• CWD research trends – interdisciplinary approach
• Cervids
• keyword analysis
• proactive management
• spatiotemporal and genetic data repository

• Wasting Disease, Chronic/epidemiology
• Wasting Disease, Chronic/transmission
• Animals
• Interdisciplinary Research
• North America
• Deer
• Humans

• Autophagy
• ER stress
• prion burden/PrPSc burden
• prion disease
• reticulophagy/er-phagy

• Endoplasmic Reticulum Stress
• Animals
• Autophagy/physiology
• Mice
• Humans
• Prion Diseases/metabolism
• Prion Diseases/pathology
• Unfolded Protein Response/physiology
• Prions/metabolism
• Prion Proteins/metabolism
• ADP-Ribosylation Factors/metabolism

• Alzheimer’s disease
• adverse events
• amyloid-?
• blood management
• blood transfusion
• tau

• CSBT-SX-2024-04 the Chinese Society of Blood Transfusion--Sansure Biotech Transfusion Medicine Development Fund
• 2019YFS0105 the Science and Technology Project of Sichuan
• CSBT-WG-2021-02 the Chinese Blood Transfusion Association Weigao Research Fund Project
• CIFMS, 2021-I2M-1-060 the CAMS Innovation Fund for Medical Sciences

• molecular diagnostics
• nanopipette
• nanopore
• single molecule
• solid-state nanopore

• Nanopores
• Biosensing Techniques
• Humans
• DNA/analysis
• Biomarkers/analysis
• Proteins/analysis
• RNA/analysis
• Electrochemical Techniques

• 075-15-2022-264 Ministry of Science and Higher Education of the Russian Federation

• Animals
• Mice
• Protein Folding
• Prion Proteins/chemistry
• Prion Proteins/metabolism
• Prion Proteins/genetics
• Amino Acid Substitution
• Protein Multimerization
• Amino Acid Sequence

• G-quadruplex
• G4 ligand
• cancer
• infection
• microbe
• neurological disease
• virus

• G-Quadruplexes
• Humans
• Drug Design
• Animals
• Neoplasms/drug therapy
• Ligands
• Molecular Targeted Therapy
• DNA
• Nervous System Diseases/drug therapy
• RNA/genetics

• Humans
• Amyloid/chemistry
• Amyloid/metabolism
• Binding Sites
• Copper/chemistry
• Copper/metabolism
• Kinetics
• Microscopy, Atomic Force
• Prion Proteins/chemistry
• Prion Proteins/metabolism
• Prion Proteins/genetics
• Protein Binding

• R01 GM094357 NIGMS NIH HHS
• R01 NS103848 NINDS NIH HHS
• S10 OD012303 NIH HHS
• National Science Foundation
• National Institutes of Health

• Uniwersytet Jagiellonski Collegium Medicum
• Ministerstwo Edukacji i Nauki
• Horizon 2020 Framework Programme

• Amyloid fibril dissociation
• Intrinsically disordered protein
• RFdiffusion
• Rosetta
• deep learning
• diagnostics
• intrinsically disordered region
• protein design

• P30 GM133893 NIGMS NIH HHS

• Alzheimer’s disease
• Apoptosis
• Autophagy
• CNS infection
• Mitophagy
• Neurodegeneration
• Neuroinflammation
• Neuronal metabolism
• Neurotransmission system
• Neurotropic virus
• Oxidative stress
• Viral infection

• Humans
• Animals
• Neurodegenerative Diseases/metabolism
• Neurodegenerative Diseases/virology
• Neurodegenerative Diseases/pathology
• Nerve Degeneration/pathology
• Nerve Degeneration/virology
• Virus Diseases/complications
• Virus Diseases/metabolism
• Virus Diseases/pathology
• Oxidative Stress
• Neurons/metabolism
• Neurons/pathology
• Neurons/virology

• RSA6280035 Thailand Research Fund
• Specific League Funds Mahidol University

• Creutzfeldt-Jakob diseases
• diagnosis
• prion diseases
• surveillance system

• Animals
• Cattle
• Humans
• Prospective Studies
• Prion Diseases/epidemiology
• Creutzfeldt-Jakob Syndrome/diagnosis
• Creutzfeldt-Jakob Syndrome/epidemiology
• Creutzfeldt-Jakob Syndrome/genetics
• Prions/genetics
• France/epidemiology

