个人简介

I graduated from the Moscow Institute of Physics and Technology (1986) and studied for PhD at the Institute of Crystallography (Moscow, USSR Academy of Sciences) in the laboratory of protein structure led by Boris Vainstein. During 1987-1989, as a member of a working group, I was involved in the USSR Academy of Sciences initiative to set up a synchrotron radiation station for protein crystallography at the Institute of Nuclear Physics (Novosibirsk, Russia). After a number of visits to European Molecular Biology Laboratory in Hamburg (1990-1992) where I worked with Keith Wilson, in 1992 I joined the laboratory of Guy Dodson at York. Since 1998 my research has been supported by the Wellcome Trust, this enabled me to set up a research group focused on studying structures and mechanisms of several protein-nucleic acid assemblies. 1998 - Wellcome Trust Research Career Development Fellowship 2002 – Wellcome Trust Senior Research Fellowship 2007 – Wellcome Trust Senior Research Fellowship, renewal for 5 years 2012 - Wellcome Trust Senior Research Fellowship, renewal for 5 years

研究领域

Protein-nucleic acid interactions

Our group's interests are in understanding the molecular events that control biological mechanisms and we are concentrating on protein - nucleic acid interactions because of their key role in many biological processes. The major aim is to study, by X-ray structural analysis combined with several biophysical/biochemical methods, the structure and function of protein-nucleic acid complexes present in molecular motors and in steady assemblies.

近期论文

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S-Adenosyl-S-carboxymethyl-L-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA. Byrne RT, Whelan F, Aller P, Bird LE, Dowle A, Lobley CMC, Reddivari Y, Nettleship JE, Owens RJ, Antson AA and Waterman DG (2013) Acta Cryst D, 69, 1090-1098. Structural basis for DNA recognition and loading into a viral packaging motor. Büttner C, Chechik M, Ortiz-Lombardíaa M, Smits M, Ebong I-O, Chechik V, Jeschke G, Dykeman E, Benini S, Robinson CV, Alonso JC, Antson (2012) AA Proc. Natl. Acad. Sci. USA, 109, 811-816. A flexible brace maintains the assembly of a hexameric replicative helicase during DNA unwinding. Whelan F, Stead J, Shkumatov AV, Svergun DI, Sanders C, Antson AA (2012) Nucleic Acids Research, 40, 2271-2283. Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage . Milic D, Demidkina TV, Faleev NG, Phillips RS, Matkovic-Calogovic D and Antson AA (2011) J. Am. Chem. Soc., 133, 16468-16476. How to change the oligomeric state of a circular protein assembly: switch from 11-subunit to 12-subunit TRAP suggests a general mechanism. Chen C-S, Smits C, Dodson GG, Shevtsov MB, Merlino N, Gollnick P and Antson AA (2011) PLoS One, 6, 1-11. Structure and Activity of a Novel Archaeal beta-CASP Protein with N-Terminal KH Domains. Silva APG, Chechik M, Byrne RT, Waterman DG, Ng CL, Dodson EJ, Koonin EV, Antson AA, Smits C (2011) Structure, 19, 622-632. The crystal structure of unmodified tRNAphe from Escherichia coli. Byrne RT, Konevega AL, Rodnina MV and Antson AA (2010), Nucleic Acids Research, 38, 4154-4162.