017
[cited by applicant]
US 20180134775A1
· El-Agnaf et al.
· 2018
[cited by applicant]
US 20180134776A1
· El-Agnaf et al.
· 2018
[cited by applicant]
US 20180134777A1
· El-Agnaf et al.
· 2018
[cited by applicant]
DE 102011008153A1
· 2012
[cited by applicant]
EP 1185296B1
· 2011
[cited by applicant]
EP 2371396B1
· 2014
[cited by applicant]
EP 2272539B1
· 2014
[cited by applicant]
EP 2807188B1
· 2014
[cited by applicant]
EP 2370466B1
· 2015
[cited by applicant]
EP 1578253B1
· 2015
[cited by applicant]
EP 2903648B1
· 2015
[cited by applicant]
EP 2949666B1
· 2015
[cited by applicant]
EP 2583978B1
· 2016
[cited by applicant]
EP 3067066B1
· 2016
[cited by applicant]
EP 2450056B1
· 2017
[cited by applicant]
EP 2361928B1
· 2017
[cited by applicant]
EP 1633189B1
· 2017
[cited by applicant]
EP 2539366B1
· 2017
[cited by applicant]
EP 2723379B1
· 2018
[cited by applicant]
EP 3369433A1
· 2018
[cited by applicant]
EP 2282758B1
· 2018
[cited by applicant]
WO 2002050121A1
· 2002
[cited by applicant]
WO 2004041067A3
· 2004
[cited by applicant]
WO 2005013889A3
· 2005
[cited by applicant]
WO 2005047860A3
· 2005
[cited by applicant]
WO 2006020581A3
· 2006
[cited by applicant]
WO 2006045037A3
· 2006
[cited by applicant]
WO 2007012061A3
· 2007
[cited by applicant]
WO 2007011907A2
· 2007
[cited by applicant]
WO 2007021255A1
· 2007
[cited by applicant]
WO 2008103472A3
· 2008
[cited by applicant]
WO 2009133521A3
· 2009
[cited by applicant]
WO 2010069603A1
· 2010
[cited by applicant]
WO 2011104696A1
· 2011
[cited by applicant]
WO 2011107544A1
· 2011
[cited by applicant]
WO 2012061785A3
· 2012
[cited by applicant]
WO 2012061786A1
· 2012
[cited by applicant]
WO 2012177972A1
· 2012
[cited by applicant]
WO 2013063516A1
· 2013
[cited by applicant]
WO 2013112945A1
· 2013
[cited by applicant]
WO 2013180201A1
· 2013
[cited by applicant]
WO 2014058924A3
· 2014
[cited by applicant]
WO 2014132210A1
· 2014
[cited by applicant]
WO 2015001504A2
· 2015
[cited by applicant]
WO 2015051159A1
· 2015
[cited by applicant]
WO 2015075011A1
· 2015
[cited by applicant]
WO 2015075635A2
· 2015
[cited by applicant]
WO 2015155694A1
· 2015
[cited by applicant]
WO 2015179867A1
· 2015
[cited by applicant]
WO 2015197772A1
· 2015
[cited by applicant]
WO 2016040903A1
· 2016
[cited by applicant]
WO 2016040905A1
· 2016
[cited by applicant]
WO 2016040907A1
· 2016
[cited by applicant]
WO 2016061389A3
· 2016
[cited by applicant]
WO 2017009312A1
· 2017
[cited by applicant]
WO 2017033152A1
· 2017
[cited by applicant]
WO 2017091512A1
· 2017
[cited by applicant]
WO 2017176835A2
· 2017
[cited by applicant]
WO 2017207739A1
· 2017
[cited by applicant]
WO 2018007817A1
· 2018
[cited by applicant]
WO 2018039147A1
· 2018
[cited by applicant]
WO 2018091444A1
· 2018
[cited by applicant]
WO 2018109058A1
· 2018
[cited by applicant]
WO 2018111670A3
· 2018
[cited by applicant]
WO 2018115225A1
· 2018
[cited by applicant]
WO 2018128454A1
· 2018
[cited by applicant]
WO 2018128722A1
· 2018
[cited by applicant]
WO 2018151821A1
· 2018
[cited by applicant]
WO 2018178950A1
· 2018
[cited by applicant]
WO 2018213440A1
· 2018
[cited by applicant]
WO 2018237338A1
· 2018
[cited by applicant]
WO 2019115674A1
· 2019
[cited by applicant]
Almandoz-Gil et al., “Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways,” Free Radical Biology and Medicine 110:421-431 (2017).
