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  1. Article ; Online: Glia in FTLD-GRN: from supporting cast to leading role.

    Pinarbasi, Emile S / Barmada, Sami J

    The Journal of clinical investigation

    2023  Volume 133, Issue 6

    Abstract: A subset of the neurodegenerative disease frontotemporal lobar degeneration (FTLD) is caused by mutations in the progranulin (GRN) gene. In this issue of the JCI, Marsan and colleagues demonstrate disease-specific transcriptional profiles in multiple ... ...

    Abstract A subset of the neurodegenerative disease frontotemporal lobar degeneration (FTLD) is caused by mutations in the progranulin (GRN) gene. In this issue of the JCI, Marsan and colleagues demonstrate disease-specific transcriptional profiles in multiple glial cell lineages - astrocytes, microglia, and oligodendroglia - that are highly conserved between patients with FTLD-GRN and the widely used Grn-/- mouse model. Additionally, the authors show that Grn-/- astrocytes fail to adequately maintain synapses in both mouse and human models. This study presents a compelling argument for a central role for glia in neurodegeneration and creates a rich resource for extending mechanistic insight into pathophysiology, identifying potential biomarkers, and developing therapeutic approaches.
    MeSH term(s) Humans ; Animals ; Mice ; Intercellular Signaling Peptides and Proteins/genetics ; Neurodegenerative Diseases ; Frontotemporal Lobar Degeneration/genetics ; Frontotemporal Dementia/genetics ; Neuroglia ; Mutation ; Progranulins/genetics
    Chemical Substances Intercellular Signaling Peptides and Proteins ; GRN protein, human ; Progranulins ; Grn protein, mouse
    Language English
    Publishing date 2023-03-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 3067-3
    ISSN 1558-8238 ; 0021-9738
    ISSN (online) 1558-8238
    ISSN 0021-9738
    DOI 10.1172/JCI168215
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  2. Article ; Online: The MLO-down on TDP-43.

    Dykstra, Megan / Barmada, Sami J

    Brain : a journal of neurology

    2023  Volume 146, Issue 9, Page(s) 3565–3567

    MeSH term(s) Humans ; DNA-Binding Proteins ; Centrosome
    Chemical Substances DNA-Binding Proteins
    Language English
    Publishing date 2023-08-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 80072-7
    ISSN 1460-2156 ; 0006-8950
    ISSN (online) 1460-2156
    ISSN 0006-8950
    DOI 10.1093/brain/awad268
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    In stock of ZB MED Cologne/Königswinter

    Ui II Zs.26: Show issues Location:
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  3. Article ; Online: Matrin 3 in neuromuscular disease: physiology and pathophysiology.

    Malik, Ahmed M / Barmada, Sami J

    JCI insight

    2021  Volume 6, Issue 1

    Abstract: RNA-binding proteins (RBPs) are essential factors required for the physiological function of neurons, muscle, and other tissue types. In keeping with this, a growing body of genetic, clinical, and pathological evidence indicates that RBP dysfunction and/ ... ...

    Abstract RNA-binding proteins (RBPs) are essential factors required for the physiological function of neurons, muscle, and other tissue types. In keeping with this, a growing body of genetic, clinical, and pathological evidence indicates that RBP dysfunction and/or gene mutation leads to neurodegeneration and myopathy. Here, we summarize the current understanding of matrin 3 (MATR3), a poorly understood RBP implicated not only in ALS and frontotemporal dementia but also in distal myopathy. We begin by reviewing MATR3's functions, its regulation, and how it may be involved in both sporadic and familial neuromuscular disease. We also discuss insights gleaned from cellular and animal models of MATR3 pathogenesis, the links between MATR3 and other disease-associated RBPs, and the mechanisms underlying RBP-mediated disorders.
    MeSH term(s) Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/physiopathology ; Animals ; Disease Models, Animal ; Distal Myopathies/genetics ; Distal Myopathies/physiopathology ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/physiopathology ; Gene Expression Regulation ; Humans ; Mice, Knockout ; Mutation ; Neuromuscular Diseases/genetics ; Neuromuscular Diseases/physiopathology ; Nuclear Matrix-Associated Proteins/chemistry ; Nuclear Matrix-Associated Proteins/deficiency ; Nuclear Matrix-Associated Proteins/genetics ; Nuclear Matrix-Associated Proteins/physiology ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/physiology ; Mice
    Chemical Substances MATR3 protein, human ; Nuclear Matrix-Associated Proteins ; RNA-Binding Proteins ; matrin-3 protein, mouse
    Language English
    Publishing date 2021-01-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ISSN 2379-3708
    ISSN (online) 2379-3708
    DOI 10.1172/jci.insight.143948
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Neuronal Puncta/Aggregate Formation by WT and Mutant UBQLN2.

