Zobrazeno 1 - 10
of 15
pro vyhledávání: '"MESH: Endoribonucleases"'
Autor:
Wickenhagen, A, Sugrue, E, Lytras, S, Kuchi, S, Noerenberg, M, Turnbull, ML, Loney, C, Herder, V, Allan, J, Jarmson, I, Cameron-Ruiz, N, Varjak, M, Pinto, RM, Lee, JY, Iselin, L, Palmalux, N, Stewart, DG, Swingler, S, Greenwood, EJD, Crozier, TWM, Gu, Q, Davies, EL, Clohisey, S, Wang, B, Trindade Maranhão Costa, F, Freire Santana, M, de Lima Ferreira, LC, Murphy, L, Fawkes, A, Meynert, A, Grimes, G, Da Silva Filho, JL, Marti, M, Hughes, J, Stanton, RJ, Wang, ECY, Ho, A, Davis, I, Jarrett, RF, Castello, A, Robertson, DL, Semple, MG, Openshaw, PJM, Palmarini, M, Lehner, PJ, Baillie, JK, Rihn, SJ, Wilson, SJ, ISARIC4C Investigators, Carson, G, Alex, B, Bach, B, Barclay, WS, Bogaert, D, Chand, M, Cooke, GS, Docherty, AB, Dunning, J, da Silva Filipe, A, Fletcher, T, Green, CA, Harrison, EM, Ho, AYW, Horby, PW, Ijaz, S, Khoo, S, Klenerman, P, Law, A, Lim, WS, Mentzer, AJ, Merson, L, Meynert, AM, Noursadeghi, M, Moore, SC, Paxton, WA, Pollakis, G, Price, N, Rambaut, A, Russell, CD, Sancho-Shimizu, V, Scott, JT, de Silva, T, Sigfrid, L, Solomon, T, Sriskandan, S, Stuart, D, Summers, C, Tedder, RS, Thomson, EC, Thompson, AAR, Thwaites, RS, Turtle, LCW, Gupta, RK, Palmieri, C, Swann, OV, Zambon, M, Dumas, M-E, Griffin, JL, Takats, Z, Chechi, K, Andrikopoulos, P, Osagie, A, Olanipekun, M, Liggi, S, Lewis, MR, Dos Santos Correia, G, Sands, CJ, Takis, P, Maslen, L, Hardwick, H, Donohue, C, Griffiths, F, Oosthuyzen, W, Donegan, C, Spencer, RG, Norman, L, Pius, R, Drake, TM, Fairfield, CJ, Knight, SR, Mclean, KA, Murphy, D, Shaw, CA, Dalton, J, Girvan, M, Saviciute, E, Roberts, S, Harrison, J, Marsh, L, Connor, M, Halpin, S, Jackson, C, Gamble, C, Plotkin, D, Lee, J, Leeming, G, Wham, M, Hendry, R, Scott-Brown, J, Greenhalf, W, Shaw, V, McDonald, SE, Keating, S, Ahmed, KA, Armstrong, JA, Ashworth, M, Asiimwe, IG, Bakshi, S, Barlow, SL, Booth, L, Brennan, B, Bullock, K, Catterall, BWA, Clark, JJ, Clarke, EA, Cole, S, Cooper, L, Cox, H, Davis, C, Dincarslan, O, Dunn, C, Dyer, P, Elliott, A, Evans, A, Finch, L, Fisher, LWS, Foster, T, Garcia-Dorival, I, Gunning, P, Hartley, C, Jensen, RL, Jones, CB, Jones, TR, Khandaker, S, King, K, Kiy, RT, Koukorava, C, Lake, A, Lant, S, Latawiec, D, Lavelle-Langham, L, Lefteri, D, Lett, L, Livoti, LA, Mancini, M, McDonald, S, McEvoy, L, McLauchlan, J, Metelmann, S, Miah, NS, Middleton, J, Mitchell, J, Murphy, EG, Penrice-Randal, R, Pilgrim, J, Prince, T, Reynolds, W, Ridley, PM, Sales, D, Shaw, VE, Shears, RK, Small, B, Subramaniam, KS, Szemiel, A, Taggart, A, Tanianis-Hughes, J, Thomas, J, Trochu, E, van