Alexander Mazin, PhD
Professor, Tenure
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Professional Background
Education
- 1984 - PhD - Biochemistry - Institute of Cytology & Genetics of the Russian Academy of Sciences, Novosibirsk
- 1979 - B.S., M.S. - Biochemistry - Novosibirsk State University, Russia.
Training
- 1999 - Postdoctoral Training Section of Microbiology - University of California Davis, California 95616-8665 USA (Dr. Steven Kowalczykowski)
- 1994 - Postdoctoral Training - Groupe d'Etude "Mutagénèse et cancérogénèse" Institut Curie- Biologie F-91405 Orsay, FRANCE (Dr. Raymond Devoret)
Highlights
1991 Fellowship Award, Inter. Agency Research on Cancer, Lyon, France
1992 Fellowship Award, Foundation ARC pour la Recherche sur la Cancer, Paris, France
1993 Science Foundation Award, Paris, France
2004 106 Club Award, Drexel Univ.
2008 Leukemia and the Lymphoma Society Scholar Award
2012 Basic Research Scientist Award, Drexel Univ. College of Medicine
2018 Jefferson Univ., Dept. of Radiation Oncology Visiting Professor Honors
Appointments
- 1990 - Visiting Scientist- Laboratory of Genetics - The Carl von Ossietzky University of Oldenburg Oldenburg, GERMANY (Prof. Wilfried Wackernagel)
- 1984-1989 - unior Research Investigator, Research Investigator, Senior Research Investigator - Institute of Cytology and Genetics, The Russian Academy of Sciences, Novosibirsk
- 1990-1991 - Interim head of the Laboratory - Institute of Cytology and Genetics, Russian Academy of Science, Novosibirsk, Russia
- 1999-2001 - Research Assistant Professor- Section of Microbiology - University of California Davis, California 95616-8665 USA
- 2001-2007 - Assistant Professor - Department of Biochemistry and Molecular Biology Drexel University College of Medicine, Philadelphia, PA 19102
- 2007-2012 - Associate Professor - Department of Biochemistry and Molecular Biology Drexel University College of Medicine, Philadelphia, PA 19102
- 2009-2012 - Tenured Associate Professor - Department of Biochemistry and Molecular Biology Drexel University College of Medicine, Philadelphia, PA 19102
- 2012-2021 - Tenured Professor - Department of Biochemistry and Molecular Biology Drexel University College of Medicine, Philadelphia, PA 19102
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Instruction & Training
2002-2013 - “Cancer”, a 1h lecture for medical students. - Drexel University College of Medicine, Philadelphia, PA2003-2015 - “Cancer”, a 3 h Small Group Seminar for medical students - Drexel University College of Medicine, Philadelphia, PA2003-2015 - “Glycogen Storage Diseases”, a 3 h Small Group Seminar for medical students - Drexel University College of Medicine, Philadelphia, PA2003-2013 - “Web-based Assignment” a 4 h conference for medical students - Drexel University College of Medicine, Philadelphia, PA2004-2021 - “Purine and pyrimidine metabolism”, a 2 h lecture for graduate students - Drexel University College of Medicine, Philadelphia, PA2004-2021 - “Isotopes” in “Experimental approaches to biochemical problems” course, a 2.5 h lecture for graduate students - Drexel University College of Medicine, Philadelphia, PA2005-2021 - “Homologous recombination and Non-Homologous End-Joining” in “Cancer Biology” - Drexel University College of Medicine, Philadelphia, PA2015-2021 - “Mismatch DNA repair, Base excision repair, Nucleotide excision repair” in “Cancer Biology” course, a 2 h lecture for graduate students - Drexel University College of Medicine, Philadelphia, PA2005-2021 - Mechanisms” in “Advanced Cell Biology” course, a 2 h seminar for graduate students - Drexel University College of Medicine, Philadelphia, PA2007-2021 - “DNA repair and mutations”, a 2 h lecture for graduate students. - Drexel University College of Medicine, Philadelphia, PA2007-2021 - “Meiosis and Mitosis”, a 2 h lecture for graduate students - Drexel University College of Medicine, Philadelphia, PA2007-2017 - Biochemistry Journal Club (BIOC-506)0- Mentor - Drexel University College of Medicine, Philadelphia, PA2008-2009 - “Meiosis” in “Advanced Cell Biology” course, a 2 h seminar for graduate students - Drexel University College of Medicine, Philadelphia, PA2008-2015 - “DNA repair”, a 1 h lecture for medical students - Drexel University College of Medicine, Philadelphia, PA2008-2016 - “DNA repair”, a 1 h lecture for medical PIL students - Drexel University College of Medicine, Philadelphia, PA2010-2021 - “DNA repair” in “Advanced Cancer Biology” course, a 2 h seminar for graduate students - Drexel University College of Medicine, Philadelphia, PA2012-2014 - Developed and taught a 1.5 h class on “DNA damage and repair” in Radiobiology course for residents at Drexel University Scholl of Medicine. - Drexel University College of Medicine, Philadelphia, PA2012-2021 - Developed and taught a 1.5 h class on “DNA damage and repair” in Radiobiology course for residents - Jefferson University.
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Research & Grants
Grants
Contribution to Science:
I. Discovery of branch migration activity of Rad54 protein. In the process of HR in the cell, a four-stranded DNA intermediate called the Holliday junction arises. HJ can migrate along the DNA axis (branch migration) and its resolution or dissolution helps determine whether DNA recombinants with chromosome arm crossover or not are made. However, the identity of the proteins that catalyze branch migration of Holliday junctions in eukaryotes remained elusive for a long time. Our work has made major contributions in this area by showing that RAD54 is the major branch migration motor in eukaryotes and determined regulatory mechanisms that underpin this RAD54 attribute.1. Bugreev, D. V., Mazina, O.M., and Mazin, A. V. (2006). Rad54 protein promotes branch migration of the Holliday junctions. Nature (London). v. 442: 590-593. PMID: 17545145. This article was rated by Faculty of 1000. 2. Mazina, O.M., Mazin, A.V. (2008) Human Rad54 protein stimulates human Mus81/Eme1 endonuclease. Proc. Natl. Acad. Sci. USA, 105(47): p. 18249-54. PMCID: PMC2587595 3. Mazina, O.M., Rossi, M.J., Deakyne, J.S., Huang, F., and Mazin, A.V. (2012). Polarity and bypass of DNA heterology during branch migration of Holliday junctions by human RAD54, BLM, and RECQ1. J. Biol. Chem. 287, 11820-11832. PMCID: PMC3320930 4. Goyal, N., Rossi, M.J., Mazina, O.M., Chi, Y., Moritz, R.L., Clurman B.E., Mazin A.V. (2018) RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis 8 with branch migration of Holliday junctions. Nature Comm., 9, article number 34, doi:10.1038/s41467-017-02497-x. PMCID: PMC5750232.
