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  1. Article ; Online: Correction to: Rare Inherited forms of Paget's Disease and Related Syndromes.

    Ralston, Stuart H / Taylor, J Paul

    Calcified tissue international

    2021  Volume 108, Issue 6, Page(s) 827

    Language English
    Publishing date 2021-04-15
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 304266-2
    ISSN 1432-0827 ; 0944-0747 ; 0008-0594 ; 0171-967X
    ISSN (online) 1432-0827
    ISSN 0944-0747 ; 0008-0594 ; 0171-967X
    DOI 10.1007/s00223-021-00850-3
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    Zs.A 317: Show issues Location:
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  2. Article ; Online: Pathological phase transitions in ALS-FTD impair dynamic RNA-protein granules.

    Nedelsky, Natalia B / Taylor, J Paul

    RNA (New York, N.Y.)

    2021  Volume 28, Issue 1, Page(s) 97–113

    Abstract: The genetics of human disease serves as a robust and unbiased source of insight into human biology, both revealing fundamental cellular processes and exposing the vulnerabilities associated with their dysfunction. Over the last decade, the genetics of ... ...

    Abstract The genetics of human disease serves as a robust and unbiased source of insight into human biology, both revealing fundamental cellular processes and exposing the vulnerabilities associated with their dysfunction. Over the last decade, the genetics of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) have epitomized this concept, as studies of ALS-FTD-causing mutations have yielded fundamental discoveries regarding the role of biomolecular condensation in organizing cellular contents while implicating disturbances in condensate dynamics as central drivers of neurodegeneration. Here we review this genetic evidence, highlight its intersection with patient pathology, and discuss how studies in model systems have revealed a role for aberrant condensation in neuronal dysfunction and death. We detail how multiple, distinct types of disease-causing mutations promote pathological phase transitions that disturb the dynamics and function of ribonucleoprotein (RNP) granules. Dysfunction of RNP granules causes pleiotropic defects in RNA metabolism and can drive the evolution of these structures to end-stage pathological inclusions characteristic of ALS-FTD. We propose that aberrant phase transitions of these complex condensates in cells provide a parsimonious explanation for the widespread cellular abnormalities observed in ALS as well as certain histopathological features that characterize late-stage disease.
    MeSH term(s) Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Binding Sites ; Biomolecular Condensates/chemistry ; Biomolecular Condensates/metabolism ; Cell Death/genetics ; Cytoplasmic Ribonucleoprotein Granules/chemistry ; Cytoplasmic Ribonucleoprotein Granules/genetics ; Cytoplasmic Ribonucleoprotein Granules/metabolism ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Humans ; Molecular Dynamics Simulation ; Mutation ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; Phase Transition ; Protein Binding ; RNA/chemistry ; RNA/genetics ; RNA/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Ribonucleoproteins/chemistry ; Ribonucleoproteins/genetics ; Ribonucleoproteins/metabolism
    Chemical Substances Nerve Tissue Proteins ; RNA-Binding Proteins ; Ribonucleoproteins ; RNA (63231-63-0)
    Language English
    Publishing date 2021-10-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.079001.121
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  3. Article ; Online: A PR plug for the nuclear pore in amyotrophic lateral sclerosis.

    Taylor, J Paul

    Proceedings of the National Academy of Sciences of the United States of America

    2017  Volume 114, Issue 7, Page(s) 1445–1447

    Language English
    Publishing date 2017-02-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1621085114
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  4. Article ; Online: Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease.

    Nedelsky, Natalia B / Taylor, J Paul

    Nature reviews. Neurology

    2019  Volume 15, Issue 5, Page(s) 272–286

    Abstract: Biomolecular condensation arising through phase transitions has emerged as an essential organizational strategy that governs many aspects of cell biology. In particular, the role of phase transitions in the assembly of large, complex ribonucleoprotein ( ... ...

