Author

V. Zila

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 5 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:microscopy & imaging analysis· 6 Organism:human· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Assay:electronic health records· 2 Assay:fluorescence / live-cell microscopy· 2 Research Focus:host-pathogen & immune response· 2

Frequent Co-Authors

B. Turonova· 3 shared H.-G. Kraeusslich· 3 shared M. Beck· 3 shared V. Laketa· 3 shared B. Mueller· 2 shared B. Müller· 2 shared C. E. Zimmerli· 2 shared H.-G. Krausslich· 2 shared

Activity by Year

2020-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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Curved chords = mutual co-authorship

3 shared papersBiophysics

B. Turonova

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Passage of the HIV capsid cracks the nuclear pore

J. P. Kreysing, M. Heidari, V. Zila, S. Cruz-Leon, A. Obarska-Kosinska, V. Laketa, S. Welsch, J. Koefinger, B. Turonova, G. Hummer, H.-G. Kraeusslich, M. Beck

This study investigates how HIV-1 capsids pass through nuclear pores, finding that capsids retain their structure and cause NPC scaffold rings to crack.

bioRxiv · Apr 23, 2024Biophysics

Nuclear pores safeguard the integrity of the nuclear envelope

R. Taniguchi, C. Orniacki, J. P. Kreysing, V. Zila, C. E. Zimmerli, S. Boehm, B. Turonova, H.-G. Kraeusslich, V. Doye, M. Beck

This study shows that nuclear pore complexes dilate during cell differentiation and that Nup133 deficiency prevents this dilation, leading to nuclear envelope instability.

bioRxiv · Feb 5, 2024Cell Biology

Direct capsid labeling of infectious HIV-1 by genetic code expansion allows detection of largely complete nuclear capsids and suggests nuclear entry of HIV-1 complexes via common routes

S. Schifferdecker, V. Zila, T. G. Mueller, V. Sakin, M. Anders-Oesswein, V. Laketa, H.-G. Kraeusslich, B. Mueller

This study uses genetic code expansion to label HIV-1 capsid proteins, enabling visualization of complete nuclear capsids and suggesting common nuclear entry routes.

bioRxiv · Sep 14, 2021Microbiology

Maturation of the matrix and viral membrane of HIV-1

K. Qu, Z. Ke, V. Zila, M. Anders-Osswein, B. Glass, B. Mueller, H.-G. Krausslich, J. A. G. Briggs

This study determines the structure of HIV-1 matrix (MA) in immature and mature virions, revealing a hexameric lattice formed during maturation that repurposes the membrane for viral entry.

Science · Aug 6, 2021Peer-reviewedMicrobiology

HIV-1 uncoating by release of viral cDNA from capsid-like structures in the nucleus of infected cells.

T. G. Müller, V. Zila, K. Peters, S. Schifferdecker, M. Stanic, B. Lucic, V. Laketa, M. Lusic, B. Müller, H.-G. Kräusslich

The paper visualizes HIV-1 cDNA in nuclei using CLEM and shows that uncoating occurs via physical disruption of capsid-like structures, not cooperative disassembly.

bioRxiv · Nov 13, 2020Microbiology

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

V. Zila, E. Margiotta, B. Turonova, T. G. Müller, C. E. Zimmerli, S. Mattei, M. Allegretti, K. Börner, J. Rada, B. Müller, M. Lusic, H.-G. Kräusslich, M. Beck

The paper shows HIV-1 capsids can enter the nucleus intact through nuclear pores, challenging the idea that uncoating must occur before nuclear import.

bioRxiv · Jul 30, 2020Microbiology

Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions

Z. Ke, J. Oton, K. Qu, M. Cortese, V. Zila, L. McKeane, T. Nakane, J. Zivanov, C. J. Neufeldt, J. M. Lu, J. Peukes, X. Xiong, H.-G. Krausslich, S. H. W. Scheres, R. Bartenschlager, J. A. G. Briggs

This study uses cryo-electron microscopy to determine the structure, conformational flexibility, and distribution of SARS-CoV-2 spike protein trimers on intact virions.

bioRxiv · Jun 27, 2020Microbiology