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  1. Book: NLR proteins

    Di Virgilio, Francesco / Pelegrin, Pablo

    methods and protocols

    (Methods in molecular biology ; 2696 ; Springer protocols)

    2023  

    Author's details edited by Pablo Pelegrín, Francesco Di Virgilio
    Series title Methods in molecular biology ; 2696
    Springer protocols
    Collection
    MeSH term(s) Nod Signaling Adaptor Proteins
    Keywords Proteins
    Subject code 572.6
    Language English
    Size xii, 299 Seiten, Illustrationen
    Edition Second edition
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT030343845
    ISBN 9781071633496 ; 9781071633502 ; 107163349X ; 1071633503
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2696- not available for loan Lesesaal EG

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  2. Book: Purinergic signaling

    Pelegrin, Pablo

    methods and protocols

    (Methods in molecular biology ; 2041 ; Springer protocols)

    2020  

    Author's details edited by Pablo Pelegrin
    Series title Methods in molecular biology ; 2041
    Springer protocols
    Collection
    Language English
    Size xii, 360 Seiten, Illustrationen
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT020289036
    ISBN 978-1-4939-9716-9 ; 9781493997176 ; 1-4939-9716-5 ; 1493997173
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2041- verfügbar in Königswinter Königswinter

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  3. Book: NLR proteins

    Di Virgilio, Francesco / Pelegrín, Pablo

    methods and protocols

    (Methods in molecular biology ; 1417 ; Springer protocols)

    2016  

    Author's details edited by Francesco Di Virgilio, Pablo Pelegrín
    Series title Methods in molecular biology ; 1417
    Springer protocols
    Collection
    Keywords Nod Signaling Adaptor Proteins / immunology
    Language English
    Size XI, 256 Seiten, Illustrationen, Diagramme, 26 cm
    Publisher Humana Press
    Publishing place New York
    Publishing country United States
    Document type Book
    Note Includes bibliographical references and index
    HBZ-ID HT019121082
    ISBN 978-1-4939-3564-2 ; 1-4939-3564-X ; 9781493935666 ; 1493935666
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

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    Zs A 7042 -1417- verfügbar in Königswinter Königswinter

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  4. Article ; Online: P2X7 receptor and the NLRP3 inflammasome: Partners in crime.

    Pelegrin, Pablo

    Biochemical pharmacology

    2020  Volume 187, Page(s) 114385

    Abstract: Adenosine triphosphate (ATP) is a molecule that on one hand plays a central role in cellular energetics and which on the other is a ubiquitous signaling molecule when released into the extracellular media. Extracellular ATP accumulates in inflammatory ... ...

    Abstract Adenosine triphosphate (ATP) is a molecule that on one hand plays a central role in cellular energetics and which on the other is a ubiquitous signaling molecule when released into the extracellular media. Extracellular ATP accumulates in inflammatory environments where it acts as a damage-associated molecular pattern and activates the purinergic P2X receptor 7 (P2X7) in immune cells. P2X7 receptor activation induces the formation of the nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing 3 (NLRP3) inflammasome and the activation of the inflammatory caspase-1. Caspase-1 causes an inflammatory type of cell death called pyroptosis through the release of pro-inflammatory cytokines and intracellular content. Consequently, intense research efforts have been devoted to the design of novel anti-inflammatory therapies, focusing in particular on the P2X7 receptor and the NLRP3 pathway and the introduction of new blocking molecules in early phase clinical trials.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Humans ; Inflammation/drug therapy ; Inflammation/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/antagonists & inhibitors ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Purinergic P2X Receptor Agonists/administration & dosage ; Purinergic P2X Receptor Antagonists/administration & dosage ; Receptors, Purinergic P2X7/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology
    Chemical Substances NLR Family, Pyrin Domain-Containing 3 Protein ; Purinergic P2X Receptor Agonists ; Purinergic P2X Receptor Antagonists ; Receptors, Purinergic P2X7 ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2020-12-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 208787-x
    ISSN 1873-2968 ; 0006-2952
    ISSN (online) 1873-2968
    ISSN 0006-2952
    DOI 10.1016/j.bcp.2020.114385
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 19: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Measuring IL-1β Processing by Bioluminescence Sensors: Using a Bioluminescence Resonance Energy Transfer Biosensor.

