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  1. Article ; Online: α-Synuclein seed amplification technology for Parkinson's disease and related synucleinopathies.

    Soto, Claudio

    Trends in biotechnology

    2024  

    Abstract: Synucleinopathies are a group of neurodegenerative diseases (NDs) associated with cerebral accumulation of α-synuclein (αSyn) misfolded aggregates. At this time, there is no effective treatment to stop or slow down disease progression, which in part is ... ...

    Abstract Synucleinopathies are a group of neurodegenerative diseases (NDs) associated with cerebral accumulation of α-synuclein (αSyn) misfolded aggregates. At this time, there is no effective treatment to stop or slow down disease progression, which in part is due to the lack of an early and objective biochemical diagnosis. In the past 5 years, the seed amplification technology has emerged for highly sensitive identification of these diseases, even at the preclinical stage of the illness. Much research has been done in multiple laboratories to validate the efficacy and reproducibility of this assay. This article provides a comprehensive review of this technology, including its conceptual basis and its multiple applications for disease diagnosis, as well for understanding of the disease biology and therapeutic development.
    Language English
    Publishing date 2024-02-22
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 47474-5
    ISSN 1879-3096 ; 0167-7799
    ISSN (online) 1879-3096
    ISSN 0167-7799
    DOI 10.1016/j.tibtech.2024.01.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2750: Show issues Location:
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  2. Article: Editorial: Prion-Like transmission of pathogenic proteins in neurodegenerative diseases: structural and molecular bases.

    Banerjee, Victor / Wang, Fei / Sarnataro, Daniela / Soto, Claudio

    Frontiers in molecular biosciences

    2023  Volume 10, Page(s) 1294465

    Language English
    Publishing date 2023-09-21
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2023.1294465
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: α-synuclein seed amplification in Parkinson's disease - Authors' reply.

    Siderowf, Andrew / Concha-Marambio, Luis / Marek, Kenneth / Soto, Claudio

    The Lancet. Neurology

    2023  Volume 22, Issue 11, Page(s) 985–986

    MeSH term(s) Humans ; alpha-Synuclein/genetics ; Parkinson Disease/genetics
    Chemical Substances alpha-Synuclein
    Language English
    Publishing date 2023-10-27
    Publishing country England
    Document type Letter ; Comment
    ZDB-ID 2081241-3
    ISSN 1474-4465 ; 1474-4422
    ISSN (online) 1474-4465
    ISSN 1474-4422
    DOI 10.1016/S1474-4422(23)00371-X
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5955: Show issues Location:
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  4. Article ; Online: PMCA for ultrasensitive detection of prions and to study disease biology.

    Wang, Fei / Pritzkow, Sandra / Soto, Claudio

    Cell and tissue research

    2022  Volume 392, Issue 1, Page(s) 307–321

    Abstract: The emergence of a novel class of infectious agent composed exclusively of a misfolded protein (termed prions) has been a challenge in modern biomedicine. Despite similarities on the behavior of prions with respect to conventional pathogens, the many ... ...

    Abstract The emergence of a novel class of infectious agent composed exclusively of a misfolded protein (termed prions) has been a challenge in modern biomedicine. Despite similarities on the behavior of prions with respect to conventional pathogens, the many uncertainties regarding the biology and virulence of prions make them a worrisome paradigm. Since prions do not contain nucleic acids and rely on a very different way of replication and spreading, it was necessary to invent a novel technology to study them. In this article, we provide an overview of such a technology, termed protein misfolding cyclic amplification (PMCA), and summarize its many applications to detect prions and understand prion biology.
    MeSH term(s) Humans ; Prions/metabolism ; Prion Diseases/diagnosis ; Prion Diseases/metabolism ; Protein Folding ; Biology
    Chemical Substances Prions
    Language English
    Publishing date 2022-12-26
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 125067-x
    ISSN 1432-0878 ; 0302-766X
    ISSN (online) 1432-0878
    ISSN 0302-766X
    DOI 10.1007/s00441-022-03727-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Development of a novel pharmacophore model to screen specific inhibitors for the serine-threonine protein phosphatase calcineurin.

    Mukherjee, Abhisek / Cuanalo-Contreras, Karina / Sood, Abha / Soto, Claudio

    Biochemistry and biophysics reports

    2022  Volume 31, Page(s) 101311

    Abstract: Calcineurin (CaN) is a calcium/calmodulin-dependent serine/threonine phosphatase with a crucial role in cellular homeostasis. It is also the target of the Food and Drug Administration (FDA) approved immunosuppressant drugs FK506 and cyclosporine A. ... ...