II. Understanding of the role of the ATPase activity of human RAD51 and its homologs. Results from previous investigations showed that the ATP binding by RAD51, the major human recombinase, is crucial for DNA strand exchange, while ATP hydrolysis is not required for DNA strand exchange, the major RAD51 activity, and results in the dissociation of RAD51 protomers from DNA. Our studies made an important contribution to the field by demonstrating that RAD51 behaves as a selfinactivating ATPase in that, upon ATP hydrolysis, ADP remains bound to RAD51 and inhibits DNA strand exchange. We then found that Ca2+ or the HR factor HOP2-MND2 complex either attenuates ATP hydrolysis by RAD51 or modulates ATP binding by RAD51, respectively, to enhance DNA strand exchange. Furthermore, our studies also revealed the mechanism that links RAD51 ATP hydrolysis to branch migration promoted by this protein. The results showed that RAD51 and its bacterial homologue RecA drive branch migration of HJ by cycles of their ATP-dependent polymerization/dissociation on the HJ. 1. Bugreev, D. V., and Mazin, A. V. (2004). Ca2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc. Natl. Acad. Sci. USA 101, 9988-9993. PMCID: PMC454202 2. Bugreev, D V., Golub, E I, Stasiak, A Z, Stasiak, A, and A, Mazin A V. (2005) Activation of human meiosis-specific recombinase Dmc1 by Ca2+. J. Biol. Chem. 280(29): p. 26886-95. PMID: 16862129 3. Rossi, M.J., Mazina, O.M., Bugreev, D.V., and Mazin, A.V. (2011). The RecA/RAD51 protein drives migration of Holliday junctions via polymerization on DNA. Proc Natl Acad Sci USA 108, 6432-6437. PMCID: PMC3080997 4. Bugreev, D.V., Huang, F., Mazina, O.M., Pezza, R.J., Voloshin, O.N., Daniel Camerini-Otero, R., and Mazin, A.V. (2014). HOP2-MND1 modulates RAD51 binding to nucleotides and DNA. Nature Com. 5, 4198. PMCID: 4279451
III. Study on the function of BLM helicase. Inactivation of BLM helicase is responsible for human cancer predisposition syndrome, known as Bloom syndrome. However, the exact BLM function remains controversial. Mutations in the BLM cause hyperrecombination between sister chromatids indicating an anti-recombination role. Conversely, other data show that BLM is required for HR. We discovered two novel activities of BLM which may account for both these BLM functions. We found that BLM disrupts the Rad51-ssDNA filament, an active species of HR. However, this disruption occurs only if RAD51 is present in an inactive ADP-bound form. When the RAD51- ssDNA is present in an active ATP-bound form, BLM stimulates DNA strand exchange activity of RAD51. Our results demonstrate the important role of the RAD51 nucleoprotein filament conformation in regulation of HR by BLM. Interestingly, the 9 nucleoprotein filaments formed by DMC1, a meiosis specific RAD51 homolog, resist BLM disruption, which may account of the role of DMC1 in meiosis. 1. Bugreev, D.V., Yu, X., Egelman, E.H., Mazin, A.V. (2007). Novel pro- and antirecombination activities of the Bloom’s syndrome helicase. Genes & Development, 21 (23): 3085-3094. PMCID: PMC2081975 2. Bugreev, D.V., Mazina, O.M., and Mazin, A.V. (2009). Bloom syndrome helicase stimulates RAD51 DNA strand exchange activity through a novel mechanism. J. Biol. Chem. 284, 26349-26359. PMCID: PMC2786030 3. Bugreev, D. V., Pezza, R. J., Mazina, O. M., Voloshin, O. N., Camerini-Otero R. D., Mazin A. V. (2011) The resistance of DMC1 D-loops to dissociation may account for the DMC1 requirement in meiosis. Nature Struct. & Mol. Biol., 18, 56-60. PMCID: PMC3058924
IV. Studies on RNA-dependent DNA repair: a) Discovery of the inverse strand exchange activity of RAD52 and its role in RNA-templated DNA repair and b) Rloop formation activity of RPA. RNA can serve as a template for DNA double-strand break repair in yeast cells, and Rad52, a member of the homologous recombination pathway, plays role in this process. However, the exact mechanism of how Rad52 contributes to RNA-dependent DSB repair remained unknown. We discovered a novel activity of yeast and human Rad52: inverse strand exchange, in which Rad52 forms a complex with dsDNA and promotes strand exchange with homologous ssRNA or ssDNA. In accord with our in vitro results, our experiments in budding yeast provide evidence that Rad52-inverse strand exchange plays an important role in RNA-templated DSB repair in vivo. 1. Keskin, H., Shen, Y., Huang, F., Patel, M., Yang, T., Ashley, K., Mazin, A.V., and Storici, F. (2014) Transcript RNA-templated DNA recombination and repair. Nature, 515, 436-439. 2. Mazina, O.M., Keskin, H., Hanamshet, K., and Storici, F., Mazin, A.V., (2017) Rad52-inverse strand exchange drives RNA-templated DNA double-strand break repair. Molecular Cell, 67, p 19-29 3e. PMCID: PMC5547995. Replication protein A (RPA), a major eukaryotic ssDNA-binding protein, is essential for all metabolic processes that involve ssDNA. While RPA is known to bind ssDNA tightly, it was presumed that it binds RNA weakly. However, recent data suggest that RPA may play a role in RNA metabolism. We investigated the RNA-binding properties of human RPA and found that RPA binds RNA with an unexpectedly high affinity (KD ≈ 100 pM). Furthermore, RPA by forming a complex with RNA can promote R-loop formation with homologous dsDNA. We showed that human DNA polymerases can utilize RPAgenerated R-loops for initiation of DNA synthesis mimicking the process of replication restart in vivo. These results support the role of RPA in RNA metabolism and suggest a 10 mechanism of genome maintenance that depends on RPA-mediated DNA replication restart. 3. Mazina, O.M., Somarowthu, S., Kadyrova, L.Y., Baranovskiy, A.G., Tahirov, T.H., Kadyrov, F.A., and A.V. Mazin (2020). Replication protein A binds RNA and promotes R-loop formation J. Biol. Chem., 295(41): p. 14203-14213 PMCID: PMC7549048 V. Development of small molecule inhibitors of the key HR proteins. Using high throughput screening (HTS) we identified several small molecule inhibitors of RAD51. We demonstrated that one of them, named B02, inhibited HR and DSB repair in vivo. B02 was the first known biologically active inhibitor of a HR protein. Using mouse xenografts, we demonstrated that B02 increases the efficacy of cisplatin in killing triplenegative breast cancer cells in vivo. 1. Huang, F., Mazina, O.M., Zentner, I J., Cocklin, S., and Mazin, A.V. (2012). Inhibition of homologous recombination in human cells by targeting RAD51 recombinase, J. Medicinal Chem., 55(7): p. 3011-20. PMID: 22380680 Faculty of 1000 rated it twice as a “must read”. 2. Huang, F., and Mazin, A.V. (2014). A Small Molecule Inhibitor of Human RAD51 Potentiates Breast Cancer Cell Killing by Therapeutic Agents in Mouse Xenografts. PLoS ONE 9, e100993. PMCID: PMC4074124 Previous studies demonstrated that while single RAD52 mutations show no significant phenotype in mice, their combination with mutations in Breast Cancer proteins 1&2 (BRCA1/2) are lethal. These observations defined RAD52 as a novel therapeutic target for BRCA1/2-deficient familial breast cancer and ovarian cancer. Recently we identified by HTS of ~400,000 compound library we identified small molecule inhibitors of RAD52. Several of these inhibitors show specific effect on BRCA1 and BRCA2-deficient cells and suppress RAD52-dependent recombination. 3. Huang, F., Goyal, N., Sullivan, K., Hanamshet, K., Patel, M., Mazina, O.M., Wang, C.X., An, W.F., Spoonamore, J., Metkar, S. Kyle A. Emmitte, Simon Cocklin, Tomasz Skorski, and Alexander
