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  1. Book: Prions

    Lawson, Victoria A.

    methods and protocols

    (Methods in molecular biology ; 1658)

    2018  

    Author's details Victoria A. Lawson editor
    Series title Methods in molecular biology ; 1658
    Collection
    Keywords prion disease ; cellular analysis ; cell free propagation ; protein misfolding ; neurodegenerative diseases ; intercellular prion-like conversion
    Subject code 610
    Language English
    Size 330 Seiten, Illustrationen, 25.4 cm x 17.8 cm
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT019404314
    ISBN 978-1-4939-7242-5 ; 1-4939-7242-1 ; 9781493972449 ; 1493972448
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -1658- verfügbar in Königswinter Königswinter

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  2. Book: The cellular and molecular biology of prion disease

    Collins, Steven J. / Lawson, Victoria A.

    2011  

    Author's details ed. Steven J. Collins ; Victoria A. Lawson
    Language English
    Size 238 S. : Ill., graph. Darst.
    Publisher Research Signpost
    Publishing place Kerala
    Publishing country India
    Document type Book
    HBZ-ID HT017382148
    ISBN 978-81-308-0446-0 ; 81-308-0446-8
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2012 A 4258 order for loan Magazin

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  3. Book: Prions

    Lawson, Victoria A

    methods and protocols

    (Methods in molecular biology ; 1658 ; Springer protocols)

    2017  

    Author's details edited by Victoria A. Lawson
    Series title Methods in molecular biology ; 1658
    Springer protocols
    Keywords Prion
    Language English
    Size xi, 371 Seiten, Illustrationen, 25.4 cm x 17.8 cm
    Document type Book
    ISBN 1493972421 ; 9781493972425
    Database Friedrich Loeffler-Institute, Federal Research Institute for Animal Health

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  4. Article ; Online: Preparation and Immunostaining of the Myenteric Plexus of Prion-Infected Mice.

    Ellett, Laura J / Lawson, Victoria A

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

    2017  Volume 1658, Page(s) 285–292

    Abstract: Intracerebral inoculation of mice with the M1000 strain of mouse-adapted human prions results in the consistent accumulation of ... ...

    Abstract Intracerebral inoculation of mice with the M1000 strain of mouse-adapted human prions results in the consistent accumulation of PrP
    MeSH term(s) Animals ; Biomarkers/metabolism ; Disease Models, Animal ; Gene Expression ; Glial Fibrillary Acidic Protein/genetics ; Glial Fibrillary Acidic Protein/metabolism ; Humans ; Ileum/metabolism ; Ileum/pathology ; Immunohistochemistry/methods ; Injections, Intraventricular ; Mice ; Mice, Transgenic ; Microdissection/methods ; Myenteric Plexus/metabolism ; Myenteric Plexus/pathology ; Neurofilament Proteins/genetics ; Neurofilament Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; PrPSc Proteins/genetics ; PrPSc Proteins/metabolism ; Prion Diseases/genetics ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Tissue Fixation/methods
    Chemical Substances Biomarkers ; Glial Fibrillary Acidic Protein ; Neurofilament Proteins ; PrPSc Proteins ; glial fibrillary astrocytic protein, mouse ; neurofilament protein M (111365-29-8)
    Language English
    Publishing date 2017
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7244-9_19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Strain variation in treatment and prevention of human prion diseases.

    Ellett, Laura J / Revill, Zoe T / Koo, Yong Qian / Lawson, Victoria A

    Progress in molecular biology and translational science

    2020  Volume 175, Page(s) 121–145

    Abstract: Transmissible spongiform encephalopathies or prion diseases describe a number of different human disorders that differ in their clinical phenotypes, which are nonetheless united by their transmissible nature and common pathology. Clinical variation in ... ...

    Abstract Transmissible spongiform encephalopathies or prion diseases describe a number of different human disorders that differ in their clinical phenotypes, which are nonetheless united by their transmissible nature and common pathology. Clinical variation in the absence of a conventional infectious agent is believed to be encoded by different conformations of the misfolded prion protein. This misfolded protein is the target of methods designed to prevent disease transmission in a surgical setting and reduction of the misfolded seed or preventing its continued propagation have been the focus of therapeutic strategies. It is therefore possible that strain variation may influence the efficacy of prevention and treatment approaches. Historically, an understanding of prion disease transmission and pathogenesis has been focused on research tools developed using agriculturally relevant strains of prion disease. However, an increased understanding of the molecular biology of human prion disorders has highlighted differences not only between different forms of the disease affecting humans and animals but also within diseases such as Creutzfeldt-Jakob Disease (CJD), which is represented by several sporadic CJD specific conformations and an additional conformation associated with variant CJD. In this chapter we will discuss whether prion strain variation can affect the efficacy of methods used to decontaminate prions and whether strain variation in pre-clinical models of prion disease can be used to identify therapeutic strategies that have the best possible chance of success in the clinic.
    MeSH term(s) Humans ; Prion Diseases/prevention & control ; Prion Diseases/therapy ; Prion Diseases/transmission ; Prions/metabolism
    Chemical Substances Prions
    Language English
    Publishing date 2020-09-11
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2471995-X
    ISSN 1878-0814 ; 0079-6603 ; 1877-1173
    ISSN (online) 1878-0814
    ISSN 0079-6603 ; 1877-1173
    DOI 10.1016/bs.pmbts.2020.08.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs 357: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: The role of lipids in α-synuclein misfolding and neurotoxicity.