[cited by applicant]
Anderson et al., “Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease,” J Biol Chem 281:29739-29752 (2006).
[cited by applicant]
Assayag et al., “Polyunsaturated fatty acids induce a-synuclein-related pathogenic changes in neuronal cells,” Am J Pathology 171(6):2000-2011 (2007).
[cited by applicant]
Baba et al., “Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies,” Am J Pathology 152(4):879-884 (1998).
[cited by applicant]
Bae et al., “Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of α-synuclein,” Antioxid. Redox Signal 18(7):770-783 (2013).
[cited by applicant]
Bengoa-Vergniory et al., “Alpha-synuclein oligomers: a new hope,” J. Acta Neuropathol 134:819-838 (2017).
[cited by applicant]
Bergström et al., “Development of Passive Immunotherapies for Synucleinopathies,” Movement Disorders 31(2):203-213 (2016).
[cited by applicant]
Bloch et al., “α-Synuclein pathology of the spinal and peripheral autonomic nervous system in neurologically unimpaired elderly subjects,” Neuropathology and Applied Neurobiology 32:284-295 (2006).
[cited by applicant]
Bosco et al., “Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate α-synuclein fibrilization,” Nature Chemical Biology 2(5):249-253 (2006).
[cited by applicant]
Chen et al., “Enhancement and destruction of antibody function by somatic mutation: unequal occurrence is controlled byV gene combinatorial associations” EMBO 14(12):2784-2794 (1995).
[cited by applicant]
Cole et al., “Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein,” JBC 277(8):6344-6352 (2002).
[cited by applicant]
Cole et al., “Metal-catalyzed Oxidation of α-Synuclein Helping to Define the Relationship Between Oligomers, Protofibrils, and Filaments,” J Biol Chem 280(10):9678-9690 (2005).
[cited by applicant]
Conway et al., “Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease,” Nature Medicine 4(11):1318-1320 (1998).
[cited by applicant]
Cremades et al., “Chapter Three—Structural Characteristics of α-Synuclein Oligomers,” International Review of Cell and Molecular Biology 329:79-143 (2017).
[cited by applicant]
Cremades et al., “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149:1048-1059 (2012).
[cited by applicant]
Croisier et al., “Comparative study of commercially available anti α-synuclein antibodies,” Neuropathology and Applied Neurobiology 32:351-356 (2006).
[cited by applicant]
Curtiss et al., “Selection of monoclonal antibodies for linear epitopes of an apolipoprotein yields antibodies with comparable affinity for lipid-free and lipid-associated apolipoprotein,” Journal of Lipid Research 37:8…
[cited by applicant]
Danzer et al., “Different species of α-synuclein oligomers induce calcium influx and seeding,” J Neuroscience 27(34):9220-9232 (2007).
[cited by applicant]
Dehay et al., “Targeting α-synuclein for treating Parkinson's disease: mechanistic and therapeutic considerations,” Lancet Neurol. 14(8): 855-866 (2015).
[cited by applicant]
Deng et al., “Projecting human pharmacokinetics of therapeutic antibodies from nonclinical data. What have we learned?” mAbs 3:1, 61-66; (2011).
[cited by applicant]
Dimitrov et al., “Therapeutic Antibodies: Current State and Future Trends—is a Paradigm Change Coming Soon?” Meth Mol Biol 525: Chapter 1, pp. 1-27 (2009).
[cited by applicant]
Duda et al., “Immunohistochemical and Biochemical Studies Demonstrate a Distinct Profile of a-Synuclein Permutations in Multiple System Atrophy,” Journal of Neuropathology and Experimental Neurology 59:9 830-841 (2000).
[cited by applicant]
El-Agnaf et al., “α-Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma,” FASEB J 17:1945-1947 (2003).
[cited by applicant]
Emadi et al., “Inhibiting aggregation of α-synuclein with human single chain antibody fragments,” Biochem 43(10):2871-2878 (2004).
