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Larissa Kolesnikova

Researcher at University of Marburg

Publications -  66
Citations -  8378

Larissa Kolesnikova is an academic researcher from University of Marburg. The author has contributed to research in topics: VP40 & Virus. The author has an hindex of 34, co-authored 65 publications receiving 7412 citations. Previous affiliations of Larissa Kolesnikova include State Research Center of Virology and Biotechnology VECTOR & Robert Koch Institute.

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An efficient method to make human monoclonal antibodies from memory B cells: potent neutralization of SARS coronavirus

TL;DR: The results show that it is possible to interrogate the memory repertoire of immune donors to rapidly and efficiently isolate neutralizing antibodies that have been selected in the course of natural infection.
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Recovery of infectious Ebola virus from complementary DNA: RNA editing of the GP gene and viral cytotoxicity.

TL;DR: To study the mechanisms underlying the high pathogenicity of Ebola virus, a system that allows the recovery of infectious virus from cloned cDNA and thus permits genetic manipulation is established and a mutant in which the editing site of the gene encoding envelope glycoprotein (GP) was eliminated.
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Structural dissection of Ebola virus and its assembly determinants using cryo-electron tomography

TL;DR: A detailed structural and architectural description of the Ebola virus can be found in this paper, where four proteins (NP, VP24, VP35, and VP40) are necessary and sufficient to mediate assembly of an NC with structure, symmetry, variability and flexibility indistinguishable from that in Ebola virus particles released from infected cells.
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Structure and assembly of the Ebola virus nucleocapsid.

TL;DR: Cryo-electron tomography and subtomogram averaging reveal the identity and arrangement of the nucleocapsid components, and suggest that the formation of an extended α-helix from the disordered carboxy-terminal region of nucleoprotein-core links nucleop protein oligomerization, nucleocapid condensation, RNA encapsidation, and accessory protein recruitment.