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  1. Article ; Online: A shared fate for nuclear and cytosolic inclusions.

    Alberti, Simon / Carra, Serena

    Nature cell biology

    2023  Volume 25, Issue 5, Page(s) 629–630

    MeSH term(s) Cell Nucleus ; Cytosol
    Language English
    Publishing date 2023-04-18
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-023-01121-z
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5169: Show issues Location:
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  2. Article: PML nuclear bodies: new players in familial amyotrophic lateral sclerosis-frontotemporal dementia?

    Goswami, Anand / Carra, Serena

    Neural regeneration research

    2023  Volume 19, Issue 9, Page(s) 1875–1876

    Language English
    Publishing date 2023-12-21
    Publishing country India
    Document type Journal Article
    ZDB-ID 2388460-5
    ISSN 1876-7958 ; 1673-5374
    ISSN (online) 1876-7958
    ISSN 1673-5374
    DOI 10.4103/1673-5374.391183
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  3. Article ; Online: Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation.

    Hibshman, Jonathan D / Carra, Serena / Goldstein, Bob

    Communications biology

    2023  Volume 6, Issue 1, Page(s) 121

    Abstract: Small heat shock proteins (sHSPs) are chaperones with well-characterized roles in heat stress, but potential roles for sHSPs in desiccation tolerance have not been as thoroughly explored. We identified nine sHSPs from the tardigrade Hypsibius exemplaris, ...

    Abstract Small heat shock proteins (sHSPs) are chaperones with well-characterized roles in heat stress, but potential roles for sHSPs in desiccation tolerance have not been as thoroughly explored. We identified nine sHSPs from the tardigrade Hypsibius exemplaris, each containing a conserved alpha-crystallin domain flanked by disordered regions. Many of these sHSPs are highly expressed. Multiple tardigrade and human sHSPs could improve desiccation tolerance of E. coli, suggesting that the capacity to contribute to desicco-protection is a conserved property of some sHSPs. Purification and subsequent analysis of two tardigrade sHSPs, HSP21 and HSP24.6, revealed that these proteins can oligomerize in vitro. These proteins limited heat-induced aggregation of the model enzyme citrate synthase. Heterologous expression of HSP24.6 improved bacterial heat shock survival, and the protein significantly reduced heat-induced aggregation of soluble bacterial protein. Thus, HSP24.6 likely chaperones against protein aggregation to promote heat tolerance. Furthermore, HSP21 and HSP24.6 limited desiccation-induced aggregation and loss of function of citrate synthase. This suggests a mechanism by which tardigrade sHSPs promote desiccation tolerance, by limiting desiccation-induced protein aggregation, thereby maintaining proteostasis and supporting survival. These results suggest that sHSPs provide a mechanism of general stress resistance that can also be deployed to support survival during anhydrobiosis.
    MeSH term(s) Animals ; Citrate (si)-Synthase ; Desiccation ; Escherichia coli/metabolism ; Heat-Shock Proteins, Small/metabolism ; Molecular Chaperones/metabolism ; Protein Aggregates ; Tardigrada
    Chemical Substances Citrate (si)-Synthase (EC 2.3.3.1) ; Heat-Shock Proteins, Small ; Molecular Chaperones ; Protein Aggregates
    Language English
    Publishing date 2023-01-30
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-023-04512-y
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  4. Article ; Online: Nucleolus: A Liquid Droplet Compartment for Misbehaving Proteins.

    Alberti, Simon / Carra, Serena

    Current biology : CB

    2019  Volume 29, Issue 19, Page(s) R930–R932

    Abstract: A new study reports an unexpected function of the nucleolus as a protein quality control compartment for misfolded and aggregation-prone proteins. These findings have important implications for protein misfolding diseases. ...

    Abstract A new study reports an unexpected function of the nucleolus as a protein quality control compartment for misfolded and aggregation-prone proteins. These findings have important implications for protein misfolding diseases.
    MeSH term(s) Cell Nucleolus ; Humans ; Protein Folding ; Proteostasis Deficiencies
    Language English
    Publishing date 2019-10-08
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2019.08.013
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  5. Article ; Online: Quality Control of Membraneless Organelles.

    Alberti, Simon / Carra, Serena

    Journal of molecular biology

    2018  Volume 430, Issue 23, Page(s) 4711–4729

    Abstract: The formation of membraneless organelles (MLOs) by phase separation has emerged as a new way of organizing the cytoplasm and nucleoplasm of cells. Examples of MLOs forming via phase separation are nucleoli in the nucleus and stress granules in the ... ...