• Creutzfelt-Jakob disease
• chronic wasting disease
• in vitro prion replication
• prions
• protein misfolding cyclic amplification (PMCA)

• P01 AI077774 NIAID NIH HHS

• drug repositioning
• neurodegeneration
• prion
• radotinib

• Cricetinae
• Animals
• Sheep
• Scrapie/metabolism
• Prions/metabolism
• PrPSc Proteins/metabolism
• Brain/metabolism
• Prion Diseases/metabolism

• HI16C0965 Ministry of Health and Welfare

• LPS
• dexamethasone
• drowsy
• hamster
• hyper
• innate immunity
• primary glial cultures

• Funded by Debbie McKenzie Natural Sciences and Engineering Research Council
• Funded by Debbie McKenzie and Judd Aiken Alberta Prion Research Institute
• Funded by Debbie McKenzie Genome Canada

• Age-period-cohort model
• Prion
• Sporadic Creutzfeldt-Jakob disease
• Temporal trend

• Institut de Veille Sanitaire Institut de Veille Sanitaire

• ancestral sequence reconstruction
• prion protein
• protein aggregation
• seeding
• structural modeling

• Pregnancy
• Animals
• Cattle
• Female
• Humans
• Prion Proteins/chemistry
• Placenta/metabolism
• Prions/metabolism
• Prion Diseases/genetics
• Prion Diseases/metabolism
• Mammals

• Alberta Prion Research Institute
• National Science Foundation
• Natural Sciences and Engineering Research Council of Canada

• Alzheimer’s disease
• amyloid-beta
• nasal cavity
• prion
• tongue

• Animals
• Mice
• Humans
• Amyloid beta-Peptides/metabolism
• Alzheimer Disease/pathology
• Mice, Transgenic
• Brain/metabolism
• Amyloidosis
• Tongue

• RF1AG059321 NIH HHS
• RF1 AG072491 NIA NIH HHS
• R01AI132695 NIH HHS
• RF1 AG059321 NIA NIH HHS
• R01 AG059321 NIA NIH HHS

Brucella ceti, a zoonotic bacterial pathogen, is known to exhibit a strong neurotropism and neuropathogenicity for striped dolphins (Stenella coeruleoalba), often leading to their stranding and death. Given the lack of information on B. ceti infection’s neuropathogenesis, we investigated, for the first time, cellular prion protein (PrP^c) expression in the brain tissue from B. ceti-infected, neurobrucellosis-affected striped dolphins. Our study was inspired by previous work, reporting PrP^c as the host cell receptor for B. abortus on the surface of murine macrophages. Immunohistochemistry (IHC) and Western blot (WB) analyses were carried out on brain tissues from 12 striped dolphins found stranded along the coasts of Italy (11 specimens) and the Canary Islands (one individual), five of which served as negative controls. While PrP^c IHC yielded inconclusive results, WB analyses showed a clear-cut PrP^c expression, albeit of different intensity, in the brain tissue of all the herein investigated, B. ceti-infected and neurobrucellosis-affected individuals. In this respect, the aforementioned PrP^c expression patterns could be influenced by a number of intrinsic host-related factors, as well as by several extrinsic factors including simultaneously occurring neuropathies and/or coinfections by other neurotropic pathogens. Additionally, an upregulation of PrP^c mRNA in the brain tissue of striped dolphins could be also hypothesized during the different stages of B. ceti infection, in a similar fashion to what is already shown in murine bone marrow cells challenged with Escherichia coli. In conclusion, much more work is needed in order to properly assess the role of PrP^c, if any, as a host cell receptor for B. ceti in striped dolphins.