V. Mazin (2016) Targeting BRCA1- and BRCA2-deficient cells with RAD52 small molecule inhibitors. Nucleic Acids Res. 44, 4189-99. PMCID: PMC4872086 We also identified by HTS an inhibitor of RAD54 protein, streptonigrin. Using this inhibitor, we found that the ATPase activity of RAD54 is important for branch migration, but not for stimulation of RAD51 4. Deakyne J.S., Huang, F., Negri, J., Tolliday, N., Cocklin, S., and Mazin, A.V. (2013). Analysis of the activities of RAD54, a SWI2/SNF2 protein, using a specific small-molecule inhibitor, J. Biol. Chem. 288, p. 31567-31580. PMCID: PMC3814753 11
Current Support:
(1) R01 CA188347, NIH/NCI “Small molecule inhibitors as a new approach to study human RAD51 recombinase” Budget period: 09/25/2015 – 08/31/2021 Role in Project: Principal Investigator The goal of this grant is to develop inhibitors of RAD51 and use it to study biological functions of RAD51 and for combination cancer therapies.
(2) R01 GM136717 NIH/NIGMS “Mechanisms of RNA-dependent DNA repair in humans” Budget period: 04/16/2020-02/29/2024 Role in Project: Principal Investigator The goal of this grant is to develop novel more effective, less toxic treatment that will impact survival of breast cancer patients carrying mutations in BRCA genes.
(3) R01 CA23728, NIH/NCI “AML mutation-guided drugging of DNA repair” Budget period: 03/01/2020-01/31/2025 Role in Project: Principal Investigator in MPI grant with Dr. Skorski The goal of this grant is to combine the approaches of personalized medicine with targeted inhibitors of DNA repair enzymes for development of efficient anti-AML therapies.
(4) BC191160, Breast Cancer, Breakthrough Award Level 2, CDMRP/BCRP “Development of inhibitors of RAD52 protein against BRCA-deficient breast cancer” Budget period: 08/01/2020-07/31/2023 Role in Project: Partnering Principal Investigator with Dr. Du The goal of this grant is to develop novel more effective, less toxic treatment that will impact survival of breast cancer patients carrying mutations in BRCA genes.
(5) The Coulter-Drexel Translational Research Partnership Program Award “Development of inhibitors of RAD52 as a therapy against BRCA-deficient breast cancer and ovarian cancer” Budget period: 07/01/2017 to 12/31/2020 Role in Project: Principal Investigator The goal of the grant is to develop a new generation of RAD52 inhibitors for attrition of BRCA-deficient cancer cells.
(6) Sponsored Research Agreement with Rain Therapeutics “Studies on application of RAD52 inhibitors” Budget period: 07/30/2020-07/29/2022. 12 Role in Project: Principal Investigator The goal of this Agreement is performing the studies which will provide the structural, molecular, cellular, and genetic basis for development drug-grade RAD52 inhibitors to treat BRCA-deficient cancers.
Previous Support:
Health research formula fund, the Tobacco Settlement Act. “The role of the homologous recombination system in tumorigenesis.” 02/01/2001 - 06/30/2003. PI.
R01CA100839, NIH/NCI: “Repair of DNA breaks in humans: the role of Rad54 protein”, 09/31/2003 – 04/30/2016. PI. The goal of the proposal is to define the functions and biochemical activities of human RAD54 protein, a motor protein that plays an important role in DNA repair.
Drexel University, Synergy grant: “Visualization of the Active Species of Homologous Recombination Machinery using Atomic Force Microscopy”, 07/01/04– 06/30/05. PI. The goal of this grant is to characterize the structure that RAD54 forms with DNA substrates.
R03MH084119, NIH/NIMH: “A screen for modulators of human Rad51, a key DNA repair protein/.” 06/01/2008 - 05/31/2009. PI. The goal is to identify small-molecule inhibitors of RAD51 strand exchange activity.
The Leukemia and the Lymphoma Society Scholar Award #1054-09: “The function of the Bloom’s syndrome helicase.” PI. 07/01/2008 - 03/30/2013. The goal is to analyze the activities of BLM and its interactions with RAD51.
KECK Foundation: Transformation of Biomolecules by Nonequilibrium Plasma. 01/01/ 2012 - 12/31/2013. Co-PI. The goal is to analyze the effect of cold temperature plasma on the activity of DNA repair enzyme RAD54.
R03DA033981, NIH/NIDA: “Identification of inhibitors of human RAD54, an important DNA repair protein.” 02/15/2012 - 01/31/2016. PI. The goal of the grant is to identify specific small molecule inhibitors of human RAD54 by high-throughput screening.
R03MH097512, NIH/NIMH: “Development of RAD52 inhibitors to induce synthetic lethality of BRCA2-deficient cells.” 03/12/2012 - 02/28/2016. PI. The goal of the grant is to identify specific small-molecule inhibitors of human RAD52 by high-throughput screening.
Basser Research Center External Research Grant Program, Basser Innovation Award: “Targeting familial breast cancer with RAD52 inhibitors.” 09/01/2014 - 08/30/2016. PI. The goal of the grant is to characterize RAD52 inhibitors and determine their biological activity in human cells.
Clinical and Translational Research Institute Drexel award: “Development of targeted therapy against BRCA-deficient familial breast cancer.” 08/01/2015 - 07/31/2017. PI. The goal of the grant is to further improve RAD52 inhibitors and determine their biological activity in human cells.
Drexel University-Ben Gurion University Interdisciplinary Projects Fund: “Targeting PI3K and DNA repair pathways with chemical inhibitors for efficient cancer therapy.” 05/01/2019 - 04/30/2019. PI. The goal of this grant to explore a potential for combination 13 cancer therapy by targeting with specific inhibitors signaling and DNA repair pathways in cancer cells.