[cited by applicant]
Emadi et al., “Isolation of a human single chain antibody fragment against oligomeric α-synuclein that inhibits aggregation and prevents α-synuclein-induced toxicity,” J. Mol. Biol. 368(4):1132-1144 (2007).
[cited by applicant]
Fagerqvist et al., “Monoclonal antibodies selective for α-synuclein oligomers/protofibrils recognize brain pathology in Lewy body disorders and α-synuclein transgenic mice with the disease-causing A30P mutation,” Journa…
[cited by applicant]
Fairfoul et al., “Alpha-synuclein RT-QuIC in the CSF of patients with alpha-synucleinopathies,” Annals of Clinical and Translational Neurology 3(10): 812-818 (2016).
[cited by applicant]
Fernagut et al., “Behavioral and histopathological consequences of paraquat intoxication in mice: Effects of α-synuclein over-expression,” Synapse 61(12):991-1001 (2007).
[cited by applicant]
Fjorback et al., “Determination of α-synuclein concentration in human plasma using ELISA,” Scandanavian Journal of Clinical & Laboratory Investigation 67:431-435 (2007).
[cited by applicant]
Fujiwara et al., “α-Synuclein is phosphorylated in synucleinopathy lesions,” Nat Cell Biol 4: 160-164 (2002).
[cited by applicant]
Games et al., “Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models,” J. Neurosci 34(28):9441-9454 (2014).
[cited by applicant]
Garambois et al., “Fully human IgG and IgM antibodies directed against the carcinoembryonic antigen (CEA) Gold 4 epitope and designed for radioimmunotherapy (RIT) of colorectal cancers,” BMC Cancer 4:75 (2004).
[cited by applicant]
George et al., “Characterization of a novel protein regulated during the critical period for song learning in the zebra finch,” Neuron 15:361-372 (1995).
[cited by applicant]
Giasson et al., “A panel of epitope-specific antibodies detects protein domains distributed throughout human a-synuclein in lewy bodies of Parkinson's disease,” J Neurosci Res 59:528-533 (2000).
[cited by applicant]
Goedert, “α-synuclein and neurodegenerative diseases,” Nature Reviews Neuroscience 2:491-501 (2001).
[cited by applicant]
Gomez-Tortosa et al., “α-Synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining,” Acta Neuropathologica 99(4):352-357 (2000).
[cited by applicant]
Guilliams et al., “Nanobodies raised against monomeric alpha-synuclein distinguish between fibrils at different maturation stages,” Journal of Molecular Biology 425:2397-2411 (2013).
[cited by applicant]
Jakes et al., “Epitope mapping of LB509, a monoclonal antibody directed against human a-synuclein,” Neuroscience Letters 269:13-16 (1999).
[cited by applicant]
Jakobovits, “A Production of fully human antibodies by transgenic mice,” Current Opinion in Biotechnology 6:561-566 (1995).
[cited by applicant]
Jankovic et al., “Safety and Tolerability of Multiple Ascending Doses of PRX002/RG7935, an Anti-α-Synuclein Monoclonal Antibody, in Patients with Parkinson Disease. A Randomized Clinical Trial,” JAMA Neurol. 75(10):1206…
[cited by applicant]
Jensen et al., “α-Synuclein binds to tau and stimulates the protein kinase A—catalyzed tau phosphorylation of serine residues 262 and 356,” J. Biol. Chem 274(36):25481-25489 (1999).
[cited by applicant]
Jensen et al., “Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds α-synuclein filaments,” JBC 275(28):21500-21507 (2000).
[cited by applicant]
Kahle et al., “Physiology and pathophysiology of alpha-synuclein. Cell culture and transgenic animal models based on a Parkinson's disease-associated protein,” Ann N Y Acad Sci 920:33-41 (2000).
[cited by applicant]
Kahle et al., “Subcellular Localization of Wild-Type and Parkinson's Disease-Associated Mutant a-Synuclein in Human and Transgenic Mouse Brain,” J. Neuroscience 20(17):6365-6373 (2000).
[cited by applicant]
Kawamata et al., “Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations,” J. Neurochem. 77:929-934 (2001).
[cited by applicant]
Kayed et al., “Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis,” Science 300:486-489 (2003).
