M. Neumann

发表

Tau Protein, Aβ42 and S-100B Protein in Cerebrospinal Fluid of Patients with Dementia with Lewy Bodies

J. Wiltfang, B. Mollenhauer, H. Kretzschmar, 2005, Dementia and Geriatric Cognitive Disorders.

Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration

J. Schneider, J. Trojanowski, C. Duyckaerts, 2007, Acta Neuropathologica.

Frontotemporal lobar degeneration: demographic characteristics of 353 patients.

B. Miller, J. Neuhaus, Hans Förstl, 2005, Archives of neurology.

[German consortium for frontotemporal lobar degeneration].

Hans Förstl, A. Danek, J. Kornhuber, 2011, Der Nervenarzt.

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Bruce L. Miller, Murray Grossman, John Q. Trojanowski, 2006, Science.

Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43

E. Buratti, C. Gloeckner, M. Neumann, 2022, Nature Communications.

Review: Neuropathology of non‐tau frontotemporal lobar degeneration

I. Mackenzie, M. Neumann, 2019, Neuropathology and applied neurobiology.

Mitochondrial Dysfunction and Decrease in Body Weight of a Transgenic Knock-in Mouse Model for TDP-43*

H. Fuchs, S. Koob, A. Reichert, 2014, The Journal of Biological Chemistry.

Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies*

J. Trojanowski, A. Chen-Plotkin, M. Neumann, 2009, Journal of Biological Chemistry.

Knockdown of transactive response DNA‐binding protein (TDP‐43) downregulates histone deacetylase 6

Tobias M. Rasse, V. Baekelandt, M. Bonin, 2010, The EMBO journal.

Physiology and Pathophysiology of α‐Synuclein: Cell Culture and Transgenic Animal Models Based on a Parkinson's Disease‐associated Protein

C. Haass, M. Neumann, L. Ozmen, 2000, Annals of the New York Academy of Sciences.

Clinical, genetic, and pathologic characteristics of patients with frontotemporal dementia and progranulin mutations.

J. Trojanowski, M. Grossman, C. Clark, 2007, Archives of neurology.

Decreased CSF amyloid β42 and normal tau levels in dementia with Lewy bodies

J. Wiltfang, W. Schulz-Schaeffer, H. Kretzschmar, 2000, Neurology.

Arginine methylation next to the PY‐NLS modulates Transportin binding and nuclear import of FUS

E. Kremmer, I. Mackenzie, T. Madl, 2012, The EMBO journal.

Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS

E. Kremmer, T. Arzberger, I. Mackenzie, 2016, Acta Neuropathologica.

High frequency of H3 K27M mutations in adult midline gliomas

G. Tabatabai, M. Schuhmann, A. Ebrahimi, 2019, Journal of Cancer Research and Clinical Oncology.

Interdisciplinary management of central nervous system metastasis and neoplastic meningitis: recent developments and future perspectives

H. Rammensee, H. Karnath, D. Wallwiener, 2016 .

Neurofilaments in spinocerebellar ataxia type 3: blood biomarkers at the preataxic and ataxic stage in humans and mice

A. Durr, R. Schüle, L. Schöls, 2020, EMBO molecular medicine.

Neurofilaments as blood biomarkers at the preataxic and ataxic stage of spinocerebellar ataxia type 3: a cross-species analysis in humans and mice

A. Durr, R. Schüle, L. Schöls, 2019 .

A New family with frontotemporal dementia with intronic 10+3 splice site mutation in the tau gene: neuropathology and molecular effects

A. Lees, H. Kretzschmar, H. Kretzschmar, 2005, Neuropathology and applied neurobiology.

Frontotemporal dementia Author : Doctor

T. Gasser, M. Neumann, 2004 .

Ultra-High Field MRI in Alzheimer's Disease: Effective Transverse Relaxation Rate and Quantitative Susceptibility Mapping of Human Brain In Vivo and Ex Vivo Compared to Histology.

