M
Maarit Hellman
Researcher at University of Jyväskylä
Publications - 43
Citations - 1076
Maarit Hellman is an academic researcher from University of Jyväskylä. The author has contributed to research in topics: Intrinsically disordered proteins & Transcription factor. The author has an hindex of 16, co-authored 42 publications receiving 915 citations. Previous affiliations of Maarit Hellman include University of Helsinki.
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Journal ArticleDOI
Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) Has a Unique Mechanism to Rescue Apoptotic Neurons
Maarit Hellman,Urmas Arumäe,Li-Ying Yu,Päivi Lindholm,Johan Peränen,Mart Saarma,Perttu Permi +6 more
TL;DR: A three-dimensional solution structure of human MANF is shown that differs drastically from other neurotrophic factors and confirms that MANF and C-MANF protect neurons intracellularly as efficiently as Ku70.
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Arabidopsis RCD1 coordinates chloroplast and mitochondrial functions through interaction with ANAC transcription factors
Alexey Shapiguzov,Alexey Shapiguzov,Julia P. Vainonen,Kerri Hunter,Helena Tossavainen,Helena Tossavainen,Arjun Tiwari,Sari Järvi,Maarit Hellman,Fayezeh Aarabi,Saleh Alseekh,Brecht Wybouw,Katrien Van Der Kelen,Lauri Nikkanen,Julia Krasensky-Wrzaczek,Nina Sipari,Markku Keinänen,Esa Tyystjärvi,Eevi Rintamäki,Bert De Rybel,Jarkko Salojärvi,Frank Van Breusegem,Alisdair R. Fernie,Mikael Brosché,Mikael Brosché,Perttu Permi,Perttu Permi,Eva-Mari Aro,Michael Wrzaczek,Jaakko Kangasjärvi +29 more
TL;DR: RCD1 integrates organellar signaling from chloroplasts and mitochondria to establish transcriptional control over the metabolic processes in both organelles, and is linked to chloroplast signaling by 3-phosphoadenosine 5'-phosphate (PAP).
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Effect of protein structure on laccase-catalyzed protein oligomerization.
Maija-Liisa Mattinen,Maarit Hellman,Perttu Permi,Karin Autio,Nisse Kalkkinen,Johanna Buchert +5 more
TL;DR: Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system and the reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates.
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Structural basis and evolutionary origin of actin filament capping by twinfilin
Ville O. Paavilainen,Maarit Hellman,Emmanuèle Helfer,Miia Bovellan,Arto Annila,Marie-France Carlier,Perttu Permi,Pekka Lappalainen +7 more
TL;DR: The domain requirement for actin filament capping by twinfilin is remarkably similar to that of gelsolin family proteins, suggesting the existence of a general barbed-end capping mechanism.
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Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly
Olli Aitio,Maarit Hellman,Arunas Kazlauskas,Didier F. Vingadassalom,John M. Leong,Kalle Saksela,Perttu Permi +6 more
TL;DR: The NMR structure of insulin receptor tyrosine kinase substrate (IRTKS) SH3 domain in complex with a repeat from Escherichia coli-secreted protein F-like protein encoded on prophage U (EspFU), a translocated effector of enterohemorrhagic E. coli that commandeers the mammalian actin assembly machinery is determined.