[cited by applicant]
Kim et al., “Transneuronal Propagation of Pathologic α-Synuclein from the Gut to the Brain Models Parkinson's Disease,” Neuron. 103(4):627-641 (2019).
[cited by applicant]
Klos et al., “α-Synuclein pathology in the spinal cords of neurologically asymptomatic aged individuals,” Neurology 66:1100-1102 (2006).
[cited by applicant]
Kramer et al., “Presynaptic alpha-Synuclein Aggregates, Not Lewy Bodies, Cause Neurodegeneration in Dementia with Lewy Bodies,” J. Neuroscience 27(6):1405-1410 (2007).
[cited by applicant]
Kunik et al., “Structural Consensus among Antibodies defines the antigen binding site,” PLoS Comput Biol 8(2) (2012).
[cited by applicant]
Kussie et al., “A Single Engineered Amino Acid Substitution Changes Antibody Fine Specificity,” J Immunol 152(1):146-52 (1994).
[cited by applicant]
Lee et al., “Characterization of Cytoplasmic alpha-Synuclein Aggregates,” J Biol Chem 277(50):48976-48983 (2002).
[cited by applicant]
Lee et al., “Intravesicular localization and exocytosis of α-synuclein and its aggregates,” J. Neuroscience 25(25):6016-6024 (2005).
[cited by applicant]
Lee et al., “Real-time analysis of amyloid fibril formation of α-synuclein using a fibrillation-state-specific fluorescent probe of JC-1,” Biochem J 418:311-323 (2009).
[cited by applicant]
Lipman et al., “Monoclonal versus polyclonal antibodies: distinguishing characteristics, applications, and information resources,” ILAR Journal 46:258-268 (2005).
[cited by applicant]
Lynch et al., “An ScFv Intrabody Against the Non-Amyloid Component of Alpha Synuclein Reduces Intracellular Aggregation and Toxicity,” J Mol Biol 377(1):136-147 (2008).
[cited by applicant]
Maguire-Zeiss et al., “Identification of human α-synuclein specific single chain antibodies,” Biochem Biophys Res Comm 349:1198-1205 (2006).
[cited by applicant]
Margutti et al., “Autoantibodies to the C-terminal subunit of RLIP76 induce oxidative stress and endothelial cell apoptosis in immune-mediated vascular diseases and atherosclerosis,” Blood 111(9):4559-4570 (2007).
[cited by applicant]
Mariuzza, R.A., “The Structural Basis of Antigen-Antibody Recognition,” Ann. Rev. Biophys. Biophys. Chem. 16:139-159 (1987).
[cited by applicant]
Masliah et al., “Effects of α-synuclein immunization in a mouse model of Parkinson's disease,” Neuron 46:857-868 (2005).
[cited by applicant]
Masliah et al., “Passive Immunization Reduces Behavioral and Neuropathological Deficits in an Alpha-Synuclein Transgenic Model of Lewy Body Disease,” PLoS One 4:1-17 (2011).
[cited by applicant]
Mayo “Parkinson's disease,” accessed from mayoclinic.org on Nov. 7, 2018.
[cited by applicant]
McLean et al., “Membrane Association and Protein Conformation of α-Synuclein in Intact Neurons Effect of Parkinson's Disease-Linked Mutations,” J. Biol. Chem 275(12):8812-8816 (2000).
[cited by applicant]
Miller et al., “α-Synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication,” Neurology 62:1835-1838 (2004).
[cited by applicant]
Milne et al., “Heat-Labile Antigens of
[cited by applicant]
Näsström et al., “P4-284: Oligomeric amorphous species of alpha-synuclein induce toxicity in a cellular model,” Alzh Dem: J Alzh Assoc 4(4):T754 (2008).
[cited by applicant]
Näsström et al., “The lipid peroxidation metabolite 4-oxo-2-nonenal cross-links α-synuclein causing rapid formation of stable oligomers,” Biochem. Biophys. Res. Comm. 378:872-876 (2009).
[cited by applicant]
Näsström et al., “Antibodies against α-synuclein reduce oligomerization in living cells,” PLoS One 6(10):e27230 (2011).
[cited by applicant]
Okochi et al., “Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein,” J Biol Chem 275: 390-397 (2000).
[cited by applicant]
Olanow et al., “Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion-Like Disorder?” Movement Disorders 28(1):31-40 (2013).