Brucella ceti, a zoonotic pathogen of major concern to cetacean health and conservation, is responsible for severe meningo-encephalitic/myelitic lesions in striped dolphins (Stenella coeruleoalba), often leading to their stranding and death. This study investigated, for the first time, the cellular prion protein (PrP^c) expression in the brain tissue from B. ceti-infected, neurobrucellosis-affected striped dolphins. Seven B. ceti-infected, neurobrucellosis-affected striped dolphins, found stranded along the Italian coastline (6) and in the Canary Islands (1), were investigated, along with five B. ceti-uninfected striped dolphins from the coast of Italy, carrying no brain lesions, which served as negative controls. Western Blot (WB) and immunohistochemistry (IHC) with an anti-PrP murine monoclonal antibody were carried out on the brain parenchyma of these dolphins. While PrP^c IHC yielded inconclusive results, a clear-cut PrP^c expression of different intensity was found by means of WB analyses in the brain tissue of all the seven herein investigated, B. ceti-infected and neurobrucellosis-affected cetacean specimens, with two dolphins stranded along the Italian coastline and one dolphin beached in Canary Islands also exhibiting a statistically significant increase in cerebral PrP^c expression as compared to the five Brucella spp.-negative control specimens. The significantly increased PrP^c expression found in three out of seven B. ceti-infected, neurobrucellosis-affected striped dolphins does not allow us to draw any firm conclusion(s) about the putative role of PrP^c as a host cell receptor for B. ceti. Should this be the case, an upregulation of PrP^c mRNA in the brain tissue of neurobrucellosis-affected striped dolphins could be hypothesized during the different stages of B. ceti infection, as previously shown in murine bone marrow cells challenged with Escherichia coli. Noteworthy, the inflammatory infiltrates seen in the brain and in the cervico-thoracic spinal cord segments from the herein investigated, B. ceti-infected and neurobrucellosis-affected striped dolphins were densely populated by macrophage/histiocyte cells, often harboring Brucella spp. antigen in their cytoplasm, similarly to what was reported in macrophages from mice experimentally challenged with B. abortus. Notwithstanding the above, much more work is needed in order to properly assess the role of PrP^c, if any, as a host cell receptor for B. ceti in striped dolphins.

Amyloid aggregation, including aggregation and propagation of prion protein, is a key factor in numerous human diseases, so-called amyloidosis, with a very poor ability for treatment or prevention. The present work describes the effect of sulfated or sulfonated polymers (sodium dextran sulfate, polystyrene sulfonate, polyanethole sulfonate, and polyvinyl sulfate) on different stages of amyloidogenic conversion and aggregation of the prion protein, which is associated with prionopathies in humans and animals. All tested polymers turned out to induce amyloid conversion of the ovine prion protein. As suggested from molecular dynamics simulations, this effect probably arises from destabilization of the native prion protein structure by the polymers. Short polymers enhanced its further aggregation, whereas addition of high-molecular poly(styrene sulfonate) inhibited amyloid fibrils formation. According to the seeding experiments, the protein–polymer complexes formed after incubation with poly(styrene sulfonate) exhibited significantly lower amyloidogenic capacity compared with the control fibrils of the free prion protein. The cytotoxicity of soluble oligomers was completely inhibited by treatment with poly(styrene sulfonate). To summarize, sulfonated polymers are a promising platform for the formulation of a new class of anti-prion and anti-amyloidosis therapeutics.

• amyloid
• amyloidosis
• artificial chaperone
• polyanion
• polystyrene sulfonate
• prion protein

• RT-QuIC
• chronic wasting disease (CWD)
• deer
• diagnostics
• immunohistochemistry
• prions

• Behavior
• Gliosis
• Tau pathology
• Tauopathy model

• amyloid
• biomolecular condensates
• intrinsically disordered proteins
• nucleic acids
• protein misfolding

Chronic-wasting disease (CWD) is a prion-derived fatal neurodegenerative disease that has affected wild cervid populations on a global scale. Susceptibility has been linked unambiguously to several amino acid variants within the prion protein gene (PRNP). Quantifying their distribution across landscapes can provide critical information for agencies attempting to adaptively manage CWD. Here we attempt to further define management implications of PRNP polymorphism by quantifying the contemporary geographic distribution (i.e., phylogeography) of PRNP variants in hunter-harvested white-tailed deer (WTD; Odocoileus virginianus, N = 1433) distributed across Arkansas (USA), including a focal spot for CWD since detection of the disease in February 2016. Of these, PRNP variants associated with the well-characterized 96S non-synonymous substitution showed a significant increase in relative frequency among older CWD-positive cohorts. We interpreted this pattern as reflective of a longer life expectancy for 96S genotypes in a CWD-endemic region, suggesting either decreased probabilities of infection or reduced disease progression. Other variants showing statistical signatures of potential increased susceptibility, however, seemingly reflect an artefact of population structure. We also showed marked heterogeneity across the landscape in the prevalence of ‘reduced susceptibility’ genotypes. This may indicate, in turn, that differences in disease susceptibility among WTD in Arkansas are an innate, population-level characteristic that is detectable through phylogeographic analysis.

