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  1. Artikel ; Online: Lack of a protective effect of the Tmem106b "protective SNP" in the Grn knockout mouse model for frontotemporal lobar degeneration.

    Cabron, Anne-Sophie / Borgmeyer, Uwe / Richter, Julia / Peisker, Helga / Gutbrod, Katharina / Dörmann, Peter / Capell, Anja / Damme, Markus

    Acta neuropathologica communications

    2023  Band 11, Heft 1, Seite(n) 21

    Abstract: Genetic variants in TMEM106B are a common risk factor for frontotemporal lobar degeneration and the most important modifier of disease risk in patients with progranulin (GRN) mutations (FTLD-GRN). TMEM106B is encoding a lysosomal transmembrane protein of ...

    Abstract Genetic variants in TMEM106B are a common risk factor for frontotemporal lobar degeneration and the most important modifier of disease risk in patients with progranulin (GRN) mutations (FTLD-GRN). TMEM106B is encoding a lysosomal transmembrane protein of unknown molecular function. How it mediates its disease-modifying function remains enigmatic. Several TMEM106B single nucleotide polymorphisms (SNPs) are significantly associated with disease risk in FTLD-GRN carriers, of which all except one are within intronic sequences of TMEM106B. Of note, the non-coding SNPs are in high linkage disequilibrium with the coding SNP rs3173615 located in exon six of TMEM106B, resulting in a threonine to serine change at amino acid 185 in the minor allele, which is protective in FTLD-GRN carriers. To investigate the functional consequences of this variant in vivo, we generated and characterized a knockin mouse model harboring the Tmem106b
    Mesh-Begriff(e) Animals ; Mice ; Amino Acids ; Frontotemporal Dementia/genetics ; Frontotemporal Lobar Degeneration/pathology ; Intercellular Signaling Peptides and Proteins/genetics ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice, Knockout ; Mutation ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Polymorphism, Single Nucleotide/genetics
    Chemische Substanzen Amino Acids ; Intercellular Signaling Peptides and Proteins ; Membrane Proteins ; Nerve Tissue Proteins ; Tmem106b protein, mouse
    Sprache Englisch
    Erscheinungsdatum 2023-01-27
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2715589-4
    ISSN 2051-5960 ; 2051-5960
    ISSN (online) 2051-5960
    ISSN 2051-5960
    DOI 10.1186/s40478-023-01510-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Buch ; Online ; Dissertation / Habilitation: Funktionelle Charakterisierung von BACE, einer für die Alzheimer Krankheit relevanten Protease

    Capell, Anja

    2005  

    Verfasserangabe von Anja Capell
    Sprache Deutsch
    Umfang Online-Ressource
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
    Dissertation / Habilitation Humboldt-Univ., Diss--Berlin, 2005
    Datenquelle Ehemaliges Sondersammelgebiet Küsten- und Hochseefischerei

    Volltext online

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  3. Buch ; Dissertation / Habilitation: Funktionelle Charakterisierung von BACE, einer für die Alzheimer Krankheit relevanten Protease

    Capell, Anja

    2005  

    Verfasserangabe Anja Capell
    Schlagwörter Alzheimer-Krankheit
    Sprache Deutsch
    Umfang X, 167 S., graph. Darst.
    Dokumenttyp Buch ; Dissertation / Habilitation
    Dissertation / Habilitation Humboldt-Univ., Diss.--Berlin, 2005
    Datenquelle Katalog der Technische Informationsbibliothek Hannover

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  4. Artikel ; Online: Impaired protein degradation in FTLD and related disorders.

    Götzl, Julia K / Lang, Christina M / Haass, Christian / Capell, Anja

    Ageing research reviews

    2016  Band 32, Seite(n) 122–139

    Abstract: Impaired protein degradation has been discussed as a cause or consequence of various neurodegenerative diseases, such as Alzheimer's, Parkinson's and Huntington's disease. More recently, evidence accumulated that dysfunctional protein degradation may ... ...

