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Exosome and ribosome coupling

CORDIS provides links to public deliverables and publications of HORIZON projects.

Links to deliverables and publications from FP7 projects, as well as links to some specific result types such as dataset and software, are dynamically retrieved from OpenAIRE .

Publications

The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs (opens in new window)

Author(s): Mahesh Lingaraju, Dennis Johnsen, Andreas Schlundt, Lukas M. Langer, Jérôme Basquin, Michael Sattler, Torben Heick Jensen, Sebastian Falk, Elena Conti
Published in: Nature Communications, Issue 10/1, 2019, Page(s) 3393, ISSN 2041-1723
Publisher: Nature Publishing Group
DOI: 10.1038/s41467-019-11339-x

The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism. (opens in new window)

Author(s): Alexander Kögel, Achim Keidel, Fabien Bonneau, Ingmar B. Schäfer, and Elena Conti.
Published in: Molecular Cell, Issue 82(4), 2022, Page(s) 756-769.e8, ISSN 1097-2765
Publisher: Cell Press
DOI: 10.1016/j.molcel.2022.01.009

Reconstitution of 3′ end processing of mammalian pre-mRNA reveals a central role of RBBP6. (opens in new window)

Author(s): Moritz Schmidt, Florian Kluge, Felix Sandmeir, Uwe Kühn, Peter Schäfer, Christian Tüting, Christian Ihling, Elena Conti, and Elmar Wahle.
Published in: Genes and Development, Issue 36, 2022, Page(s) 195-209, ISSN 0890-9369
Publisher: Cold Spring Harbor Laboratory Press
DOI: 10.1101/gad.349217.121

Distinct and evolutionary conserved structural features of the human nuclear exosome complex (opens in new window)

Author(s): Piotr Gerlach, Jan M Schuller, Fabien Bonneau, Jérôme Basquin, Peter Reichelt, Sebastian Falk, Elena Conti
Published in: eLife, Issue 7, 2018, ISSN 2050-084X
Publisher: eLife Sciences Publications
DOI: 10.7554/elife.38686

Structure of the nuclear exosome captured on a maturing preribosome (opens in new window)

Author(s): Jan Michael Schuller, Sebastian Falk, Lisa Fromm, Ed Hurt, Elena Conti
Published in: Science, Issue 360/6385, 2018, Page(s) 219-222, ISSN 0036-8075
Publisher: American Association for the Advancement of Science
DOI: 10.1126/science.aar5428

Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase (opens in new window)

Author(s): Ingmar B. Schäfer, Masami Yamashita, Jan Michael Schuller, Steffen Schüssler, Peter Reichelt, Mike Strauss, Elena Conti
Published in: Cell, Issue 177/6, 2019, Page(s) 1619-1631.e21, ISSN 0092-8674
Publisher: Cell Press
DOI: 10.1016/j.cell.2019.04.013

Structure and regulation of the Nuclear Exosome Targeting Complex guide RNA substrates to the exosome. (opens in new window)

Author(s): Gerlach P., Garland W., Lingaraju M., Salerno-Kochan A., Bonneau F., Basquin J., Jensen T.H. and Conti E. (2022).
Published in: Molecular Cell, Issue 82/13, 2022, Page(s) 2505-2518.e7, ISSN 1097-2765
Publisher: Cell Press
DOI: 10.1016/j.molcel.2022.04.011

Structure of substrate-bound SMG1-8-9 kinase complex reveals molecular basis for phosphorylation specificity (opens in new window)

Author(s): Lukas M Langer, Yair Gat, Fabien Bonneau, Elena Conti
Published in: eLife, Issue 9, 2020, Page(s) 57127, ISSN 2050-084X
Publisher: eLife Sciences Publications
DOI: 10.7554/elife.57127

Cryo-EM reconstructions of inhibitor-bound SMG1 kinase reveal an autoinhibitory state dependent on SMG8. (opens in new window)

Author(s): Lukas M. Langer, Fabien Bonneau, Yair Gat, and Elena Conti
Published in: eLife, Issue 10, 2021, Page(s) e72353, ISSN 2050-084X
Publisher: eLife Sciences Publications
DOI: 10.7554/elife.72353

To Process or to Decay: A Mechanistic View of the Nuclear RNA Exosome (opens in new window)

Author(s): Mahesh Lingaraju, Jan M. Schuller, Sebastian Falk, Piotr Gerlach, Fabien Bonneau, Jérôme Basquin, Christian Benda, Elena Conti
Published in: Cold Spring Harbor Symposia on Quantitative Biology, Issue 84, 2019, Page(s) 155-163, ISSN 0091-7451
Publisher: Cold Spring Harbor Laboratory Press
DOI: 10.1101/sqb.2019.84.040295

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