A
Arunas Kazlauskas
Researcher at Lithuanian University of Health Sciences
Publications - 18
Citations - 689
Arunas Kazlauskas is an academic researcher from Lithuanian University of Health Sciences. The author has contributed to research in topics: Glioma & Astrocytoma. The author has an hindex of 10, co-authored 18 publications receiving 611 citations. Previous affiliations of Arunas Kazlauskas include University of Helsinki & Helsinki University Central Hospital.
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SH3 Domain-Mediated Recruitment of Host Cell Amphiphysins by Alphavirus nsP3 Promotes Viral RNA Replication
TL;DR: Data establish SH3 domain-mediated binding of nsP3 with amphiphysin as an important host cell interaction promoting alphavirus replication and establishes a carboxyterminal proline-rich sequence motif shared by many alphAViral nsP 3 proteins.
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Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation.
Didier F. Vingadassalom,Arunas Kazlauskas,Brian M. Skehan,Hui-Chun Cheng,Loranne Magoun,Douglas Robbins,Michael K. Rosen,Kalle Saksela,John M. Leong +8 more
TL;DR: Enterohemorrhagic E. coli translocates 2 effectors that bind to distinct domains of a common host factor to promote the formation of a complex that triggers robust actin assembly at the plasma membrane.
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Avian and 1918 Spanish influenza a virus NS1 proteins bind to Crk/CrkL Src homology 3 domains to activate host cell signaling.
Leena S. Heikkinen,Arunas Kazlauskas,Krister Melén,Ralf Wagner,Thedi Ziegler,Ilkka Julkunen,Kalle Saksela +6 more
TL;DR: The Spanish Flu virus resembles avian influenza A viruses in its ability to recruit Crk/CrkL to modulate host cell signaling and was associated with enhanced phosphatidylinositol 3-kinase signaling, as evidenced by increased Akt phosphorylation.
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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.
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Molecular priming of Lyn by GPVI enables an immune receptor to adopt a hemostatic role.
Alec A. Schmaier,Zhiying Zou,Arunas Kazlauskas,Lori A. Emert-Sedlak,Karen P. Fong,Keith B. Neeves,Sean F. Maloney,Scott L. Diamond,Satya P. Kunapuli,Jerry Ware,Lawrence F. Brass,Thomas E. Smithgall,Kalle Saksela,Mark L. Kahn +13 more
TL;DR: It is shown that the GPVI receptor utilizes a unique intracellular proline-rich domain (PRD) to accelerate platelet activation, a requirement for efficient platelet adhesion to collagen under flow.