    Abstract Impaired protein degradation has been discussed as a cause or consequence of various neurodegenerative diseases, such as Alzheimer's, Parkinson's and Huntington's disease. More recently, evidence accumulated that dysfunctional protein degradation may play a role in frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Since in almost all neurodegenerative diseases, protein aggregates are disease-defining hallmarks, it is most likely that impaired protein degradation contributes to disease onset and progression. In the majority of FTD cases, the pathological protein aggregates contain either microtubuleassociated protein tau or TAR DNA-binding protein (TDP)-43. Aggregates are also positive for ubiquitin and p62/sequestosome 1 (SQSTM1) indicating that these aggregates are targeted for degradation. FTD-linked mutations in genes encoding three autophagy adaptor proteins, p62/SQSTM1, ubiquilin 2 and optineurin, indicate that impaired autophagy might cause FTD. Furthermore, the strongest evidence for lysosomal impairment in FTD is provided by the progranulin (GRN) gene, which is linked to FTD and neuronal ceroid lipofuscinosis. In this review, we summarize the observations that have been made during the last years linking the accumulation of disease-associated proteins in FTD to impaired protein degradation pathways. In addition, we take resent findings for nucleocytoplasmic transport defects of TDP-43, as discussed for hexanucleotide repeat expansions in C9orf72 into account and provide a hypothesis how the interplay of altered nuclear transport and protein degradation leads to the accumulation of protein deposits.
    Mesh-Begriff(e) Active Transport, Cell Nucleus/physiology ; Autophagy/physiology ; Cell Cycle Proteins/genetics ; DNA-Binding Proteins/metabolism ; Frontotemporal Dementia/metabolism ; Humans ; Lysosomes/metabolism ; Mutation ; Nerve Degeneration/metabolism ; Neuronal Ceroid-Lipofuscinoses/metabolism ; Proteolysis ; Sequestosome-1 Protein/genetics ; Transcription Factor TFIIIA/genetics ; Ubiquitins/genetics
    Chemische Substanzen Cell Cycle Proteins ; DNA-Binding Proteins ; OPTN protein, human ; SQSTM1 protein, human ; Sequestosome-1 Protein ; Transcription Factor TFIIIA ; UBQLN2 protein, human ; Ubiquitins
    Sprache Englisch
    Erscheinungsdatum 2016-05-07
    Erscheinungsland England
    Dokumenttyp Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2075672-0
    ISSN 1872-9649 ; 1568-1637
    ISSN (online) 1872-9649
    ISSN 1568-1637
    DOI 10.1016/j.arr.2016.04.008
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Progranulin transcripts with short and long 5' untranslated regions (UTRs) are differentially expressed via posttranscriptional and translational repression.

    Capell, Anja / Fellerer, Katrin / Haass, Christian

    The Journal of biological chemistry

    2014  Band 289, Heft 37, Seite(n) 25879–25889

    Abstract: Frontotemporal lobar degeneration is associated with cytoplasmic or nuclear deposition of the TAR DNA-binding protein 43 (TDP-43). Haploinsufficiency of progranulin (GRN) is a major genetic risk factor for frontotemporal lobar degeneration associated ... ...

    Abstract Frontotemporal lobar degeneration is associated with cytoplasmic or nuclear deposition of the TAR DNA-binding protein 43 (TDP-43). Haploinsufficiency of progranulin (GRN) is a major genetic risk factor for frontotemporal lobar degeneration associated with TDP-43 deposition. Therefore, understanding the mechanisms that control cellular expression of GRN is required not only to understand disease etiology but also for the development of potential therapeutic strategies. We identified different GRN transcripts with short (38-93 nucleotides) or long (219 nucleotides) 5' UTRs and demonstrate a cellular mechanism that represses translation of GRN mRNAs with long 5' UTRs. The long 5' UTR of GRN mRNA contains an upstream open reading frame (uORF) that is absent in all shorter transcripts. Because such UTRs can be involved in translational control as well as in mRNA stability, we compared the expression of GRN in cells expressing cDNAs with and without 5' UTRs. This revealed a selective repression of GRN translation and a reduction of mRNA levels by the 219-nucleotide-long 5' UTR. The specific ability of this GRN 5' UTR to repress protein expression was further confirmed by its transfer to an independent reporter. Deletion analysis identified a short stretch between nucleotides 76 and 125 containing two start codons within one uORF that is required and sufficient for repression of protein expression. Mutagenesis of the two AUG codons within the uORF is sufficient to reduce translational repression. Therefore initiating ribosomes at the AUGs of the uORF fail to efficiently initiate translation at the start codon of GRN. In parallel the 5' UTR also affects mRNA stability; thus two independent mechanisms determine GRN expression via mRNA stability and translational efficiency.
    Mesh-Begriff(e) 3' Untranslated Regions/genetics ; 5' Untranslated Regions/genetics ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Frontotemporal Lobar Degeneration/genetics ; Frontotemporal Lobar Degeneration/metabolism ; Frontotemporal Lobar Degeneration/pathology ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Mutation ; Open Reading Frames ; Peptide Chain Termination, Translational/genetics ; Progranulins ; Protein Isoforms/genetics ; RNA, Messenger/genetics
    Chemische Substanzen 3' Untranslated Regions ; 5' Untranslated Regions ; DNA-Binding Proteins ; GRN protein, human ; Intercellular Signaling Peptides and Proteins ; Progranulins ; Protein Isoforms ; RNA, Messenger
    Sprache Englisch
    Erscheinungsdatum 2014-07-23
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M114.560128
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Hefte anzeigen Standort:
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  6. Buch ; Online ; Dissertation / Habilitation: Funktionelle Charakterisierung von BACE, einer für die Alzheimer Krankheit relevanten Protease