K. Scheffler, G. Hagberg, R. Pohmann, 2020, Journal of Alzheimer's disease : JAD.

α-Synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies

E. Kremmer, R. Benecke, H. Kretzschmar, 2000, Acta Neuropathologica.

Genome-wide analyses as part of the international FTLD-TDP whole-genome sequencing consortium reveals novel disease risk factors and increases support for immune dysfunction in FTLD

Kevin F. Bieniek, B. Miller, C. Geula, 2019, Acta Neuropathologica.

Neuropathological assessments of the pathology in frontotemporal lobar degeneration with TDP43-positive inclusions: an inter-laboratory study by the BrainNet Europe consortium

T. Hortobágyi, I. Ferrer, S. Al-Sarraj, 2014, Journal of Neural Transmission.

Missense Mutations in the Progranulin Gene Linked to Frontotemporal Lobar Degeneration with Ubiquitin-immunoreactive Inclusions Reduce Progranulin Production and Secretion*

C. Haass, M. Neumann, A. Capell, 2008, Journal of Biological Chemistry.

Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies.

J. Trojanowski, W. Spooren, T. Iwatsubo, 2002, The Journal of clinical investigation.

A harmonized classification system for FTLD-TDP pathology

J. Trojanowski, V. Lee, D. Mann, 2011, Acta Neuropathologica.

Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations

J. Trojanowski, V. Lee, N. Cairns, 2007, Annals of neurology.

TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis

Murray Grossman, James B Leverenz, Maria Martinez-Lage, 2008, The Lancet Neurology.

Molecular Neuropathology of TDP-43 Proteinopathies

M. Neumann, Manuela Neumann, 2009, International journal of molecular sciences.

Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations.

J. Trojanowski, V. Lee, H. Kretzschmar, 2008, Archives of neurology.

TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis.

J. Trojanowski, V. Lee, M. Neumann, 2007, Archives of neurology.

Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)*

C. Haass, M. Neumann, D. Dormann, 2012, The Journal of Biological Chemistry.

Nucleolar Disruption in Dopaminergic Neurons Leads to Oxidative Damage and Parkinsonism through Repression of Mammalian Target of Rapamycin Signaling

A. Schober, I. Grummt, R. Parlato, 2011, The Journal of Neuroscience.

TDP‐43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations

N. Cairns, W. Markesbery, M. Forman, 2007, Journal of neuropathology and experimental neurology.

Microglial activation mediates neurodegeneration related to oligodendroglial α‐synucleinopathy: Implications for multiple system atrophy

W. Poewe, G. Wenning, N. Stefanova, 2007, Movement disorders : official journal of the Movement Disorder Society.

TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease

J. Trojanowski, V. Lee, M. Neumann, 2007, Acta Neuropathologica.

[A Pair of Siblings with a rare R5H-Mutation in Exon 1 of the MAPT-Gene].

A. Danek, A. Rominger, M. Neumann, 2015, Fortschritte der Neurologie-Psychiatrie.

Phenotypic heterogeneity and genetic modifiers in prion disease caused by a Pro102Leu mutation in the PRNP gene

M. Neumann, 2009, Nature Clinical Practice Neurology.

Frontotemporal lobar degeneration and amyotrophic lateral sclerosis: molecular similarities and differences.

M. Neumann, 2013, Revue neurologique.

Fused in Sarcoma Neuropathology in Neurodegenerative Disease.

I. Mackenzie, M. Neumann, 2017, Cold Spring Harbor perspectives in medicine.

TMEM106B is a genetic modifier of frontotemporal lobar degeneration with C9orf72 hexanucleotide repeat expansions

N. Fox, C. Cotman, J. Grafman, 2014, Acta Neuropathologica.

Frontotemporal Lobar Degeneration with TDP‐43 Pathology

I. Mackenzie, M. Neumann, 2011 .

FUS pathology deﬁnes the majority of tau- and TDP-43-negative frontotemporal lobar degeneration

P. Deyn, J. Trojanowski, M. Rossor, 2010 .

A new subtype of frontotemporal lobar degeneration with FUS pathology.

