Full Text Journal Articles by
Author Cyril V Privezentzev

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Single domain shark VNAR antibodies neutralize SARS-CoV-2 infection in vitro.

Aziz Gauhar, Cyril V Privezentzev, Mykhaylo Demydchuk, Tanja Gerlza, Julia Rieger, Andreas J Kungl, Frank S Walsh, J Lynn Rutkowski, Pawel Stocki,

Single domain shark variable domain of new antigen receptor (VNAR) antibodies can offer a viable alternative to conventional Ig-based monoclonal antibodies in treating COVID-19 disease during the current pandemic. Here we report the identification of neutralizing single domain VNAR antibodies selected against the severe acute respiratory syndrome coronavirus 2 spike ... Read more >>

FASEB J (FASEB journal : official publication of the Federation of American Societies for Experimental Biology)
[2021, 35(11):e21970]

Cited: 0 times

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The role of RuvA octamerization for RuvAB function in vitro and in vivo.

Cyril V Privezentzev, Anthony Keeley, Barbara Sigala, Irina R Tsaneva,

RuvA plays an essential role in branch migration of the Holliday junction by RuvAB as part of the RuvABC pathway for processing Holliday junctions in Escherichia coli. Two types of RuvA-Holliday junction complexes have been characterized: 1) complex I containing a single RuvA tetramer and 2) complex II in which ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2005, 280(5):3365-3375]

Cited: 15 times

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Hijacking of the human alkyl-N-purine-DNA glycosylase by 3,N4-ethenocytosine, a lipid peroxidation-induced DNA adduct.

Laurent Gros, Andrei V Maksimenko, Cyril V Privezentzev, Jacques Laval, Murat K Saparbaev,

Lipid peroxidation generates aldehydes, which react with DNA bases, forming genotoxic exocyclic etheno(epsilon)-adducts. E-bases have been implicated in vinyl chloride-induced carcinogenesis, and increased levels of these DNA lesions formed by endogenous processes are found in human degenerative disorders. E-adducts are repaired by the base excision repair pathway. Here, we report ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2004, 279(17):17723-17730]

Cited: 29 times

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Characterisation of new substrate specificities of Escherichia coli and Saccharomyces cerevisiae AP endonucleases.

Alexander A Ishchenko, Guenhaël Sanz, Cyril V Privezentzev, Andrei V Maksimenko, Murat Saparbaev,

Despite the progress in understanding the base excision repair (BER) pathway it is still unclear why known mutants deficient in DNA glycosylases that remove oxidised bases are not sensitive to oxidising agents. One of the back-up repair pathways for oxidative DNA damage is the nucleotide incision repair (NIR) pathway initiated ... Read more >>

Nucleic Acids Res (Nucleic acids research)
[2003, 31(21):6344-6353]

Cited: 38 times

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1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase.

Murat Saparbaev, Sophie Langouët, Cyril V Privezentzev, F Peter Guengerich, Hongliang Cai, Rhoderick H Elder, Jacques Laval,

The promutagenic and genotoxic exocyclic DNA adduct 1,N(2)-ethenoguanine (1,N(2)-epsilonG) is a major product formed in DNA exposed to lipid peroxidation-derived aldehydes in vitro. Here, we report that two structurally unrelated proteins, the Escherichia coli mismatch-specific uracil-DNA glycosylase (MUG) and the human alkylpurine-DNA-N-glycosylase (ANPG), can release 1,N(2)-epsilonG from defined oligonucleotides containing ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2002, 277(30):26987-26993]

Cited: 56 times

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Repair of oxidized purines and damaged pyrimidines by E. coli Fpg protein: different roles of proline 2 and lysine 57 residues.

Murat Saparbaev, Olga M Sidorkina, Juan Jurado, Cyril V Privezentzev, Marc M Greenberg, Jacques Laval,

The Escherichia coli Fpg protein is involved in the repair of oxidized purines, including the highly mutagenic 7,8-dihydro-8-oxoguanine (8-oxoG). The Fpg protein also excises various oxidized pyrimidines with high efficiency. We examined, by targeted mutagenesis, the role of two highly conserved amino acid residues, proline 2 (P2) and lysine 57 ... Read more >>

Environ Mol Mutagen (Environmental and molecular mutagenesis)
[2002, 39(1):10-17]

Cited: 10 times

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