Tonder, L, Wilcock, E, Zhang, JE, Flaherty, L, Maziere, N, Cass, E, Carracedo, AD, Carlucci, N, Holmes, A, Massey, H, Wrobel, N, McCafferty, S, Morrice, K, MacLean, A, Adeniji, K, Agranoff, D, Agwuh, K, Ail, D, Aldera, EL, Alegria, A, Allen, S, Angus, B, Ashish, A, Atkinson, D, Bari, S, Barlow, G, Barnass, S, Barrett, N, Bassford, C, Basude, S, Baxter, D, Beadsworth, M, Bernatoniene, J, Berridge, J, Berry, C, Best, N, Bothma, P, Chadwick, D, Brittain-Long, R, Bulteel, N, Burden, T, Burtenshaw, A, Caruth, V, Chambler, D, Chee, N, Child, J, Chukkambotla, S, Clark, T, Collini, P, Cosgrove, C, Cupitt, J, Cutino-Moguel, M-T, Dark, P, Dawson, C, Dervisevic, S, Donnison, P, Douthwaite, S, Drummond, A, DuRand, I, Dushianthan, A, Dyer, T, Evans, C, Eziefula, C, Fegan, C, Finn, A, Fullerton, D, Garg, S, Garg, A, Gkrania-Klotsas, E, Godden, J, Goldsmith, A, Graham, C, Hardy, E, Hartshorn, S, Harvey, D, Havalda, P, Hawcutt, DB, Hobrok, M, Hodgson, L, Hormis, A, Jacobs, M, Jain, S, Jennings, P, Kaliappan, A, Kasipandian, V, Kegg, S, Kelsey, M, Kendall, J, Kerrison, C, Kerslake, I, Koch, O, Koduri, G, Koshy, G, Laha, S, Laird, S, Larkin, S, Leiner, T, Lillie, P, Limb, J, Linnett, V, Little, J, Lyttle, M, MacMahon, M, MacNaughton, E, Mankregod, R, Masson, H, Matovu, E, McCullough, K, McEwen, R, Meda, M, Mills, G, Minton, J, Mirfenderesky, M, Mohandas, K, Mok, Q, Moon, J, Moore, E, Morgan, P, Morris, C, Mortimore, K, Moses, S, Mpenge, M, Mulla, R, Murphy, M, Nagel, M, Nagarajan, T, Nelson, M, Norris, L, O'Shea, MK, Otahal, I, Ostermann, M, Pais, M, Panchatsharam, S, Papakonstantinou, D, Paraiso, H, Patel, B, Pattison, N, Pepperell, J, Peters, M, Phull, M, Pintus, S, Singh Pooni, J, Planche, T, Post, F, Price, D, Prout, R, Rae, N, Reschreiter, H, Reynolds, T, Richardson, N, Roberts, M, Roberts, D, Rose, A, Rousseau, G, Ruge, B, Ryan, B, Saluja, T, Schmid, ML, Shah, A, Shanmuga, P, Sharma, A, Shawcross, A, Sizer, J, Shankar-Hari, M, Smith, R, Snelson, C, Spittle, N, Staines, N, Stambach, T, Stewart, R, Subudhi, P, Szakmany, T, Tatham, K, Thompson, C, Thompson, R, Tridente, A, Tupper-Carey, D, Twagira, M, Vallotton, N, Vancheeswaran, R, Vincent-Smith, L, Visuvanathan, S, Vuylsteke, A, Waddy, S, Wake, R, Walden, A, Welters, I, Whitehouse, T, Whittaker, P, Whittington, A, Papineni, P, Wijesinghe, M, Williams, M, Wilson, L, Winchester, S, Wiselka, M, Wolverson, A, Wootton, DG, Workman, A, Yates, B, Young, P
Publikováno v:
2021, ' A prenylated dsRNA sensor protects against severe COVID-19 ', Science (New York, N.Y.) . https://doi.org/10.1126/science.abj3624
Investigators, ISARICC & Dark, P 2021, ' A prenylated dsRNA sensor protects against severe COVID-19 ', Science (New York, N.Y.), vol. 374, no. 6567, eabj3624 . https://doi.org/10.1126/science.abj3624
Science
Science, American Association for the Advancement of Science, 2021, 374 (6567), pp.eabj3624. ⟨10.1126/science.abj3624⟩
Investigators, ISARICC & Dark, P 2021, ' A prenylated dsRNA sensor protects against severe COVID-19 ', Science (New York, N.Y.), vol. 374, no. 6567, eabj3624 . https://doi.org/10.1126/science.abj3624
Science
Science, American Association for the Advancement of Science, 2021, 374 (6567), pp.eabj3624. ⟨10.1126/science.abj3624⟩