R01GM115927, NIH/ NIGMS: “RNA-mediated DNA break repair.” 7/1/2015 – 6/30/2019. Co-PI. The goal of this grant is to analyze the role of RAD52 in RNA-dependent repair of DNA breaks in mammals and yeast.
Patents:
1. Inventor: Alexander V. Mazin and Huang Fei Patent No.: US 9,750,742, September 5, 2017, Title: “Small Molecule Inhibitors of RAD51 Recombinase and Methods Thereof”
2. Inventor: Alexander V. Mazin. Patent No.: US 10,738,061, Date of Patent: August 11, 2020. Title: “Inhibitors of RAD52 Recombination Protein and Methods Using Same”.
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Service
Institutional
2003-2012 Member, Biosafety Committee, Drexel University College of Medicine
2002-current Judge, Discovery Annual Day of Research
2002-current Member, Biochemistry Graduate Student Admission Committee
2010-2013 Alternative, Steering Committee of the Faculty of Drexel University College of Medicine
2012-current Member, Biochemistry and Molecular Biology Faculty Promotion Committee
2018-present Member, Faculty Development Committee
2018-current Member, Finance Committee of Drexel University College of Medicine
2018-current Member, Tenure Committee of Drexel University College of Medicine
2020 Member, Committee on Appointments and Promotions
Professional
Professional Committees and other activities
Ad hoc Reviewer: Nature, Nature of Structural and Molecular Biology, Nature Communications, Molecular and Cellular Biology, PNAS USA, Journal of Biological Chemistry, EMBO Journal, Biochemistry, FEBS Letters, Journal of Molecular Biology, Genes & Development, Nucleic Acids Research, Nucleic Acids Research Cancer, Molecules, DNA repair, FEBS Journal.
Grant reviewer: National Science Foundation, U.S. Civilian Research & Development Foundation (CRDF), Ohio University Research Committee, Netherlands Organisation for Scientific Research, Chemical Sciences, Cancer Research (UK)
2005 Ad hoc reviewer of the MGA study section, NIH, Washington, DC.
2006 Ad hoc reviewer of the MGA study section, NIH, Washington, DC
2007 Ad hoc reviewer of the MGC study section, NIH, Washington, DC
2009 Ad hoc reviewer of the MGA study section, NIH, Washington, DC.
2020 Ad hoc reviewer of the RIVER R35 Special Emphasis Panel NIEHS/NIH, Washington DC
National
Editorial boards
2011-2016 Member, Editorial Board of the Journal of Biological Chemistry
2019-current Member, Editorial Board of Nucleic Acids Research Cancer
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Publications
List of Publications, The asterisk (*) marks peer reviewed publications.
1. *Dianov G, Mazin A, Vavilin V, Zajtsev A and Salganik R (1980) Addressed modification of T7 phage early DNA by its alkylation in the R-loop formed with modified transcript Mol. Biol. 14: 261-264. (Russian).
2. *Salganik R, Dianov G, Ovchinnikova L, Voronina E, Kokoza E and Mazin A (1980) Gene-directed mutagenesis in bacteriophage T7 provided by polyalkylating RNAs complementary to selected DNA sites. Proc. Natl. Acad. Sci. USA 77: 2796-2800.
3. *Mazin A, Dianov G and Salganik R (1981) Application of alkylating DNA derivatives for addressed modification of genome. Mol. Biol. 15: 252-256. (Russian).
4. *Mazin A, Dianov G, Ovchinnikova L and Salganik R (1983) Induction of directed mutation in the tetracycline resistance gene of plasmid pBR322 by complementary single-stranded DNA fragments carrying alkylating groups. Dokl. Acad. Nauk SSSR [Proceedings of the Academy of Science of the USSR] 268: 979-982. (Russian).
5. *Mazin A, Dianov G and Safronov P (1984) Directed modification of the tet gene region of pBR322 using complementary single-stranded DNA fragments carrying alkylating groups. Mol. Biol. 18: 1081-1089. (Russian).
6. *Salganik R, Mazin A, Dianov G and Ovchinnikova L (1984) Induction of repetitive nucleotide sequences in the tet gene of plasmid pBR322 resulting from gene-directed mutagenesis. Dokl Akad Nauk SSSR [Proceedings of the Academy of Science of the USSR] 274: 197-201. (Russian).
7. *Salganik R, Mazin A, Dianov G and Ovchinnikova L (1984) Induction of repeated DNA sequences. Tentative mechanisms of genome evolution and gene conversion. Genetika 20: 1244-1254. (Russian).
8. *Mazin A, Kuzminov A, Dianov G and Salganik R (1985) A new method for probing the conformation of DNA by chemical modification. Bioorg. chimia 11: 1690-1692. (Russian).
9. *Saparbaev M, Mazin A, Kuzminov A, Salganik R and Shigaeva M (1986) Characterization of the mutations induced in pBR322 by site-directed mutagenesis. Vestnik Acad. Nauk Kaz. SSR 11: 41- 46. (Russian).
10. Mazin A. and Kuznedelov K (1986) Procedures in genetic engineering. Novosibirsk. (Russian).
11. *Mazin A, Kuzminov A, Saparbaev M, Dianov G and Salganik R (1986) Induction of deletions predetermined by DNA primary structure in plasmid pBR322. Dokl. Acad. Nauk SSSR [Proceedings of the Academy of Science of the USSR] 239: 503-506. (Russian).
12. *Salganik R, Dianov G and Mazin A (1986) Mutations predetermined by DNA primary structure. Genetika 22: 2398-2407. (Russian).
13. *Saparbaev M, Mazin A, Ovchinnikova L, Dianov G, Salganik R and Shigaeva M (1988) Heteroduplex-initiated site-directed insertion of alien polynucleotide sequences. Mol. Genetics, Microbiology and Virology 2:12-16. (Russian).
14. *Mazin A, Kuzminov A, Dianov G and Salganik R (1989) A new reagent for discrimination of DNA single- and double-stranded regions in DNA. FEBS Lett. 258: 244-247
15. Sergeev D and Mazin A (1989) Molecular genetics and genetic engineering. Practical course. Novosibirsk University. (Russian).
16. *Mazin A, Saparbaev M, Ovchinnikova L, Dianov G and Salganik R (1990) Sitedirected insertion of long single-stranded DNA fragments into plasmid DNA. DNA and Cell Biology 9: 63-68
17. Mazin A, Kuznedelov K, Kraev A, Holodilov N, Blinov A, Kuzminov A, Golovin S, Naiakshin A, Soloviev V, Jamshikov V, Kokoza V, Ivanov S, Potapov V, Saparbaev M, Dianov G, Protopopov M, Kalachikov S, Bogachev S and Chikaev N (1990) Methods of molecular genetics and genetic engineering. Nauka, Novosibirsk. (Russian).
18. Saparbaev M, Mazin A, Ovchinnikova L, Dianov G and Salganik R (1990) Insertion of new DNA sequences into plasmid by partially homologous singlestranded fragment DNA. In: Molecular Mechanisms of Genetic Process, Moscow, Nauka, p. 229-237. (Russian).
