Author

A. Nans

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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Biochemistry· 4 Microbiology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Assay:cryo-EM· 4 Approach:microscopy & imaging analysis· 4 Organism:human· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2

Frequent Co-Authors

P. Cherepanov· 4 shared P. B. Rosenthal· 2 shared V. E. Pye· 2 shared A. Ballandras-Colas· 1 shared A. Borg· 1 shared A. BriegeliD· 1 shared A. Costa· 1 shared A. Fung· 1 shared

Activity by Year

2018-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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4 shared papersBiochemistry

P. Cherepanov

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Preservation of memory B cell homeostasis in an individual producing broadly neutralising antibodies against HIV-1

S. Griffith, L. Muir, O. Suchanek, J. Hope, C. Pade, J. M. Gibbons, Z. K. Tuong, A. Fung, E. Touizer, C. Rees-Spear, A. Nans, C. Roustan, Y. Alguel, D. Fink, C. Orkin, , L. E. McCoy

The paper isolates a broadly neutralizing HIV-1 antibody from an untreated HIV-1 patient and shows memory B cells remain functional despite viral infection.

bioRxiv · Feb 5, 2024 · PreprintMicrobiology

Cryo-ET of infected cells reveals that a succession of two lattices drives vaccinia virus assembly

M. Hernandez-Gonzalez, T. Calcraft, A. Nans, P. B. Rosenthal, M. Way

This study uses cryo-ET to show that vaccinia virus maturation involves a new pseudohexagonal lattice that controls virion shape and dimensions.

bioRxiv · Aug 11, 2022 · PreprintMicrobiology

Multivalent interactions essential for lentiviral integrase function

A. Ballandras-Colas, V. Chivukula, D. T. Gruszka, Z. Shan, P. K. Singh, V. E. Pye, R. K. McLean, G. J. Bedwell, W. Li, A. Nans, N. J. Cook, H. J. Fadel, E. M. Poeschla, D. J. Griffiths, J. Vargas, , P. Cherepanov

This study reports cryo-EM structures of the lentiviral intasome and shows that multivalent interactions are essential for integrase function and virus infectivity.

bioRxiv · Jan 26, 2022Biochemistry

A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing

S. Adams, A. G. Purkiss, P. P. Knowles, A. Nans, D. C. Briggs, A. Borg, C. P. Earl, K. M. Goodman, A. Nawrotek, A. J. Borg, P. B. McIntosh, F. M. Houghton, S. Kjaer, N. Q. McDonald

The paper reports crystal and cryo-EM structures of zebrafish RET revealing conformational flexibility and strict geometric spacing in ligand-co-receptor recognition.

bioRxiv · Sep 13, 2020Biophysics

CRYO-EM STRUCTURE OF THE DELTA-RETROVIRAL INTASOME IN COMPLEX WITH THE PP2A REGULATORY SUBUNIT B56gamma

M. S. Barski, J. J. Minnell, Z. Hodakova, V. Pye, A. Nans, P. Cherepanov, G. N. Maertens

The paper determines the structure of the delta-retroviral intasome complexed with the PP2A regulatory subunit B56gamma using cryo-EM, revealing key interactions and binding mechanisms.

bioRxiv · Jun 19, 2020Biochemistry

Visual Biochemistry: modular microfluidics enables kinetic insight from time-resolved cryo-EM

M.-E. Maeots, B. Lee, A. Nans, S.-G. Jeong, M. M. N. Esfahani, D. J. Smith, C.-S. Lee, S. S. Lee, M. Peter, R. I. Enchev

This paper introduces a time-resolved cryo-EM method using modular microfluidics to visualize biochemical reactions at near-atomic resolution and millisecond timescales, demonstrating its application to RecA filament formation.

bioRxiv · Mar 4, 2020Biochemistry

Retroviral integration into nucleosomes throughDNA looping and sliding along the histone octamer

M. D. Wilson, L. Renault, D. P. Maskell, M. Ghoneim, V. E. Pye, A. Nans, D. S. Rueda, P. Cherepanov, A. Costa

This study reveals that retroviral integrase uses a looping-and-sliding mechanism to reposition nucleosomal DNA for integration, similar to chromatin remodelers.

bioRxiv · Jun 7, 2019Biochemistry

γ-proteobacteria eject their polar flagella under nutrient depletion, retaining flagellar motor relic structures

J. L. Ferreira, F. Z. Gao, F. M. Rossmann, A. Nans, S. Brenzinger, R. Hosseini, A. Briegel, K. M. Thormann, P. B. Rosenthal, M. Beeby

The paper shows γ-proteobacteria eject their polar flagella under nutrient depletion, leaving behind motor relic structures in the outer membrane.

bioRxiv · Jul 18, 2018Microbiology