International audience; INTRODUCTIONInterferons (IFNs) are cytokines that are rapidly deployed in response to invading pathogens. By initiating a signaling cascade that stimulates the expression of hundreds of genes, IFNs create an antiviral state in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d185dac789dae326bac2a1eff3e76148
https://www.pure.ed.ac.uk/ws/files/235518845/science.abj3624.pdf
https://www.pure.ed.ac.uk/ws/files/235518845/science.abj3624.pdf
Autor:
Arisa Higa, Raphael Pineau, Michael Hallett, Stéphanie Lhomond, Olivier Pluquet, Marion Bouchecareilh, Anne Vital, Sandrine Loriot, Gaelle Cubel, Jann N. Sarkaria, Maylis Delugin, Hugues Loiseau, Wenting Wu, Nicolas Dejeans, Keith Anderson, Sara J. C. Gosline, Frédéric Saltel, Martin E. Fernandez-Zapico, Fausto J. Rodriguez, C. Combe, Jean Rosenbaum, Eric Chevet, Nathalie Dugot-Senant, Saïd Taouji
Publikováno v:
Cancer Research
Cancer Research, American Association for Cancer Research, 2013, 73 (15), pp.4732-4743. ⟨10.1158/0008-5472.CAN-12-3989⟩
Cancer Research, 2013, 73 (15), pp.4732-4743. ⟨10.1158/0008-5472.CAN-12-3989⟩
Cancer Research, American Association for Cancer Research, 2013, 73 (15), pp.4732-4743. ⟨10.1158/0008-5472.CAN-12-3989⟩
Cancer Research, 2013, 73 (15), pp.4732-4743. ⟨10.1158/0008-5472.CAN-12-3989⟩
Growing evidence supports a role for the unfolded protein response (UPR) in carcinogenesis; however, the precise molecular mechanisms underlying this phenomenon remain elusive. Herein, we identified the circadian clock PER1 mRNA as a novel substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bfc10e690b81b99ff91f9bf2ddd7579
https://hal.archives-ouvertes.fr/hal-02400356
https://hal.archives-ouvertes.fr/hal-02400356
Autor:
Damien Rondet, Livia Merendino, Thomas Pfannschmidt, Silva Lerbs-Mache, Mustafa Malik Ghulam, Fabien Chevalier
Publikováno v:
Plant Molecular Biology Reporter
Plant Molecular Biology Reporter, Springer Verlag, 2015, 88 (4-5), pp.357-67. ⟨10.1007/s11103-015-0325-y⟩
Plant Molecular Biology Reporter, Springer Verlag, 2015, 88 (4-5), pp.357-67
Plant Molecular Biology Reporter, 2015, 88 (4-5), pp.357-67. ⟨10.1007/s11103-015-0325-y⟩
Plant Molecular Biology Reporter, Springer Verlag, 2015, 88 (4-5), pp.357-67. ⟨10.1007/s11103-015-0325-y⟩
Plant Molecular Biology Reporter, Springer Verlag, 2015, 88 (4-5), pp.357-67
Plant Molecular Biology Reporter, 2015, 88 (4-5), pp.357-67. ⟨10.1007/s11103-015-0325-y⟩
International audience; The plastid psbB operon harbours 5 genes, psbB, psbT, psbH, petB and petD. A sixth gene, the psbN gene, is located on the opposite DNA strand in the psbT/psbH intergenic region. Its transcription produces antisense RNA to a la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46704a351495bb6fdab72df76210ea3f
https://hal.archives-ouvertes.fr/hal-01166959
https://hal.archives-ouvertes.fr/hal-01166959
Autor:
Meyer Elbaz, Cécile Vindis, Mary E. Reyland, Anne Nègre-Salvayre, Robert Salvayre, Cécile Ingueneau, Audrey Swiader, P Larroque-Cardoso
Publikováno v:
Cell Death & Disease
Cell Death and Disease
Cell Death and Disease, Nature Publishing Group, 2013, 4 (2), pp.e520-e520. ⟨10.1038/cddis.2013.47⟩