H. Kretzschmar, I. Mackenzie, M. Baker, 2009, Brain : a journal of neurology.

Concomitant TAR-DNA-Binding Protein 43 Pathology Is Present in Alzheimer Disease and Corticobasal Degeneration but Not in Other Tauopathies

J. Trojanowski, M. Grossman, C. Clark, 2008, Journal of neuropathology and experimental neurology.

Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

J. Trojanowski, M. Grossman, C. Clark, 2008, The American journal of pathology.

An immunohistochemical study of cases of sporadic and inherited frontotemporal lobar degeneration using 3R- and 4R-specific tau monoclonal antibodies

D. Dickson, E. Bigio, D. Mann, 2006, Acta Neuropathologica.

Distinct pathological subtypes of FTLD-FUS

N. Cairns, H. Kretzschmar, D. Munoz, 2011, Acta Neuropathologica.

Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

H. Kretzschmar, I. Mackenzie, M. Baker, 2009, Acta Neuropathologica.

FAS-Dependent Cell Death in α-Synuclein Transgenic Oligodendrocyte Models of Multiple System Atrophy

G. Halliday, C. Richter-Landsberg, C. Haass, 2013, PloS one.

Cerebral Involvement in McLeod Syndrome: The First Autopsy Revisited

M. Brin, A. Danek, M. Neumann, 2008 .

Oxidative stress in transgenic mice with oligodendroglial alpha-synuclein overexpression replicates the characteristic neuropathology of multiple system atrophy.

Werner Poewe, Markus Reindl, Christian Haass, 2005, The American journal of pathology.

Hyperphosphorylation and insolubility of alpha-synuclein in transgenic mouse oligodendrocytes.

W. Spooren, T. Iwatsubo, H. Kretzschmar, 2002, EMBO reports.

Novel Types of Frontotemporal Lobar Degeneration: Beyond Tau and TDP-43

N. Cairns, D. Munoz, I. Mackenzie, 2011, Journal of Molecular Neuroscience.

Sensitivity to MPTP is not increased in Parkinson's disease‐associated mutant α‐synuclein transgenic mice

J B Schulz, M. Okochi, C. Haass, 2001, Journal of neurochemistry.

Neurodegeneration and Motor Dysfunction in a Conditional Model of Parkinson's Disease

Bernd J. Pichler, Jörg B. Schulz, Jürgen Winkler, 2008, The Journal of Neuroscience.

Selective insolubility of alpha-synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model.

J. Trojanowski, P. Riederer, T. Iwatsubo, 2001, The American journal of pathology.

Age-dependent cognitive decline and amygdala pathology in alpha-synuclein transgenic mice.

W. Spooren, H. Kretzschmar, C. Haass, 2007, Neurobiology of aging.

Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations

S. Lorenzl, E. Kremmer, D. Troost, 2013, Acta Neuropathologica.

Subcortical TDP-43 pathology patterns validate cortical FTLD-TDP subtypes and demonstrate unique aspects of C9orf72 mutation cases

I. Mackenzie, M. Neumann, 2019, Acta Neuropathologica.

Tau protein, Abeta42 and S-100B protein in cerebrospinal fluid of patients with dementia with Lewy bodies.

J. Wiltfang, B. Mollenhauer, H. Kretzschmar, 2005, Dementia and geriatric cognitive disorders.

PRKAR1B mutation associated with a new neurodegenerative disorder with unique pathology.

J. Lebbink, A. Smit, W. Kamphorst, 2014, Brain : a journal of neurology.

Nicht-Alzheimer-Demenzen

M. Neumann, 2012 .

Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone.

A. Wright, J. Taylor, Hongbo Lu, 2010, Human molecular genetics.

The neuropathology associated with repeat expansions in the C9ORF72 gene

I. Mackenzie, M. Neumann, P. Frick, 2014, Acta Neuropathologica.

Quantitative analysis and clinico-pathological correlations of different dipeptide repeat protein pathologies in C9ORF72 mutation carriers

L. Petrucelli, E. Kremmer, D. Troost, 2015, Acta Neuropathologica.

[Frontotemporal lobar degeneration. Part 1: diagnosis and treatment].

