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  1. Book: Pore forming toxins

    Goot, Françoise Gisou van der

    with 1 table

    (Current topics in microbiology and immunology ; 257)

    2001  

    Title variant Pore-forming toxins
    Author's details ed. by F. Gisou van der Goot
    Series title Current topics in microbiology and immunology ; 257
    Collection
    Keywords Pore ; Biomembran ; Bakteriengift
    Subject Bakterientoxin ; Bakterielles Toxin ; Biologische Membran ; Einheitsmembran ; Zelle ; Zellmembran
    Language English
    Size 166 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book
    HBZ-ID HT012947227
    ISBN 3-540-41386-3 ; 978-3-540-41386-8
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Ud II Zs 24 -257- verfügbar in Königswinter Königswinter

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  2. Article ; Online: Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications.

    Anwar, Muhammad U / van der Goot, F Gisou

    The Journal of cell biology

    2023  Volume 222, Issue 11

    Abstract: With a limited number of genes, cells achieve remarkable diversity. This is to a large extent achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid modifications that have the unique ability to confer ... ...

    Abstract With a limited number of genes, cells achieve remarkable diversity. This is to a large extent achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid modifications that have the unique ability to confer hydrophobicity. The last decade has revealed that lipid modifications of proteins are extremely frequent and affect a great variety of cellular pathways and physiological processes. This is particularly true for S-acylation, the only reversible lipid modification. The enzymes involved in S-acylation and deacylation are only starting to be understood, and the list of proteins that undergo this modification is ever-increasing. We will describe the state of knowledge on the enzymes that regulate S-acylation, from their structure to their regulation, how S-acylation influences target proteins, and finally will offer a perspective on how alterations in the balance between S-acylation and deacylation may contribute to disease.
    MeSH term(s) Acylation ; Lipid Metabolism ; Protein Processing, Post-Translational ; Lipids
    Chemical Substances Lipids
    Language English
    Publishing date 2023-09-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202307103
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mechanisms and functions of protein S-acylation.

    S Mesquita, Francisco / Abrami, Laurence / Linder, Maurine E / Bamji, Shernaz X / Dickinson, Bryan C / van der Goot, F Gisou

    Nature reviews. Molecular cell biology

    2024  

    Abstract: Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty ...

    Abstract Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a protein. Maintenance of the equilibrium between protein S-acylation and deacylation has demonstrated profound effects on various cellular processes, including innate immunity, inflammation, glucose metabolism and fat metabolism, as well as on brain and heart function. This Review provides an overview of current understanding of S-acylation and deacylation enzymes, their spatiotemporal regulation by sophisticated multilayered mechanisms, and their influence on protein function, cellular processes and physiological pathways. Furthermore, we examine how disruptions in protein S-acylation are associated with a broad spectrum of diseases from cancer to autoinflammatory disorders and neurological conditions.
    Language English
    Publishing date 2024-02-14
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-024-00700-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  4. Article ; Online: S-acylation: an orchestrator of the life cycle and function of membrane proteins.

    Mesquita, Francisco S / Abrami, Laurence / Samurkas, Arthur / van der Goot, F Gisou

    The FEBS journal

    2023  Volume 291, Issue 1, Page(s) 45–56

    Abstract: S-acylation is a covalent post-translational modification of proteins with fatty acids, achieved by enzymatic attachment via a labile thioester bond. This modification allows for dynamic control of protein properties and functions in association with ... ...

    Abstract S-acylation is a covalent post-translational modification of proteins with fatty acids, achieved by enzymatic attachment via a labile thioester bond. This modification allows for dynamic control of protein properties and functions in association with cell membranes. This lipid modification regulates a substantial portion of the human proteome and plays an increasingly recognized role throughout the lifespan of affected proteins. Recent technical advancements have propelled the S-acylation field into a 'molecular era', unveiling new insights into its mechanistic intricacies and far-reaching implications. With a striking increase in the number of studies on this modification, new concepts are indeed emerging on the roles of S-acylation in specific cell biology processes and features. After a brief overview of the enzymes involved in S-acylation, this viewpoint focuses on the importance of S-acylation in the homeostasis, function, and coordination of integral membrane proteins. In particular, we put forward the hypotheses that S-acylation is a gatekeeper of membrane protein folding and turnover and a regulator of the formation and dynamics of membrane contact sites.
    MeSH term(s) Humans ; Animals ; Membrane Proteins/metabolism ; Lipoylation ; Cell Membrane/metabolism ; Acylation ; Life Cycle Stages ; Protein Processing, Post-Translational
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2023-10-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16972
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
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  5. Article ; Online: Harnessing the Membrane Translocation Properties of AB Toxins for Therapeutic Applications.