Cell Death Dis
Cell Death Dis, 2013, 4, pp.e520. ⟨10.1038/cddis.2013.47⟩
Cell Death and Disease
Cell Death and Disease, Nature Publishing Group, 2013, 4 (2), pp.e520-e520. ⟨10.1038/cddis.2013.47⟩
Cell Death Dis
Cell Death Dis, 2013, 4, pp.e520. ⟨10.1038/cddis.2013.47⟩
International audience; During atherogenesis, excess amounts of low-density lipoproteins (LDL) accumulate in the subendothelial space where they undergo oxidative modifications. Oxidized LDL (oxLDL) alter the fragile balance between survival and deat
Autor:
Dejeans, N., Pluquet, O., Lhomond, S., Grise, F., Bouchecareilh, M., Juin, A., Meynard-Cadars, M., Bidaud-Meynard, A., Gentil, C., Moreau, V., Saltel, F., Chevet, E.
Publikováno v:
Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2012, 125 (18), pp.4278-4287. ⟨10.1242/jcs.099291⟩
Journal of Cell Science, Company of Biologists, 2012, 125 (18), pp.4278-4287. ⟨10.1242/jcs.099291⟩
International audience; The endoplasmic reticulum (ER) is an organelle specialized for the folding and assembly of secretory and transmembrane proteins. ER homeostasis is often perturbed in tumor cells because of dramatic changes in the microenvironm
Publikováno v:
ChemMedChem
ChemMedChem, Wiley-VCH Verlag, 2011, 6 (10), pp.1797-805. ⟨10.1002/cmdc.201100281⟩
ChemMedChem, 2011, 6 (10), pp.1797-805. ⟨10.1002/cmdc.201100281⟩
6 (2011): 1797–1805. doi:10.1002/cmdc.201100281
info:cnr-pdr/source/autori:Ragno R, Gioia U, Laneve P, Bozzoni I, Mai A, Caffarelli E./titolo:Identification of Small-Molecule Inhibitors of the XendoU Endoribonucleases Family/doi:10.1002%2Fcmdc.201100281/rivista:ChemMedChem (Print)/anno:2011/pagina_da:1797/pagina_a:1805/intervallo_pagine:1797–1805/volume:6
Chemmedchem
ChemMedChem, Wiley-VCH Verlag, 2011, 6 (10), pp.1797-805. ⟨10.1002/cmdc.201100281⟩
ChemMedChem, 2011, 6 (10), pp.1797-805. ⟨10.1002/cmdc.201100281⟩
6 (2011): 1797–1805. doi:10.1002/cmdc.201100281
info:cnr-pdr/source/autori:Ragno R, Gioia U, Laneve P, Bozzoni I, Mai A, Caffarelli E./titolo:Identification of Small-Molecule Inhibitors of the XendoU Endoribonucleases Family/doi:10.1002%2Fcmdc.201100281/rivista:ChemMedChem (Print)/anno:2011/pagina_da:1797/pagina_a:1805/intervallo_pagine:1797–1805/volume:6
Chemmedchem
The XendoU family of enzymes includes several proteins displaying high sequence homology. The members characterized so far are endoribonucleases sharing similar biochemical properties and a common architecture in their active sites. Despite their sim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e661b3a8e0aedde65af355aa69925b8
http://hdl.handle.net/11573/418879
http://hdl.handle.net/11573/418879
Autor:
Stéphan Hardivillé, Annick Pierce, Christophe Mariller, Esthelle Hoedt, Monique Benaïssa, Joël Mazurier
Publikováno v:
Biochimie
Biochimie, Elsevier, 2009, 91 (1), pp.109-22. ⟨10.1016/j.biochi.2008.07.009⟩
Biochimie, 2009, 91 (1), pp.109-22. ⟨10.1016/j.biochi.2008.07.009⟩
Biochimie, Elsevier, 2009, 91 (1), pp.109-22. ⟨10.1016/j.biochi.2008.07.009⟩