    Abstract The formation of membraneless organelles (MLOs) by phase separation has emerged as a new way of organizing the cytoplasm and nucleoplasm of cells. Examples of MLOs forming via phase separation are nucleoli in the nucleus and stress granules in the cytoplasm. The main components of these MLOs are macromolecules such as RNAs and proteins. In order to assemble by phase separation, these proteins and RNAs have to undergo many cooperative interactions. These cooperative interactions are supported by specific molecular features within phase-separating proteins, such as multivalency and the presence of disordered domains that promote weak and transient interactions. However, these features also predispose phase-separating proteins to aberrant behavior. Indeed, evidence is emerging for a strong link between phase-separating proteins, MLOs, and age-related diseases. In this review, we discuss recent progress in understanding the formation, properties, and functions of MLOs. We pay special attention to the emerging link between MLOs and age-related diseases, and we explain how changes in the composition and physical properties of MLOs promote their conversion into an aberrant state. Furthermore, we discuss the key role of the protein quality control machinery in regulating the properties and functions of MLOs and thus in preventing age-related diseases.
    MeSH term(s) Animals ; Cytoplasm/metabolism ; Humans ; Intranuclear Space/metabolism ; Organelles/metabolism ; Proteins/metabolism ; Quality Control ; RNA/metabolism
    Chemical Substances Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2018-05-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2018.05.013
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  6. Article ; Online: Studying heat shock proteins through single-molecule mechanical manipulation.

    Choudhary, Dhawal / Mediani, Laura / Carra, Serena / Cecconi, Ciro

    Cell stress & chaperones

    2020  Volume 25, Issue 4, Page(s) 615–628

    Abstract: Imbalances of cellular proteostasis are linked to ageing and human diseases, including neurodegenerative and neuromuscular diseases. Heat shock proteins (HSPs) and small heat shock proteins (sHSPs) together form a crucial core of the molecular chaperone ... ...

    Abstract Imbalances of cellular proteostasis are linked to ageing and human diseases, including neurodegenerative and neuromuscular diseases. Heat shock proteins (HSPs) and small heat shock proteins (sHSPs) together form a crucial core of the molecular chaperone family that plays a vital role in maintaining cellular proteostasis by shielding client proteins against aggregation and misfolding. sHSPs are thought to act as the first line of defence against protein unfolding/misfolding and have been suggested to act as "sponges" that rapidly sequester these aberrant species for further processing, refolding, or degradation, with the assistance of the HSP70 chaperone system. Understanding how these chaperones work at the molecular level will offer unprecedented insights for their manipulation as therapeutic avenues for the treatment of ageing and human disease. The evolution in single-molecule force spectroscopy techniques, such as optical tweezers (OT) and atomic force microscopy (AFM), over the last few decades have made it possible to explore at the single-molecule level the structural dynamics of HSPs and sHSPs and to examine the key molecular mechanisms underlying their chaperone activities. In this paper, we describe the working principles of OT and AFM and the experimental strategies used to employ these techniques to study molecular chaperones. We then describe the results of some of the most relevant single-molecule manipulation studies on HSPs and sHSPs and discuss how these findings suggest a more complex physiological role for these chaperones than previously assumed.
    MeSH term(s) Animals ; Bacteria ; Heat-Shock Proteins, Small/chemistry ; Heat-Shock Proteins, Small/physiology ; Humans ; Microscopy, Atomic Force/methods ; Optical Tweezers ; Plants ; Protein Folding ; Proteostasis ; Stress, Mechanical
    Chemical Substances Heat-Shock Proteins, Small
    Language English
    Publishing date 2020-04-06
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1362749-1
    ISSN 1466-1268 ; 1355-8145
    ISSN (online) 1466-1268
    ISSN 1355-8145
    DOI 10.1007/s12192-020-01096-y
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    Zs.A 4797: Show issues Location:
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  7. Article ; Online: Targeting the NEDP1 enzyme to ameliorate ALS phenotypes through stress granule disassembly.

    Kassouf, Toufic / Shrivastava, Rohit / Meszka, Igor / Bailly, Aymeric / Polanowska, Jolanta / Trauchessec, Helene / Mandrioli, Jessica / Carra, Serena / Xirodimas, Dimitris P

    Science advances

    2023  Volume 9, Issue 13, Page(s) eabq7585

    Abstract: The elimination of aberrant inclusions is regarded as a therapeutic approach in neurodegeneration. In amyotrophic lateral sclerosis (ALS), mutations in proteins found within cytoplasmic condensates called stress granules (SGs) are linked to the formation ...

    Abstract The elimination of aberrant inclusions is regarded as a therapeutic approach in neurodegeneration. In amyotrophic lateral sclerosis (ALS), mutations in proteins found within cytoplasmic condensates called stress granules (SGs) are linked to the formation of pathological SGs, aberrant protein inclusions, and neuronal toxicity. We found that inhibition of NEDP1, the enzyme that processes/deconjugates the ubiquitin-like molecule NEDD8, promotes the disassembly of physiological and pathological SGs. Reduction in poly(ADP-ribose) polymerase1 activity through hyper-NEDDylation is a key mechanism for the observed phenotype. These effects are related to improved cell survival in human cells, and in
    MeSH term(s) Animals ; Humans ; Amyotrophic Lateral Sclerosis/drug therapy ; Amyotrophic Lateral Sclerosis/genetics ; Caenorhabditis elegans/genetics ; Stress Granules ; Ubiquitin ; Phenotype
    Chemical Substances Ubiquitin
    Language English
    Publishing date 2023-03-31
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abq7585
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  8. Article: Case report: p.Glu134del

    Gianferrari, Giulia / Martinelli, Ilaria / Simonini, Cecilia / Zucchi, Elisabetta / Fini, Nicola / Carra, Serena / Moglia, Cristina / Mandrioli, Jessica

    Frontiers in neurology

    2023  Volume 13, Page(s) 1052341

    Abstract: With upcoming personalized approaches based on genetics, it is important to report new mutations in amyotrophic lateral sclerosis (ALS) genes in order to understand their pathogenicity and possible patient responses to specific therapies. ...

