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Journal of structural biology, 2024

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bioRxiv, 2024

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Nature structural & molecular biology, 2023

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Hibernating ribosomes tether to mitochondria as an adaptive response to cellular stress during glucose depletion.

Gemin O, Gluc M, Purdy M, Rosa H, Niemann M, Peskova Y, Mattei S, Jomaa A

bioRxiv, 2023

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Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style.

Pfister S, Rabl J, Wiegand T, Mattei S, Malär AA, Lecoq L, Seitz S, Bartenschlager R, Böckmann A, Nassal M, Boehringer D, Meier BH

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Science advances, 2022

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Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.

Lee JH, Jomaa A, Chung SY, Fu YHH, Qian RL, Sun XM, Hsieh HH, Chandrasekar S, Bo XT, Mattei S, Boehringer D, Weiss S, Ban N, Shan SO

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Strategies for optimization of cryogenic electron tomography data acquisition.

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Cone-shaped HIV-1 capsids are transported through intact nuclear pores.

Zila V, Margiotta E, Turoňová B, Müller TG, Zimmerli CE, Mattei S, Allegretti M, Börner K, Rada J, Müller B, Lusic M, Kräusslich HG, Beck M

Cell, 2021

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Nature communications, 2020

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Structural insights into the mechanism of mitoribosomal large subunit biogenesis.

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Molecular cell, 2020

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Mitoribosomal small subunit biogenesis in trypanosomes involves an extensive assembly machinery.

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High-resolution structures of HIV-1 Gag cleavage mutants determine structural switch for virus maturation.

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Deciphering the Origin and Evolution of Hepatitis B Viruses by Means of a Family of Non-enveloped Fish Viruses.

Lauber C, Seitz S, Mattei S, Suh A, Beck J, Herstein J, Börold J, Salzburger W, Kaderali L, Briggs JAG, Bartenschlager R

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eIF6 over-expression increases the motility and invasiveness of cancer cells by modulating the expression of a critical subset of membrane-bound proteins.

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Spike-in SILAC proteomic approach reveals the vitronectin as an early molecular signature of liver fibrosis in hepatitis C infections with hepatic iron overload.

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