 Endoribonucleases
"Endoribonucleases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.
| Descriptor ID |
D004722
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| MeSH Number(s) |
D08.811.277.352.355.350 D08.811.277.352.700.350
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Endoribonucleases".
Below are MeSH descriptors whose meaning is more specific than "Endoribonucleases".
This graph shows the total number of publications written about "Endoribonucleases" by people in this website by year, and whether "Endoribonucleases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 3 | 0 | 3 | | 1997 | 1 | 0 | 1 | | 1998 | 2 | 0 | 2 | | 1999 | 1 | 0 | 1 | | 2000 | 2 | 0 | 2 | | 2001 | 1 | 1 | 2 | | 2002 | 2 | 1 | 3 | | 2003 | 1 | 0 | 1 | | 2004 | 0 | 1 | 1 | | 2005 | 0 | 3 | 3 | | 2006 | 1 | 0 | 1 | | 2007 | 2 | 2 | 4 | | 2008 | 2 | 1 | 3 | | 2010 | 1 | 1 | 2 | | 2011 | 2 | 0 | 2 | | 2013 | 2 | 1 | 3 | | 2014 | 4 | 1 | 5 | | 2015 | 4 | 2 | 6 | | 2016 | 1 | 1 | 2 | | 2017 | 2 | 1 | 3 | | 2018 | 1 | 0 | 1 | | 2019 | 3 | 0 | 3 | | 2020 | 0 | 1 | 1 | | 2021 | 2 | 1 | 3 | | 2022 | 0 | 1 | 1 | | 2024 | 1 | 1 | 2 | | 2025 | 2 | 1 | 3 |
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Below are the most recent publications written about "Endoribonucleases" by people in Profiles.
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Youle RL, Lista MJ, Brudenell EL, Thompson B, Bouton C, Morris ER, Neil SJD, Swanson CM, Taylor IA. KHNYN is a manganese-dependent endoribonuclease required for ZAP-mediated antiviral restriction. Nucleic Acids Res. 2025 Nov 26; 53(22).
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Youle RL, Lista MJ, Bouton C, Kunzelmann S, Wilson H, Cottee MA, Purkiss AG, Morris ER, Neil SJD, Taylor IA, Swanson CM. Structural and functional characterization of the extended-diKH domain from the antiviral endoribonuclease KHNYN. J Biol Chem. 2025 04; 301(4):108336.
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Oguh AU, Haemmerle MW, Sen S, Rozo AV, Shrestha S, Cartailler JP, Fazelinia H, Ding H, Preza S, Yang J, Yang X, Sussel L, Alvarez-Dominguez JR, Doliba N, Spruce LA, Arrojo E Drigo R, Stoffers DA. E3 ligase substrate adaptor SPOP fine-tunes the UPR of pancreatic ß cells. Genes Dev. 2025 02 03; 39(3-4):261-279.
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Zhu J, Lai Y, Cheng M, Dash RC, Guo S, Guo J, Su Y, Wolek A, Issacs B, Liu Z, Li Q, Mishra N, Garmendia A, Hadden MK, Tian XC, He X, Tang Y. Discovery of small molecules against porcine reproductive and respiratory syndrome virus replication by targeting NendoU activity. J Virol. 2025 02 25; 99(2):e0203424.
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Murthy A, Rodriguez LR, Dimopoulos T, Bui S, Iyer S, Chavez K, Tomer Y, Abraham V, Cooper C, Renner DM, Katzen JB, Bentley ID, Ghadiali SN, Englert JA, Weiss SR, Beers MF. Activation of alveolar epithelial ER stress by ß-coronavirus infection disrupts surfactant homeostasis in mice: implications for COVID-19 respiratory failure. Am J Physiol Lung Cell Mol Physiol. 2024 Aug 01; 327(2):L232-L249.
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Cooley JC, Redente EF. Getting the Timing Right: Controlling BCL-2 Inhibition as an Antifibrotic Therapy. Am J Respir Cell Mol Biol. 2024 Apr; 70(4):231-232.
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Cusic R, Watkins JM, Burke JM. Single-cell analysis of RNase L-mediated mRNA decay. Methods Enzymol. 2023; 692:157-175.
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Tepe B, Macke EL, Niceta M, Weisz Hubshman M, Kanca O, Schultz-Rogers L, Zarate YA, Schaefer GB, Granadillo De Luque JL, Wegner DJ, Cogne B, Gilbert-Dussardier B, Le Guillou X, Wagner EJ, Pais LS, Neil JE, Mochida GH, Walsh CA, Magal N, Drasinover V, Shohat M, Schwab T, Schmitz C, Clark K, Fine A, Lanpher B, Gavrilova R, Blanc P, Burglen L, Afenjar A, Steel D, Kurian MA, Prabhakar P, Gößwein S, Di Donato N, Bertini ES, Wangler MF, Yamamoto S, Tartaglia M, Klee EW, Bellen HJ. Bi-allelic variants in INTS11 are associated with a complex neurological disorder. Am J Hum Genet. 2023 05 04; 110(5):774-789.
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Burke JM. Regulation of ribonucleoprotein condensates by RNase L during viral infection. Wiley Interdiscip Rev RNA. 2023 Jul-Aug; 14(4):e1770.
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Burke JM, Ripin N, Ferretti MB, St Clair LA, Worden-Sapper ER, Salgado F, Sawyer SL, Perera R, Lynch KW, Parker R. RNase L activation in the cytoplasm induces aberrant processing of mRNAs in the nucleus. PLoS Pathog. 2022 11; 18(11):e1010930.
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