    Capell, Anja [Verfasser]

    2005  

    Verfasserangabe von Anja Capell
    Schlagwörter Medizin, Gesundheit ; Medicine, Health
    Thema/Rubrik (Code) sg610
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
    Datenquelle Digitale Dissertationen im Internet

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  7. Artikel ; Online: Early lysosomal maturation deficits in microglia triggers enhanced lysosomal activity in other brain cells of progranulin knockout mice.

    Götzl, Julia K / Colombo, Alessio-Vittorio / Fellerer, Katrin / Reifschneider, Anika / Werner, Georg / Tahirovic, Sabina / Haass, Christian / Capell, Anja

    Molecular neurodegeneration

    2018  Band 13, Heft 1, Seite(n) 48

    Abstract: Background: Heterozygous loss-of-function mutations in the progranulin gene (GRN) lead to frontotemporal lobar degeneration (FTLD) while the complete loss of progranulin (PGRN) function results in neuronal ceroid lipofuscinosis (NCL), a lysosomal ... ...

    Abstract Background: Heterozygous loss-of-function mutations in the progranulin gene (GRN) lead to frontotemporal lobar degeneration (FTLD) while the complete loss of progranulin (PGRN) function results in neuronal ceroid lipofuscinosis (NCL), a lysosomal storage disease. Thus the growth factor-like protein PGRN may play an important role in lysosomal degradation. In line with a potential lysosomal function, PGRN is partially localized and processed in lysosomes. In the central nervous system (CNS), PGRN is like other lysosomal proteins highly expressed in microglia, further supporting an important role in protein degradation. We have previously reported that cathepsin (Cat) D is elevated in GRN-associated FTLD patients and Grn knockout mice. However, the primary mechanism that causes impaired protein degradation and elevated CatD levels upon PGRN deficiency in NCL and FTLD remains unclear.
    Methods: mRNA expression analysis of selected lysosomal hydrolases, lysosomal membrane proteins and autophagy-related genes was performed by NanoString nCounter panel. Protein expression, maturation and in vitro activity of Cat D, B and L in mouse embryonic fibroblasts (MEF) and brains of Grn knockout mice were investigated. To selectively characterize microglial and non-microglial brain cells, an acutely isolated microglia fraction using MACS microbeads (Miltenyi Biotec) conjugated with CD11b antibody and a microglia-depleted fraction were analyzed for protein expression and maturation of selected cathepsins.
    Results: We demonstrate that loss of PGRN results in enhanced expression, maturation and in vitro activity of Cat D, B and L in mouse embryonic fibroblasts and brain extracts of aged Grn knockout mice. Consistent with an overall enhanced expression and activity of lysosomal proteases in brain of Grn knockout mice, we observed an age-dependent transcriptional upregulation of certain lysosomal proteases. Thus, lysosomal dysfunction is not reflected by transcriptional downregulation of lysosomal proteases but rather by the upregulation of certain lysosomal proteases in an age-dependent manner. Surprisingly, cell specific analyses identified early lysosomal deficits in microglia before enhanced cathepsin levels could be detected in other brain cells, suggesting different functional consequences on lysosomal homeostasis in microglia and other brain cells upon lack of PGRN.
    Conclusions: The present study uncovers early and selective lysosomal dysfunctions in Grn knockout microglia/macrophages. Dysregulated lysosomal homeostasis in microglia might trigger compensatory lysosomal changes in other brain cells.
    Mesh-Begriff(e) Animals ; Brain/metabolism ; Disease Models, Animal ; Frontotemporal Lobar Degeneration/genetics ; Frontotemporal Lobar Degeneration/metabolism ; Intercellular Signaling Peptides and Proteins/genetics ; Lysosomes/metabolism ; Mice, Knockout ; Microglia/metabolism ; Neuronal Ceroid-Lipofuscinoses/genetics ; Neuronal Ceroid-Lipofuscinoses/metabolism ; Neurons/metabolism ; Progranulins/genetics ; Proteins/metabolism
    Chemische Substanzen Intercellular Signaling Peptides and Proteins ; Progranulins ; Proteins ; lysosomal proteins
    Sprache Englisch
    Erscheinungsdatum 2018-09-04
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1750-1326
    ISSN (online) 1750-1326
    DOI 10.1186/s13024-018-0281-5
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Loss of TMEM106B potentiates lysosomal and FTLD-like pathology in progranulin-deficient mice.