19. *Angulo J F, Rouer E R, Mazin A, Mattei M-G, Tissier A, Horellou P, Benarous R and Devoret R (1991) Identification and expression of the cDNA of KIN17, zinc-finger gene located on mouse chromosome 2, encoding a new DNAbinding protein. Nucl. Acids. Res. 19: 5117-5123
20. *Dianov G, Kuzminov A, Mazin A and Salganik R (1991) Molecular mechanisms of deletion formation in Escherichia coli plasmids I. Deletion formation mediated by long direct repeats. Mol. Gen. Genet. 228: 153-159
21. *Mazin A, Kuzminov A, Dianov G and Salganik R (1991) Molecular mechanisms of deletion formation in Escherichia coli plasmids. II. Deletion formation mediated by short direct repeats. Mol. Gen. Genet. 228: 209-214
22. *Dianov G, Saparbaev M, Mazin A and Salganik R (1991) The chemical mutagen dimethyl sulphate induces homologous recombination of plasmid DNA by increasing the binding of RecA protein to duplex DNA. Mut. Research 249: 189-194
23. *Karamysheva T, Mazin AV, Saparbaev M, Dianov G and Salganik R (1991) Efficiency of chemical mutagenesis resulted from multiple damages of one and two strands of plasmid DNA. Genetika 27: 210-216. (Russian).
24. *Makarova K, Bulf Iu, Mazin A and Soloviev V (1992) "DIROM"-an interactive system for planning experiments on directed mutagenesis and design of artificial genes. Mol. Biol. 26: 93-103. (Russian).
25. *Makarova K.S, Mazin A.V, Wolf Y.I, Soloviev V.V. (1992) DIROM: an experimental design interactive system for directed mutagenesis and nucleic acids engineering. Comput. Appl. Biosci. 8(5): 425-31
26. *Mazin A, Timchenko T, Menissier de Murcia J, Schreiber V, Angulo J F, de Murcia G and Devoret R (1994) KIN17, a mouse zinc finger protein that binds preferentially to curved DNA. Nucl. Acids Res. 22(20): 4335-4341
27. *Mazin A, Milot E, Devoret R and Chartrand P (1994) KIN17, a mouse nuclear protein, binds to bent DNA fragments that are found at illegitimate recombination junctions in mammalian cells. Mol. Gen. Genet. 244(4): 435-8.
28. *Tissier A, Kannouche P, Biard DSF, Timchenko T, Mazin A, Araneda S, Allemand I, Mauffrey Ph, Frelat G, Angulo J.F (1995) The mouse Kin-17 gene codes for a new protein involved DNA transactions and is akin to the bacterial RecA protein. Biochimie. 77: 854-860.
29. *Mazin A V and Kowalczykowski S C (1996) The specificity of the secondary site of RecA protein defines its role in DNA strand exchange. Proc. Natl. Acad. Sci. USA, 93: 10673-10678
30. *Mazin A V, Timchenko T V, Saparbaev M K, Mazina O M (1996) Dimerization of plasmid DNA accelerates selection for antibiotic resistance. Mol. Microbiology. 20: 101-108.
31. *Mazin A V and Kowalczykowski S C (1998) The function of the secondary site of RecA protein during DNA strand exchange. EMBO J. 18: 1161-1168.
32. *Ponomarenko M, Ponomarenko J, Titov I, Kolchanov N, Mazin A and Kowalczykowski S. (1998) DNA binding specificity of the RecA-filament correlates with genetic code. Doklady Rossiiskoi Akademii Nauk [Proceedings of the Russian Academy of Science], 363: 122-125. (Russian).
33. *Mazin A V and Kowalczykowski S C (1999) A novel property of RecA nucleoprotein filament: activation of double-stranded DNA for strand exchange in trans. Genes Dev. 13:2005-2016.
34. *Mazin A V, Bornarth C J, Solinger J, Heyer W-D., and Kowalczykowski S C (2000). Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament. Mol. Cell., 6: 583-592.
35. *Mazin A V, Zaitseva E, Sung P and Kowalczykowski S C (2000). Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing. EMBO J., 19: 1148-1156.
36. *Lio, Y.-C., Mazin, A. V., Kowalczykowski, S. C., and Chen, D. J. (2003). Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro. J. Biol. Chem., 278: 2469-2478.
37. *Mazin A V, Alexeev A. A., and Kowalczykowski S. C. (2003) A novel presynaptic function of Rad54 protein: stabilization of the Rad51 nucleoprotein filament. J. Biol. Chem. 278: 14029-14036.
38. *Alexeev A A, Mazin A V, and Kowalczykowski S C. (2003) Rad54 protein possesses chromatin remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament. Nature Structural Biology, 10: 182-186. Faculty of 1000 Biology: evaluations for Alexeev et al. Nature Structural Biology, 10:182-186
39. *Mazina, O. M., Mazin, A. V., Nakagawa T., Kolodner R. D., and Kowalczykowski S. C. (2004). Saccharomyces cerevisiae Mer3 helicase stimulates 3’-5’ heteroduplex extension by Rad51: Implications for crossover control in meiotic recombination. Cell, 117: 47-56.
40. *Bugreev, D. V., and Mazin, A. V. (2004). Ca2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc. Natl. Acad. Sci. USA 101: 9988-9993 (Truck II submission).
41. *Mazina, O. M., and Mazin, A. V. (2004). Human Rad54 protein stimulates DNA strand exchange activity of hRad51 protein in the presence of Ca2+. J. Biol. Chem. 279: 52041-52051. Selected by the J. Biol. Chem. editors as a Paper of the Week (top 1-2% of J. Biol. Chem. papers).
42. *Thoma, N. H., Czyzewski, B. K., Alexeev, A. A., Mazin, A. V., Kowalczykowski, S. C., Pavletich, N.P. (2005) Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54. Nature Struc. and Mol. Biol., 12: 350-356.
43. *Bugreev, D V., Golub, E I, Stasiak, A Z, Stasiak, A, and A, Mazin A V. (2005) Activation of human meiosis-specific recombinase Dmc1 by Ca2+. J. Biol. Chem. 280(29): 26886-26895.
44. Bugreev, D. V., Mazina, O.M., and Mazin, A. V. (2006). Analysis of branch migration activities of proteins using synthetic DNA substrates. Nature Protocols, DOI: 10.1038/nprot.2006.217.
45. *Bugreev, D. V., Mazina, O.M., and Mazin, A. V. (2006). Rad54 protein promotes branch migration of the Holliday junctions. Nature (London). v. 442: 590-593. Faculty of 1000 Biology: evaluations for Bugreev DV et al Nature 2006 Aug 3 442 (7102) :590-3 http://www.f1000biology.com/article/id/1033843/evaluation
46. *Mazina, O. M., Rossi, M. J., Thoma, N., and Mazin A V (2007). Interactions of hRad54 protein with branched DNA molecules. J. Biol. Chem., 282 (29): 21068- 21080.
