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  1. Book: Phagocytosis and phagosomes

    Botelho, Roberto

    methods and protocols

    (Methods in molecular biology ; 2692 ; Springer protocols)

    2023  

    Author's details edited by Roberto J. Botelho
    Series title Methods in molecular biology ; 2692
    Springer protocols
    Collection
    Keywords Phagocytosis ; Phagosomes
    Subject code 616.079
    Language English
    Size xi, 387 Seiten, Illustrationen, 26 cm
    Edition Second edition
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT030078140
    ISBN 978-1-0716-3337-3 ; 9781071633380 ; 1-0716-3337-6 ; 1071633384
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2692- not available for loan Lesesaal EG

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  2. Book: Phosphoinositides

    Botelho, Roberto J.

    methods and protocols

    (Methods in molecular biology ; 2251 ; Springer protocols)

    2021  

    Author's details edited by Roberto J. Botelho
    Series title Methods in molecular biology ; 2251
    Springer protocols
    Collection
    Language English
    Size XI, 239 Seiten, Illustrationen
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT020804021
    ISBN 978-1-0716-1141-8 ; 9781071611425 ; 1-0716-1141-0 ; 1071611429
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2251- verfügbar in Königswinter Königswinter

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  3. Book: Phagocytosis and phagosomes

    Botelho, Roberto

    methods and protocols

    (Methods in molecular biology ; 1519 ; Springer protocols)

    2017  

    Author's details edited by Roberto Botelho
    Series title Methods in molecular biology ; 1519
    Springer protocols
    Collection
    Keywords Western blotting ; cell fractionation ; pathogens ; phagocytes ; phagosome maturation ; proteomics
    Language English
    Size xii, 360 Seiten, Illustrationen, Diagramme, 25.4 cm x 17.8 cm, 0 g
    Publisher Humana Press
    Publishing place New York
    Publishing country United States
    Document type Book
    HBZ-ID HT019124797
    ISBN 978-1-4939-6579-3 ; 1-4939-6579-4 ; 9781493965816 ; 1493965816
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -1519- verfügbar in Königswinter Königswinter

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  4. Article ; Online: Lysosome identity crisis: Phosphoinositides and mTORC1 negotiate lysosomal behavior.

    Mansat, Mélanie / Botelho, Roberto J

    Molecular cell

    2024  Volume 84, Issue 1, Page(s) 17–19

    Abstract: Ebner et al. ...

    Abstract Ebner et al.
    MeSH term(s) Phosphatidylinositols ; Identity Crisis ; Lysosomes ; Mechanistic Target of Rapamycin Complex 1/genetics
    Chemical Substances phosphatidylinositol 3-phosphate ; Phosphatidylinositols ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
    Language English
    Publishing date 2024-01-04
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2023.12.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5055: Show issues Location:
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  5. Article ; Online: Quantifying Phagocytosis by Immunofluorescence and Microscopy.

    Soffiaturo, Sierra / Choy, Christopher / Botelho, Roberto J

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

    2023  Volume 2692, Page(s) 25–39

    Abstract: Phagocytosis is carried out by cells such as macrophages of the immune system, whereby particulates like bacteria and apoptotic bodies are engulfed and sequestered within phagosomes for subsequent degradation. Hence, phagocytosis is important for ... ...

    Abstract Phagocytosis is carried out by cells such as macrophages of the immune system, whereby particulates like bacteria and apoptotic bodies are engulfed and sequestered within phagosomes for subsequent degradation. Hence, phagocytosis is important for infection resolution and tissue homeostasis. Aided by the innate and adaptive immune system, the activation of various phagocytic receptors triggers a cascade of downstream signaling mediators that drive actin and plasma membrane remodeling to entrap the bound particulate within the phagosome. Modulation of these molecular players can lead to distinct changes in the capacity and rates of phagocytosis. Here, we present a fluorescence microscopy-based technique to quantify phagocytosis using a macrophage-like cell line. We exemplify the technique through the phagocytosis of antibody-opsonized polystyrene beads and Escherichia coli. This method can be extended to other phagocytes and phagocytic particles.
    MeSH term(s) Phagocytosis ; Macrophages/metabolism ; Phagosomes/metabolism ; Microscopy, Fluorescence/methods ; Fluorescent Antibody Technique
    Language English
    Publishing date 2023-06-29
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3338-0_3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Quantitative Immunofluorescence to Study Phagosome Maturation and Resolution.

