Zobrazeno 1 - 10
of 33
pro vyhledávání: '"S Kundhavai, Natchiar"'
Autor:
F. Aaron Cruz-Navarrete, Wezley C. Griffin, Yuk-Cheung Chan, Maxwell I. Martin, Jose L. Alejo, Ryan A. Brady, S. Kundhavai Natchiar, Isaac J. Knudson, Roger B. Altman, Alanna Schepartz, Scott J. Miller, Scott C. Blanchard
Publikováno v:
ACS Central Science, Vol 10, Iss 6, Pp 1262-1275 (2024)
Externí odkaz:
https://doaj.org/article/ba1dc3cf6463484dbb80acadc7def01d
Autor:
Mikael Holm, S. Kundhavai Natchiar, Emily J. Rundlet, Alexander G. Myasnikov, Zoe L. Watson, Roger B. Altman, Hao-Yuan Wang, Jack Taunton, Scott C. Blanchard
Publikováno v:
Nature. 617:200-207
In all species, ribosomes synthesize proteins by faithfully decoding messenger RNA (mRNA) nucleotide sequences using aminoacyl-tRNA substrates. Current knowledge of the decoding mechanism derives principally from studies on bacterial systems1. Althou
Autor:
Varun Bhaskar, Alexandra Graff-Meyer, Andreas D. Schenk, Simone Cavadini, Ottilie von Loeffelholz, S. Kundhavai Natchiar, Caroline G. Artus-Revel, Hans-Rudolf Hotz, Gabriel Bretones, Bruno P. Klaholz, Jeffrey A. Chao
Publikováno v:
Cell Reports, Vol 31, Iss 1, Pp - (2020)
Summary: Ribosomes undergo multiple conformational transitions during translation elongation. Here, we report the high-resolution cryoelectron microscopy (cryo-EM) structure of the human 80S ribosome in the post-decoding pre-translocation state (clas
Externí odkaz:
https://doaj.org/article/ab271bc4b7cf423480279f3743614470
Autor:
Alexander G. Myasnikov, S. Kundhavai Natchiar, Marielle Nebout, Isabelle Hazemann, Véronique Imbert, Heena Khatter, Jean-François Peyron, Bruno P. Klaholz
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
The ribosome of bacteria and other unicellular pathogens is a common target for antibiotic drugs. Here the authors determine a structure of the human ribosome bound to the translation inhibitor cycloheximide, and provide evidence that targeting the r
Externí odkaz:
https://doaj.org/article/5c015c0b3ce04e609d082a4c3d51b4f2
Autor:
Franck Martin, Jean-François Ménétret, Angelita Simonetti, Alexander G. Myasnikov, Quentin Vicens, Lydia Prongidi-Fix, S. Kundhavai Natchiar, Bruno P. Klaholz, Gilbert Eriani
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-7 (2016)
Prokaryotic translation initiation involves mRNA-ribosomal RNA base pairing interactions. Here, the authors provide evidence for a similar base pairing interactions occurring between the human h4 mRNA and helix 16 of the small subunit rRNA to positio
Externí odkaz:
https://doaj.org/article/13bf703b19f34a32b972880d5c0ed24e
Publikováno v:
Biomolecules, Vol 8, Iss 4, p 125 (2018)
Chemical modifications of RNA have recently gained new attention in biological sciences. They occur notably on messenger RNA (mRNA) and ribosomal RNA (rRNA) and are important for various cellular functions, but their molecular mechanism of action is
Externí odkaz:
https://doaj.org/article/24e8706a4f684455bf1ea7b76cc377e1
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
Cryo-EM can produce maps with resolutions that are sufficiently high that fine structural details can be discerned. Using calculated electrostatic potential maps, it is shown that it is possible to identify Mg2+ ions bound to nucleotide bases at whic
Autor:
Glen R. Nemerow, Tina-Marie Mullen, Sangita Venkataraman, Vijay S. Reddy, S. Kundhavai Natchiar
Publikováno v:
Journal of Molecular Biology. 430:4132-4141
We report the revised crystal structure of a pseudo-typed human adenovirus at 3.8-Å resolution that is consistent with the atomic models of minor proteins determined by cryo-electron microscopy. The diffraction data from multiple crystals were resca
Autor:
Hanna Kratzat, Jean-François Ménétret, Ottilie von Loeffelholz, S. Kundhavai Natchiar, Alexander G. Myasnikov, Isabelle Hazemann, Bruno P. Klaholz, Nadia Djabeur
Publikováno v:
Current Opinion in Structural Biology
Current Opinion in Structural Biology, Elsevier, 2017, 46 (9), pp.140-148. ⟨10.1016/j.sbi.2017.07.007⟩
Current Opinion in Structural Biology, 2017, 46 (9), pp.140-148. ⟨10.1016/j.sbi.2017.07.007⟩
Current Opinion in Structural Biology, Elsevier, 2017, 46 (9), pp.140-148. ⟨10.1016/j.sbi.2017.07.007⟩
Current Opinion in Structural Biology, 2017, 46 (9), pp.140-148. ⟨10.1016/j.sbi.2017.07.007⟩
International audience; Cryo electron microscopy (cryo-EM) historically has had a strong impact on the structural and mechanistic analysis of protein synthesis by the prokaryotic and eukaryotic ribosomes. Vice versa, studying ribosomes has helped mov
Autor:
Karima Tazibt, Lorenza di Pompeo, Kareem Mohideen, Alexander G. Myasnikov, Morgan Torchy, Igor Orlov, Heena Khatter, Jean-François Ménétret, Finaritra Raivoniaina, S. Kundhavai Natchiar, Leonid Andronov, Isabelle M. L. Billas, Hanna Kratzat, Rachel Tabaroni, Alexandre Urzhumtsev, Tatiana Bruxelles, Bruno P. Klaholz, Brice Beinsteiner, Nadia Djabeur, Isabelle Hazemann
Publikováno v:
Biology of the Cell. 109:81-93
After gradually moving away from preparation methods prone to artefacts such as plastic embedding and negative staining for cell sections and single particles, the field of cryo electron microscopy (cryo-EM) is now heading off at unprecedented speed