Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

Autor: Aldo R. Camacho-Zarco, Sissy Kalayil, Damien Maurin, Nicola Salvi, Elise Delaforge, Sigrid Milles, Malene Ringkjøbing Jensen, Darren J. Hart, Stephen Cusack, Martin Blackledge

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)

Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or

Externí odkaz: https://doaj.org/article/f3b9b8f89aab4c209ce56f87f7cfa567

Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA

Autor: Evgenij Fiskin, Sagar Bhogaraju, Lina Herhaus, Sissy Kalayil, Marcel Hahn, Ivan Dikic

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)

The HECT-like E3 ligase SopA inSalmonellahas been suggested to activate host RING ligases TRIM56 and TRIM65. Here, the authors use mass spectrometry, crystal structures and biochemistry to examine the interactions between these proteins in detail.

Externí odkaz: https://doaj.org/article/78042980b2f648278c555491f0992e50

Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

Autor: Elise Delaforge, Damien Maurin, Sigrid Milles, Nicola Salvi, Martin Blackledge, Stephen Cusack, Darren J. Hart, Malene Ringkjøbing Jensen, Aldo Camacho Zarco, Sissy Kalayil

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), ⟨10.1038/s41467-020-17407-x⟩
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3656. ⟨10.1038/s41467-020-17407-x⟩
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications, 2020, 11 (1), pp.3656. ⟨10.1038/s41467-020-17407-x⟩

Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Adaptive mutants are localised on the C-terminal (627-NLS) domains of the PB2 subunit. In particular, mutation of PB2 residue 627 from E to K rescu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce095ca25613cf9567243b52a9f08146
https://hal.archives-ouvertes.fr/hal-03079958

SPRTN is a mammalian DNA-binding metalloprotease that resolves DNA-protein crosslinks

Autor: Janoš Terzić, Karthik Maddi, Stefan Prgomet, Ivan Dikic, Sissy Kalayil, Ivana Marinović-Terzić, Jaime Lopez-Mosqueda

Publikováno v: eLife, Vol 5 (2016)
eLife

Ruijs-Aalfs syndrome is a segmental progeroid syndrome resulting from mutations in the SPRTN gene. Cells derived from patients with SPRTN mutations elicit genomic instability and people afflicted with this syndrome developed hepatocellular carcinoma.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ccdef4ff64056bba2d44c20dd7a740e
http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/42158

Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination

Autor: Sagar Bhogaraju, Florian Bonn, Ivan Matic, Ivan Dikic, Thomas Colby, Yaobin Liu, Sissy Kalayil

Publikováno v: Cell

Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a01e45af53791df1fa66fb060ff8c58
https://hdl.handle.net/21.11116/0000-000B-B37B-1