    Ugalde, Cathryn L / Lawson, Victoria A / Finkelstein, David I / Hill, Andrew F

    The Journal of biological chemistry

    2019  Volume 294, Issue 23, Page(s) 9016–9028

    Abstract: The misfolding and aggregation of α-synuclein (αsyn) in the central nervous system is associated with a group of neurodegenerative disorders referred to as the synucleinopathies. In addition to being a pathological hallmark of disease, it is now well- ... ...

    Abstract The misfolding and aggregation of α-synuclein (αsyn) in the central nervous system is associated with a group of neurodegenerative disorders referred to as the synucleinopathies. In addition to being a pathological hallmark of disease, it is now well-established that upon misfolding, αsyn acquires pathogenic properties, such as neurotoxicity, that can contribute to disease development. The mechanisms that produce αsyn misfolding and the molecular events underlying the neuronal damage caused by these misfolded species are not well-defined. A consistent observation that may be relevant to αsyn's pathogenicity is its ability to associate with lipids. This appears important not only to how αsyn aggregates, but also to the mechanism by which the misfolded protein causes intracellular damage. This review discusses the current literature reporting a role of lipids in αsyn misfolding and neurotoxicity in various synucleinopathy disorders and provides an overview of current methods to assess protein misfolding and pathogenicity both
    MeSH term(s) Central Nervous System/metabolism ; Fatty Acids, Unsaturated/chemistry ; Fatty Acids, Unsaturated/metabolism ; Humans ; Lipids/chemistry ; Protein Aggregation, Pathological ; Proteostasis Deficiencies/metabolism ; Proteostasis Deficiencies/pathology ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism
    Chemical Substances Fatty Acids, Unsaturated ; Lipids ; alpha-Synuclein
    Language English
    Publishing date 2019-05-07
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.REV119.007500
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  7. Article: Quantitative bioassay of surface-bound prion infectivity.

    Lawson, Victoria A

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

    2008  Volume 459, Page(s) 265–273

    Abstract: The unconventional nature of the infectious agent of prion diseases poses a challenge to conventional infection control methodologies. The extra neural tissue distribution of variant and sporadic Creutzfeldt-Jakob disease has increased concern regarding ... ...

    Abstract The unconventional nature of the infectious agent of prion diseases poses a challenge to conventional infection control methodologies. The extra neural tissue distribution of variant and sporadic Creutzfeldt-Jakob disease has increased concern regarding the risk of prion disease transmission via general surgical procedures and highlighted the need for decontamination procedures that can be incorporated into routine processing. This chapter describe a quantitative method for assessing the prionocidal activity of chemical and physical decontamination methods against surface-bound prion infectivity.
    MeSH term(s) Animals ; Biological Assay/methods ; Brain/pathology ; Decontamination ; Mice ; PrPC Proteins/pathogenicity ; Surface Properties
    Chemical Substances PrPC Proteins
    Language English
    Publishing date 2008
    Publishing country United States
    Document type Journal Article
    ISSN 1064-3745
    ISSN 1064-3745
    DOI 10.1007/978-1-59745-234-2_18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Understanding the nature of prion diseases using cell-free assays.

    Lawson, Victoria A

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

    2008  Volume 459, Page(s) 97–103

    Abstract: A central event in the transmission and pathogenesis of transmissible spongiform encephalopathy diseases is the misfolding of the prion protein. Considerable progress has been made in our understanding of this misfolding event through the development of ... ...

    Abstract A central event in the transmission and pathogenesis of transmissible spongiform encephalopathy diseases is the misfolding of the prion protein. Considerable progress has been made in our understanding of this misfolding event through the development of cell-free assays that mimic the molecular features of prion propagation. This chapter reviews the contribution of cell-free assays to our understanding of prion propagation.
    MeSH term(s) Animals ; Biological Assay/methods ; Cell-Free System ; Humans ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Prions/metabolism
    Chemical Substances Prions
    Language English
    Publishing date 2008
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 1064-3745
    ISSN 1064-3745
    DOI 10.1007/978-1-59745-234-2_7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Prion Diseases.