    Abstract Calcineurin (CaN) is a calcium/calmodulin-dependent serine/threonine phosphatase with a crucial role in cellular homeostasis. It is also the target of the Food and Drug Administration (FDA) approved immunosuppressant drugs FK506 and cyclosporine A. Recent work from our group and others indicated that an uncontrolled increase in CaN activity causes synaptic dysfunction and neuronal death in various models of neurodegenerative diseases associated with calcium dysregulation. Furthermore, pharmacological normalization of CaN activity can prevent disease progression in animal models. However, none of the FDA-approved CaN inhibitors bind CaN directly, leading to adverse side effects. The development of direct CaN inhibitors is required to reduce off-target effects, but its highly conserved active site and similar mechanism of action with other protein serine/threonine phosphatases impose a significant challenge. In this work, we developed a novel pharmacophore model to screen for CaN-specific inhibitors. Then, we performed a virtual screen for molecules having the pharmacophore model. We also show that the molecules identified in this screen can inhibit CaN with a low micromolar IC
    Language English
    Publishing date 2022-08-12
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2831046-9
    ISSN 2405-5808 ; 2405-5808
    ISSN (online) 2405-5808
    ISSN 2405-5808
    DOI 10.1016/j.bbrep.2022.101311
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  6. Article ; Online: Prion Dissemination through the Environment and Medical Practices: Facts and Risks for Human Health.

    Pritzkow, Sandra / Gorski, Damian / Ramirez, Frank / Soto, Claudio

    Clinical microbiology reviews

    2021  Volume 34, Issue 4, Page(s) e0005919

    Abstract: Prion diseases are a group of fatal, infectious neurodegenerative disorders affecting various species of mammals, including humans. The infectious agent in these diseases, termed prion, is composed exclusively of a misfolded protein that can spread and ... ...

    Abstract Prion diseases are a group of fatal, infectious neurodegenerative disorders affecting various species of mammals, including humans. The infectious agent in these diseases, termed prion, is composed exclusively of a misfolded protein that can spread and multiply in the absence of genetic materials. In this article, we provide an overview of the mechanisms of prion replication, interindividual transmission, and dissemination in communities. In particular, we review the potential role of the natural environment in prion transmission, including the mechanisms and pathways for prion entry and accumulation in the environment as well as its roles in prion mutation, adaptation, evolution, and transmission. We also discuss the transmission of prion diseases through medical practices, scientific research, and use of biological products. Detailed knowledge of these aspects is crucial to limit the spreading of existing prion diseases as well as to prevent the emergence of new diseases with possible catastrophic consequences for public health.
    MeSH term(s) Animals ; Humans ; Prion Diseases/epidemiology ; Prions/genetics
    Chemical Substances Prions
    Language English
    Publishing date 2021-07-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 645015-5
    ISSN 1098-6618 ; 0893-8512
    ISSN (online) 1098-6618
    ISSN 0893-8512
    DOI 10.1128/CMR.00059-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2409: Show issues Location:
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  7. Article ; Online: Uptake, Retention, and Excretion of Infectious Prions by Experimentally Exposed Earthworms.

    Pritzkow, Sandra / Morales, Rodrigo / Camacho, Manuel / Soto, Claudio

    Emerging infectious diseases

    2021  Volume 27, Issue 12, Page(s) 3151–3154

    Abstract: Prions are proteinaceous infectious agents that can be transmitted through various components of the environment, including soil particles. We found that earthworms exposed to prion-contaminated soil can bind, retain, and excrete prions, which remain ... ...

    Abstract Prions are proteinaceous infectious agents that can be transmitted through various components of the environment, including soil particles. We found that earthworms exposed to prion-contaminated soil can bind, retain, and excrete prions, which remain highly infectious. Our results suggest that earthworms potentially contribute to prion disease spread in the environment.
    MeSH term(s) Animals ; Communicable Diseases ; Oligochaeta ; Prion Diseases ; Prions ; Soil ; Wasting Disease, Chronic
    Chemical Substances Prions ; Soil
    Language English
    Publishing date 2021-11-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1380686-5
    ISSN 1080-6059 ; 1080-6040
    ISSN (online) 1080-6059
    ISSN 1080-6040
    DOI 10.3201/eid2712.204236
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4778: Show issues Location:
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  8. Article ; Online: Seed amplification assay for the detection of pathologic alpha-synuclein aggregates in cerebrospinal fluid.

    Concha-Marambio, Luis / Pritzkow, Sandra / Shahnawaz, Mohammad / Farris, Carly M / Soto, Claudio

    Nature protocols

    2023  Volume 18, Issue 4, Page(s) 1179–1196

    Abstract: Misfolded alpha-synuclein (αSyn) aggregates are a hallmark event in Parkinson's disease (PD) and other synucleinopathies. Recently, αSyn seed amplification assays (αSyn-SAAs) have shown promise as a test for biochemical diagnosis of synucleinopathies. ... ...