Biochimie, 2009, 91 (1), pp.109-22. ⟨10.1016/j.biochi.2008.07.009⟩
International audience; The expression of the transcription factor DeltaLf is deregulated in cancer cells. Its overexpression provokes cell cycle arrest along with antiproliferative effects and we recently showed that the Skp1 gene promoter was a tar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fb1acb0280df33ddf1f3cc553101aa2
https://hal.archives-ouvertes.fr/hal-00348813
https://hal.archives-ouvertes.fr/hal-00348813
Autor:
Marilena D. Papaioannou, Wei Yan, Bernard Jégou, Françoise Kühne, Jean-Luc Pitetti, Evgeny M. Zdobnov, Michael T. McManus, Olivier Schaad, Florence Aubry, Serge Nef, Patrick Descombes, Seungil Ro, Brian D. Harfe, Florian Guillou, Chanjae Park, Charles E. Vejnar
Publikováno v:
Developmental biology, Vol. 326, No 1 (2009) pp. 250-9
Developmental Biology
Developmental Biology, Elsevier, 2009, 326 (1), pp.250-9. ⟨10.1016/j.ydbio.2008.11.011⟩
Developmental Biology, 2009, 326 (1), pp.250-9. ⟨10.1016/j.ydbio.2008.11.011⟩
Developmental biology
Developmental Biology
Developmental Biology, Elsevier, 2009, 326 (1), pp.250-9. ⟨10.1016/j.ydbio.2008.11.011⟩
Developmental Biology, 2009, 326 (1), pp.250-9. ⟨10.1016/j.ydbio.2008.11.011⟩
Developmental biology
International audience; Spermatogenesis requires intact, fully competent Sertoli cells. Here, we investigate the functions of Dicer, an RNaseIII endonuclease required for microRNA and small interfering RNA biogenesis, in mouse Sertoli cell function.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6efa06a66540bf7953dcc7b5c44a391b
https://archive-ouverte.unige.ch/unige:1297
https://archive-ouverte.unige.ch/unige:1297
Publikováno v:
Nature
Nature, Nature Publishing Group, 2008, 456 (7224), pp.993-6. ⟨10.1038/nature07480⟩
Nature, 2008, 456 (7224), pp.993-6. ⟨10.1038/nature07480⟩
Nature 7224 (456), 993-996. (2008)
Nature, Nature Publishing Group, 2008, 456 (7224), pp.993-6. ⟨10.1038/nature07480⟩
Nature, 2008, 456 (7224), pp.993-6. ⟨10.1038/nature07480⟩
Nature 7224 (456), 993-996. (2008)
International audience; The exosome is a major eukaryotic nuclease located in both the nucleus and the cytoplasm that contributes to the processing, quality control and/or turnover of a large number of cellular RNAs. This large macromolecular assembl
Publikováno v:
Trends in Biochemical Sciences
Trends in Biochemical Sciences, Elsevier, 2006, 31 (5), pp.241-3. ⟨10.1016/j.tibs.2006.03.001⟩
Trends in Biochemical Sciences, Elsevier, 2006, 31 (5), pp.241-3. ⟨10.1016/j.tibs.2006.03.001⟩
mRNA decapping irreversibly targets mRNAs for fast decay. Cap removal is catalyzed by decapping protein Dcp2 but also requires Dcp1. Recently, two groups have provided a first glimpse of the regulation mechanism of this crucial step in gene expressio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0ad4eb646c99ab9db53295ddcedafb8
https://hal.archives-ouvertes.fr/hal-00133099
https://hal.archives-ouvertes.fr/hal-00133099