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  1. Article: Antimicrobial quaternary ammonium silane K21 promotes wound healing.

    Rongo, Christopher / Prusty, Bhupesh / Baban, Babak / Daood, Umer / Ilyas, Muhammad Sharjeel / Kimmerling, Kirk

    Journal of wound care

    2024  Volume 33, Issue Sup3, Page(s) S11–S12

    MeSH term(s) Humans ; Ammonium Compounds ; Silanes ; Anti-Infective Agents/pharmacology ; Anti-Bacterial Agents ; Wound Healing
    Chemical Substances Ammonium Compounds ; Silanes ; Anti-Infective Agents ; Anti-Bacterial Agents
    Language English
    Publishing date 2024-03-08
    Publishing country England
    Document type Journal Article
    ZDB-ID 1353951-6
    ISSN 0969-0700
    ISSN 0969-0700
    DOI 10.12968/jowc.2024.33.Sup3.S11a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4572: Show issues Location:
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  2. Article ; Online: Better to burn out than it is to rust: coordinating cellular redox states during aging and stress.

    Rongo, Christopher

    The EMBO journal

    2015  Volume 34, Issue 18, Page(s) 2310–2311

    MeSH term(s) Aging/metabolism ; Animals ; Caenorhabditis elegans/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Proteostasis Deficiencies/metabolism
    Language English
    Publishing date 2015-09-14
    Publishing country England
    Document type Comment ; News
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201592504
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    Zs.A 1808: Show issues Location:
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  3. Article ; Online: Going mobile: AMPA receptors move synapse to synapse in vivo.

    Rongo, Christopher

    Neuron

    2013  Volume 80, Issue 6, Page(s) 1339–1341

    Abstract: Plasticity models invoke the synaptic delivery of AMPARs, yet we know little about how receptors move in vivo. In this issue of Neuron, Hoerndli et al. (2013) show that lateral diffusion and kinesin-mediated transport move AMPARs between synapses in vivo. ...

    Abstract Plasticity models invoke the synaptic delivery of AMPARs, yet we know little about how receptors move in vivo. In this issue of Neuron, Hoerndli et al. (2013) show that lateral diffusion and kinesin-mediated transport move AMPARs between synapses in vivo.
    MeSH term(s) Animals ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans Proteins/physiology ; Cell Cycle Proteins/physiology ; Kinesin/physiology ; Receptors, AMPA/metabolism ; Synaptic Transmission/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; Receptors, AMPA ; UNC-116 protein, C elegans ; glr-1 protein, C elegans ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2013-12-06
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2013.11.031
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    Zs.A 2496: Show issues Location:
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  4. Article: NEKL-4 regulates microtubule stability and mitochondrial health in

    Power, Kaiden M / Nguyen, Ken C / Silva, Andriele / Singh, Shaneen / Hall, David H / Rongo, Christopher / Barr, Maureen M

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Ciliopathies are often caused by defects in the ciliary microtubule core. Glutamylation is abundant in cilia, and its dysregulation may contribute to ciliopathies and neurodegeneration. Mutation of the deglutamylase CCP1 causes infantile-onset ... ...

    Abstract Ciliopathies are often caused by defects in the ciliary microtubule core. Glutamylation is abundant in cilia, and its dysregulation may contribute to ciliopathies and neurodegeneration. Mutation of the deglutamylase CCP1 causes infantile-onset neurodegeneration. In
    Language English
    Publishing date 2024-02-14
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.02.14.580304
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  5. Article ; Online: RPM-1 and DLK-1 regulate pioneer axon outgrowth by controlling Wnt signaling.

    Park, Eun Chan / Rongo, Christopher

    Development (Cambridge, England)

    2018  Volume 145, Issue 18

    Abstract: Axons must correctly reach their targets for proper nervous system function, although we do not fully understand the underlying mechanism, particularly for the first 'pioneer' axons. ... ...

    Abstract Axons must correctly reach their targets for proper nervous system function, although we do not fully understand the underlying mechanism, particularly for the first 'pioneer' axons. In
    MeSH term(s) Animals ; Axons/metabolism ; CCAAT-Enhancer-Binding Proteins/metabolism ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Differentiation/genetics ; Cell Proliferation/genetics ; Glycoproteins/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; MAP Kinase Kinase Kinases/genetics ; MAP Kinase Kinase Kinases/metabolism ; Neurons/metabolism ; Wnt Proteins/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
    Chemical Substances CCAAT-Enhancer-Binding Proteins ; Caenorhabditis elegans Proteins ; Cebp-1 protein, C elegans ; Egl-20 protein, C elegans ; Glycoproteins ; Guanine Nucleotide Exchange Factors ; RPM-1 protein, C elegans ; Wnt Proteins ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; DLK-1 protein, C elegans (EC 2.7.11.25) ; MAP Kinase Kinase Kinases (EC 2.7.11.25)
    Language English
    Publishing date 2018-09-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.164897
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    Ub I Zs.183: Show issues Location:
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  6. Article ; Online: Epidermal growth factor and aging: a signaling molecule reveals a new eye opening function.

