Author

A. A. Antson

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· 7 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 9 Organism:human· 4 Organism:bacteria (other)· 3 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Research Focus:chromatin & epigenetic regulation· 2 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2

Frequent Co-Authors

K. V. Tugaeva· 4 shared N. N. Sluchanko· 4 shared A. A. Sysoev· 2 shared D.-S. Ker· 2 shared H. T. Jenkins· 2 shared J. L. R. Smith· 2 shared M. Chechik· 2 shared O. W. Bayfield· 2 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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4 shared papersBiochemistry

K. V. Tugaeva

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Dominant CIZ1 fragments drive epigenetic instability and are expressed in early stage cancers

G. Turvey, E. Lopez de Alba, E. Stewart, L. Byrom, H. Cook, S. Sofi, A. Alati, J. Ainscough, A. S. Mason, A. A. Antson, D. Coverley

This study identifies that elevated CIZ1 anchor domain fragments in early stage cancers disrupt SMACs, leading to epigenetic instability by destabilizing PRC1-dependent histone modifications.

bioRxiv · Sep 22, 2023 · PreprintCell Biology

Structure of HK97 small terminase:DNA complex unveils a novel DNA binding mechanism by a circular protein.

M. Chechik, S. J. Greive, A. A. Antson, H. T. Jenkins

The paper determines the structure of the HK97 small terminase:DNA complex, revealing a novel DNA binding mechanism involving a circular protein that recognizes DNA through a substructure formed by adjacent protomers.

bioRxiv · Jul 17, 2023Biochemistry

Structural basis of DNA packaging by a ring-type ATPase from an archetypal viral system

H. K. H. Fung, S. Grimes, A. Huet, R. L. Duda, M. Chechik, J. Gault, C. V. Robinson, R. W. Hendrix, P. J. Jardine, J. F. Conway, C. G. Baumann, A. A. Antson

This study describes the structural and biochemical mechanisms of DNA packaging by the HK97 bacteriophage's terminase complex, revealing similarities to other viral systems.

bioRxiv · May 10, 2022Biochemistry

Human 14-3-3 proteins site-selectively bind the mutational hotspot region of SARS-CoV-2 nucleoprotein modulating its phosphoregulation

K. V. Tugaeva, A. A. Sysoev, A. A. Kapitonova, J. L. R. Smith, P. Zhu, R. B. Cooley, A. A. Antson, N. N. Sluchanko

This study shows that 14-3-3 proteins bind specific phosphorylation sites in SARS-CoV-2 nucleoprotein, affecting its phosphoregulation and potentially influencing viral replication.

bioRxiv · Dec 23, 2021Biochemistry

The mechanism of SARS-CoV-2 nucleocapsid protein recognition by the human 14-3-3 proteins

K. V. Tugaeva, D. E. D. P. Hawkins, J. L. R. Smith, O. W. Bayfield, D.-S. Ker, A. A. Sysoev, O. I. Klychnikov, A. A. Antson, N. N. Sluchanko

This paper identifies the molecular mechanism by which phosphorylated SARS-CoV-2 nucleocapsid protein binds to human 14-3-3 proteins, showing that Ser197 phosphorylation is critical for this interaction.

bioRxiv · Dec 26, 2020Biochemistry

Molecular basis for the recognition of steroidogenic acute regulatory protein by the 14-3-3 protein family

K. V. Tugaeva, J. Titterington, D. V. Sotnikov, E. G. Maksimov, A. A. Antson, N. N. Sluchanko

The paper investigates how phosphorylation of STARD1 at specific sites enables interaction with 14-3-3 proteins, modulating its activity and mitochondrial import.

bioRxiv · Apr 14, 2020Biochemistry

CryoEM structure of the Nipah virus nucleocapsid assembly

D.-S. Ker, H. T. Jenkins, S. J. Greive, A. A. Antson

The paper reports the CryoEM structure of the Nipah virus nucleocapsid protein-RNA assembly, revealing its helical organization and key interactions.

bioRxiv · Jan 20, 2020Biophysics

Cryo-EM analysis of a viral portal protein in situ reveals a switch in the DNA tunnel

O. W. Bayfield, A. C. Steven, A. A. Antson

The paper uses cryo-EM to analyze the portal protein of bacteriophage P23-45, revealing structural changes in the DNA tunnel that may regulate DNA translocation.

bioRxiv · Jul 25, 2019 · PreprintBiochemistry

Chimeric 14-3-3 Proteins For Unravelling Interactions With Intrinsically Disordered Partners

N. N. Sluchanko, K. V. Tugaeva, A. A. Antson

This paper introduces chimeric 14-3-3 proteins to study interactions with intrinsically disordered partners, showing they enable structural analysis of phosphopeptide binding.

bioRxiv · Apr 24, 2017Biochemistry