    Mansat, Mélanie / Dayam, Roya M / Botelho, Roberto J

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

    2023  Volume 2692, Page(s) 121–137

    Abstract: Cells such as macrophages and neutrophils can internalize a diverse set of particulate matter, illustrated by bacteria and apoptotic bodies through the process of phagocytosis. These particles are sequestered into phagosomes, which then fuse with early ... ...

    Abstract Cells such as macrophages and neutrophils can internalize a diverse set of particulate matter, illustrated by bacteria and apoptotic bodies through the process of phagocytosis. These particles are sequestered into phagosomes, which then fuse with early and late endosomes and ultimately with lysosomes to mature into phagolysosomes, through a process known as phagosome maturation. Ultimately, after particle degradation, phagosomes then fragment to reform lysosomes through phagosome resolution. As phagosomes change, they acquire and divest proteins that are associated with the various stages of phagosome maturation and resolution. These changes can be assessed at the single-phagosome level by using immunofluorescence methods. Typically, we use indirect immunofluorescence methods that rely on primary antibodies against specific molecular markers that track phagosome maturation. Commonly, progression of phagosomes into phagolysosomes can be determined by staining cells for Lysosomal-Associated Membrane Protein I (LAMP1) and measuring the fluorescence intensity of LAMP1 around each phagosome by microscopy or flow cytometry. However, this method can be used to detect any molecular marker for which there are compatible antibodies for immunofluorescence.
    MeSH term(s) Phagocytosis ; Phagosomes/metabolism ; Macrophages/metabolism ; Lysosomes/metabolism ; Fluorescent Antibody Technique ; Lysosomal-Associated Membrane Protein 1/metabolism
    Chemical Substances Lysosomal-Associated Membrane Protein 1
    Language English
    Publishing date 2023-06-29
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3338-0_9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: A tail of their own: regulation of cardiolipin and phosphatidylinositol fatty acyl profile by the acyltransferase LCLAT1.

    Zhang, Kai / Chan, Victoria / Botelho, Roberto J / Antonescu, Costin N

    Biochemical Society transactions

    2023  Volume 51, Issue 5, Page(s) 1765–1776

    Abstract: Cardiolipin and phosphatidylinositol along with the latter's phosphorylated derivative phosphoinositides, control a wide range of cellular functions from signal transduction, membrane traffic, mitochondrial function, cytoskeletal dynamics, and cell ... ...

    Abstract Cardiolipin and phosphatidylinositol along with the latter's phosphorylated derivative phosphoinositides, control a wide range of cellular functions from signal transduction, membrane traffic, mitochondrial function, cytoskeletal dynamics, and cell metabolism. An emerging dimension to these lipids is the specificity of their fatty acyl chains that is remarkably distinct from that of other glycerophospholipids. Cardiolipin and phosphatidylinositol undergo acyl remodeling involving the sequential actions of phospholipase A to hydrolyze acyl chains and key acyltransferases that re-acylate with specific acyl groups. LCLAT1 (also known as LYCAT, AGPAT8, LPLAT6, or ALCAT1) is an acyltransferase that contributes to specific acyl profiles for phosphatidylinositol, phosphoinositides, and cardiolipin. As such, perturbations of LCLAT1 lead to alterations in cardiolipin-dependent phenomena such as mitochondrial respiration and dynamics and phosphoinositide-dependent processes such as endocytic membrane traffic and receptor signaling. Here we examine the biochemical and cellular actions of LCLAT1, as well as the contribution of this acyltransferase to the development and specific diseases.
    MeSH term(s) Acyltransferases/metabolism ; Cardiolipins/metabolism ; Phosphatidylinositols ; Glycerophospholipids
    Chemical Substances Acyltransferases (EC 2.3.-) ; Cardiolipins ; Phosphatidylinositols ; Glycerophospholipids
    Language English
    Publishing date 2023-09-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20220603
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 944: Show issues Location:
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  8. Article: The Lysosome Signaling Platform: Adapting With the Times.