    Abstract Misfolded alpha-synuclein (αSyn) aggregates are a hallmark event in Parkinson's disease (PD) and other synucleinopathies. Recently, αSyn seed amplification assays (αSyn-SAAs) have shown promise as a test for biochemical diagnosis of synucleinopathies. αSyn-SAAs use the intrinsic self-replicative nature of misfolded αSyn aggregates (seeds) to multiply them in vitro. In these assays, αSyn seeds circulating in biological fluids are amplified by a cyclical process that includes aggregate fragmentation into smaller self-propagating seeds, followed by elongation at the expense of recombinant αSyn (rec-αSyn). Amplification of the seeds allows detection by fluorescent dyes specific for amyloids, such as thioflavin T. Several αSyn-SAA reports have been published in the past under the names 'protein misfolding cyclic amplification' (αSyn-PMCA) and 'real-time quaking-induced conversion'. Here, we describe a protocol for αSyn-SAA, originally reported as αSyn-PMCA, which allows detection of αSyn aggregates in cerebrospinal fluid samples from patients affected by PD, dementia with Lewy bodies or multiple-system atrophy (MSA). Moreover, this αSyn-SAA can differentiate αSyn aggregates from patients with PD versus those from patients with MSA, even in retrospective samples from patients with pure autonomic failure who later developed PD or MSA. We also describe modifications to the original protocol introduced to develop an optimized version of the assay. The optimized version shortens the assay length, decreases the amount of rec-αSyn required and reduces the number of inconclusive results. The protocol has a hands-on time of ~2 h per 96-well plate and can be performed by personnel trained to perform basic experiments with specimens of human origin.
    MeSH term(s) Humans ; alpha-Synuclein/cerebrospinal fluid ; Synucleinopathies ; Retrospective Studies ; Parkinson Disease/cerebrospinal fluid ; Parkinson Disease/diagnosis
    Chemical Substances alpha-Synuclein
    Language English
    Publishing date 2023-01-18
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2244966-8
    ISSN 1750-2799 ; 1754-2189
    ISSN (online) 1750-2799
    ISSN 1754-2189
    DOI 10.1038/s41596-022-00787-3
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  9. Article: Extensive accumulation of misfolded protein aggregates during natural aging and senescence.

    Cuanalo-Contreras, Karina / Schulz, Jonathan / Mukherjee, Abhisek / Park, Kyung-Won / Armijo, Enrique / Soto, Claudio

    Frontiers in aging neuroscience

    2023  Volume 14, Page(s) 1090109

    Abstract: Accumulation of misfolded protein aggregates is a hallmark event in many age-related protein misfolding disorders, including some of the most prevalent and insidious neurodegenerative diseases. Misfolded protein aggregates produce progressive cell damage, ...

    Abstract Accumulation of misfolded protein aggregates is a hallmark event in many age-related protein misfolding disorders, including some of the most prevalent and insidious neurodegenerative diseases. Misfolded protein aggregates produce progressive cell damage, organ dysfunction, and clinical changes, which are common also in natural aging. Thus, we hypothesized that aging is associated to the widespread and progressive misfolding and aggregation of many proteins in various tissues. In this study, we analyzed whether proteins misfold, aggregate, and accumulate during normal aging in three different biological systems, namely senescent cells,
    Language English
    Publishing date 2023-01-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2022.1090109
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  10. Article ; Online: A retrospective study of Cerebrolysin in patients with moderate to severe traumatic brain injury: Cognitive and functional outcomes.

    Soto, Claudio / Salinas, Pablo / Muñoz, Daniel / Olivares, Sandra / González, Javiera / Sáez, Virginia / Romero, Violeta

    Journal of medicine and life

    2023  Volume 16, Issue 7, Page(s) 1017–1021

    Abstract: In this retrospective study, we aimed to evaluate the effects of the neurotrophic compound Cerebrolysin on executive, cognitive, and functional performance in patients with traumatic brain injury (TBI) with a highly severe disability level. A total of 44 ...

    Abstract In this retrospective study, we aimed to evaluate the effects of the neurotrophic compound Cerebrolysin on executive, cognitive, and functional performance in patients with traumatic brain injury (TBI) with a highly severe disability level. A total of 44 patients were included in the study, with 33 patients in the control group and 11 patients in the interventional group who received intravenous infusions of 30 mL Cerebrolysin. Both groups received standard rehabilitation therapy following the rehabilitation protocol for patients with TBI at Hospital Clínico Mutual de Seguridad. Functional and cognitive scales were evaluated at baseline, at four months, and at the endpoint of the intervention therapy at seven months (on average). The results revealed a significant improvement in the Cerebrolysin-treated group compared to the control group. Specifically, patients who received Cerebrolysin showed a moderate residual disability and a significant reduction in the need for care. Concerning the promising results and considering the limitations of the retrospective study design, we suggest that randomized controlled studies be initiated to corroborate the positive findings for Cerebrolysin in patients with moderate to severe brain trauma.
    MeSH term(s) Humans ; Retrospective Studies ; Brain Injuries/rehabilitation ; Brain Injuries, Traumatic/drug therapy ; Cognition ; Recovery of Function
    Chemical Substances cerebrolysin (37KZM6S21G)
    Language English
    Publishing date 2023-06-09
    Publishing country Romania
    Document type Journal Article
    ZDB-ID 2559353-5
    ISSN 1844-3117 ; 1844-3117 ; 1844-3109
    ISSN (online) 1844-3117
    ISSN 1844-3117 ; 1844-3109
    DOI 10.25122/jml-2023-0125
    Database MEDical Literature Analysis and Retrieval System OnLINE

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