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    Nlrp1b NLR family, pyrin domain containing 1B [ Mus musculus (house mouse) ]

    Gene ID: 637515, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    UVB-Induced Skin Autoinflammation Due to Nlrp1b Mutation and Its Inhibition by Anti-IL-1beta Antibody.

    UVB-Induced Skin Autoinflammation Due to Nlrp1b Mutation and Its Inhibition by Anti-IL-1β Antibody.
    Murase Y, Takeichi T, Koseki J, Miyasaka Y, Muro Y, Ohno T, Shimamura T, Akiyama M., Free PMC Article

    07/9/2022
    NLRP1B and NLRP3 Control the Host Response following Colonization with the Commensal Protist Tritrichomonas musculis.

    NLRP1B and NLRP3 Control the Host Response following Colonization with the Commensal Protist Tritrichomonas musculis.
    Chiaranunt P, Burrows K, Ngai L, Cao EY, Liang H, Tai SL, Streutker CJ, Girardin SE, Mortha A.

    04/16/2022
    NLRP1 inflammasome involves in learning and memory impairments and neuronal damages during aging process in mice.

    NLRP1 inflammasome involves in learning and memory impairments and neuronal damages during aging process in mice.
    Sun D, Gao G, Zhong B, Zhang H, Ding S, Sun Z, Zhang Y, Li W., Free PMC Article

    01/22/2022
    Nlrp1b1 negatively modulates obesity-induced inflammation by promoting IL-18 production.

    Nlrp1b1 negatively modulates obesity-induced inflammation by promoting IL-18 production.
    Salazar-León J, Valdez-Hernández AL, García-Jiménez S, Román-Domínguez L, Huanosta-Murillo E, Bonifaz LC, Pérez-Martínez L, Pedraza-Alva G., Free PMC Article

    10/31/2020
    NLRP1B also encompassessome additional unique structural features.For instance, the NLRP1B bears a C-termi-nal caspase activation and recruitmentdomain (CARD).

    When Degradation Elicits the Alarm: N-Terminal Degradation of NLRP1B Unleashes Its Inflammasome Activity.
    Eldeeb MA, Fahlman RP, Esmaili M, Fon EA.

    10/19/2019
    Lethal factor directly cleaves NLRP1B, inducing the N-end rule-mediated degradation of the NLRP1B N terminus and freeing the NLRP1B C terminus to activate caspase-1.

    N-terminal degradation activates the NLRP1B inflammasome.
    Chui AJ, Okondo MC, Rao SD, Gai K, Griswold AR, Johnson DC, Ball DP, Taabazuing CY, Orth EL, Vittimberga BA, Bachovchin DA., Free PMC Article

    06/23/2019
    NLRP1B senses cellular infection by distinct invasive pathogens.

    Listeria monocytogenes and Shigella flexneri Activate the NLRP1B Inflammasome.
    Neiman-Zenevich J, Stuart S, Abdel-Nour M, Girardin SE, Mogridge J., Free PMC Article

    10/28/2017
    ASC-driven caspase-1 autoprocessing and speck formation are dispensable for the activation of caspase-1 and the NLRP1b inflammasome.

    Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation.
    Van Opdenbosch N, Gurung P, Vande Walle L, Fossoul A, Kanneganti TD, Lamkanfi M., Free PMC Article

    10/31/2015
    Identification of the inflammasome Nlrp1b as the candidate gene conferring diabetes risk at the Idd4.1 locus in the nonobese diabetic mouse.

    Identification of the inflammasome Nlrp1b as the candidate gene conferring diabetes risk at the Idd4.1 locus in the nonobese diabetic mouse.
    Motta VN, Markle JG, Gulban O, Mortin-Toth S, Liao KC, Mogridge J, Steward CA, Danska JS.

    08/22/2015
    Data suggest that caspase-1 autoproteolysis in NLR family pyrin domain containing 1b (NLRP1b) and NLR family pyrin domain containing 3 (NLRP3) inflammasome function may have implications for pathogen recognition and response.

    Caspase-1 autoproteolysis is differentially required for NLRP1b and NLRP3 inflammasome function.
    Guey B, Bodnar M, Manié SN, Tardivel A, Petrilli V., Free PMC Article

    05/2/2015
    NLRP1 functions primarily as a sensor of protease activity and thus could conceivably detect a broader spectrum of pathogens than just B. anthracis.

    Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor.
    Chavarría-Smith J, Vance RE., Free PMC Article

    01/18/2014
    macrophages from some inbred mouse strains simultaneously express different splice variants of Nlrp1b

    Transcriptional analysis of the three Nlrp1 paralogs in mice.
    Sastalla I, Crown D, Masters SL, McKenzie A, Leppla SH, Moayeri M., Free PMC Article

    10/26/2013
    Mouse Nlrp1b proteins are also cleaved by lethal factor.

    Anthrax lethal factor cleaves mouse nlrp1b in both toxin-sensitive and toxin-resistant macrophages.
    Hellmich KA, Levinsohn JL, Fattah R, Newman ZL, Maier N, Sastalla I, Liu S, Leppla SH, Moayeri M., Free PMC Article

    05/11/2013
    Proteolysis of Nlrp1b was shown to be required for the assembly of a functional inflammasome

    Proteolytic processing of Nlrp1b is required for inflammasome activity.
    Frew BC, Joag VR, Mogridge J., Free PMC Article

    08/25/2012
    data confirm an inverse relationship between murine macrophage sensitivity to lethal toxin and mouse susceptibility to spore infection, and establish roles for Nlrp1b(S), caspase-1, and IL-1beta in countering anthrax infection.

    Inflammasome sensor Nlrp1b-dependent resistance to anthrax is mediated by caspase-1, IL-1 signaling and neutrophil recruitment.
    Moayeri M, Crown D, Newman ZL, Okugawa S, Eckhaus M, Cataisson C, Liu S, Sastalla I, Leppla SH., Free PMC Article

    05/21/2011
    animals expressing a lethal toxin (LT)-sensitive allele of Nlrp1b showed an early inflammatory response to LT and increased resistance to infection by B. anthracis

    Cutting edge: resistance to Bacillus anthracis infection mediated by a lethal toxin sensitive allele of Nalp1b/Nlrp1b.
    Terra JK, Cote CK, France B, Jenkins AL, Bozue JA, Welkos SL, LeVine SM, Bradley KA., Free PMC Article

    01/21/2010
    The authors demonstrate that transfection of human fibroblasts with plasmids encoding murine Nlrp1b and procaspase-1 was sufficient to confer susceptibility to lethal toxin-mediated death on the cells.

    Expression of Nlrp1b inflammasome components in human fibroblasts confers susceptibility to anthrax lethal toxin.
    Liao KC, Mogridge J., Free PMC Article

    01/21/2010
    an extremely polymorphic gene in this locus, Nalp1b, is the primary mediator of mouse macrophage susceptibility to LeTx (lethal toxin)

    Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin.
    Boyden ED, Dietrich WF.

    01/21/2010
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