    Werner, Georg / Damme, Markus / Schludi, Martin / Gnörich, Johannes / Wind, Karin / Fellerer, Katrin / Wefers, Benedikt / Wurst, Wolfgang / Edbauer, Dieter / Brendel, Matthias / Haass, Christian / Capell, Anja

    EMBO reports

    2020  Band 21, Heft 10, Seite(n) e50241

    Abstract: Single nucleotide polymorphisms (SNPs) in TMEM106B encoding the lysosomal type II transmembrane protein 106B increase the risk for frontotemporal lobar degeneration (FTLD) of GRN (progranulin gene) mutation carriers. Currently, it is unclear if ... ...

    Abstract Single nucleotide polymorphisms (SNPs) in TMEM106B encoding the lysosomal type II transmembrane protein 106B increase the risk for frontotemporal lobar degeneration (FTLD) of GRN (progranulin gene) mutation carriers. Currently, it is unclear if progranulin (PGRN) and TMEM106B are synergistically linked and if a gain or a loss of function of TMEM106B is responsible for the increased disease risk of patients with GRN haploinsufficiency. We therefore compare behavioral abnormalities, gene expression patterns, lysosomal activity, and TDP-43 pathology in single and double knockout animals. Grn
    Mesh-Begriff(e) Animals ; Frontotemporal Lobar Degeneration/genetics ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Lysosomes ; Membrane Proteins/genetics ; Mice ; Mice, Knockout ; Nerve Tissue Proteins ; Progranulins/genetics
    Chemische Substanzen Intercellular Signaling Peptides and Proteins ; Membrane Proteins ; Nerve Tissue Proteins ; Progranulins ; TMEM106B protein, human
    Sprache Englisch
    Erscheinungsdatum 2020-09-14
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.202050241
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5433: Hefte anzeigen Standort:
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    Zs.MG 41: Hefte anzeigen

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  9. Artikel ; Online: Beneficial Effect of ACI-24 Vaccination on Aβ Plaque Pathology and Microglial Phenotypes in an Amyloidosis Mouse Model.

    Rudan Njavro, Jasenka / Vukicevic, Marija / Fiorini, Emma / Dinkel, Lina / Müller, Stephan A / Berghofer, Anna / Bordier, Chiara / Kozlov, Stanislav / Halle, Annett / Buschmann, Katrin / Capell, Anja / Giudici, Camilla / Willem, Michael / Feederle, Regina / Lichtenthaler, Stefan F / Babolin, Chiara / Montanari, Paolo / Pfeifer, Andrea / Kosco-Vilbois, Marie /
    Tahirovic, Sabina

    Cells

    2022  Band 12, Heft 1

    Abstract: Amyloid-β (Aβ) deposition is an initiating factor in Alzheimer's disease (AD). Microglia are the brain immune cells that surround and phagocytose Aβ plaques, but their phagocytic capacity declines in AD. This is in agreement with studies that associate ... ...