    Safren, Nathaniel / Sharkey, Lisa M / Barmada, Sami J

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2551, Page(s) 561–573

    Abstract: Protein aggregates are a common feature of nearly all neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). Here we describe a method to quickly and accurately measure protein aggregation ...

    Abstract Protein aggregates are a common feature of nearly all neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). Here we describe a method to quickly and accurately measure protein aggregation in cells expressing a fluorescently tagged aggregation-prone protein. This unbiased method obviates the need for manual scoring and facilitates the identification of factors governing protein self-assembly and its downstream consequences for cell heath.
    MeSH term(s) Humans ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Neurons/metabolism ; Protein Aggregates ; Neurodegenerative Diseases/metabolism ; Parkinson Disease/metabolism ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism
    Chemical Substances Protein Aggregates ; UBQLN2 protein, human ; Autophagy-Related Proteins ; Adaptor Proteins, Signal Transducing
    Language English
    Publishing date 2022-09-28
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2597-2_34
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: TDP-43 Nuclear Bodies: A NEAT Response to Stress?

    Malik, Ahmed M / Barmada, Sami J

    Molecular cell

    2020  Volume 79, Issue 3, Page(s) 362–364

    Abstract: In this issue of Molecular Cell, Wang et al. (2020) investigate stress-induced nuclear condensates of the RNA-binding protein TDP-43, uncovering a protective function for these granules as well as an RNA-dependent mechanism for scaffolding them. ...

    Abstract In this issue of Molecular Cell, Wang et al. (2020) investigate stress-induced nuclear condensates of the RNA-binding protein TDP-43, uncovering a protective function for these granules as well as an RNA-dependent mechanism for scaffolding them.
    MeSH term(s) Amyotrophic Lateral Sclerosis ; DNA-Binding Proteins ; Humans ; RNA, Long Noncoding ; RNA-Binding Proteins
    Chemical Substances DNA-Binding Proteins ; RNA, Long Noncoding ; RNA-Binding Proteins ; TARDBP protein, human
    Language English
    Publishing date 2020-08-07
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.07.018
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  6. Article ; Online: Linking RNA Dysfunction and Neurodegeneration in Amyotrophic Lateral Sclerosis.

    Barmada, Sami J

    Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

    2015  Volume 12, Issue 2, Page(s) 340–351

    Abstract: The degeneration of motor neurons in amyotrophic lateral sclerosis (ALS) inevitably causes paralysis and death within a matter of years. Mounting genetic and functional evidence suggest that abnormalities in RNA processing and metabolism underlie motor ... ...

