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  1. Book ; Online ; E-Book: Organelle contact sites

    Tagaya, Mitsuo / Simmen, Thomas

    from molecular mechanism to disease

    (Advances in experimental medicine and biology ; 997)

    2017  

    Author's details Mitsuo Tagaya, Thomas Simmen editors
    Series title Advances in experimental medicine and biology ; 997
    Collection
    Keywords Life sciences ; Cancer research ; Human physiology ; Immunology ; Molecular biology ; Biochemistry ; Cell biology
    Subject code 571.6
    Language English
    Size 1 Online-Ressource (VIII, 257 Seiten), Illustrationen
    Publisher Springer
    Publishing place Singapore
    Publishing country Singapore
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT019439337
    ISBN 978-981-10-4567-7 ; 9789811045660 ; 981-10-4567-4 ; 9811045666
    DOI 10.1007/978-981-10-4567-7
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Organelle contact sites

    Tagaya, Mitsuo / Simmen, Thomas

    from molecular mechanism to disease

    (Advances in experimental medicine and biology ; 997)

    2017  

    Author's details Mitsuo Tagaya, Thomas Simmen editors
    Series title Advances in experimental medicine and biology ; 997
    Collection
    Keywords Mitochondria ; Mitochondria-associated membrane ; Membrane contact sites ; Endoplasmic reticulum ; Alzheimer’s disease ; Parkinson’s disease ; Type II diabetes ; Hepatitis C virus ; Cancer ; Lipid synthesis ; Apoptosis ; Calcium ; Neurodegenerative disease ; Pathogen infection
    Subject code 570
    Language English
    Size VI, 300 Seiten, Illustrationen, 25.4 cm x 17.8 cm
    Publisher Springer
    Publishing place Singapore
    Publishing country Singapore
    Document type Book
    HBZ-ID HT019377225
    ISBN 978-981-10-4566-0 ; 981-10-4566-6 ; 9789811045677 ; 9811045674
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 3192 -997- not available for loan Zeitschriften-Lesesaal

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  3. Article ; Online: Ironing out the mitochondria.

    Chen, Junsheng / Makio, Tadashi / Simmen, Thomas

    Nature chemical biology

    2024  

    Language English
    Publishing date 2024-01-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-023-01509-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6251: 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)
    Zs.MG 90: Show issues

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  4. Article ; Online: LUBAC and NF-κB trigger a nuclear response from mitochondria.

    Chen, Junsheng / Simmen, Thomas

    The EMBO journal

    2022  Volume 41, Issue 24, Page(s) e112920

    Abstract: Mitochondria are key signaling hubs for innate immune responses. In this issue, Wu et al (2022) report that remodeling of the outer mitochondrial membrane by the linear ubiquiting chain assembly complex (LUBAC) facilitates transport of activated NF-κB to ...

    Abstract Mitochondria are key signaling hubs for innate immune responses. In this issue, Wu et al (2022) report that remodeling of the outer mitochondrial membrane by the linear ubiquiting chain assembly complex (LUBAC) facilitates transport of activated NF-κB to the nucleus in response to TNF signaling.
    MeSH term(s) NF-kappa B/metabolism ; Ubiquitination ; Ubiquitin-Protein Ligases/metabolism ; Signal Transduction ; Mitochondria/metabolism
    Chemical Substances NF-kappa B ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2022-11-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2022112920
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: 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)
    Zs.MG 100: Show issues

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  5. Article ; Online: S-Palmitoylation of calcineurin β1 connects cellular Ca

    Bassot, Arthur / Mina, Lucas / Chen, Junsheng / Simmen, Thomas

    Cell calcium

    2022  Volume 103, Page(s) 102545

    MeSH term(s) 1-Phosphatidylinositol 4-Kinase/metabolism ; Calcineurin/metabolism ; Cell Membrane/metabolism ; Homeostasis ; Lipoylation ; Phosphoric Monoester Hydrolases
    Chemical Substances 1-Phosphatidylinositol 4-Kinase (EC 2.7.1.67) ; calcineurin phosphatase (EC 3.1.3.-) ; Calcineurin (EC 3.1.3.16) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
    Language English
    Publishing date 2022-01-31
    Publishing country Netherlands
    Document type Journal Article ; Comment
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2022.102545
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1596: 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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  6. Article ; Online: Post-Translational Modification of Cysteines: A Key Determinant of Endoplasmic Reticulum-Mitochondria Contacts (MERCs).