    Compan, Vincent / Pelegrín, Pablo

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

    2023  Volume 2696, Page(s) 47–53

    Abstract: IL-1β processing is one of the hallmarks of inflammasome activation and drives the initiation of the inflammatory response. For decades, Western blot or ELISA has been extensively used to study this inflammatory event. Here, we describe the use of a ... ...

    Abstract IL-1β processing is one of the hallmarks of inflammasome activation and drives the initiation of the inflammatory response. For decades, Western blot or ELISA has been extensively used to study this inflammatory event. Here, we describe the use of a bioluminescence resonance energy transfer (BRET) biosensor to monitor IL-1β processing in real time and in living macrophages either using a plate reader or a microscope.
    Language English
    Publishing date 2023-08-14
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3350-2_3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: ASC nanobodies to counteract the consequences of inflammasome activation.

    Adriouch, Sahil / Pelegrin, Pablo

    EMBO molecular medicine

    2022  Volume 14, Issue 6, Page(s) e16087

    Abstract: Inflammasomes are multiprotein complexes that signal by oligomerizing the apoptosis speck-like protein with caspase recruitment and activator domain (ASC) and are involved in multiple inflammatory, metabolic and degenerative diseases. Pharmacological ... ...

    Abstract Inflammasomes are multiprotein complexes that signal by oligomerizing the apoptosis speck-like protein with caspase recruitment and activator domain (ASC) and are involved in multiple inflammatory, metabolic and degenerative diseases. Pharmacological targeting of specific inflammasomes with small molecules is leading to the development of novel drugs for most common diseases. The targeting of ASC oligomers will result in a pan-inflammasome treatment. In their study, Bertheloot et al (2022) developed specific anti-ASC nanobodies and showed their efficacy to disaggregate already formed ASC oligomers and to treat inflammatory diseases in animal models. This approach represents a novel biologic-based treatment for inflammasomes-initiated inflammatory diseases.
    MeSH term(s) Animals ; Apoptosis ; CARD Signaling Adaptor Proteins/metabolism ; Inflammasomes/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Single-Domain Antibodies
    Chemical Substances CARD Signaling Adaptor Proteins ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Single-Domain Antibodies
    Language English
    Publishing date 2022-05-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2467145-9
    ISSN 1757-4684 ; 1757-4676
    ISSN (online) 1757-4684
    ISSN 1757-4676
    DOI 10.15252/emmm.202216087
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6784: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Reprogramming macrophages by plasmin.

    Pelegrín, Pablo

    Blood

    2017  Volume 129, Issue 21, Page(s) 2823–2824

    MeSH term(s) Cells, Cultured ; Fibrinolysin ; Humans ; Macrophages
    Chemical Substances Fibrinolysin (EC 3.4.21.7)
    Language English
    Publishing date 2017-05-25
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2017-04-776377
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 364: Show issues

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  8. Article ; Online: Evolution of the gasdermin family and pyroptosis.

    Angosto-Bazarra, Diego / Guijarro, Adriana / Pelegrín, Pablo

    Developmental and comparative immunology

    2023  Volume 149, Page(s) 105060

    Abstract: Gasdermins have been identified as playing a prominent role in the innate immune response as the executors of a specific type of cell death called pyroptosis. Specific proteolytic cleavage of gasdermins generates an N-terminal that oligomerizes and forms ...