    Abstract The degeneration of motor neurons in amyotrophic lateral sclerosis (ALS) inevitably causes paralysis and death within a matter of years. Mounting genetic and functional evidence suggest that abnormalities in RNA processing and metabolism underlie motor neuron loss in sporadic and familial ALS. Abnormal localization and aggregation of essential RNA-binding proteins are fundamental pathological features of sporadic ALS, and mutations in genes encoding RNA processing enzymes cause familial disease. Also, expansion mutations occurring in the noncoding region of C9orf72-the most common cause of inherited ALS-result in nuclear RNA foci, underscoring the link between abnormal RNA metabolism and neurodegeneration in ALS. This review summarizes the current understanding of RNA dysfunction in ALS, and builds upon this knowledge base to identify converging mechanisms of neurodegeneration in ALS. Potential targets for therapy development are highlighted, with particular emphasis on early and conserved pathways that lead to motor neuron loss in ALS.
    MeSH term(s) Amyotrophic Lateral Sclerosis/complications ; Amyotrophic Lateral Sclerosis/genetics ; Animals ; DNA-Binding Proteins/genetics ; Humans ; MicroRNAs/genetics ; Nerve Degeneration/etiology ; RNA/genetics ; RNA/metabolism ; RNA Splicing/genetics ; RNA-Binding Protein FUS/genetics
    Chemical Substances DNA-Binding Proteins ; FUS protein, human ; MicroRNAs ; RNA-Binding Protein FUS ; TARDBP protein, human ; RNA (63231-63-0)
    Language English
    Publishing date 2015-02-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2316693-9
    ISSN 1878-7479 ; 1933-7213
    ISSN (online) 1878-7479
    ISSN 1933-7213
    DOI 10.1007/s13311-015-0340-3
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    Zs.A 6156: Show issues Location:
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  7. Article: RNA Degradation in Neurodegenerative Disease.

    Weskamp, Kaitlin / Barmada, Sami J

    Advances in neurobiology

    2018  Volume 20, Page(s) 103–142

    Abstract: Ribonucleic acid (RNA) homeostasis is dynamically modulated in response to changing physiological conditions. Tight regulation of RNA abundance through both transcription and degradation determines the amount, timing, and location of protein translation. ...

    Abstract Ribonucleic acid (RNA) homeostasis is dynamically modulated in response to changing physiological conditions. Tight regulation of RNA abundance through both transcription and degradation determines the amount, timing, and location of protein translation. This balance is of particular importance in neurons, which are among the most metabolically active and morphologically complex cells in the body. As a result, any disruptions in RNA degradation can have dramatic consequences for neuronal health. In this chapter, we will first discuss mechanisms of RNA stabilization and decay. We will then explore how the disruption of these pathways can lead to neurodegenerative disease.
    MeSH term(s) Humans ; Neurodegenerative Diseases/metabolism ; RNA Stability/physiology ; RNA, Messenger
    Chemical Substances RNA, Messenger
    Language English
    Publishing date 2018-06-17
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2190-5215
    ISSN 2190-5215
    DOI 10.1007/978-3-319-89689-2_5
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  8. Article ; Online: TDP43 and RNA instability in amyotrophic lateral sclerosis.

    Weskamp, Kaitlin / Barmada, Sami J

    Brain research

    2018  Volume 1693, Issue Pt A, Page(s) 67–74

    Abstract: The nuclear RNA-binding protein TDP43 is integrally involved in RNA processing. In accord with this central function, TDP43 levels are tightly regulated through a negative feedback loop, in which TDP43 recognizes its own RNA transcript, destabilizes it, ... ...

