U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    TMPRSS13 transmembrane serine protease 13 [ Homo sapiens (human) ]

    Gene ID: 84000, updated on 17-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    IL4I1 binds to TMPRSS13 and competes with SARS-CoV-2 spike.

    IL4I1 binds to TMPRSS13 and competes with SARS-CoV-2 spike.
    Gatineau J, Nidercorne C, Dupont A, Puiffe ML, Cohen JL, Molinier-Frenkel V, Niedergang F, Castellano F., Free PMC Article

    10/1/2022
    Posttranslational modifications of serine protease TMPRSS13 regulate zymogen activation, proteolytic activity, and cell surface localization.

    Posttranslational modifications of serine protease TMPRSS13 regulate zymogen activation, proteolytic activity, and cell surface localization.
    Martin CE, Murray AS, Sala-Hamrick KE, Mackinder JR, Harrison EC, Lundgren JG, Varela FA, List K., Free PMC Article

    11/27/2021
    Crystal structure of inhibitor-bound human MSPL that can activate high pathogenic avian influenza.

    Crystal structure of inhibitor-bound human MSPL that can activate high pathogenic avian influenza.
    Ohno A, Maita N, Tabata T, Nagano H, Arita K, Ariyoshi M, Uchida T, Nakao R, Ulla A, Sugiura K, Kishimoto K, Teshima-Kondo S, Okumura Y, Nikawa T., Free PMC Article

    04/17/2021
    TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein.

    TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein.
    Kishimoto M, Uemura K, Sanaki T, Sato A, Hall WW, Kariwa H, Orba Y, Sawa H, Sasaki M., Free PMC Article

    03/27/2021
    The cell-surface anchored serine protease TMPRSS13 promotes breast cancer progression and resistance to chemotherapy.

    The cell-surface anchored serine protease TMPRSS13 promotes breast cancer progression and resistance to chemotherapy.
    Murray AS, Hyland TE, Sala-Hamrick KE, Mackinder JR, Martin CE, Tanabe LM, Varela FA, List K., Free PMC Article

    12/12/2020
    TMPRSS13 promotes cell survival, invasion, and resistance to drug-induced apoptosis in colorectal cancer.

    TMPRSS13 promotes cell survival, invasion, and resistance to drug-induced apoptosis in colorectal cancer.
    Varela FA, Foust VL, Hyland TE, Sala-Hamrick KE, Mackinder JR, Martin CE, Murray AS, Todi SV, List K., Free PMC Article

    12/12/2020
    The data provide novel insight into the cellular properties of TMPRSS13 and highlight phosphorylation of TMPRSS13 as a novel post-translational modification of this TTSP family member and potentially other members of this family of proteases.

    Phosphorylation of the type II transmembrane serine protease, TMPRSS13, in hepatocyte growth factor activator inhibitor-1 and -2-mediated cell-surface localization.
    Murray AS, Varela FA, Hyland TE, Schoenbeck AJ, White JM, Tanabe LM, Todi SV, List K., Free PMC Article

    09/30/2017
    study demonstrates that two cellular serine proteases, DESC1 and MSPL, activate influenza viruses and emerging coronaviruses in cell culture and, because of their expression in human lung tissue, might promote viral spread in the infected host

    DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.
    Zmora P, Blazejewska P, Moldenhauer AS, Welsch K, Nehlmeier I, Wu Q, Schneider H, Pöhlmann S, Bertram S., Free PMC Article

    11/29/2014
    results suggest that TMPRSS13 functions as an HGF-converting protease, the activity of which may be regulated by HAI-1

    TMPRSS13, a type II transmembrane serine protease, is inhibited by hepatocyte growth factor activator inhibitor type 1 and activates pro-hepatocyte growth factor.
    Hashimoto T, Kato M, Shimomura T, Kitamura N.

    01/1/2011
    The authors report that serine proteases, MSPL and its splice variant TMPRSS13, are novel candidates for proteases processing HA proteins of highly pathogenic avian influenza (HPAI) viruses.

    Novel type II transmembrane serine proteases, MSPL and TMPRSS13, Proteolytically activate membrane fusion activity of the hemagglutinin of highly pathogenic avian influenza viruses and induce their multicycle replication.
    Okumura Y, Takahashi E, Yano M, Ohuchi M, Daidoji T, Nakaya T, Böttcher E, Garten W, Klenk HD, Kido H., Free PMC Article

    05/10/2010
    cloning of MSPL/TMPRSS13, which may play roles in the proteolytic processing of prohormones, precursors of growth factors, and also play roles in the pathogenicity of many viruses and bacteria in vivo

    MSPL/TMPRSS13.
    Kido H, Okumura Y.

    01/21/2010
    firstprevious page of 1 nextlast