• Adaptive management
• chronic-wasting disease
• demography
• disease susceptibility
• haplotype
• selection
• white-tailed deer

Brain‐matter vacuolation is a defining trait of all prion diseases, yet its cause is unknown. Here, we report that prion infection and prion‐mimetic antibodies deplete the phosphoinositide kinase PIKfyve—which controls endolysosomal maturation—from mouse brains, cultured cells, organotypic brain slices, and brains of Creutzfeldt‐Jakob disease victims. We found that PIKfyve is acylated by the acyltransferases zDHHC9 and zDHHC21, whose juxtavesicular topology is disturbed by prion infection, resulting in PIKfyve deacylation and rapid degradation, as well as endolysosomal hypertrophy and activation of TFEB‐dependent lysosomal enzymes. A protracted unfolded protein response (UPR), typical of prion diseases, also induced PIKfyve deacylation and degradation. Conversely, UPR antagonists restored PIKfyve levels in prion‐infected cells. Overexpression of zDHHC9 and zDHHC21, administration of the antiprion polythiophene LIN5044, or supplementation with the PIKfyve reaction product PI(3,5)P₂ suppressed prion‐induced vacuolation and restored lysosomal homeostasis. Thus, PIKfyve emerges as a central mediator of vacuolation and neurotoxicity in prion diseases.

• neurodegeneration
• palmitoylation
• prion
• spongiosis
• unfolded protein response

• Animals
• Cattle
• Encephalopathy, Bovine Spongiform
• Mice
• Mice, Transgenic
• Models, Molecular
• PrPSc Proteins/chemistry

• Alberta Prion Research Institute
• Canadian Institutes of Health

• adeno-associated virus
• gene therapy
• immunotherapy
• vaccines
• vectors

• Communicable Diseases/therapy
• Dependovirus
• Genetic Vectors
• Humans
• Immunotherapy/methods
• Vaccines

• UG3 HL147367 NHLBI NIH HHS
• R01 HL097088 NHLBI NIH HHS
• P01 HL131471 NHLBI NIH HHS
• U19 AI149646 NIAID NIH HHS
• R01 NS076991 NINDS NIH HHS

• aluminosilicate
• chronic wasting disease
• clay
• decontamination
• prion
• scrapie

The conversion of cellular prion protein (PrP^C) to disease-provoking conformer (PrP^Sc) is crucial in the pathogenesis of prion diseases. Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken, it is interesting to explore the influence of heparin on the conversion of chicken prion protein (ChPrP). Herein, we investigated the influences of heparin on biochemical properties of full-length recombinant ChPrP, with murine prion protein (MoPrP) as control. The results showed that at low heparin concentration (10 μg/mL), a great loss of solubility was observed for both MoPrP and ChPrP using solubility assays. In contrast, when the concentration of heparin was high (30 μg/mL), the solubility of MoPrP and ChPrP both decreased slightly. Using circular dichroism, PK digestion and transmission electron microscopy, significantly increased β-sheet content, PK resistance and size of aggregates were observed for MoPrP interacted with 30 μg/mL heparin, whereas 30 μg/mL heparin-treated ChPrP showed less PK resistance and slight increase of β-sheet structure. Therefore, heparin can induce conformational changes in both MoPrP and ChPrP and the biochemical properties of the aggregates induced by heparin could be modified by heparin concentration. These results highlight the importance of concentration of cofactors affecting PrP misfolding.

• Animals
• Chickens
• Circular Dichroism
• Endopeptidase K/metabolism
• Heparin/pharmacology
• Mice
• Microscopy, Electron, Transmission
• Models, Molecular
• Prion Proteins/chemistry
• Prion Proteins/genetics
• Prion Proteins/metabolism
• Protein Conformation
• Protein Conformation, beta-Strand
• Proteolysis
• Recombinant Proteins/chemistry
• Recombinant Proteins/metabolism
• Solubility

• National Natural Science Foundation of China
• Natural Science Foundation of Shandong Province
• Shandong Provincial Natural Science Foundation

• Alzheimer’s disease
• amyloid β
• mirror-image peptides
• prion protein (PrP)
• receptor-mediated internalization

• Parkinson′s disease
• amyloid
• amyloid fibrils
• curcumin
• derivatives of hydroxycinnamic acid
• neurodegenerative diseases
• prevention of amyloid transformation
• prion protein
• α-synuclein