[cited by applicant]
Oueslati, “Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?” Journal of Parkinson's Disease 6:39-51 (2016).
[cited by applicant]
Perez De La Lastra et al., “Epitope mapping of 10 monoclonal antibodies against the pig analogue of human membrane cofactor protein (MCP),” Immunology 96(4):663-670 (1999).
[cited by applicant]
Qin et al., “Effect of 4-hydroxy-2-nonenal modification on α-synuclein aggregation,” J Biol Chem 282(8):5862-5870 (2007).
[cited by applicant]
Reichmann et al., “Reshaping human antibodies for therapy,” Nature 332:323-327 (1988).
[cited by applicant]
Ruesink et al., “Stabilization of α-synuclein oligomers using formaldehyde,” PLoS One 14(10): e0216764 (2019).
[cited by applicant]
Schenk et al., “First in human assessment of PRX002, an anti-alpha-synuclein monoclonal antibody, in healthy volunteers,” Movement Disorders 32(2):211-218 (2017).
[cited by applicant]
Schneider et al., “Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation,” Human Molecular Genetics 16(6):651-666 (2007).
[cited by applicant]
Shen et al., “Identifying the Pathological Domain of Alpha-Synuclein as a Therapeutic for Parkinson's Disease,” Int J Mol Sci. 20(9):2338 (2019).
[cited by applicant]
Seo et al., “α-Synuclein regulates neuronal survival via Bcl-2 family expression and PI3/Akt kinase pathway,” FASEB J 16(13):1826-1828 (2002).
[cited by applicant]
Serpell et al., “Fiber diffraction of synthetic a-synuclein filaments shows amyloid-like cross-β conformation,” PNAS 97(9):4897-4902 (2000).
[cited by applicant]
Shamoto-Nagai et al., “In parkinsonian substantia nigra, α-synuclein is modified by acrolein, a lipid-peroxidation product, and accumulates in the dopamine neurons with inhibition of proteasome activity,” J Neural Trans…
[cited by applicant]
Sharma et al., “A close association of torsinA and α-synuclein in lewy bodies: a fluorescence resonance energy transfer study,” American J. Pathology 159(1):339-344 (2001).
[cited by applicant]
Sharon et al., “The Formation of Highly Soluble Oligomers of alpha-Synuclein is Regulated by Fatty Acids and Enhanced in Parkinson's Disease,” Neuron 37:583-595 (2003).
[cited by applicant]
Souza et al., “Dityrosine Cross-linking Promotes Formation of Stable a-Synuclein Polymers,” JBC 275:24 18344-18349 (2000).
[cited by applicant]
Stefanis, “A-Synuclein in Parkinson's Disease,” Cold Spring Harb Perspect Med 4:a009399 (2012).
[cited by applicant]
Sumikura et al., “Distribution of α-synuclein in the spinal cord and dorsal root ganglia in an autopsy cohort of elderly persons,” Acta neuropathologica communications 3(1):1-11 (2015).
[cited by applicant]
Tickle et al., “A fully automated primary screening system for the discovery of therapeutic antibodies directly from B cells,” J Biomol Screen 20(4):492-497 (2015).
[cited by applicant]
Toyokuni et al., “The monoclonal antibody specific for the 4-hydroxy-2-nonenal histidine adduct,” FEBS Letters 359:189-191 (1995).
[cited by applicant]
Tran et al., “α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded alpha-Synuclein and Neurodegeneration,” Cell Reports 7(6):2054-2065 (2014).
[cited by applicant]
Trostchansky et al., “Interaction with phospholipids modulates α-synuclein nitration and lipid-protein adduct formation,” Biochem. J. 393: 343-349 (2006).
[cited by applicant]
Vaikath et al., “Generation and Characterization of novel conformation-specific monoclonal antibodies for alpha-synuclein pathology,” Neurobiology of Disease 79: 81-99 (2015).
[cited by applicant]
Van Der Putten et al., “Neuropathology in mice expressing human α-synuclein,” J. Neuroscience 20(16):6021-6029 (2000).
[cited by applicant]
Van Diggelen et al., “Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation,” PLoS One 14(3):e0213663 (2019).