Hans Förstl, A. Kurz, A. Danek, 2009, Fortschritte der Neurologie-Psychiatrie.

TDP-43 proteinopathies: a new class of proteinopathies

M. Neumann, 2007 .

Reappraisal of TDP-43 pathology in FTLD-U subtypes

I. Mackenzie, M. Neumann, 2017, Acta Neuropathologica.

Mechanisms of Disease in FTLD: Gain of Function versus Loss of Function Effects

N. Cairns, E. Bigio, D. Mann, 2014 .

TDP-43-negative FTLD-U is a significant new clinico-pathological subtype of FTLD

H. Kretzschmar, I. Mackenzie, M. Neumann, 2008, Acta Neuropathologica.

Length of normal alleles of C9ORF72 GGGGCC repeat do not influence disease phenotype

R. Petersen, B. Boeve, D. Knopman, 2012, Neurobiology of Aging.

Transactive response DNA-binding protein 43 burden in familial Alzheimer disease and Down syndrome.

J. Trojanowski, V. Lee, A. Rosso, 2009, Archives of neurology.

Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations

H. Kretzschmar, D. Munoz, I. Mackenzie, 2012, Acta Neuropathologica.

Novel antibodies reveal presynaptic localization of C9orf72 protein and reduced protein levels in C9orf72 mutation carriers

M. Oulad-Abdelghani, I. Mackenzie, J. Prudlo, 2018, Acta Neuropathologica Communications.

Common Variants Near ZIC1 and ZIC4 in Autopsy-Confirmed Multiple System Atrophy

Alan J. Thomas, G. Schellenberg, G. Deuschl, 2022, Movement disorders : official journal of the Movement Disorder Society.

Potential genetic modifiers of disease risk and age at onset in patients with frontotemporal lobar degeneration and GRN mutations: a genome-wide association study

Kevin F. Bieniek, C. Geula, M. Mesulam, 2018, Lancet Neurology.

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations

C. Broeckhoven, M. Cruts, H. Kretzschmar, 2013, Acta Neuropathologica.

Absence of heterogeneous nuclear ribonucleoproteins and survival motor neuron protein in TDP-43 positive inclusions in frontotemporal lobar degeneration

J. Trojanowski, G. Dreyfuss, V. Lee, 2007, Acta Neuropathologica.

Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS

B. Boeve, D. Dickson, W. Seeley, 2013, Neurobiology of Aging.

FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis

I. Mackenzie, M. Neumann, 2012, Brain Research.

Frontotemporal Lobar Degeneration with FUS Immunoreactive Inclusions

I. Mackenzie, M. Neumann, 2011 .

Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation

A. Eisen, I. Mackenzie, M. Strong, 2011, Acta Neuropathologica.

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

I. Mackenzie, M. Neumann, Rosa Rademakers, 2010, The Lancet Neurology.

Recent biomarker approaches in the diagnosis of frontotemporal lobar degeneration/Neurochemische Ansätze in der Diagnose der Frontotemporalen Lobärdegeneration

M. Neumann, P. Steinacker, M. Otto, 2012 .

FTLD-TDP pathological subtypes: clinical and mechanistic significance.

I. Mackenzie, M. Neumann, Edward B. Lee, 2021 .

Frontotemporal Lobar Degeneration TDP-43-Immunoreactive Pathological Subtypes: Clinical and Mechanistic Significance.

I. Mackenzie, Eddie B. Lee, M. Neumann, 2021, Advances in experimental medicine and biology.

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

I. Mackenzie, E. Buratti, M. Neumann, 2020, Acta Neuropathologica.

Novel cases of amyotrophic lateral sclerosis after treatment of cerebral arteriovenous malformationss.