    Piot, Numa / van der Goot, F Gisou / Sergeeva, Oksana A

    Toxins

    2021  Volume 13, Issue 1

    Abstract: Over the last few decades, proteins and peptides have become increasingly more common as FDA-approved drugs, despite their inefficient delivery due to their inability to cross the plasma membrane. In this context, bacterial two-component systems, termed ... ...

    Abstract Over the last few decades, proteins and peptides have become increasingly more common as FDA-approved drugs, despite their inefficient delivery due to their inability to cross the plasma membrane. In this context, bacterial two-component systems, termed AB toxins, use various protein-based membrane translocation mechanisms to deliver toxins into cells, and these mechanisms could provide new insights into the development of bio-based drug delivery systems. These toxins have great potential as therapies both because of their intrinsic properties as well as the modular characteristics of both subunits, which make them highly amenable to conjugation with various drug classes. This review focuses on the therapeutical approaches involving the internalization mechanisms of three representative AB toxins: botulinum toxin type A, anthrax toxin, and cholera toxin. We showcase several specific examples of the use of these toxins to develop new therapeutic strategies for numerous diseases and explain what makes these toxins promising tools in the development of drugs and drug delivery systems.
    MeSH term(s) Bacterial Toxins/pharmacology ; Protein Transport/drug effects ; Protein Transport/physiology
    Chemical Substances Bacterial Toxins
    Language English
    Publishing date 2021-01-06
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins13010036
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Harnessing the Membrane Translocation Properties of AB Toxins for Therapeutic Applications

    Numa Piot / F. Gisou van der Goot / Oksana A. Sergeeva

    Toxins, Vol 13, Iss 36, p

    2021  Volume 36

    Abstract: Over the last few decades, proteins and peptides have become increasingly more common as FDA-approved drugs, despite their inefficient delivery due to their inability to cross the plasma membrane. In this context, bacterial two-component systems, termed ... ...

    Abstract Over the last few decades, proteins and peptides have become increasingly more common as FDA-approved drugs, despite their inefficient delivery due to their inability to cross the plasma membrane. In this context, bacterial two-component systems, termed AB toxins, use various protein-based membrane translocation mechanisms to deliver toxins into cells, and these mechanisms could provide new insights into the development of bio-based drug delivery systems. These toxins have great potential as therapies both because of their intrinsic properties as well as the modular characteristics of both subunits, which make them highly amenable to conjugation with various drug classes. This review focuses on the therapeutical approaches involving the internalization mechanisms of three representative AB toxins: botulinum toxin type A, anthrax toxin, and cholera toxin. We showcase several specific examples of the use of these toxins to develop new therapeutic strategies for numerous diseases and explain what makes these toxins promising tools in the development of drugs and drug delivery systems.
    Keywords botulinum toxin ; anthrax toxin ; cholera toxin ; membrane translocation ; endocytosis ; therapeutic applications ; Medicine ; R
    Language English
    Publishing date 2021-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Mammalian membrane trafficking as seen through the lens of bacterial toxins.

    Mesquita, Francisco Sarmento / van der Goot, F Gisou / Sergeeva, Oksana A

    Cellular microbiology

    2020  Volume 22, Issue 4, Page(s) e13167

    Abstract: A fundamental question of eukaryotic cell biology is how membrane organelles are organised and interact with each other. Cell biologists address these questions by characterising the structural features of membrane compartments and the mechanisms that ... ...

    Abstract A fundamental question of eukaryotic cell biology is how membrane organelles are organised and interact with each other. Cell biologists address these questions by characterising the structural features of membrane compartments and the mechanisms that coordinate their exchange. To do so, they must rely on variety of cargo molecules and treatments that enable targeted perturbation, localisation, and labelling of specific compartments. In this context, bacterial toxins emerged in cell biology as paradigm shifting molecules that enabled scientists to not only study them from the side of bacterial infection but also from the side of the mammalian host. Their selectivity, potency, and versatility made them exquisite tools for uncovering much of our current understanding of membrane trafficking mechanisms. Here, we will follow the steps that lead toxins until their intracellular targets, highlighting how specific events helped us comprehend membrane trafficking and establish the fundamentals of various cellular organelles and processes. Bacterial toxins will continue to guide us in answering crucial questions in cellular biology while also acting as probes for new technologies and applications.
    MeSH term(s) Animals ; Bacterial Toxins/metabolism ; Cell Biology ; Cell Membrane/physiology ; Cell Movement ; Host Microbial Interactions ; Mammals/microbiology ; Mammals/physiology ; Protein Transport
    Chemical Substances Bacterial Toxins
    Language English
    Publishing date 2020-03-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.13167
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5288: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  8. Article ; Online: Converging physiological roles of the anthrax toxin receptors.