47. *Bugreev, D. V., Hanaoka, F., and Mazin, A. V. (2007). Rad54 dissociates homologous recombination intermediates by branch migration. Nature Struct. & Mol. Biol., 14 (8): 746-753.
48. Bugreev, D.V., Mazin, A.V. (2007) Reconstitution of DNA double-stranded breaks in vitro using human proteins of homologous recombination. Nature Protocols, published online 2 August 2007 (doi: 2010.1038/nprot.2007.2342).
49. *Bugreev, D.V., Yu, X., Egelman, E.H., Mazin, A.V. (2007). Novel pro- and antirecombination activities of the Bloom’s syndrome helicase. Genes & Development, 21 (23): 3085-3094.
50. *Bugreev, D.V., Brosh, R.M., Jr., and Mazin, A.V. (2008). RECQ1 possesses DNA branch migration activity. J. Biol. Chem., 283(29): 20231-20242.
51. *Rossi, M.J. and Mazin, A.V. (2008). Rad51 protein stimulates the branch migration activity of Rad54 protein. J. Biol. Chem., v. 283 (36): 24698-24706
52. * Mazina, O.M., Mazin, A.V. (2008) Human Rad54 protein stimulates human Mus81/Eme1 endonuclease. Proc. Natl. Acad. Sci. USA, 105(47): 18249-54 (Truck II submission).
53. *Sommers, J.A., Rawtani, N., Gupta, R., Bugreev, D.V., Mazin, A.V., Cantor, S.B., and Brosh, R.M., Jr. (2009). FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange. J. Biol. Chem. 284: 7505-7517.
54. *Kumari, A., Mazina, O.M., Shinde, U., Mazin, A.V., and Lu, H. (2009). A role for SSRP1 in recombination-mediated DNA damage response. J. Cell. Biochem. 108: 508-518.
55. *Bugreev, D.V., Mazina, O.M., and Mazin, A.V. (2009). Bloom syndrome helicase stimulates RAD51 DNA strand exchange activity through a novel mechanism. J. Biol. Chem. 284: 26349-26359.
56. *Mazin, A.V., Mazina,O.M., Bugreev, D.V., Rossi.M.J. (2010). Rad54, the motor of homologous recombination. DNA Repair (Amst) 9: 286-302.
57. *Grimme, J. M., M. Honda, R. Wright, Y. Okuno, E. Rothenberg, A. V. Mazin, T. Ha, and M. Spies. Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes. Nucleic Acids Res. 38: 2917-2930.
58. *Okorokov, A. L., Y. L. Chaban, D. V. Bugreev, J. Hodgkinson, A. V. Mazin, and E. V. Orlova. Structure of the hDmc1-ssDNA filament reveals the principles of its architecture. PLoS ONE 5:e8586.
59. *Rossi, M. J., O. M. Mazina, D. V. Bugreev, and A. V. Mazin. (2010) Analyzing the branch migration activities of eukaryotic proteins. Methods. 51: 336-346.
60. *Wu, Y., J.A. Sommers, A.N. Suhasini, T. Leonard, J.S. Deakyne, A.V. Mazin, K. Shin-Ya, H. Kitao and R.M. Brosh, Jr., (2010) Fanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes. Blood, 116(19): 3780-91.
61. *Bugreev, D.V., M.J. Rossi and A.V. Mazin, (2010) Cooperation of RAD51 and RAD54 in regression of a model replication fork. Nucleic Acids Res39 (6): 2153-64. This article was rates a “must read” by Faculty of 1000.
62. *Deakyne JS, Mazin AV. (2011) Fanconi anemia: at the crossroads of DNA repair. Biochemistry (Mosc). 2011 76: 36-48. Review.
63. Rossi MJ, Bugreev DV, Mazina OM, Mazin AV. (2011) Reconstituting the key steps of the DNA double-strand break repair in vitro. Methods Mol Biol. 745: 407-20.
64. *Bugreev, D. V., Pezza, R. J., Mazina, O. M., Voloshin, O. N., Camerini-Otero R. D., Mazin A. V. (2011) The resistance of DMC1 D-loops to dissociation may account for the DMC1 requirement in meiosis. Nature Struct. & Mol. Biol., 18: 56-60.
65. *Huang, F., Motlekar, N.A., Burgwin, C.M., Napper, A.D., Diamond, S.L., and Mazin, A.V. (2011). Identification of Specific Inhibitors of Human RAD51 Recombinase Using High-Throughput Screening. ACS Chemical Biology. 6: 628-635.
66. *Rossi, M.J., Mazina, O.M., Bugreev, D.V., and Mazin, A.V. (2011). The RecA/RAD51 protein drives migration of Holliday junctions via polymerization on DNA. Proc Natl Acad Sci USA 108: 6432-6437.
67. *Mazina, O.M., Rossi, M.J., Deakyne, J.S., Huang, F., and Mazin, A.V. (2012). Polarity and bypass of DNA heterology during branch migration of Holliday junctions by human RAD54, BLM, and RECQ1. J. Biol. Chem., 287 (15): 11820-11832.
68. *Huang, F., Mazina, O.M., Zentner, I J., Cocklin, S., and Mazin, A.V. (2012). Inhibition of homologous recombination in human cells by targeting RAD51 recombinase, J. Medicinal Chemistry., 55(7): 3011-20. This article was rated twice as a “must read” by Faculty of 1000.
69. *Deakyne, J.S., Huang, F., Negri, J., Tolliday, N., Cocklin, S., and Mazin, A.V. (2013). Analysis of the activities of RAD54, a SWI2/SNF2 protein, using a specific small-molecule inhibitor, J. Biol. Chem. 288: 31567-31580.
70. Rossi, M.J., and Mazin A.V. (2013) DNA repair and recombination. Encyclopedia of Biophysics. European Biophysical Societies' Association (EBSA). 10.1007/978-3-642-16712-6_436.
71. *Pezza, R.J., Voloshin, O.N., Volodin, A.A., Boateng, K.A., Bellani, M.A., Mazin, A.V., and Camerini-Otero, R.D. (2014). The dual role of HOP2 in mammalian meiotic homologous recombination. Nucleic Acids Res., 42: 2346-2357.
72. *Shahar, O.D., Kalousi, A., Eini, L., Fisher, B., Weiss, A., Darr, J., Mazina, O., Bramson, S., Kupiec, M., Eden, A., Meshorer E, Mazin AV, Brino L, Goldberg M, Soutoglou E. (2014). A high-throughput chemical screen with FDA approved drugs reveals that the antihypertensive drug Spironolactone impairs cancer cell survival by inhibiting homology directed repair. Nucleic Acids Res., 42: 5689-5701.