M. Weller, A. Valavanis, J. Prudlo, 2016, Swiss medical weekly.

Novel PS1 Mutation in a Bavarian Kindred With Familial Alzheimer Disease

P. S. St George-Hyslop, E. Rogaeva, H. Kretzschmar, 2004, Alzheimer disease and associated disorders.

TDP-43 Mediates Degeneration in a Novel Drosophila Model of Disease Caused by Mutations in VCP/p97

J. Trojanowski, V. Lee, Brian D. Freibaum, 2010, The Journal of Neuroscience.

Neurofilament Light Chain in Blood and CSF as Marker of Disease Progression in Mouse Models and in Neurodegenerative Diseases

M. Staufenbiel, M. Jucker, J. Kuhle, 2016, Neuron.

Novel G335V mutation in the tau gene associated with early onset familial frontotemporal dementia

B. Bogerts, H. Kretzschmar, M. Neumann, 2005, Neurogenetics.

Advances in understanding the molecular basis of frontotemporal dementia.

I. Mackenzie, M. Neumann, R. Rademakers, 2012, Nature reviews. Neurology.

Frontotemporal dementia: from molecular mechanisms to therapy

C. Haass, M. Neumann, 2016, Journal of neurochemistry.

A multi-omics dataset for the analysis of frontotemporal dementia genetic subtypes

C. Blauwendraat, Margherita Francescatto, P. Heutink, 2020, bioRxiv.

PART is part of Alzheimer disease

H. Braak, L. Buée, C. Duyckaerts, 2015, Acta Neuropathologica.

γH2AX foci assay in glioblastoma: surgical specimen versus corresponding stem cell culture.

M. Tatagiba, D. Zips, M. Neumann, 2021, Radiotherapy and oncology : journal of the European Society for Therapeutic Radiology and Oncology.

The amyloid-beta (Abeta) peptide pattern in cerebrospinal fluid in Alzheimer's disease: evidence of a novel carboxyterminally elongated Abeta peptide.

P. Lewczuk, E. Rüther, J. Kornhuber, 2003, Rapid communications in mass spectrometry : RCM.

LATE-NC staging in routine neuropathologic diagnosis: an update

Janna H. Neltner, J. Schneider, T. Montine, 2022, Acta Neuropathologica.

Accumulation of TMEM106B C-terminal fragments in neurodegenerative disease and aging

I. Mackenzie, M. Baker, M. Neumann, 2022, Acta Neuropathologica.

Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies.

Hideo Fujiwara, Takeshi Iwatsubo, John Q. Trojanowski, 2002, The Journal of clinical investigation.

Hyperphosphorylation and insolubility of α‐synuclein in transgenic mouse oligodendrocytes

Hideo Fujiwara, Takeshi Iwatsubo, Masato Hasegawa, 2002 .

Reply: Very early onset frontotemporal dementia with no family history predicts underlying fused in sarcoma pathology

M. Neumann, 2010 .

Neurofilament Light Chain in Blood and CSF as Marker of Disease Progression in Mouse Models and in Neurodegenerative Diseases

M. Staufenbiel, M. Jucker, J. Kuhle, 2016, Neuron.

β‐amyloid peptides in cerebrospinal fluid of patients with Creutzfeldt–Jakob disease

H. Hampel, J. Kornhuber, J. Wiltfang, 2003 .

Beta-amyloid peptides in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease.

H. Hampel, J. Kornhuber, J. Wiltfang, 2003, Annals of neurology.

Decreased beta-amyloid1-42 in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease.

J. Kornhuber, J. Wiltfang, H. Kretzschmar, 2000, Neurology.

Childhood supratentorial ependymomas with YAP1‐MAMLD1 fusion: an entity with characteristic clinical, radiological, cytogenetic and histopathological features

C. Sommer, P. Varlet, T. Acker, 2018, Brain pathology.

A Pathogenic Presenilin-1 Deletion Causes Abberrant Aβ42 Production in the Absence of Congophilic Amyloid Plaques*

J. Hardy, T. Révész, H. Kretzschmar, 2001, The Journal of Biological Chemistry.

The molecular basis of frontotemporal dementia

I. Mackenzie, M. Neumann, M. Tolnay, 2009, Expert Reviews in Molecular Medicine.

Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies

I. Mackenzie, M. Neumann, 2016, Journal of neurochemistry.

ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import

I. Mackenzie, C. Haass, M. Neumann, 2010, The EMBO journal.

Contribution of RNA/DNA Binding Protein Dysfunction in Oligodendrocytes in the Pathogenesis of the Amyotrophic Lateral Sclerosis/Frontotemporal Lobar Degeneration Spectrum Diseases

M. Neumann, C. F. Valori, 2021, Frontiers in Neuroscience.

Does Sporadic Amyotrophic Lateral Sclerosis Spread via Axonal Connectivities?