    Abstract Biomolecular condensation arising through phase transitions has emerged as an essential organizational strategy that governs many aspects of cell biology. In particular, the role of phase transitions in the assembly of large, complex ribonucleoprotein (RNP) granules has become appreciated as an important regulator of RNA metabolism. In parallel, genetic, histopathological and cell and molecular studies have provided evidence that disturbance of phase transitions is an important driver of neurological diseases, notably amyotrophic lateral sclerosis (ALS), but most likely also other diseases. Indeed, our growing knowledge of the biophysics underlying biological phase transitions suggests that this process offers a unifying mechanism to explain the numerous and diverse disturbances in RNA metabolism that have been observed in ALS and some related diseases - specifically, that these diseases are driven by disturbances in the material properties of RNP granules. Here, we review the evidence for this hypothesis, emphasizing the reciprocal roles in which disease-related protein and disease-related RNA can lead to disturbances in the material properties of RNP granules and consequent pathogenesis. Additionally, we review evidence that implicates aberrant phase transitions as a contributing factor to a larger set of neurodegenerative diseases, including frontotemporal dementia, certain repeat expansion diseases and Alzheimer disease.
    MeSH term(s) Biophysics ; Brain/metabolism ; Humans ; Neurodegenerative Diseases/metabolism ; Phase Transition ; Ribonucleoproteins/metabolism
    Chemical Substances Ribonucleoproteins
    Language English
    Publishing date 2019-03-13
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2491514-2
    ISSN 1759-4766 ; 1759-4758
    ISSN (online) 1759-4766
    ISSN 1759-4758
    DOI 10.1038/s41582-019-0157-5
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  5. Article ; Online: Rare Inherited forms of Paget's Disease and Related Syndromes.

    Ralston, Stuart H / Taylor, J Paul

    Calcified tissue international

    2019  Volume 104, Issue 5, Page(s) 501–516

    Abstract: Several rare inherited disorders have been described that show phenotypic overlap with Paget's disease of bone (PDB) and in which PDB is a component of a multisystem disorder affecting muscle and the central nervous system. These conditions are the ... ...

    Abstract Several rare inherited disorders have been described that show phenotypic overlap with Paget's disease of bone (PDB) and in which PDB is a component of a multisystem disorder affecting muscle and the central nervous system. These conditions are the subject of this review article. Insertion mutations within exon 1 of the TNFRSF11A gene, encoding the receptor activator of nuclear factor kappa B (RANK), cause severe PDB-like disorders including familial expansile osteolysis, early-onset familial PDB and expansile skeletal hyperphosphatasia. The mutations interfere with normal processing of RANK and cause osteoclast activation through activation of nuclear factor kappa B (NFκB) independent of RANK ligand stimulation. Recessive, loss-of-function mutations in the TNFRSF11B gene, which encodes osteoprotegerin, cause juvenile PDB and here the bone disease is due to unopposed activation of RANK by RANKL. Multisystem proteinopathy is a disorder characterised by myopathy and neurodegeneration in which PDB is often an integral component. It may be caused by mutations in several genes including VCP, HNRNPA1, HNRNPA2B1, SQSTM1, MATR3, and TIA1, some of which are involved in classical PDB. The mechanisms of osteoclast activation in these conditions are less clear but may involve NFκB activation through sequestration of IκB. The evidence base for management of these disorders is somewhat limited due to the fact they are extremely rare. Bisphosphonates have been successfully used to gain control of elevated bone remodelling but as yet, no effective treatment exists for the treatment of the muscle and neurological manifestations of MSP syndromes.
    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Bone and Bones/pathology ; Family Health ; Genetic Predisposition to Disease ; Humans ; Ligands ; Mutation ; Osteitis Deformans/diagnosis ; Osteitis Deformans/genetics ; Osteoclasts/metabolism ; Phenotype ; RANK Ligand/genetics ; RNA, Messenger/metabolism ; Receptor Activator of Nuclear Factor-kappa B/genetics ; Signal Transduction
    Chemical Substances Adaptor Proteins, Signal Transducing ; Ligands ; RANK Ligand ; RNA, Messenger ; Receptor Activator of Nuclear Factor-kappa B ; TNFRSF11A protein, human ; TNFSF11 protein, human
    Language English
    Publishing date 2019-02-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 304266-2
    ISSN 1432-0827 ; 0944-0747 ; 0008-0594 ; 0171-967X
    ISSN (online) 1432-0827
    ISSN 0944-0747 ; 0008-0594 ; 0171-967X
    DOI 10.1007/s00223-019-00520-5
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  6. Article ; Online: Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration.

    Taylor, J Paul

    Neurology

    2015  Volume 85, Issue 8, Page(s) 658–660

    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Distal Myopathies/genetics ; Humans ; Male ; Vacuoles/pathology
    Chemical Substances Adaptor Proteins, Signal Transducing
    Language English
    Publishing date 2015-08-25
    Publishing country United States
    Document type Comment ; Editorial
    ZDB-ID 207147-2
    ISSN 1526-632X ; 0028-3878
    ISSN (online) 1526-632X
    ISSN 0028-3878
    DOI 10.1212/WNL.0000000000001862
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  7. Article: Metastable condensates suppress conversion to amyloid fibrils.