    Bassot, Arthur / Chen, Junsheng / Simmen, Thomas

    Contact (Thousand Oaks (Ventura County, Calif.))

    2021  Volume 4, Page(s) 25152564211001213

    Abstract: Cells must adjust their redox state to an ever-changing environment that could otherwise result in compromised homeostasis. An obvious way to adapt to changing redox conditions depends on cysteine post-translational modifications (PTMs) to adapt ... ...

    Abstract Cells must adjust their redox state to an ever-changing environment that could otherwise result in compromised homeostasis. An obvious way to adapt to changing redox conditions depends on cysteine post-translational modifications (PTMs) to adapt conformation, localization, interactions and catalytic activation of proteins. Such PTMs should occur preferentially in the proximity of oxidative stress sources. A particular concentration of these sources is found near membranes where the endoplasmic reticulum (ER) and the mitochondria interact on domains called MERCs (Mitochondria-Endoplasmic Reticulum Contacts). Here, fine inter-organelle communication controls metabolic homeostasis. MERCs achieve this goal through fluxes of Ca
    Language English
    Publishing date 2021-03-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2964312-0
    ISSN 2515-2564 ; 2515-2564
    ISSN (online) 2515-2564
    ISSN 2515-2564
    DOI 10.1177/25152564211001213
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Amyotrophic Lateral Sclerosis (ALS): Stressed by Dysfunctional Mitochondria-Endoplasmic Reticulum Contacts (MERCs).

    Chen, Junsheng / Bassot, Arthur / Giuliani, Fabrizio / Simmen, Thomas

    Cells

    2021  Volume 10, Issue 7

    Abstract: Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease for which there is currently no cure. Progress in the characterization of other neurodegenerative mechanisms has shifted the spotlight onto an intracellular structure called ... ...

    Abstract Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease for which there is currently no cure. Progress in the characterization of other neurodegenerative mechanisms has shifted the spotlight onto an intracellular structure called mitochondria-endoplasmic reticulum (ER) contacts (MERCs) whose ER portion can be biochemically isolated as mitochondria-associated membranes (MAMs). Within the central nervous system (CNS), these structures control the metabolic output of mitochondria and keep sources of oxidative stress in check via autophagy. The most relevant MERC controllers in the ALS pathogenesis are vesicle-associated membrane protein-associated protein B (VAPB), a mitochondria-ER tether, and the ubiquitin-specific chaperone valosin containing protein (VCP). These two systems cooperate to maintain mitochondrial energy output and prevent oxidative stress. In ALS, mutant VAPB and VCP take a central position in the pathology through MERC dysfunction that ultimately alters or compromises mitochondrial bioenergetics. Intriguingly, both proteins are targets themselves of other ALS mutant proteins, including C9orf72, FUS, or TDP-43. Thus, a new picture emerges, where different triggers cause MERC dysfunction in ALS, subsequently leading to well-known pathological changes including endoplasmic reticulum (ER) stress, inflammation, and motor neuron death.
    MeSH term(s) Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/physiology ; Humans ; Mitochondria/metabolism ; Neurodegenerative Diseases/metabolism ; Oxidative Stress/physiology
    Language English
    Publishing date 2021-07-15
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10071789
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Mechanistic Connections between Endoplasmic Reticulum (ER) Redox Control and Mitochondrial Metabolism.

    Fan, Yuxiang / Simmen, Thomas

    Cells

    2019  Volume 8, Issue 9

    Abstract: The past decade has seen the emergence of endoplasmic reticulum (ER) chaperones as key determinants of contact formation between mitochondria and the ER on the mitochondria-associated membrane (MAM). Despite the known roles of ER-mitochondria tethering ... ...

    Abstract The past decade has seen the emergence of endoplasmic reticulum (ER) chaperones as key determinants of contact formation between mitochondria and the ER on the mitochondria-associated membrane (MAM). Despite the known roles of ER-mitochondria tethering factors like PACS-2 and mitofusin-2, it is not yet entirely clear how they mechanistically interact with the ER environment to determine mitochondrial metabolism. In this article, we review the mechanisms used to communicate ER redox and folding conditions to the mitochondria, presumably with the goal of controlling mitochondrial metabolism at the Krebs cycle and at the electron transport chain, leading to oxidative phosphorylation (OXPHOS). To achieve this goal, redox nanodomains in the ER and the interorganellar cleft influence the activities of ER chaperones and Ca
    MeSH term(s) Autophagy ; Calcium Signaling ; Endoplasmic Reticulum/metabolism ; Homeostasis/physiology ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Dynamics/physiology ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/metabolism ; Molecular Chaperones/metabolism ; Oxidation-Reduction ; Oxidoreductases/metabolism
    Chemical Substances Membrane Proteins ; Mitochondrial Proteins ; Molecular Chaperones ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2019-09-12
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8091071
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Hax-1: a regulator of calcium signaling and apoptosis progression with multiple roles in human disease.