    Abstract Gasdermins have been identified as playing a prominent role in the innate immune response as the executors of a specific type of cell death called pyroptosis. Specific proteolytic cleavage of gasdermins generates an N-terminal that oligomerizes and forms pores in the cell membrane. Although pyroptosis has been widely described in mammals, the importance of gasdermins and gasdermin-like proteins in inducing cell death in other vertebrates, in invertebrates and in other taxa including fungi and bacteria is still being determined. Mammalian, fungal and bacterial gasdermins have in common the fact that they go through the same stages (such as proteolytic activation) when inducing membrane rupture, which suggests that pyroptosis is as an ancient mechanism. In this review, we summarize the evolution and function of the gasdermin and gasdermin-like proteins in animals, fungi and bacteria.
    Language English
    Publishing date 2023-09-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 752411-0
    ISSN 1879-0089 ; 0145-305X
    ISSN (online) 1879-0089
    ISSN 0145-305X
    DOI 10.1016/j.dci.2023.105060
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1327: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  9. Article ; Online: Pyroptosis and Redox Balance in Kidney Diseases.

    Cuevas, Santiago / Pelegrín, Pablo

    Antioxidants & redox signaling

    2021  Volume 35, Issue 1, Page(s) 40–60

    Abstract: Significance: ...

    Abstract Significance:
    MeSH term(s) Acute Kidney Injury/metabolism ; Acute Kidney Injury/pathology ; Alarmins/metabolism ; Animals ; Caspase 1/metabolism ; Cytokines/metabolism ; Extracellular Space ; Fibrosis ; Humans ; Inflammasomes/metabolism ; Kidney/metabolism ; Kidney/pathology ; Kidney Diseases/metabolism ; Kidney Diseases/pathology ; Mitochondria/metabolism ; Oxidation-Reduction ; Pathogen-Associated Molecular Pattern Molecules/metabolism ; Phosphate-Binding Proteins/metabolism ; Pore Forming Cytotoxic Proteins/metabolism ; Pyroptosis/physiology ; Reactive Oxygen Species/metabolism ; Renal Insufficiency, Chronic/metabolism ; Renal Insufficiency, Chronic/pathology
    Chemical Substances Alarmins ; Cytokines ; GSDMD protein, human ; Inflammasomes ; Pathogen-Associated Molecular Pattern Molecules ; Phosphate-Binding Proteins ; Pore Forming Cytotoxic Proteins ; Reactive Oxygen Species ; Caspase 1 (EC 3.4.22.36)
    Language English
    Publishing date 2021-03-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1483836-9
    ISSN 1557-7716 ; 1523-0864
    ISSN (online) 1557-7716
    ISSN 1523-0864
    DOI 10.1089/ars.2020.8243
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5488: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  10. Article ; Online: Physiological and pathophysiological functions of NLRP6: pro- and anti-inflammatory roles.

    Angosto-Bazarra, Diego / Molina-López, Cristina / Pelegrín, Pablo

    Communications biology

    2022  Volume 5, Issue 1, Page(s) 524

    Abstract: The nucleotide-binding oligomerization and leucine-rich repeat receptor (NLR) protein family consists of important immune sensors that form inflammasomes, a cytosolic multi-protein platform that induces caspase-1 activation and is involved in different ... ...

    Abstract The nucleotide-binding oligomerization and leucine-rich repeat receptor (NLR) protein family consists of important immune sensors that form inflammasomes, a cytosolic multi-protein platform that induces caspase-1 activation and is involved in different inflammatory pathologies. The NLR family pyrin domain containing 6 (NLRP6) is a receptor that can signal by forming inflammasomes, but which can also play an important role without forming inflammasomes. NLRP6 regulates intestinal homeostasis and inflammation, but also is involved in cancer, the nervous system or liver diseases, with both protective and deleterious consequences. In the present article, we review the different roles of NLRP6 in these processes and offer new insights into NLRP6 activation.
    MeSH term(s) Anti-Inflammatory Agents/pharmacology ; Carrier Proteins ; Humans ; Inflammasomes/metabolism ; Inflammation/pathology ; Intestines ; Intracellular Signaling Peptides and Proteins/metabolism
    Chemical Substances Anti-Inflammatory Agents ; Carrier Proteins ; Inflammasomes ; Intracellular Signaling Peptides and Proteins ; NLRP6 protein, human
    Language English
    Publishing date 2022-06-01
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-03491-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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