    Abstract The nuclear RNA-binding protein TDP43 is integrally involved in RNA processing. In accord with this central function, TDP43 levels are tightly regulated through a negative feedback loop, in which TDP43 recognizes its own RNA transcript, destabilizes it, and reduces new TDP43 protein production. In the neurodegenerative disorder amyotrophic lateral sclerosis (ALS), cytoplasmic mislocalization and accumulation of TDP43 disrupt autoregulation; conversely, inefficient TDP43 autoregulation can lead to cytoplasmic TDP43 deposition and subsequent neurodegeneration. Because TDP43 plays a multifaceted role in maintaining RNA metabolism, its mislocalization and accumulation interrupt several RNA processing pathways that in turn affect RNA stability and gene expression. TDP43-mediated disruption of these pathways-including alternative mRNA splicing, non-coding RNA processing, and RNA granule dynamics-may directly or indirectly contribute to ALS pathogenesis. Therefore, strategies that restore effective TDP43 autoregulation may ultimately prevent neurodegeneration in ALS and related disorders.
    MeSH term(s) Alternative Splicing ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Fragile X Mental Retardation Protein/genetics ; Humans ; Motor Neurons/metabolism ; RNA/genetics ; RNA/metabolism ; RNA Stability
    Chemical Substances DNA-Binding Proteins ; FMR1 protein, human ; TARDBP protein, human ; TDP-43 protein, mouse ; Tardbp protein, rat ; Fragile X Mental Retardation Protein (139135-51-6) ; RNA (63231-63-0)
    Language English
    Publishing date 2018-01-31
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1200-2
    ISSN 1872-6240 ; 0006-8993
    ISSN (online) 1872-6240
    ISSN 0006-8993
    DOI 10.1016/j.brainres.2018.01.015
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    Zs.A 161: Show issues Location:
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  9. Article: TDP-43 Nuclear Bodies: A NEAT Response to Stress?

    Malik, Ahmed M / Barmada, Sami J

    Molecular cell. 2020 Aug. 06, v. 79, no. 3

    2020  

    Abstract: In this issue of Molecular Cell, Wang et al. (2020) investigate stress-induced nuclear condensates of the RNA-binding protein TDP-43, uncovering a protective function for these granules as well as an RNA-dependent mechanism for scaffolding them. ...

    Abstract In this issue of Molecular Cell, Wang et al. (2020) investigate stress-induced nuclear condensates of the RNA-binding protein TDP-43, uncovering a protective function for these granules as well as an RNA-dependent mechanism for scaffolding them.
    Keywords RNA-binding proteins ; condensates ; granules ; stress response
    Language English
    Dates of publication 2020-0806
    Size p. 362-364.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2020.07.018
    Database NAL-Catalogue (AGRICOLA)

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    Z 2005/501: Show issues

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  10. Article ; Online: Autophagy and ALS: mechanistic insights and therapeutic implications.

    Chua, Jason P / De Calbiac, Hortense / Kabashi, Edor / Barmada, Sami J

    Autophagy

    2021  Volume 18, Issue 2, Page(s) 254–282

    Abstract: Mechanisms of protein homeostasis are crucial for overseeing the clearance of misfolded and toxic proteins over the lifetime of an organism, thereby ensuring the health of neurons and other cells of the central nervous system. The highly conserved ... ...

    Abstract Mechanisms of protein homeostasis are crucial for overseeing the clearance of misfolded and toxic proteins over the lifetime of an organism, thereby ensuring the health of neurons and other cells of the central nervous system. The highly conserved pathway of autophagy is particularly necessary for preventing and counteracting pathogenic insults that may lead to neurodegeneration. In line with this, mutations in genes that encode essential autophagy factors result in impaired autophagy and lead to neurodegenerative conditions such as amyotrophic lateral sclerosis (ALS). However, the mechanistic details underlying the neuroprotective role of autophagy, neuronal resistance to autophagy induction, and the neuron-specific effects of autophagy-impairing mutations remain incompletely defined. Further, the manner and extent to which non-cell autonomous effects of autophagy dysfunction contribute to ALS pathogenesis are not fully understood. Here, we review the current understanding of the interplay between autophagy and ALS pathogenesis by providing an overview of critical steps in the autophagy pathway, with special focus on pivotal factors impaired by ALS-causing mutations, their physiologic effects on autophagy in disease models, and the cell type-specific mechanisms regulating autophagy in non-neuronal cells which, when impaired, can contribute to neurodegeneration. This review thereby provides a framework not only to guide further investigations of neuronal autophagy but also to refine therapeutic strategies for ALS and related neurodegenerative diseases.
    MeSH term(s) Amyotrophic Lateral Sclerosis/metabolism ; Autophagy/physiology ; Frontotemporal Dementia/genetics ; Humans ; Proteostasis ; Unfolded Protein Response
    Language English
    Publishing date 2021-05-31
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2021.1926656
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