LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 66

Search options

  1. Article ; Online: Cellular Senescence in Postmitotic Cells: Beyond Growth Arrest.

    Sapieha, Przemyslaw / Mallette, Frédérick A

    Trends in cell biology

    2018  Volume 28, Issue 8, Page(s) 595–607

    Abstract: In mitotic cells, cellular senescence is a permanent state of G1 arrest, that may have evolved in parallel to apoptosis, to limit proliferation of damaged cells and oncogenesis. Recent studies have suggested that postmitotic cells are also capable of ... ...

    Abstract In mitotic cells, cellular senescence is a permanent state of G1 arrest, that may have evolved in parallel to apoptosis, to limit proliferation of damaged cells and oncogenesis. Recent studies have suggested that postmitotic cells are also capable of entering a state of senescence, although the repercussions of postmitotic cellular senescence (PoMiCS) on tissue health and function are currently ill-defined. In tissues made largely of post-mitotic cells, it is evolutionary advantageous to preserve cellular integrity and cellular senescence of post-mitotic cells may prevent stressor-induced tissue degeneration and promote tissue repair. Paradoxically, PoMiCS may also contribute to disease progression through the generation of inflammatory mediators, termed the senescence-associated secretory phenotype. Here, we discuss the potential roles of PoMiCS and propose to enlarge the current definition of cellular senescence to postmitotic terminally differentiated cells.
    MeSH term(s) Animals ; Apoptosis ; Cell Proliferation ; Cellular Senescence ; Humans ; Mitosis
    Language English
    Publishing date 2018-04-25
    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.2018.03.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.MG 25: Show issues
    Zs.MO 113: Show issues
    Zs.A 3410: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: The Rise of FXR1: Escaping Cellular Senescence in Head and Neck Squamous Cell Carcinoma.

    Fernández, Erlinda / Mallette, Frédérick A

    PLoS genetics

    2016  Volume 12, Issue 11, Page(s) e1006344

    MeSH term(s) Cellular Senescence ; Humans ; RNA ; RNA-Binding Proteins ; Squamous Cell Carcinoma of Head and Neck ; Telomerase ; Tumor Suppressor Protein p53
    Chemical Substances FXR1 protein, human ; RNA-Binding Proteins ; Tumor Suppressor Protein p53 ; telomerase RNA ; RNA (63231-63-0) ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2016-11-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1006344
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: Translation Links Nutrient Availability with Inflammation.

    Boulay, Karine / Topisirovic, Ivan / Mallette, Frédérick A

    Trends in biochemical sciences

    2018  Volume 43, Issue 11, Page(s) 849–852

    Abstract: Translation plays a crucial role in shaping the proteome during adaptation to various types of stress. A recent study by Gameiro and Struhl identified an inflammatory response which comprises coordination of transcriptional and translational programs, ... ...

    Abstract Translation plays a crucial role in shaping the proteome during adaptation to various types of stress. A recent study by Gameiro and Struhl identified an inflammatory response which comprises coordination of transcriptional and translational programs, and which appears to be required for recovery from nutrient deprivation.
    MeSH term(s) Humans ; Inflammation ; Nutrients ; Proteome
    Chemical Substances Nutrients ; Proteome
    Language English
    Publishing date 2018-09-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2018.08.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes.

    Barbour, Haithem / Nkwe, Nadine Sen / Estavoyer, Benjamin / Messmer, Clémence / Gushul-Leclaire, Mila / Villot, Romain / Uriarte, Maxime / Boulay, Karine / Hlayhel, Sari / Farhat, Bassel / Milot, Eric / Mallette, Frédérick A / Daou, Salima / Affar, El Bachir

    iScience

    2023  Volume 26, Issue 5, Page(s) 106276

    Abstract: Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. ... ...

    Abstract Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. Much progress has been made during the last three decades in understanding how ubiquitin ligases recognize their substrates and how ubiquitination is orchestrated. Several mechanisms of regulation have evolved to prevent promiscuity including the assembly of ubiquitin ligases in multi-protein complexes with dedicated subunits and specific post-translational modifications of these enzymes and their co-factors. Here, we outline another layer of complexity involving the coordinated access of E3 ligases to substrates. We provide an extensive inventory of ubiquitination crosstalk with multiple PTMs including SUMOylation, phosphorylation, methylation, acetylation, hydroxylation, prolyl isomerization, PARylation, and O-GlcNAcylation. We discuss molecular mechanisms by which PTMs orchestrate ubiquitination, thus increasing its specificity as well as its crosstalk with other signaling pathways to ensure cell homeostasis.
    Language English
    Publishing date 2023-02-26
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2023.106276
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article: ZNF768: controlling cellular senescence and proliferation with ten fingers.