H. Braak, K. Tredici, K. Del Tredici, 2017, Neurology International Open.

Which Nerve Cell Types Develop TDP-43-immunoreactive Inclusions in sALS?

H. Braak, A. Ludolph, K. Tredici, 2017 .

Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects

N. Cairns, E. Bigio, D. Mann, 2012, Acta Neuropathologica.

Advances in understanding the molecular basis of frontotemporal dementia

I. Mackenzie, M. Neumann, R. Rademakers, 2012, Nature Reviews Neurology.

FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations.

Olaf Ansorge, Christian Haass, H. Kretzschmar, 2011, Brain : a journal of neurology.

Neuropathological background of phenotypical variability in frontotemporal dementia

J. Hodges, D. Dickson, D. Mann, 2011, Acta Neuropathologica.

FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration

R. Petersen, J. Trojanowski, M. Rossor, 2010, Acta Neuropathologica.

Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update

John Q. Trojanowski, Bernardino Ghetti, Paul G. Ince, 2009, Acta Neuropathologica.

FUS pathology in basophilic inclusion body disease

D. Munoz, I. Mackenzie, S. Terada, 2009, Acta Neuropathologica.

EIF2AK3 variants in Dutch patients with Alzheimer's disease

A. Uitterlinden, C. V. van Duijn, M. Hulsman, 2019, Neurobiology of Aging.

EIF 2 AK 3 variants in Dutch patients with Alzheimer ' s disease

A. Uitterlinden, C. Duijn, M. Hulsman, 2018 .

Delft University of Technology EIF2AK3 variants in Dutch patients with Alzheimer's disease

A. Uitterlinden, C. Duijn, M. Hulsman, 2018 .

Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeldt–Jakob disease

J. Wiltfang, B. Mollenhauer, H. Kretzschmar, 2002, Neurology.

Germline findings in patients with advanced malignancies screened with paired blood-tumour testing for personalised treatment approaches.

C. Schroeder, S. Ossowski, T. Haack, 2022, European journal of cancer.

Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions

M. J. Fresnadillo Martínez, H. Hakonarson, G. Schellenberg, 2010, Nature Genetics.

Cerebral gene expression profiles in sporadic Creutzfeldt–Jakob disease

H. Kretzschmar, I. Zerr, W. Xiang, 2005, Annals of neurology.

Immunotherapy targeting the C-terminal domain of TDP-43 decreases neuropathology and confers neuroprotection in mouse models of ALS/FTD

P. Nelson, J. Stöhr, S. Porta, 2023, Neurobiology of Disease.

Clinical and pathological continuum of multisystem TDP-43 proteinopathies.

John L. Robinson, J. Trojanowski, M. Grossman, 2009, Archives of neurology.

TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions.

J. Morris, J. Trojanowski, V. Lee, 2007, The American journal of pathology.

Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies.

J. Trojanowski, M. Grossman, V. Lee, 2006, The American journal of pathology.

Congenic expression of poly-GA but not poly-PR in mice triggers selective neuron loss and interferon responses found in C9orf72 ALS

W. Wurst, W. Enard, T. Arzberger, 2020, Acta Neuropathologica.

Ataxin-2 as potential disease modifier in C9ORF72 expansion carriers

M. Mesulam, L. Petrucelli, R. Petersen, 2014, Neurobiology of Aging.

The spectrum of mutations in progranulin: a collaborative study screening 545 cases of neurodegeneration.