    Rongo, Christopher

    Aging

    2011  Volume 3, Issue 9, Page(s) 896–905

    Abstract: Epidermal Growth Factor (EGF) is known for its role in promoting cell division and cellular differentiation in developing animals, but we know surprising little about what EGF does in vivo in mature adult animals. Here I review EGF signaling, emphasizing ...

    Abstract Epidermal Growth Factor (EGF) is known for its role in promoting cell division and cellular differentiation in developing animals, but we know surprising little about what EGF does in vivo in mature adult animals. Here I review EGF signaling, emphasizing several recent studies that uncovered an unexpected role for EGF in promoting longevity and healthspan in mature adult C. elegans. EGF, acting through phospholipase Cγ and the IP3 receptor signaling, maintains pharyngeal and body wall muscle function in aging adults, and delays the accumulation of lipofuscin-enriched aging pigments within intestinal cells. EGF also acts through the Ras/ERK pathway to regulate protein homeostasis by promoting the expression of antioxidant genes, stimulating the activity of the Ubiquitin Proteasome System (UPS), and repressing the expression of small heat shock protein chaperones. The effects of EGF signaling on lifespan are largely independent of Insulin/IGF-like Signaling (IIS), as the effects of EGF signaling mutants on lifespan and heathspan are not affected by mutations in the DAF-2 insulin receptor or the DAF-16 FOXO transcription factor. Nevertheless, these two signal pathways have multiple points of overlap, coordination, and cross regulation. I propose that the IIS and EGF signaling pathways respond to environment and to developmental timing, respectively, so as to coordinate the appropriate physiological strategy that cells use to maintain protein homeostasis.
    MeSH term(s) Aging/physiology ; Animals ; Epidermal Growth Factor/metabolism ; Homeostasis ; Humans ; Insulin/metabolism ; Insulin-Like Growth Factor I/metabolism ; Longevity/physiology ; Proteasome Endopeptidase Complex/metabolism ; Signal Transduction/physiology ; Ubiquitin/metabolism
    Chemical Substances Insulin ; Ubiquitin ; Epidermal Growth Factor (62229-50-9) ; Insulin-Like Growth Factor I (67763-96-6) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2011-09-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 1945-4589
    ISSN (online) 1945-4589
    DOI 10.18632/aging.100384
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  7. Article ; Online: Reply to: Potential contribution of PEP carboxykinase-dependent malate dismutation to the hypoxia response in C. elegans.

    Vora, Mehul / Pyonteck, Stephanie M / Popovitchenko, Tatiana / Matlack, Tarmie L / Prashar, Aparna / Kane, Nanci S / Favate, John / Shah, Premal / Rongo, Christopher

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 3937

    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Malates ; Phosphoenolpyruvate Carboxykinase (GTP)/metabolism ; Photosynthesis
    Chemical Substances malic acid (817L1N4CKP) ; Malates ; Phosphoenolpyruvate Carboxykinase (GTP) (EC 4.1.1.32)
    Language English
    Publishing date 2023-07-04
    Publishing country England
    Document type Letter ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-39511-4
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  8. Article ; Online: The p38 MAP kinase pathway modulates the hypoxia response and glutamate receptor trafficking in aging neurons.

    Park, Eun Chan / Rongo, Christopher

    eLife

    2016  Volume 5

    Abstract: Neurons are sensitive to low oxygen (hypoxia) and employ a conserved pathway to combat its effects. Here, we show that p38 MAP Kinase (MAPK) modulates this hypoxia response pathway in C. elegans. Mutants lacking p38 MAPK components pmk-1 or sek-1 ... ...

    Abstract Neurons are sensitive to low oxygen (hypoxia) and employ a conserved pathway to combat its effects. Here, we show that p38 MAP Kinase (MAPK) modulates this hypoxia response pathway in C. elegans. Mutants lacking p38 MAPK components pmk-1 or sek-1 resemble mutants lacking the hypoxia response component and prolyl hydroxylase egl-9, with impaired subcellular localization of Mint orthologue LIN-10, internalization of glutamate receptor GLR-1, and depression of GLR-1-mediated behaviors. Loss of p38 MAPK impairs EGL-9 protein localization in neurons and activates the hypoxia-inducible transcription factor HIF-1, suggesting that p38 MAPK inhibits the hypoxia response pathway through EGL-9. As animals age, p38 MAPK levels decrease, resulting in GLR-1 internalization; this age-dependent downregulation can be prevented through either p38 MAPK overexpression or removal of CDK-5, an antagonizing kinase. Our findings demonstrate that p38 MAPK inhibits the hypoxia response pathway and determines how aging neurons respond to hypoxia through a novel mechanism.
    MeSH term(s) Animals ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/metabolism ; Cell Hypoxia ; MAP Kinase Signaling System ; Neurons/physiology ; Receptors, Glutamate/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Receptors, Glutamate ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2016-01-05
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.12010
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  9. Article ; Online: Biogenic amine neurotransmitters promote eicosanoid production and protein homeostasis.