• Amyloidogenic Proteins/chemistry
• Animals
• Coumaric Acids/chemical synthesis
• Coumaric Acids/chemistry
• Coumaric Acids/pharmacology
• Humans
• Neurodegenerative Diseases/metabolism
• Protein Aggregation, Pathological/metabolism
• alpha-Synuclein/chemistry

• research core funding No. P1-0208, project grant BI-RU/19-20-040 Javna Agencija za Raziskovalno Dejavnost RS
• 19-34-80004 Russian Foundation for Basic Research

• ERK1/2
• LRP1
• N-methyl-d-aspartate receptor (NMDA receptor
• NMDA-R)
• PC12 cells
• PrPC
• Schwann cells
• TRK1-transforming tyrosine kinase protein (TrkA)
• cell-signaling
• extracellular signal–regulated kinase (ERK)
• lipid raft
• neurite outgrowth

Prion diseases are fatal transmissible neurodegenerative conditions of humans and animals that arise through neurotoxicity induced by PrP misfolding. The cellular and molecular mechanisms of prion-induced neurotoxicity remain undefined. Understanding these processes will underpin therapeutic and control strategies for human and animal prion diseases, respectively. Prion diseases are difficult to study in their natural hosts and require the use of tractable animal models. Here we used RNA-Seq-based transcriptome analysis of prion-exposed Drosophila to probe the mechanism of prion-induced neurotoxicity. Adult Drosophila transgenic for pan neuronal expression of ovine PrP targeted to the plasma membrane exhibit a neurotoxic phenotype evidenced by decreased locomotor activity after exposure to ovine prions at the larval stage. Pathway analysis and quantitative PCR of genes differentially expressed in prion-infected Drosophila revealed up-regulation of cell cycle activity and DNA damage response, followed by down-regulation of eIF2 and mTOR signalling. Mitochondrial dysfunction was identified as the principal toxicity pathway in prion-exposed PrP transgenic Drosophila. The transcriptomic changes we observed were specific to PrP targeted to the plasma membrane since these prion-induced gene expression changes were not evident in similarly treated Drosophila transgenic for cytosolic pan neuronal PrP expression, or in non-transgenic control flies. Collectively, our data indicate that aberrant cell cycle activity, repression of protein synthesis and altered mitochondrial function are key events involved in prion-induced neurotoxicity, and correlate with those identified in mammalian hosts undergoing prion disease. These studies highlight the use of PrP transgenic Drosophila as a genetically well-defined tractable host to study mammalian prion biology.

• Drosophila melanogaster
• neurodegeneration
• prion
• transcriptomics

• Alzheimer’s disease
• Cellular prion protein
• Promoter
• Tau
• Tauopathies

Prion diseases are fatal infectious neurodegenerative disorders in human and animals caused by misfolding of the cellular prion protein (PrP^C) into the pathological isoform PrP^Sc. Elucidating the molecular and cellular mechanisms underlying prion propagation may help to develop disease interventions. Cell culture systems for prion propagation have greatly advanced molecular insights into prion biology, but translation of in vitro to in vivo findings is often disappointing. A wider range of cell culture systems might help overcome these shortcomings. Here, we describe an immortalized mouse neuronal astrocyte cell line (C8D1A) that can be infected with murine prions. Both PrP^C protein and mRNA levels in astrocytes were comparable with those in neuronal and non-neuronal cell lines permitting persistent prion infection. We challenged astrocytes with three mouse-adapted prion strains (22L, RML, and ME7) and cultured them for six passages. Immunoblotting results revealed that the astrocytes propagated 22L prions well over all six passages, whereas ME7 prions did not replicate, and RML prions replicated only very weakly after five passages. Immunofluorescence analysis indicated similar results for PrP^Sc. Interestingly, when we used prion conversion activity as a readout in real-time quaking-induced conversion assays with RML-infected cell lysates, we observed a strong signal over all six passages, comparable with that for 22L-infected cells. These data indicate that the C8D1A cell line is permissive to prion infection. Moreover, the propagated prions differed in conversion and proteinase K–resistance levels in these astrocytes. We propose that the C8D1A cell line could be used to decipher prion strain biology.