    Whitechurch, Benjamin C / Welton, Jeremy M / Collins, Steven J / Lawson, Victoria A

    Advances in neurobiology

    2017  Volume 15, Page(s) 335–364

    Abstract: Prion diseases are a group of invariably fatal and transmissible neurodegenerative disorders that are associated with the misfolding of the normal cellular prion protein, with the misfolded conformers constituting an infectious unit referred to as a " ... ...

    Abstract Prion diseases are a group of invariably fatal and transmissible neurodegenerative disorders that are associated with the misfolding of the normal cellular prion protein, with the misfolded conformers constituting an infectious unit referred to as a "prion". Prions can spread within an affected organism by directly propagating this misfolding within and between cells and can transmit disease between animals of the same and different species. Prion diseases have a range of clinical phenotypes in humans and animals, with a principle determinant of this attributed to different conformations of the misfolded protein, referred to as prion strains. This chapter will describe the different clinical manifestations of prion diseases, the evidence that these diseases can be transmitted by an infectious protein and how the misfolding of this protein causes disease.
    MeSH term(s) Animals ; Astrocytes/metabolism ; Astrocytes/pathology ; Cattle ; Creutzfeldt-Jakob Syndrome/metabolism ; Creutzfeldt-Jakob Syndrome/pathology ; Creutzfeldt-Jakob Syndrome/transmission ; Deer ; Encephalopathy, Bovine Spongiform/metabolism ; Encephalopathy, Bovine Spongiform/pathology ; Encephalopathy, Bovine Spongiform/transmission ; Gliosis/metabolism ; Gliosis/pathology ; Humans ; Hyperplasia ; Hypertrophy ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Prion Diseases/transmission ; Prion Proteins/metabolism ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Protein Folding ; Scrapie/metabolism ; Scrapie/pathology ; Scrapie/transmission ; Wasting Disease, Chronic/metabolism ; Wasting Disease, Chronic/pathology ; Wasting Disease, Chronic/transmission
    Chemical Substances Prion Proteins
    Language English
    Publishing date 2017-07-03
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2190-5215
    ISSN 2190-5215
    DOI 10.1007/978-3-319-57193-5_13
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: In Vivo-Near Infrared Imaging of Neurodegeneration.

    Lawson, Victoria A / Tumpach, Carolin / Haigh, Cathryn L / Drew, Simon C

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

    2017  Volume 1658, Page(s) 253–262

    Abstract: In vivo near-infrared (NIR) imaging of molecular processes at the preclinical stage promises to provide more valuable mechanistic information about pathological pathways involved in neurodegeneration. NIR imaging has the potential to improve in vivo ... ...

    Abstract In vivo near-infrared (NIR) imaging of molecular processes at the preclinical stage promises to provide more valuable mechanistic information about pathological pathways involved in neurodegeneration. NIR imaging has the potential to improve in vivo therapeutic screening protocols by enabling noninvasive monitoring of presymptomatic responses to treatment. We have developed new NIR fluorescent contrast agents conjugated to markers of cell death, and using these agents we have identified molecular pathways associated with prion-induced neurodegeneration and determined the optimal window for meaningful therapeutic intervention in prion disease. This chapter provides a description of the synthesis and purification of our NIR cell Death (NIRD) contrast agent and the application of in vivo NIRD (iNIRD) imaging to a prion model of neurodegeneration.
    MeSH term(s) Amino Acid Chloromethyl Ketones/chemistry ; Amino Acid Chloromethyl Ketones/pharmacokinetics ; Animals ; Brain/diagnostic imaging ; Brain/metabolism ; Brain/pathology ; Caspase Inhibitors/chemistry ; Caspase Inhibitors/pharmacokinetics ; Caspases/genetics ; Caspases/metabolism ; Cell Death ; Contrast Media/chemical synthesis ; Contrast Media/pharmacokinetics ; Injections, Intravenous ; Mice ; Molecular Imaging/methods ; Prion Diseases/diagnostic imaging ; Prion Diseases/genetics ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Spectroscopy, Near-Infrared/methods ; Staining and Labeling/methods ; Succinimides/chemistry
    Chemical Substances Amino Acid Chloromethyl Ketones ; Caspase Inhibitors ; Contrast Media ; Succinimides ; benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone ; Caspases (EC 3.4.22.-)
    Language English
    Publishing date 2017
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7244-9_17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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