[cited by applicant]
Msanji et al., “α-Synuclein-Based Animal Models of Parkinson's Disease: Challenges and Opportunities in a New Era,” Trends in Neurosciences, 39(11) 750-762 (2016).
[cited by applicant]
Vogiatzi et al., “Wild type α-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells,” JBC 283(35):23542-23556 (2008).
[cited by applicant]
Volpicelli-Daley et al., “Exogenous a-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death,” Neuron 72, 57-71 (2011).
[cited by applicant]
Wahlberg et al., “Development of oligomer-specific alpha-synuclein antibodies,” Alzheimer's & Dementia 4(4) Suppl. T481-T482, P2-372 (2008).
[cited by applicant]
Weber et al., “From rabbit antibody repertoires to rabbit monoclonal antibodies,” Experimental and Molecular Medicine 49: e305 (2017).
[cited by applicant]
Yamashita et al., “Recent advances in the generation of human monoclonal Antibody,” Cytotechnology 55:55-60 (2007).
[cited by applicant]
Zhou et al., “Intrabody and Parkinson's disease,” Biochim Biophys Acta 1792:634-642 (2009).
[cited by applicant]
The International Search Report issued in PCT/EP2018/084689 dated Mar. 25, 2019.
[cited by applicant]
Information on H3C Ab from U Iowa—D2 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Datasheet for the 211 antibody—D14 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Cosmo Bio News Topics Digest 2004—D17 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Webpage for 610787 antibody—D20 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Datasheet for 610787 antibody—D21 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Screenshot for MAB3249 antibody—D29 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
MAb3249 Datasheet—D30 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Screenshot for ab48506 antibody—D33 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Screenshot of HNEJ-2 antibody—D34 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Asano thesis 2007 Marshall University—D36 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Experimental report for 8A5 antibody—D40 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Product sheet for 8A5 producing cell line—D41 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Patentee's letter of Jul. 9, 2014 re EP2539366—D45 in Opposition of EP 2282758 submitted Aug. 16, 2019.
[cited by applicant]
Technical Report—Binding data of anti-alpha synuclein antibodies—D1 in Opposition of EP 2282758 submitted Aug. 21, 2019.
[cited by applicant]
Tocris—Datasheet for DHA—D6 in Opposition of EP 2282758 submitted Aug. 21, 2019.
[cited by applicant]
Exhibit 1 submitted by patentee Feb. 27, 2018—D12 in Opposition of EP 2282758 submitted Aug. 21, 2019.
[cited by applicant]
EP Appl. No. 08022188—priority to WO2010069603—E6 in Opposition of EP 2282758 submitted Aug. 21, 2019.
[cited by applicant]
Letter dated Mar. 14, 2017—D1 in Opposition of EP3067066 submitted Dec. 24, 2019.
[cited by applicant]
Letter dated Jan. 8, 2018 filed during examination—D2 in Opposition of EP 3067066 submitted Dec. 24, 2019.
[cited by applicant]
Letter dated Jul. 30, 2018 filed during examination—D3 in Opposition of EP 3067066 submitted Dec. 24, 2019.
[cited by applicant]
Letter dated Aug. 24, 2018 filed during examination—D4 in Opposition of EP 3067066 submitted Dec. 24, 2019.
[cited by applicant]
Response filed May 31, 2011 in U.S. Appl. No. 12/037,081—D5 in Opposition of EP 3067066 submitted Dec. 24, 2019.
[cited by applicant]
ATCC deposit receipt for antibody 9E4 dated Feb. 26, 2007—D6 in Opposition of EP 3067066 submitted Dec. 24, 2019.
[cited by applicant]
Declaration of E Masliah filed in U.S. Pat. No. 11,710,248—D27 in Opposition of EP 3067066 submitted Jun. 8, 2020.
[cited by applicant]
Declaration of Leda Alfonso Trujillo filed in Ecuador Application SENADI-2020-39610, mailed May 5, 2021.
[cited by applicant]
Declaration of Leda Alfonso Trujillo filed in Ecuador Application SENADI-2020-39623, mailed May 5, 2021.
[cited by applicant]
Non-final Office Action in U.S. Appl. No. 16/771,993 dated May 5, 2021.
[cited by applicant]
Notice of Allowance in U.S. Appl. No. 16/771,993 dated Nov. 5, 2021.
[cited by applicant]