• C8D1A
• Creutzfeldt–Jakob disease
• astrocyte
• astrocytes
• bovine spongiform encephalopathy
• neurodegeneration
• neurodegenerative disease
• prion
• prion disease
• prion infection
• prion strain
• protein misfolding
• scrapie

• Parkinson’s disease
• amyloid
• fibril strain
• propagation
• secondary nucleation
• α-Synuclein

Cellular (also termed ‘natural’) prion protein has been extensively studied for many years for its pathogenic role in prionopathies after misfolding. However, neuroprotective properties of the protein have been demonstrated under various scenarios. In this line, the involvement of the cellular prion protein in neurodegenerative diseases other than prionopathies continues to be widely debated by the scientific community. In fact, studies on knock-out mice show a vast range of physiological functions for the protein that can be supported by its ability as a cell surface scaffold protein. In this review, we first summarize the most commonly described roles of cellular prion protein in neuroprotection, including antioxidant and antiapoptotic activities and modulation of glutamate receptors. Second, in light of recently described interaction between cellular prion protein and some amyloid misfolded proteins, we will also discuss the molecular mechanisms potentially involved in protection against neurodegeneration in pathologies such as Alzheimer’s, Parkinson’s, and Huntington’s diseases.

• Alzheimer’s disease
• Huntington’s disease
• Parkinson’s disease
• Tau
• neuroprotection
• prion

• Aged
• Animals
• Brain/pathology
• Humans
• Mice
• Mice, Knockout
• Nervous System Diseases/physiopathology
• Prion Proteins/metabolism

• Luciferase assay
• Prion
• Quadruplex
• Scrapie
• Transcription
• Transmissible spongiform encephalopathy

• Cells, Cultured
• Feedback, Physiological
• G-Quadruplexes
• Gene Expression Regulation
• Humans
• Prion Proteins/biosynthesis
• Prion Proteins/chemistry
• Prion Proteins/genetics
• Prion Proteins/metabolism
• Promoter Regions, Genetic
• Transcription, Genetic

• Animals
• Mice
• PrPSc Proteins/chemistry
• PrPSc Proteins/drug effects
• Prion Proteins/chemistry
• Prion Proteins/drug effects
• Protein Conformation
• Protein Domains/drug effects
• Single-Domain Antibodies/pharmacology
• Structure-Activity Relationship

• R01 NS060729 NINDS NIH HHS
• National Institute of Neurological Disorders and Stroke
• Research Vlaanderen (FWOVlaanderen)

• Alzheimer’s disease
• Aβ seeding
• amyloid plaques
• cerebral amyloidosis
• cross-seeding

• Amyloid fibrils
• Magic-angle spinning
• Protein structure and dynamics
• Solid-state NMR

• Amyloid/chemistry
• Amyloidogenic Proteins/chemistry
• Humans
• Nuclear Magnetic Resonance, Biomolecular/methods
• Protein Conformation

• R01 GM094357 NIGMS NIH HHS
• R01 GM123743 NIGMS NIH HHS
• R01 NS103848 NINDS NIH HHS
• RF1 AG061797 NIA NIH HHS

• Alzheimer's disease (AD)
• Blood brain barrier (BBB)
• Brain-targeted nanoparticles
• Magnetic resonance imaging (MRI)
• Nanomedicine
• Neurodegenerative disorders
• Neuroimaging
• Neurotheranostics
• Parkinson's disease (PD)
• Single photon emission computed tomography (SPECT/CT)
• Theranostics

• Drug Delivery Systems
• Humans
• Nanostructures/chemistry
• Nanotechnology
• Nervous System Diseases/diagnosis
• Nervous System Diseases/drug therapy
• Neuroprotective Agents/chemistry
• Neuroprotective Agents/therapeutic use
• Precision Medicine

• R01 NS036126 NINDS NIH HHS
• P01 DA028555 NIDA NIH HHS
• P30 MH062261 NIMH NIH HHS
• P01 NS031492 NINDS NIH HHS
• T32 NS105594 NINDS NIH HHS
• R56 AI138613 NIAID NIH HHS
• P30 GM127200 NIGMS NIH HHS
• P01 MH064570 NIMH NIH HHS
• R01 MH104147 NIMH NIH HHS
• R13 NS083315 NINDS NIH HHS
• P20 GM103480 NIGMS NIH HHS
• R01 NS034239 NINDS NIH HHS
• R24 OD018546 NIH HHS
• R01 MH115860 NIMH NIH HHS
• P01 NS043985 NINDS NIH HHS
• R37 NS036126 NINDS NIH HHS
• R01 AG043540 NIA NIH HHS