    Inpanathan, Subothan / Botelho, Roberto J

    Frontiers in cell and developmental biology

    2019  Volume 7, Page(s) 113

    Abstract: Lysosomes are the terminal degradative compartment of autophagy, endocytosis and phagocytosis. What once was viewed as a simple acidic organelle in charge of macromolecular digestion has emerged as a dynamic organelle capable of integrating cellular ... ...

    Abstract Lysosomes are the terminal degradative compartment of autophagy, endocytosis and phagocytosis. What once was viewed as a simple acidic organelle in charge of macromolecular digestion has emerged as a dynamic organelle capable of integrating cellular signals and producing signal outputs. In this review, we focus on the concept that the lysosome surface serves as a platform to assemble major signaling hubs like mTORC1, AMPK, GSK3 and the inflammasome. These molecular assemblies integrate and facilitate cross-talk between signals such as amino acid and energy levels, membrane damage and infection, and ultimately enable responses such as autophagy, cell growth, membrane repair and microbe clearance. In particular, we review how molecular machinery like the vacuolar-ATPase proton pump, sestrins, the GATOR complexes, and the Ragulator, modulate mTORC1, AMPK, GSK3 and inflammation. We then elaborate how these signals control autophagy initiation and resolution, TFEB-mediated lysosome adaptation, lysosome remodeling, antigen presentation, inflammation, membrane damage repair and clearance. Overall, by being at the cross-roads for several membrane pathways, lysosomes have emerged as the ideal surveillance compartment to sense, integrate and elicit cellular behavior and adaptation in response to changing environmental and cellular conditions.
    Language English
    Publishing date 2019-06-20
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2019.00113
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Lysosome Fission: Planning for an Exit.

    Saffi, Golam T / Botelho, Roberto J

    Trends in cell biology

    2019  Volume 29, Issue 8, Page(s) 635–646

    Abstract: Lysosomes are acidic and degradative organelles that receive and digest a plethora of molecular and particulate cargo delivered by endocytosis, autophagy, and phagocytosis. The mechanisms responsible for sorting, transporting, and ultimately delivering ... ...

    Abstract Lysosomes are acidic and degradative organelles that receive and digest a plethora of molecular and particulate cargo delivered by endocytosis, autophagy, and phagocytosis. The mechanisms responsible for sorting, transporting, and ultimately delivering membranes and cargo to lysosomes through fusion have been intensely investigated. Much less is understood about lysosome fission, which is necessary to balance the incessant flow of cargo into lysosomes and maintain steady-state number, size, and function of lysosomes. Here, we review the emerging picture of how lipid signals, coat and adaptor proteins, and motor-cytoskeletal assemblies drive budding, tubulation, splitting, and 'kiss-and-run' events that enable fission and exit from lysosomes and related organelles.
    MeSH term(s) Animals ; Humans ; Lysosomes/metabolism
    Language English
    Publishing date 2019-06-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2019.05.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: BioEssays in phosphoinositides: a special collection.

    Botelho, Roberto J

    BioEssays : news and reviews in molecular, cellular and developmental biology

    2014  Volume 36, Issue 2, Page(s) 123–124

    MeSH term(s) Animals ; Biological Assay ; Humans ; Phosphatidylinositols/analysis
    Chemical Substances Phosphatidylinositols
    Language English
    Publishing date 2014-02
    Publishing country United States
    Document type Editorial
    ZDB-ID 50140-2
    ISSN 1521-1878 ; 0265-9247
    ISSN (online) 1521-1878
    ISSN 0265-9247
    DOI 10.1002/bies.201300179
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