    Joshi, Kishore K / Matlack, Tarmie L / Pyonteck, Stephanie / Vora, Mehul / Menzel, Ralph / Rongo, Christopher

    EMBO reports

    2021  Volume 22, Issue 3, Page(s) e51063

    Abstract: Metazoans use protein homeostasis (proteostasis) pathways to respond to adverse physiological conditions, changing environment, and aging. The nervous system regulates proteostasis in different tissues, but the mechanism is not understood. Here, we show ... ...

    Abstract Metazoans use protein homeostasis (proteostasis) pathways to respond to adverse physiological conditions, changing environment, and aging. The nervous system regulates proteostasis in different tissues, but the mechanism is not understood. Here, we show that Caenorhabditis elegans employs biogenic amine neurotransmitters to regulate ubiquitin proteasome system (UPS) proteostasis in epithelia. Mutants for biogenic amine synthesis show decreased poly-ubiquitination and turnover of a GFP-based UPS substrate. Using RNA-seq and mass spectrometry, we found that biogenic amines promote eicosanoid production from poly-unsaturated fats (PUFAs) by regulating expression of cytochrome P450 monooxygenases. Mutants for one of these P450s share the same UPS phenotype observed in biogenic amine mutants. The production of n-6 eicosanoids is required for UPS substrate turnover, whereas accumulation of n-6 eicosanoids accelerates turnover. Our results suggest that sensory neurons secrete biogenic amines to modulate lipid signaling, which in turn activates stress response pathways to maintain UPS proteostasis.
    MeSH term(s) Animals ; Biogenic Amines ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Neurotransmitter Agents ; Proteostasis
    Chemical Substances Biogenic Amines ; Caenorhabditis elegans Proteins ; Neurotransmitter Agents
    Language English
    Publishing date 2021-01-20
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.202051063
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    Zs.A 5433: Show issues Location:
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  10. Article ; Online: The hypoxia response pathway promotes PEP carboxykinase and gluconeogenesis in C. elegans.

    Vora, Mehul / Pyonteck, Stephanie M / Popovitchenko, Tatiana / Matlack, Tarmie L / Prashar, Aparna / Kane, Nanci S / Favate, John / Shah, Premal / Rongo, Christopher

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 6168

    Abstract: Actively dividing cells, including some cancers, rely on aerobic glycolysis rather than oxidative phosphorylation to generate energy, a phenomenon termed the Warburg effect. Constitutive activation of the Hypoxia Inducible Factor (HIF-1), a transcription ...

    Abstract Actively dividing cells, including some cancers, rely on aerobic glycolysis rather than oxidative phosphorylation to generate energy, a phenomenon termed the Warburg effect. Constitutive activation of the Hypoxia Inducible Factor (HIF-1), a transcription factor known for mediating an adaptive response to oxygen deprivation (hypoxia), is a hallmark of the Warburg effect. HIF-1 is thought to promote glycolysis and suppress oxidative phosphorylation. Here, we instead show that HIF-1 can promote gluconeogenesis. Using a multiomics approach, we reveal the genomic, transcriptomic, and metabolomic landscapes regulated by constitutively active HIF-1 in C. elegans. We use RNA-seq and ChIP-seq under aerobic conditions to analyze mutants lacking EGL-9, a key negative regulator of HIF-1. We integrate these approaches to identify over two hundred genes directly and functionally upregulated by HIF-1, including the PEP carboxykinase PCK-1, a rate-limiting mediator of gluconeogenesis. This activation of PCK-1 by HIF-1 promotes survival in response to both oxidative and hypoxic stress. Our work identifies functional direct targets of HIF-1 in vivo, comprehensively describing the metabolome induced by HIF-1 activation in an organism.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Gluconeogenesis/genetics ; Transcription Factors/genetics ; Cell Hypoxia ; Hypoxia/genetics ; Oxygen ; Hypoxia-Inducible Factor 1, alpha Subunit/genetics
    Chemical Substances Transcription Factors ; Oxygen (S88TT14065) ; Hypoxia-Inducible Factor 1, alpha Subunit
    Language English
    Publishing date 2022-10-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; 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/s41467-022-33849-x
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