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  1. Article ; Online: Lipocalin-2 deficiency may predispose to the progression of spontaneous age-related adiposity in mice.

    Meyers, Keya / López, María / Ho, Joanna / Wills, Savannah / Rayalam, Srujana / Taval, Shashidharamurthy

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 14589

    Abstract: Lipocalin-2 (Lcn2) is an innate immune protein elevated by several orders of magnitude in various inflammatory conditions including aging and obesity. Recent studies have shown that Lcn2 is secreted by adipocytes in response to inflammation and is ... ...

    Abstract Lipocalin-2 (Lcn2) is an innate immune protein elevated by several orders of magnitude in various inflammatory conditions including aging and obesity. Recent studies have shown that Lcn2 is secreted by adipocytes in response to inflammation and is categorized as a new adipokine cross-linking innate immunity and metabolic disorders including obesity. However, the involvement of Lcn2 and its function during the progression of obesity is largely unknown. Recently, browning of white adipose tissue (WAT) has gained attention as a therapeutic strategy to combat obesity. Herein, we have shown that treatment of mature 3T3-L1 adipocytes with recombinant Lcn2 (rec-Lcn2) resulted in the up-regulation of thermogenic and beige/brown markers (UCP1, PRDM16, ZIC-1 and TBX1) and increased mitochondrial activity. Additionally, global Lcn2 genetic knockout (Lcn2KO) mice exhibited accelerated weight gain and visceral fat deposition with age, when compared to wild type (WT) mice. Taken together, both in vitro and in vivo studies suggest that Lcn2 is a naturally occurring adipokine, and may serve as an anti-obesity agent by upregulating the thermogenic markers resulting in the browning of WAT. Therefore, Lcn2 and its downstream signaling pathways could be a potential therapeutic target for obesity.
    MeSH term(s) 3T3-L1 Cells ; Adipose Tissue/metabolism ; Adipose Tissue/pathology ; Aging ; Animals ; Female ; Intra-Abdominal Fat/metabolism ; Intra-Abdominal Fat/pathology ; Lipocalin-2/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Obesity/physiopathology ; Thermogenesis ; Weight Gain
    Chemical Substances Lipocalin-2 ; Lcn2 protein, mouse (126469-30-5)
    Language English
    Publishing date 2020-09-03
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-71249-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Aloin isoforms (A and B) selectively inhibits proteolytic and deubiquitinating activity of papain like protease (PLpro) of SARS-CoV-2 in vitro.

    Lewis, Devin S M / Ho, Joanna / Wills, Savannah / Kawall, Anasha / Sharma, Avini / Chavada, Krishna / Ebert, Maximilian C C J C / Evoli, Stefania / Singh, Ajay / Rayalam, Srujana / Mody, Vicky / Taval, Shashidharamurthy

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 2145

    Abstract: The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the ... ...

    Abstract The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the commercially available oral and nasal rinse products are effective in inhibiting the viral replication. However, the anti-viral mechanism of the active ingredients present in the oral rinses have not been studied. In the present study, we have assessed in vitro enzymatic inhibitory activity of active ingredients in the oral mouth rinse products: aloin A and B, chlorhexidine, eucalyptol, hexetidine, menthol, triclosan, methyl salicylate, sodium fluoride and povidone, against two important proteases of SARS-CoV-2 PLpro and 3CLpro. Our results indicate only aloin A and B effectively inhibited proteolytic activity of PLpro with an IC
    MeSH term(s) Animals ; Binding Sites ; COVID-19/pathology ; COVID-19/virology ; Cell Survival/drug effects ; Chlorocebus aethiops ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/metabolism ; Coronavirus Papain-Like Proteases/antagonists & inhibitors ; Coronavirus Papain-Like Proteases/metabolism ; Emodin/analogs & derivatives ; Emodin/chemistry ; Emodin/metabolism ; Emodin/pharmacology ; Humans ; Molecular Dynamics Simulation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Protein Isoforms/pharmacology ; SARS-CoV-2/enzymology ; SARS-CoV-2/isolation & purification ; Vero Cells
    Chemical Substances Protein Isoforms ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Emodin (KA46RNI6HN) ; alloin (W41H6S09F4)
    Language English
    Publishing date 2022-02-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-06104-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents.

    Mody, Vicky / Ho, Joanna / Wills, Savannah / Mawri, Ahmed / Lawson, Latasha / Ebert, Maximilian C C J C / Fortin, Guillaume M / Rayalam, Srujana / Taval, Shashidharamurthy

    Communications biology

    2021  Volume 4, Issue 1, Page(s) 93

    Abstract: Emerging outbreak of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection is a major threat to public health. The morbidity is increasing due to lack of SARS-CoV-2 specific drugs. Herein, we have identified potential drugs that target ... ...

    Abstract Emerging outbreak of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection is a major threat to public health. The morbidity is increasing due to lack of SARS-CoV-2 specific drugs. Herein, we have identified potential drugs that target the 3-chymotrypsin like protease (3CLpro), the main protease that is pivotal for the replication of SARS-CoV-2. Computational molecular modeling was used to screen 3987 FDA approved drugs, and 47 drugs were selected to study their inhibitory effects on SARS-CoV-2 specific 3CLpro enzyme in vitro. Our results indicate that boceprevir, ombitasvir, paritaprevir, tipranavir, ivermectin, and micafungin exhibited inhibitory effect towards 3CLpro enzymatic activity. The 100 ns molecular dynamics simulation studies showed that ivermectin may require homodimeric form of 3CLpro enzyme for its inhibitory activity. In summary, these molecules could be useful to develop highly specific therapeutically viable drugs to inhibit the SARS-CoV-2 replication either alone or in combination with drugs specific for other SARS-CoV-2 viral targets.
    MeSH term(s) Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; COVID-19/virology ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/chemistry ; Coronavirus 3C Proteases/metabolism ; Cysteine Proteinase Inhibitors/chemistry ; Cysteine Proteinase Inhibitors/pharmacology ; Drug Discovery ; Humans ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; Structure-Activity Relationship ; Virus Replication/drug effects
    Chemical Substances Antiviral Agents ; Cysteine Proteinase Inhibitors ; Ligands ; Coronavirus 3C Proteases (EC 3.4.22.28)
    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
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-020-01577-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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