73. *Huang, F., and Mazin, A.V. (2014). Targeting the homologous recombination pathway by small molecule modulators. Bioorg. Med. Chem. Lett., 24: 3006-3013.
74. *Huang, F., and Mazin, A.V. (2014). A Small Molecule Inhibitor of Human RAD51 Potentiates Breast Cancer Cell Killing by Therapeutic Agents in Mouse Xenografts. PLoS ONE 9, e100993.
75. *Bugreev, D.V., Huang, F., Mazina, O.M., Pezza, R.J., Voloshin, O.N., Daniel Camerini-Otero, R., and Mazin, A.V. (2014). HOP2-MND1 modulates RAD51 binding to nucleotides and DNA. Nature Commun 5: 4198.
76. *Keskin, H., Shen, Y., Huang, F., Patel, M., Yang, T., Ashley, K., Mazin, A.V., and Storici, F. (2014) Transcript RNA-templated DNA recombination and repair. Nature, 515: 436-439.
77. *Martinez, J.S., C. von Nicolai, T. Kim, A. Ehlen, A.V. Mazin, S.C. Kowalczykowski and A. Carreira, (2016) BRCA2 regulates DMC1-mediated recombination through the BRC repeats. Proc. Natl. Acad. Sci. USA, 113(13): 3515-20.
78. *Kelso, A.A., S.D. Goodson, S. Chavan, A.F. Say, A. Turchick, D. Sharma, L.L. Ledford, E. Ratterman, K. Leskoske, A.V. King, C.C. Attaway, Y. Bandera, S.H. Foulger, A.V. Mazin, L.A. Temesvari and M.G. Sehorn, (2016) Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase. Mol Biochem Parasitol., 210 (1-2): 71-84.
79. *Hanamshet, K., O.M. Mazina and A.V. Mazin, (2016) Reappearance from Obscurity: Mammalian Rad52 in Homologous Recombination. Genes (Basel), 7(9): p. 63-81.
80. *Huang, F., Goyal, N., Sullivan, K., Hanamshet, K., Patel, M., Mazina, O.M., Wang, C.X., An, W.F., Spoonamore, J., Metkar, S. Kyle A. Emmitte, Simon Cocklin, Tomasz Skorski, and Alexander V. Mazin (2016) Targeting BRCA1- and BRCA2-deficient cells with RAD52 small molecule inhibitors. Nucleic Acids Res. 44: 4189-99
81. *Mazina, O.M., Keskin, H., Nahamshet, K., and Storici, F., Mazin, A.V., (2017) Rad52-inverse strand exchange drives RNA-templated DNA double-strand break repair. Molecular Cell, 67(1): p 19-29 3e. PMCID: PMC5547995.
82. *Goyal, N., Rossi, M.J., Mazina, O.M., Chi, Y., Moritz, R.L., Clurman B.E., Mazin A.V. (2018) RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions. Nature Comm., 9 (1): article number 34, doi:10.1038/s41467-017-02497-x. PMCID: PMC5750232.
83. *Mazina, O.M. and A.V. Mazin, (2018). Reconstituting the 4-Strand DNA Strand Exchange. Methods Enzymol,. 600: 285-305. PMCID: PMC6070308
84. *Sullivan-Reed, K., Bolton-Gillespie, E., Dasgupta, Y., Langer, S., Siciliano, M., Nieborowska-Skorska, M., Hanamshet, K., Belyaeva, E. A., Bernhardy, A. J., Lee, J., Moore, M., Zhao, H., Valent, P., Matlawska-Wasowska, K., Muschen, M., Bhatia, S., Bhatia, R., Johnson, N., Wasik, M. A., Mazin, A. V., and Skorski, T. (2018) Simultaneous Targeting of PARP1 and RAD52 Triggers Dual Synthetic Lethality in BRCA-Deficient Tumor Cells. Cell Rep., 23(11): 3127- 3136. PMCID: PMC6082171.
85. *Benitez, A., Liu, W., Palovcak, A., Wang, G., Moon, J., An, K., Kim, A., Zheng, K., Zhang, Y., Bai, F., Mazin, A.V., Pei, X.H., Yan, F., Zhang, Y. (2018). FANCA Promotes DNA Double-Strand Break Repair by Catalyzing Single-Strand Annealing and Strand Exchange. Mol Cell, 71(4): 621-628 e4. PMCID: PMC6097932.
86. *Wang, C.X., Jimenez-Sainz, J., Jensen, R.B., and Mazin, A.V. (2019). The Post-Synaptic Function of Brca2. Sci Rep., 9(1): 4554. PMCID: PMC6418147
87. *Chi, Y., Carter, J.H., Swanger, J., Mazin, A.V., Moritz, R.L., and Clurman, B.E. (2020). A novel landscape of nuclear human CDK2 substrates revealed by in situ phosphorylation. Sci Adv, 6(16), eaaz9899. PMCID: PMC7164936.
88. Meers, C., Keskin, H., Banyai, G., Mazina, O., Yang, T., Gombolay, A.L., Mukherjee, K., Kaparos, E.I., Newnam, G., Mazin, A. and Storici, F. (2020) Genetic characterization of three distinct mechanisms supporting RNAdriven DNA repair and modification reveals major role of DNA polymerase Zeta. Mol. Cell, 79(6): 1037-1050 e5. PMCID: PMC7502545.
89. *Hanamshet, K. and A.V. Mazin (2020). The function of RAD52 N-terminal domain is essential for viability of BRCA-deficient cells. Nucleic Acids Res, 48(22): 12778-12791. PMCID: PMC7736796
90. *Mazina, O.M., Somarowthu, S., Kadyrova, L.Y., Baranovskiy, A.G., Tahirov, T.H., Kadyrov, F.A., and A.V. Mazin (2020). Replication protein A binds RNA and promotes R-loop formation. J. Biol. Chem. 295(41): 14203-14213. PMCID: PMC7549048.
91. *Mazin, A.V. and Mazina O. M., (2021) Branch migration activity of Rad54 protein. Methods Mol Biol., 2153: 145-167. DOI: 10.1007/978-1-0716-0644- 5_11.
92. *Hanamshet, K. Hwang, N., Patel, M. Kulp, J., Lam, P., Du, Y. and A.V. Mazin (2020). Development and characterization of new generation of RAD52 inhibitors (in preparation).
93. Mazina, O.M. and A.V. Mazin, (2020). Characterization of inverse RNA strand exchagne activity of human RAD52 protein. (in preparation).
94. Shkundina, I.S., Dick, A., Cocklin, S., Gall, A.A. and A.V. Mazin (2020). New RAD51 inhibitors to improve the efficacy of anticancer therapy. (in preparation).
Book chapters:
1. Saparbaev M, Mazin A, Ovchinnikova L, Dianov G and Salganik R (1990) Insertion of new DNA sequences into plasmid by partially homologous singlestranded fragment DNA. In: Molecular Mechanisms of Genetic Process, Moscow, Nauka, 229-237. (Russian).