    Villot, Romain / Poirier, Audrey / Devillers, Romain / Kolnoguz, Aliona / Elowe, Sabine / Manem, Venkata S K / Joubert, Philippe / Mallette, Frédérick A / Laplante, Mathieu

    Molecular & cellular oncology

    2021  Volume 8, Issue 6, Page(s) 1985930

    Abstract: We recently identified Zinc-finger protein 768 (ZNF768) as a novel transcription factor controlling cell fate decision downstream of Rat sarcoma virus (RAS). We showed that ZNF768 depletion impairs cell cycle progression and triggers cellular senescence, ...

    Abstract We recently identified Zinc-finger protein 768 (ZNF768) as a novel transcription factor controlling cell fate decision downstream of Rat sarcoma virus (RAS). We showed that ZNF768 depletion impairs cell cycle progression and triggers cellular senescence, while its overexpression allows cells to bypass oncogene-induced senescence. Elevated ZNF768 levels is common in tumors, suggesting that ZNF768 may help to escape cellular senescence, sustain proliferation and promote malignant transformation. Here, we discuss these recent findings and highlight key questions emerging from our work.
    Language English
    Publishing date 2021-12-08
    Publishing country United States
    Document type Journal Article
    ISSN 2372-3556
    ISSN 2372-3556
    DOI 10.1080/23723556.2021.1985930
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article: MyD88 Regulates the Expression of SMAD4 and the Iron Regulatory Hormone Hepcidin.

    Samba-Mondonga, Macha / Calvé, Annie / Mallette, Frédérick A / Santos, Manuela M

    Frontiers in cell and developmental biology

    2018  Volume 6, Page(s) 105

    Abstract: The myeloid differentiation primary response gene 88 (MyD88) is an adaptive protein that is essential for the induction of inflammatory cytokines through almost all the Toll-like receptors (TLRs). TLRs recognize molecular patterns present in ... ...

    Abstract The myeloid differentiation primary response gene 88 (MyD88) is an adaptive protein that is essential for the induction of inflammatory cytokines through almost all the Toll-like receptors (TLRs). TLRs recognize molecular patterns present in microorganisms called pathogen-associated molecular patterns. Therefore, MyD88 plays an important role in innate immunity since its activation triggers the first line of defense against microorganisms. Herein, we describe the first reported role of MyD88 in an interconnection between innate immunity and the iron-sensing pathway (BMP/SMAD4). We found that direct interaction of MyD88 with SMAD4 protein activated hepcidin expression. The iron regulatory hormone hepcidin is indispensable for the intestinal regulation of iron absorption and iron recycling by macrophages. We show that MyD88 induces hepcidin expression in a manner dependent on the proximal BMP responsive element on the hepcidin gene (
    Language English
    Publishing date 2018-08-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2018.00105
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: O-GlcNAcylation of FOXK1 orchestrates the E2F pathway and promotes oncogenesis.

    Masclef, Louis / Ahmed, Oumaima / Iannantuono, Nicholas / Gagnon, Jessica / Gushul-Leclaire, Mila / Boulay, Karine / Estavoyer, Benjamin / Echbicheb, Mohamed / Poy, Marty / Boubacar, Kalidou Ali / Boubekeur, Amina / Menggad, Saad / Schcolnik-Cabrera, Alejandro / Balsalobre, Aurelio / Bonneil, Eric / Thibault, Pierre / Hulea, Laura / Tanaka, Yoshiaki / Antoine-Mallette, Frédérick /
    Drouin, Jacques / Affar, El Bachir

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Gene transcription is a highly regulated process, and deregulation of transcription factors activity underlies numerous pathologies including cancer. Albeit near four decades of studies have established that the E2F pathway is a core transcriptional ... ...

    Abstract Gene transcription is a highly regulated process, and deregulation of transcription factors activity underlies numerous pathologies including cancer. Albeit near four decades of studies have established that the E2F pathway is a core transcriptional network that govern cell division in multi-cellular organisms
    Language English
    Publishing date 2024-03-01
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.01.582838
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  8. Article ; Online: Tyrosine phosphorylation of DEPTOR functions as a molecular switch to activate mTOR signaling.

    M Gagné, Laurence / Morin, Nadine / Lavoie, Noémie / Bisson, Nicolas / Lambert, Jean-Philippe / Mallette, Frédérick A / Huot, Marc-Étienne

    The Journal of biological chemistry

    2021  Volume 297, Issue 5, Page(s) 101291

    Abstract: Metabolic dysfunction is a major driver of tumorigenesis. The serine/threonine kinase mechanistic target of rapamycin (mTOR) constitutes a key central regulator of metabolic pathways promoting cancer cell proliferation and survival. mTOR activity is ... ...