    Das, Tapojyoti / Zaidi, Fatima / Farag, Mina / Ruff, Kiersten M / Messing, James / Taylor, J Paul / Pappu, Rohit V / Mittag, Tanja

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Stress granules form via co-condensation of RNA binding proteins with prion-like low complexity domains (PLCDs) and RNA molecules released by stress-induced polysomal runoff. Homotypic interactions among PLCDs can drive amyloid fibril formation and this ... ...

    Abstract Stress granules form via co-condensation of RNA binding proteins with prion-like low complexity domains (PLCDs) and RNA molecules released by stress-induced polysomal runoff. Homotypic interactions among PLCDs can drive amyloid fibril formation and this is enhanced by ALS-associated mutations. We find that homotypic interactions that drive condensation versus fibril formation are separable for A1-LCD, the PLCD of hnRNPA1. These separable interactions lead to condensates that are metastable versus fibrils that are globally stable. Metastable condensates suppress fibril formation, and ALS-associated mutations enhance fibril formation by weakening condensate metastability. Mutations designed to enhance A1-LCD condensate metastability restore wild-type behaviors of stress granules in cells even when ALS-associated mutations are present. This suggests that fibril formation can be suppressed by enhancing condensate metastability through condensate-driving interactions.
    Language English
    Publishing date 2024-03-03
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.02.28.582569
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  8. Article ; Online: Neurodegenerative diseases: G-quadruplex poses quadruple threat.

    Taylor, J Paul

    Nature

    2014  Volume 507, Issue 7491, Page(s) 175–177

    MeSH term(s) DNA Repeat Expansion/genetics ; Humans ; Open Reading Frames/genetics
    Language English
    Publishing date 2014-03-05
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature13067
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  9. Article: Linking hnRNP Function to ALS and FTD Pathology.

    Purice, Maria D / Taylor, J Paul

    Frontiers in neuroscience

    2018  Volume 12, Page(s) 326

    Abstract: Following years of rapid progress identifying the genetic underpinnings of amyotrophic lateral sclerosis (ALS) and related diseases such as frontotemporal dementia (FTD), remarkable consistencies have emerged pointing to perturbed biology of ... ...

    Abstract Following years of rapid progress identifying the genetic underpinnings of amyotrophic lateral sclerosis (ALS) and related diseases such as frontotemporal dementia (FTD), remarkable consistencies have emerged pointing to perturbed biology of heterogeneous nuclear ribonucleoproteins (hnRNPs) as a central driver of pathobiology. To varying extents these RNA-binding proteins are deposited in pathological inclusions in affected tissues in ALS and FTD. Moreover, mutations in hnRNPs account for a significant number of familial cases of ALS and FTD. Here we review the normal function and potential pathogenic contribution of TDP-43, FUS, hnRNP A1, hnRNP A2B1, MATR3, and TIA1 to disease. We highlight recent evidence linking the low complexity sequence domains (LCDs) of these hnRNPs to the formation of membraneless organelles and discuss how alterations in the dynamics of these organelles could contribute to disease. In particular, we discuss the various roles of disease-associated hnRNPs in stress granule assembly and disassembly, and examine the emerging hypothesis that disease-causing mutations in these proteins lead to accumulation of persistent stress granules.
    Language English
    Publishing date 2018-05-15
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2018.00326
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  10. Article ; Online: Beyond aggregation: Pathological phase transitions in neurodegenerative disease.

    Mathieu, Cécile / Pappu, Rohit V / Taylor, J Paul

    Science (New York, N.Y.)

    2020  Volume 370, Issue 6512, Page(s) 56–60

    Abstract: Over the past decade, phase transitions have emerged as a fundamental mechanism of cellular organization. In parallel, a wealth of evidence has accrued indicating that aberrations in phase transitions are early events in the pathogenesis of several ... ...

    Abstract Over the past decade, phase transitions have emerged as a fundamental mechanism of cellular organization. In parallel, a wealth of evidence has accrued indicating that aberrations in phase transitions are early events in the pathogenesis of several neurodegenerative diseases. We review the key evidence of defects at multiple levels, from phase transition of individual proteins to the dynamic behavior of complex, multicomponent condensates in neurodegeneration. We also highlight two concepts, dynamical arrest and heterotypic buffering, that are key to understanding how pathological phase transitions relate to pleiotropic defects in cellular functions and the accrual of proteinaceous deposits at end-stage disease. These insights not only illuminate disease etiology but also are likely to guide the development of therapeutic interventions to restore homeostasis.
    MeSH term(s) Animals ; Disease Models, Animal ; Humans ; Neurodegenerative Diseases/metabolism ; Phase Transition ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism
    Chemical Substances Protein Aggregates
    Language English
    Publishing date 2020-09-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abb8032
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