    Abstract With upcoming personalized approaches based on genetics, it is important to report new mutations in amyotrophic lateral sclerosis (ALS) genes in order to understand their pathogenicity and possible patient responses to specific therapies.
    Language English
    Publishing date 2023-01-04
    Publishing country Switzerland
    Document type Case Reports
    ZDB-ID 2564214-5
    ISSN 1664-2295
    ISSN 1664-2295
    DOI 10.3389/fneur.2022.1052341
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  9. Article ; Online: SerpinA1 levels in amyotrophic lateral sclerosis patients: An exploratory study.

    Martinelli, Ilaria / Zucchi, Elisabetta / Simonini, Cecilia / Gianferrari, Giulia / Bedin, Roberta / Biral, Chiara / Ghezzi, Andrea / Fini, Nicola / Carra, Serena / Mandrioli, Jessica

    European journal of neurology

    2023  Volume 31, Issue 1, Page(s) e16054

    Abstract: Background: SerpinA1, a serine protease inhibitor, is involved in the modulation of microglial-mediated inflammation in neurodegenerative diseases. We explored SerpinA1 levels in cerebrospinal fluid (CSF) and serum of amyotrophic lateral sclerosis (ALS) ...

    Abstract Background: SerpinA1, a serine protease inhibitor, is involved in the modulation of microglial-mediated inflammation in neurodegenerative diseases. We explored SerpinA1 levels in cerebrospinal fluid (CSF) and serum of amyotrophic lateral sclerosis (ALS) patients to understand its potential role in the pathogenesis of the disease.
    Methods: SerpinA1, neurofilament light (NfL) and heavy (NfH) chain, and chitinase-3-like protein-1 (CHI3L1) were determined in CSF and serum of ALS patients (n = 110) and healthy controls (n = 10) (automated next-generation ELISA), and correlated with clinical parameters, after identifying three classes of progressors (fast, intermediate, slow). Biomarker levels were analyzed for diagnostic power and association with progression and survival.
    Results: SerpinA1
    Conclusions: Higher SerpinA1
    MeSH term(s) Humans ; Amyotrophic Lateral Sclerosis/diagnosis ; Disease Progression ; Neurofilament Proteins/cerebrospinal fluid ; Prognosis ; Biomarkers
    Chemical Substances Neurofilament Proteins ; Biomarkers
    Language English
    Publishing date 2023-09-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1280785-0
    ISSN 1468-1331 ; 1351-5101 ; 1471-0552
    ISSN (online) 1468-1331
    ISSN 1351-5101 ; 1471-0552
    DOI 10.1111/ene.16054
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    Zs.A 4738: Show issues Location:
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    Zs.MO 592: Show issues

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  10. Article ; Online: ALS and FTD: Where RNA metabolism meets protein quality control.

    Mandrioli, Jessica / Mediani, Laura / Alberti, Simon / Carra, Serena

    Seminars in cell & developmental biology

    2019  Volume 99, Page(s) 183–192

    Abstract: Recent genetic and biochemical evidence has improved our understanding of the pathomechanisms that lead to amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), two devastating neurodegenerative diseases with overlapping symptoms and ... ...

    Abstract Recent genetic and biochemical evidence has improved our understanding of the pathomechanisms that lead to amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), two devastating neurodegenerative diseases with overlapping symptoms and causes. Impaired RNA metabolism, enhanced aggregation of protein-RNA complexes, aberrant formation of ribonucleoprotein (RNP) granules and dysfunctional protein clearance via autophagy are emerging as crucial events in ALS/FTD pathogenesis. Importantly, these processes interact at the molecular level, converging on a common pathogenic cascade. In this review, we summarize key principles underlying ALS and FTD, and we discuss how mutations in genes involved in RNA metabolism, protein quality control and protein degradation meet mechanistically to impair the functionality and dynamics of RNP granules, and how this leads to cellular toxicity and death. Finally, we describe recent advances in understanding signaling pathways that become dysfunctional in ALS/FTD, partly due to altered RNP granule dynamics, but also with stress granule-independent mechanisms and, thus could be promising targets for future therapeutic intervention.
    MeSH term(s) Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Humans ; RNA/genetics ; RNA/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances RNA-Binding Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2019-07-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2019.06.003
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