    Abstract Metabolic dysfunction is a major driver of tumorigenesis. The serine/threonine kinase mechanistic target of rapamycin (mTOR) constitutes a key central regulator of metabolic pathways promoting cancer cell proliferation and survival. mTOR activity is regulated by metabolic sensors as well as by numerous factors comprising the phosphatase and tensin homolog/PI3K/AKT canonical pathway, which are often mutated in cancer. However, some cancers displaying constitutively active mTOR do not carry alterations within this canonical pathway, suggesting alternative modes of mTOR regulation. Since DEPTOR, an endogenous inhibitor of mTOR, was previously found to modulate both mTOR complexes 1 and 2, we investigated the different post-translational modification that could affect its inhibitory function. We found that tyrosine (Tyr) 289 phosphorylation of DEPTOR impairs its interaction with mTOR, leading to increased mTOR activation. Using proximity biotinylation assays, we identified SYK (spleen tyrosine kinase) as a kinase involved in DEPTOR Tyr 289 phosphorylation in an ephrin (erythropoietin-producing hepatocellular carcinoma) receptor-dependent manner. Altogether, our work reveals that phosphorylation of Tyr 289 of DEPTOR represents a novel molecular switch involved in the regulation of both mTOR complex 1 and mTOR complex 2.
    MeSH term(s) HEK293 Cells ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; Signal Transduction ; TOR Serine-Threonine Kinases/genetics ; TOR Serine-Threonine Kinases/metabolism ; Tyrosine/genetics ; Tyrosine/metabolism
    Chemical Substances Intracellular Signaling Peptides and Proteins ; Tyrosine (42HK56048U) ; DEPTOR protein, human (EC 2.7.1.1) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2021-10-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.101291
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: HIF1α-dependent hypoxia response in myeloid cells requires IRE1α.

    Mawambo, Gaëlle / Oubaha, Malika / Ichiyama, Yusuke / Blot, Guillaume / Crespo-Garcia, Sergio / Dejda, Agnieszka / Binet, François / Diaz-Marin, Roberto / Sawchyn, Christina / Sergeev, Mikhail / Juneau, Rachel / Kaufman, Randal J / Affar, El Bachir / Mallette, Frédérick A / Wilson, Ariel M / Sapieha, Przemyslaw

    Journal of neuroinflammation

    2023  Volume 20, Issue 1, Page(s) 145

    Abstract: Cellular adaptation to low oxygen tension triggers primitive pathways that ensure proper cell function. Conditions of hypoxia and low glucose are characteristic of injured tissues and hence successive waves of inflammatory cells must be suited to ... ...

    Abstract Cellular adaptation to low oxygen tension triggers primitive pathways that ensure proper cell function. Conditions of hypoxia and low glucose are characteristic of injured tissues and hence successive waves of inflammatory cells must be suited to function under low oxygen tension and metabolic stress. While Hypoxia-Inducible Factor (HIF)-1α has been shown to be essential for the inflammatory response of myeloid cells by regulating the metabolic switch to glycolysis, less is known about how HIF1α is triggered in inflammation. Here, we demonstrate that cells of the innate immune system require activity of the inositol-requiring enzyme 1α (IRE1α/XBP1) axis in order to initiate HIF1α-dependent production of cytokines such as IL1β, IL6 and VEGF-A. Knockout of either HIF1α or IRE1α in myeloid cells ameliorates vascular phenotypes in a model of retinal pathological angiogenesis driven by sterile inflammation. Thus, pathways associated with ER stress, in partnership with HIF1α, may co-regulate immune adaptation to low oxygen.
    MeSH term(s) Humans ; Protein Serine-Threonine Kinases/genetics ; Endoribonucleases ; Hypoxia ; Oxygen/metabolism ; Myeloid Cells/metabolism ; Inflammation/metabolism ; Hypoxia-Inducible Factor 1, alpha Subunit
    Chemical Substances Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-) ; Oxygen (S88TT14065) ; Hypoxia-Inducible Factor 1, alpha Subunit
    Language English
    Publishing date 2023-06-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2156455-3
    ISSN 1742-2094 ; 1742-2094
    ISSN (online) 1742-2094
    ISSN 1742-2094
    DOI 10.1186/s12974-023-02793-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: The fight of the Tudor domain "Royal family" for a broken DNA throne.

    Mallette, Frédérick A / Richard, Stéphane

    Cell cycle (Georgetown, Tex.)

    2012  Volume 11, Issue 8, Page(s) 1483–1484

    MeSH term(s) DNA Damage ; DNA Repair ; Histones/chemistry ; Histones/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; Jumonji Domain-Containing Histone Demethylases/chemistry ; Jumonji Domain-Containing Histone Demethylases/metabolism ; Methylation ; Protein Structure, Secondary ; Tumor Suppressor p53-Binding Protein 1 ; Ubiquitination
    Chemical Substances Histones ; Intracellular Signaling Peptides and Proteins ; TP53BP1 protein, human ; Tumor Suppressor p53-Binding Protein 1 ; Jumonji Domain-Containing Histone Demethylases (EC 1.14.11.-)
    Language English
    Publishing date 2012-04-15
    Publishing country United States
    Document type Editorial
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.4161/cc.20124
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5881: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top