    Abstract Amyloid-β (Aβ) deposition is an initiating factor in Alzheimer's disease (AD). Microglia are the brain immune cells that surround and phagocytose Aβ plaques, but their phagocytic capacity declines in AD. This is in agreement with studies that associate AD risk loci with genes regulating the phagocytic function of immune cells. Immunotherapies are currently pursued as strategies against AD and there are increased efforts to understand the role of the immune system in ameliorating AD pathology. Here, we evaluated the effect of the Aβ targeting ACI-24 vaccine in reducing AD pathology in an amyloidosis mouse model. ACI-24 vaccination elicited a robust and sustained antibody response in APPPS1 mice with an accompanying reduction of Aβ plaque load, Aβ plaque-associated ApoE and dystrophic neurites as compared to non-vaccinated controls. Furthermore, an increased number of NLRP3-positive plaque-associated microglia was observed following ACI-24 vaccination. In contrast to this local microglial activation at Aβ plaques, we observed a more ramified morphology of Aβ plaque-distant microglia compared to non-vaccinated controls. Accordingly, bulk transcriptomic analysis revealed a trend towards the reduced expression of several disease-associated microglia (DAM) signatures that is in line with the reduced Aβ plaque load triggered by ACI-24 vaccination. Our study demonstrates that administration of the Aβ targeting vaccine ACI-24 reduces AD pathology, suggesting its use as a safe and cost-effective AD therapeutic intervention.
    Mesh-Begriff(e) Mice ; Animals ; Microglia/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Mice, Transgenic ; Amyloid beta-Peptides/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/therapy ; Alzheimer Disease/metabolism ; Amyloidosis/metabolism ; Plaque, Amyloid/metabolism ; Phenotype ; Vaccination
    Chemische Substanzen Amyloid beta-Protein Precursor ; Amyloid beta-Peptides
    Sprache Englisch
    Erscheinungsdatum 2022-12-24
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12010079
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Depletion and activation of microglia impact metabolic connectivity of the mouse brain.

    Gnörich, Johannes / Reifschneider, Anika / Wind, Karin / Zatcepin, Artem / Kunte, Sebastian T / Beumers, Philipp / Bartos, Laura M / Wiedemann, Thomas / Grosch, Maximilian / Xiang, Xianyuan / Fard, Maryam K / Ruch, Francois / Werner, Georg / Koehler, Mara / Slemann, Luna / Hummel, Selina / Briel, Nils / Blume, Tanja / Shi, Yuan /
    Biechele, Gloria / Beyer, Leonie / Eckenweber, Florian / Scheifele, Maximilian / Bartenstein, Peter / Albert, Nathalie L / Herms, Jochen / Tahirovic, Sabina / Haass, Christian / Capell, Anja / Ziegler, Sibylle / Brendel, Matthias

    Journal of neuroinflammation

    2023  Band 20, Heft 1, Seite(n) 47

    Abstract: Aim: We aimed to investigate the impact of microglial activity and microglial FDG uptake on metabolic connectivity, since microglial activation states determine FDG-PET alterations. Metabolic connectivity refers to a concept of interacting metabolic ... ...

    Abstract Aim: We aimed to investigate the impact of microglial activity and microglial FDG uptake on metabolic connectivity, since microglial activation states determine FDG-PET alterations. Metabolic connectivity refers to a concept of interacting metabolic brain regions and receives growing interest in approaching complex cerebral metabolic networks in neurodegenerative diseases. However, underlying sources of metabolic connectivity remain to be elucidated.
    Materials and methods: We analyzed metabolic networks measured by interregional correlation coefficients (ICCs) of FDG-PET scans in WT mice and in mice with mutations in progranulin (Grn) or triggering receptor expressed on myeloid cells 2 (Trem2) knockouts (
    Results: Microglia depletion by CSF1R inhibition resulted in a strong decrease of metabolic connectivity defined by decrease of mean cortical ICCs in WT mice at both ages studied (6-7 m; p = 0.0148, 9-10 m; p = 0.0191), when compared to vehicle-treated age-matched WT mice. Grn
    Conclusions: Presence, absence, and activation of microglia have a strong impact on metabolic connectivity of the mouse brain. Enhanced metabolic connectivity is associated with increased microglial FDG allocation.
    Mesh-Begriff(e) Animals ; Mice ; Microglia/metabolism ; Fluorodeoxyglucose F18/metabolism ; Progranulins/metabolism ; Brain/metabolism ; Positron-Emission Tomography ; Membrane Glycoproteins/metabolism ; Receptors, Immunologic/metabolism
    Chemische Substanzen Fluorodeoxyglucose F18 (0Z5B2CJX4D) ; Progranulins ; Trem2 protein, mouse ; Membrane Glycoproteins ; Receptors, Immunologic
    Sprache Englisch
    Erscheinungsdatum 2023-02-24
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2156455-3
    ISSN 1742-2094 ; 1742-2094
    ISSN (online) 1742-2094
    ISSN 1742-2094
    DOI 10.1186/s12974-023-02735-8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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