    Sergeeva, Oksana A / van der Goot, F Gisou

    F1000Research

    2019  Volume 8

    Abstract: The anthrax toxin receptors-capillary morphogenesis gene 2 (CMG2) and tumor endothelial marker 8 (TEM8)-were identified almost 20 years ago, although few studies have moved beyond their roles as receptors for the anthrax toxins to address their ... ...

    Abstract The anthrax toxin receptors-capillary morphogenesis gene 2 (CMG2) and tumor endothelial marker 8 (TEM8)-were identified almost 20 years ago, although few studies have moved beyond their roles as receptors for the anthrax toxins to address their physiological functions. In the last few years, insight into their endogenous roles has come from two rare diseases: hyaline fibromatosis syndrome, caused by mutations in CMG2, and growth retardation, alopecia, pseudo-anodontia, and optic atrophy (GAPO) syndrome, caused by loss-of-function mutations in TEM8. Although CMG2 and TEM8 are highly homologous at the protein level, the difference in disease symptoms points to variations in the physiological roles of the two anthrax receptors. Here, we focus on the similarities between these receptors in their ability to regulate extracellular matrix homeostasis, angiogenesis, cell migration, and skin elasticity. In this way, we shed light on how mutations in these two related proteins cause such seemingly different diseases and we highlight the existing knowledge gaps that could form the focus of future studies.
    MeSH term(s) Alopecia/genetics ; Anodontia/genetics ; Cell Movement ; Elasticity ; Extracellular Matrix ; Growth Disorders/genetics ; Humans ; Hyaline Fibromatosis Syndrome/genetics ; Microfilament Proteins/genetics ; Microfilament Proteins/physiology ; Mutation ; Neovascularization, Physiologic ; Optic Atrophies, Hereditary/genetics ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/physiology ; Receptors, Peptide/genetics ; Receptors, Peptide/physiology ; Skin Physiological Phenomena
    Chemical Substances ANTXR1 protein, human ; ANTXR2 protein, human ; Microfilament Proteins ; Receptors, Cell Surface ; Receptors, Peptide ; anthrax toxin receptors
    Language English
    Publishing date 2019-08-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2699932-8
    ISSN 2046-1402 ; 2046-1402
    ISSN (online) 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.19423.1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo.

    Solis, Gonzalo P / Kazemzadeh, Arghavan / Abrami, Laurence / Valnohova, Jana / Alvarez, Cecilia / van der Goot, F Gisou / Katanaev, Vladimir L

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 2072

    Abstract: Peripheral membrane proteins (PMPs) associate with cellular membranes through post-translational modifications like S-palmitoylation. The Golgi apparatus is generally viewed as the transitory station where palmitoyl acyltransferases (PATs) modify PMPs, ... ...

    Abstract Peripheral membrane proteins (PMPs) associate with cellular membranes through post-translational modifications like S-palmitoylation. The Golgi apparatus is generally viewed as the transitory station where palmitoyl acyltransferases (PATs) modify PMPs, which are then transported to their ultimate destinations such as the plasma membrane (PM). However, little substrate specificity among the many PATs has been determined. Here we describe the inherent partitioning of Gαo - α-subunit of heterotrimeric Go proteins - to PM and Golgi, independent from Golgi-to-PM transport. A minimal code within Gαo N-terminus governs its compartmentalization and re-coding produces G protein versions with shifted localization. We establish the S-palmitoylation at the outer nuclear membrane assay ("SwissKASH") to probe substrate specificity of PATs in intact cells. With this assay, we show that PATs localizing to different membrane compartments display remarkable substrate selectivity, which is the basis for PMP compartmentalization. Our findings uncover a mechanism governing protein localization and establish the basis for innovative drug discovery.
    MeSH term(s) Acyltransferases/metabolism ; Cell Membrane/metabolism ; Golgi Apparatus/metabolism ; Lipoylation ; Protein Transport
    Chemical Substances Acyltransferases (EC 2.3.-)
    Language English
    Publishing date 2022-04-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-29685-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo

    Gonzalo P. Solis / Arghavan Kazemzadeh / Laurence Abrami / Jana Valnohova / Cecilia Alvarez / F. Gisou van der Goot / Vladimir L. Katanaev

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 21

    Abstract: How palmitoylated proteins specifically localize is not fully understood. Here, authors created the SwissKASH assay to visualize S-palmitoylation in cells and uncovered a striking substrate selectivity of acyltransferases at the core of this process. ...

    Abstract How palmitoylated proteins specifically localize is not fully understood. Here, authors created the SwissKASH assay to visualize S-palmitoylation in cells and uncovered a striking substrate selectivity of acyltransferases at the core of this process.
    Keywords Science ; Q
    Language English
    Publishing date 2022-04-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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