    Simmen, Thomas

    Expert opinion on therapeutic targets

    2011  Volume 15, Issue 6, Page(s) 741–751

    Abstract: Introduction: Hax-1, the hematopoietic cell-specific protein-associated protein X-1, is an inhibitor of apoptosis, which has been implicated in severe congenital neutropenia (SCN), neurological disorders and cancer. Hax-1 over-expression, as found in ... ...

    Abstract Introduction: Hax-1, the hematopoietic cell-specific protein-associated protein X-1, is an inhibitor of apoptosis, which has been implicated in severe congenital neutropenia (SCN), neurological disorders and cancer. Hax-1 over-expression, as found in numerous types of cancer, results in resistance to granzyme B and caspase-3 and stabilizes the X-linked inhibitor of apoptosis, whereas its absence or knockdown promotes apoptosis. Hax-1 is bound to the cytosolic faces of mitochondria and the endoplasmic reticulum (ER). Interestingly, numerous viral proteins, including the classical swine fever virus N-terminal protease (N(pro)) and human immunodeficiency virus Vpr, interact with Hax-1 and disrupt its normal localization pattern. Recent findings have demonstrated that the localization to the ER allows Hax-1 to modulate calcium signaling via interactions with polycystin-2 and sarco(endo)plasmic reticulum calcium transport ATPase 2 (SERCA2).
    Areas covered: This review discusses how the interaction of Hax-1 with calcium-handling proteins could dominate over its other roles in apoptosis, since Hax-1 no longer blocks apoptosis on over-expression of SERCA2.
    Expert opinion: To facilitate pharmacological interference with the apoptosis-regulating functions of this protein, a better understanding of the Hax-1 intracellular targeting and protein-protein interactions is needed. Such an improved understanding would allow the generation of small molecule inhibitors that interfere with apoptosis-modulating functions of Hax-1 as seen in SCN.
    MeSH term(s) Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Antineoplastic Agents/pharmacology ; Apoptosis ; Calcium Signaling ; Drug Delivery Systems ; Humans ; Neoplasms/drug therapy ; Neoplasms/physiopathology ; Neutropenia/congenital ; Neutropenia/drug therapy ; Neutropenia/physiopathology ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Antineoplastic Agents ; HAX1 protein, human ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; ATP2A2 protein, human (EC 7.2.2.10)
    Language English
    Publishing date 2011-03-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2055208-7
    ISSN 1744-7631 ; 1472-8222
    ISSN (online) 1744-7631
    ISSN 1472-8222
    DOI 10.1517/14728222.2011.561787
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5244: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  10. Article ; Online: Post-Translational Modification of Cysteines

    Arthur Bassot / Junsheng Chen / Thomas Simmen

    Contact, Vol

    A Key Determinant of Endoplasmic Reticulum-Mitochondria Contacts (MERCs)

    2021  Volume 4

    Abstract: Cells must adjust their redox state to an ever-changing environment that could otherwise result in compromised homeostasis. An obvious way to adapt to changing redox conditions depends on cysteine post-translational modifications (PTMs) to adapt ... ...

    Abstract Cells must adjust their redox state to an ever-changing environment that could otherwise result in compromised homeostasis. An obvious way to adapt to changing redox conditions depends on cysteine post-translational modifications (PTMs) to adapt conformation, localization, interactions and catalytic activation of proteins. Such PTMs should occur preferentially in the proximity of oxidative stress sources. A particular concentration of these sources is found near membranes where the endoplasmic reticulum (ER) and the mitochondria interact on domains called MERCs (Mitochondria-Endoplasmic Reticulum Contacts). Here, fine inter-organelle communication controls metabolic homeostasis. MERCs achieve this goal through fluxes of Ca 2+ ions and inter-organellar lipid exchange. Reactive oxygen species (ROS) that cause PTMs of mitochondria-associated membrane (MAM) proteins determine these intertwined MERC functions. Chronic changes of the pattern of these PTMs not only control physiological processes such as the circadian clock but could also lead to or worsen many human disorders such as cancer and neurodegenerative diseases.
    Keywords Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2021-03-01T00:00:00Z
    Publisher SAGE Publishing
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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