G. Schellenberg, T. Montine, J. Trojanowski, 2010, Archives of neurology.

Malignant optic glioma – the spectrum of disease in a case series

M. Weller, M. Neumann, K. Landau, 2015, Graefe's Archive for Clinical and Experimental Ophthalmology.

Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations

J. Trojanowski, D. Dickson, N. Cairns, 2008, Acta Neuropathologica.

Creutzfeldt-Jakob disease in a patient with an R208H mutation of the prion protein gene (PRNP) and a 17-kDa prion protein fragment

H. Kretzschmar, E. Grasbon-Frodl, I. Zerr, 2005, Acta Neuropathologica.

Age-dependent cognitive decline and amygdala pathology in α-synuclein transgenic mice

W. Spooren, H. Kretzschmar, C. Haass, 2007, Neurobiology of Aging.

Selective Insolubility of α-Synuclein in Human Lewy Body Diseases Is Recapitulated in a Transgenic Mouse Model

J. Trojanowski, P. Riederer, T. Iwatsubo, 2001 .

Subcellular Localization of Wild-Type and Parkinson's Disease-Associated Mutant α-Synuclein in Human and Transgenic Mouse Brain

Christian Haass, E. Kremmer, H. Kretzschmar, 2000, The Journal of Neuroscience.

AAV-mediated expression of a new conformational anti-aggregated α-synuclein antibody prolongs survival in a genetic model of α-synucleinopathies

M. Neumann, T. Ciossek, B. Stierstorfer, 2022, bioRxiv.

Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

J. Trojanowski, V. Lee, E. Kremmer, 2009, Acta Neuropathologica.

Elevation of β-Amyloid Peptide 2–42 in Sporadic and Familial Alzheimer's Disease and Its Generation in PS1 Knockout Cells*

E. Rüther, B. de Strooper, J. Wiltfang, 2001, The Journal of Biological Chemistry.

Regional Distribution of Proteinase K‐Resistant α‐Synuclein Correlates with Lewy Body Disease Stage

H. Kretzschmar, C. Haass, M. Neumann, 2004, Journal of neuropathology and experimental neurology.

Aβ seeds resist inactivation by formaldehyde

K. Nilsson, M. Jucker, M. Neumann, 2014, Acta Neuropathologica.

The amyloid-β (Aβ) peptide pattern in cerebrospinal fluid in Alzheimer's disease: evidence of a novel carboxyterminally elongated Aβ peptide

P. Lewczuk, E. Rüther, J. Kornhuber, 2003 .

Neuropathological consensus criteria for the evaluation of Lewy pathology in post-mortem brains: a multi-centre study

K. Jellinger, T. Hortobágyi, J. Trojanowski, 2021, Acta Neuropathologica.

TDP-43 pathology and cognition in ALS

S. Teipel, A. Büttner, E. Kasper, 2016, Neurology.

Pick's disease associated with the novel Tau gene mutation K369I

R. Crowther, M. Goedert, M. Spillantini, 2001, Annals of neurology.

LATE to the PART-y

M. Grossman, M. Frosch, J. Parisi, 2019, Brain : a journal of neurology.

Frontotemporale Lobärdegenerationen

A Danek, Hans Förstl, A. Kurz, 2009 .

Proteolytic processing of TAR DNA binding protein‐43 by caspases produces C‐terminal fragments with disease defining properties independent of progranulin

E. Kremmer, M. Nishihara, C. Haass, 2009, Journal of neurochemistry.

C9ORF72 knockdown triggers FTD-like symptoms and cell pathology in mice

A. Brice, D. Saracino, S. Boluda, 2023, Frontiers in Cellular Neuroscience.

TDP-43-Positive White Matter Pathology in Frontotemporal Lobar Degeneration With Ubiquitin-Positive Inclusions

Murray Grossman, John Q Trojanowski, J. Trojanowski, 2007, Journal of neuropathology and experimental neurology.

Dopaminergic midbrain neurons are the prime target for mitochondrial DNA deletions

M. Elstner, D. Turnbull, K. J. Krishnan, 2008, Journal of Neurology.

Nuclear and neuritic distribution of serine-129 phosphorylated α-synuclein in transgenic mice

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Correction to: Antibody against TDP-43 phosphorylated at serine 369 suggests conformational differences of TDP-43 aggregates among FTLD-TDP subtypes