Výsledky vyhledávání - "Ribosomal Proteins/*metabolism"

Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome

Autor: Gary Loughran, Jeffrey W. Bode, Pramod R. Bhatt, Kate M. O’Connor, David Gatfield, Annika Kratzel, Volker Thiel, Nenad Ban, John F. Atkins, René Dreos, Marc Leibundgut, Romane Meurs, Alain Scaiola, Angus McMillan

Publikováno v: Science (New York, N.y.)
Science, vol. 372, no. 6548, pp. 1306-1313

Shifting frames to make more proteins Severe acute respiratory syndrome coronavirus 2 critically depends on the ribosomal frameshifting that occurs between two large open reading frames in its genomic RNA for expression of viral replicase. Programmed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b048a2925451cc1fd784af0742d4b762

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The in vivo endothelial cell translatome is highly heterogeneous across vascular beds

Autor: Martijn A. van der Ent, Grietje Molema, David Ginsburg, Kristina L. Hunker, William C. Aird, Audrey C. A. Cleuren, Santhi K. Ganesh, Hui Jiang, Andrew Yee, David R. Siemieniak

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 116(47), 23618-23624. NATL ACAD SCIENCES
Proc Natl Acad Sci U S A

Endothelial cells (ECs) are highly specialized across vascular beds. However, given their interspersed anatomic distribution, comprehensive characterization of the molecular basis for this heterogeneity in vivo has been limited. By applying endotheli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3844edf4e9540fe28c17ded36731085
https://doi.org/10.1101/708701

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New substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approach

Autor: Roland Brosch, María Noel Alvarez, Mariana Piuri, Alessandro Cascioferro, Analía Lima, Rosario Durán, Paulo C. Carvalho, Estefanía Urdániz, María-Natalia Lisa, Ana Denicola, Marco Bellinzoni, Otto Pritsch, Federico Carrion, Magdalena Gil, Annemarie Wehenkel, Pedro M. Alzari, Carlos Batthyány, Bernardina Rivera, Jessica Rossello

Publikováno v: Journal of Proteomics
Journal of Proteomics, Elsevier, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
Journal of Proteomics, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩

International audience; PknG from Mycobacterium tuberculosis is a multidomain Serine/Threonine protein kinase that regulates bacterial metabolism as well as the pathogen's ability to survive inside the host by still uncertain mechanisms. To uncover P

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48d6e591b08630f1c8a11067058c5008
https://hal-pasteur.archives-ouvertes.fr/pasteur-02046106

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Influenza A Virus Induces Autophagosomal Targeting of Ribosomal Proteins

Autor: Jörn Dengjel, Verónica I. Dumit, Lea Bühler, Carole Roubaty, Martin Schwemmle, Shadi Abou-Eid, Christine Gretzmeier, Monique Gannagé, Zehan Hu, Stéphanie Kaeser-Pebernard, Andrea C. Becker, Christian Münz, Sebastian Giese, Petra Paul

Publikováno v: Mol Cell Proteomics, vol. 17, no. 10, pp. 1909-1921
Molecular & Cellular Proteomics : MCP

Seasonal epidemics of influenza A virus are a major cause of severe illness and are of high socio-economic relevance. For the design of effective antiviral therapies, a detailed knowledge of pathways perturbed by virus infection is critical. We perfo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9b836ddff6ce1f7f577757ebf89952c
https://www.zora.uzh.ch/id/eprint/165546/

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Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site

Autor: Kam-Bo Wong, Yuen Ting Wong, Pang-Chui Shaw, Shannon Wing-Ngor Au, Young Jun An, Kong-Hung Sze, Amanda Nga-Sze Mak, Sun-Shin Cha

Publikováno v: Nucleic Acids Research

Maize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form. As the first structu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5155cc9cccfc098c3f48ee176fbe377e
http://europepmc.org/articles/PMC2094058

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The de novo synthesis of ubiquitin: Identification of deubiquitinases acting on ubiquitin precursors

Autor: Jorge E. Azevedo, Manuel P. Pinto, Cláudia P. Grou, Andreia V. Mendes, Pedro Domingues

Publikováno v: Scientific Reports
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP

Protein ubiquitination, a major post-translational modification in eukaryotes, requires an adequate pool of free ubiquitin. Cells maintain this pool by two pathways, both involving deubiquitinases (DUBs): recycling of ubiquitin from ubiquitin conjuga

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e88c7208f50f47172e6fd0e46a582ae1
https://repositorio-aberto.up.pt/handle/10216/117908

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ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis

Autor: Régis Dieckmann, Jean-Charles Sanchez, Laurent Bezin, Jean-Jacques Diaz, Karine Kindbeiter, Laurent Duret, Yohann Couté, Stephane Belin

Publikováno v: Molecular and Cellular Proteomics, Vol. 7, No 3 (2008) pp. 546-559
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2007, epub ahead of print. ⟨10.1074/mcp.M700510-MCP200⟩
Molecular and Cellular Proteomics, 2008, 7, epub ahead of print. ⟨10.1074/mcp.M700510-MCP200⟩
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2008, 7, pp.546-559

International audience; Proteomic analyses of human nucleoli provided molecular bases for an understanding of the multiple functions fulfilled by these nuclear domains. However, the biological roles of about 100 of the identified proteins are unpredi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0a71e81b3f41eb6223d8c167c4ffb07
https://archive-ouverte.unige.ch/unige:795

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Herpes simplex virus type-1-induced stimulation of ribosomal protein S6 phosphorylation is inhibited in neomycin-treated human epidermoid carcinoma 2 cells and in ras-transformed cells

Autor: Thierry Massé, Bernard Jacquemont, Dominique Garcin, Jean-Jacques Madjar

Publikováno v: European Journal of Biochemistry, Vol. 194, No 1 (1990) pp. 287-91

Neomycin, an inhibitor of inositol phospholipid turnover, prevents Herpes-simplex-virus-type-1 (HSV-1)-induced stimulation of ribosomal protein S6 phosphorylation, but does not impair the S6 phosphorylation induced by serum. Long-term treatment with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be423b1285c57cd2f9944750d6fd103c
https://pubmed.ncbi.nlm.nih.gov/2174778

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RNA-protein interactions in the ribosome. Binding of proteins L1, L3, L6, L13 and L23 to specific fragments of the 23S RNA

Autor: Pierre Spierer, Robert A. Zimmermann

Publikováno v: FEBS Letters, Vol. 68, No 1 (1976) pp. 71-5

Ten of the 33 proteins found in the 50 S subunit of the Escherichia coli ribosome associate independently and specifically to the 23 S ribosomal RNA [l]. The location of the binding sites for these proteins has been studied in two different ways. Bra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b562e748f1aa99043af1f5335a259a82
https://doi.org/10.1016/0014-5793(76)80407-3

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RNA-protein interactions in the ribosome. Binding of 50-S-subunit proteins to 5' and 3' terminal segments of the 23-S RNA

Autor: Robert A. Zimmermann, George A. Mackie, Pierre Spierer

Publikováno v: European Journal of Biochemistry, Vol. 52, No 3 (1975) pp. 459-68

Limited digestion of the Escherichia coli 50-S subunit permits the isolation of two large fragments of the 23-S RNA. One arises from the 5' end of the 23-S RNA and contains about 1200 nucleotides. The other arises from the 3' end of the 23-S RNA and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52b20bb5188a08efdc996e8b7920b42a
https://pubmed.ncbi.nlm.nih.gov/800986

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