2. Mazin A V, and Kowalczykowski S C (1999) The synergistic interaction between RecA protein and SSB protein during DNA strand exchange. In: “Modern Concepts In Evolutionary Genetics”, Novosibirsk, Russia, Ed. V K Shumny, A L Markel. Novosibirsk, Nauka, 1999
3. Mazin A V (2002) An ensemble of proteins that repairs DNA double-stranded breaks in eukaryotes. In: Molecular Genetics, Biophysics, and Medicine Today (Bresler Memorial Lectures), ed. V.A. Lanzov, PNPI Press, St. Petersburg/Gatchina, p. 298-309.
4. Bugreev, D. V., Rossi, M. J., Mazina, O. M. and Mazin A V (2007). The Late Step of Homologous Recombination: Branch Migration of Holliday Junction. In: Molecular Genetics, Biophysics, and Medicine Today (Bresler Memorial Lectures), ed. V.A. Lanzov, PNPI Press, St. Petersburg/Gatchina, P. 141-158.
5. Mazin, A.V. and Mazina O. M., (2012). RAD51 is a key protein of homologous recombination in humans. In Advances DNA Repair in Cancer Therapy; eds L. Panasci, R. Aloyz, M. Alaoui-Jamali, 2nd Ed, Humana Press.
6. Mazin, A.V. and Mazina O. M., (2014). RAD51 and DMC1 recombinases. In Molecular Life Sciences. Springer Science + Business Media, New York.
Presentations
2002 Invited Speaker. Conference on Bioinformatics, Akademgorodok, Russia, “A Combinatorial Principle in Organization of the Homologous Recombination System in Eukaryotes”
2002 Invited Speaker. Peter the Great St. Petersburg Polytechnic University. Russia, “DNA Pairing Activity of Human Rad51C Protein”
2004 Invited Speaker. National Institutes of Health, Genetic and Biochemistry Section, Bethesda, MD “Ca2+ activates human proteins of recombinational DNA repair”.
2005 Speaker chosen from selected abstracts. Keystone Symposium of DNA Replication and Recombination. “The role of Ca2+ in activation of human homologous recombination proteins”.
2005 Invited Speaker. Sloan Kettering Cancer Center, New York, NY, “Ca2+ activates human proteins of recombinational DNA repair”
2006 Invited Speaker. Eppley Institute, University Nebraska Medical Center, Omaha, NE, “Who is Who in Recombinational DNA Repair in Humans”
2006 Invited Speaker. Conference on Physico-Chemical Biology, Akademgorodok, Russia, “Rad54 protein: the motor of genetic recombination”.
2006 Invited Speaker. University of Illinois, Urbana-Champaign. ”Rad54 protein: the motor of genetic recombination”
2007 Invited Speaker. FASEB Summer Conference on Genetic Recombination and Genome Rearrangements. Snowmass Village, CO, “Branch migration of Holliday junctions by Rad54”
2007 Invited Speaker. Rowan University, School of Osteopathic Medicine, Stratford, NJ, “Rad54 protein: the motor of genetic recombination”.
2008 Invited Speaker. The workshop Molecular and Clinical Mechanisms in Bloom's Syndrome and Related Disorders, Chicago, IL, “Pro- and anti-recombination activities of the Bloom’s syndrome helicase”.
2008 Invited Speaker. GCOE symposium at Tokyo Institute of Technology, Tokyo, Japan, “Novel activities of the Bloom’s syndrome helicase”
2008 Invited Speaker. The 6th 3R Symposium. Tsumagoi Resort, Japan, “Interaction of the Bloom’s Syndrome Helicase with RAD51 recombinase”
2008 Invited Speaker. Yokohama City University, Yokohama, Japan, “Branch migration of Holliday junctions in Homologous Recombination”
2008 Invited Speaker. National Institutes of Health, Genetic and Biochemistry Section, Bethesda, MD “Bloom’s syndrome helicase novel and surprising activities”.
2008 Invited Speaker. Conference on Fundamental Science to Medicine, Akademgorodok, Russia, “The function of Bloom’s syndrome helicase”.
2008 Invited Speaker. Conference on Bioinformatics, Akademgorodok, Russia, “Branch migration of Holliday junctions in Homologous Recombination”
2009 Invited Speaker. Unified Services University of Health Sciences, Bethesda, MD, “Bloom’s syndrome helicase and Rad54 protein: twins or antipodes of DNA repair?”
2009 Invited Speaker. Cantoblanco Workshop on Molecular Mechanisms of Genomic Stability. Madrid, Spain. “Branch Migration of Holliday Junctions by human RAD51” 2
009 Invited Speaker. National Institute on Aging, Baltimore, MD, “Rad54 protein and Bloom’s syndrome helicase: twins or antipodes of DNA repair?”
2009 Invited Speaker. Fels Institute for Cancer Research and Molecular Biology. Temple University Lewis Katz School of Medicine. Philadelphia, PA, “Helicase-like and non-helicase-like motor proteins in biology and medicine”.
2009 Invited Speaker. Temple University Lewis Katz School of Medicine. Philadelphia, PA, “Bloom’s syndrome helicase and Rad54 protein: twins or antipodes of DNA repair?”.
2009 Invited Speaker. University of Pennsylvania Veterinary School. Philadelphia, PA, “New Insights in Branch Migration of Holliday junctions”.
2010 Invited Speaker. Conference on Bioinformatics, Akademgorodok, Russia, “Why does RecA/RAD51 need ATP hydrolysis?”
2011 Invited Speaker. Fox Chase Cancer Center, Philadelphia, PA, “Why does RecA/RAD51, a key homologous recombination protein, hydrolyze ATP?”.
2011 Invited Speaker, Conference on Physico-Chemical Biology, Novosibirsk, Russia, “Basic and translational studies on homologous recombination in humans”.
2011 Invited Speaker, Institute of Chemical Biology and Fundamental Medicine, Novosibirsk, Russia, “Interaction of the Bloom’s Syndrome Helicase with RAD51 recombinase”.
2013 Invited Speaker, Saint Louis University, Saint Louis, “New insights in regulation of human RAD51 activities”.
2013 Invited Speaker, Institute for Biotechnology & Virology Research, DUCOM, Doylestown, Pennsylvania, “New insights in regulation of human RAD51 activities”.
2014 Invited Speaker, Institut Curie, Orsay, France, “New insights in regulation of human RAD51 activities”.
2014 Invited Speaker, Basser Conference, University of Pennsylvania, Philadelphia, “Targeting the homologous recombination machinery with small molecules”.
2014 Invited Speaker, A Children Hospital of Philadelphia-Drexel University-Hebrew University Collaborative Symposium, Advancing the healthcare of Children Symposium, Philadelphia, “Inhibition of Homologous Recombination in Human Cells by Targeting RAD51 Recombinase”.
2014 Invited Speaker, Pennsylvania State University Hershey, Hershey, PA, USA, “New insights in regulation of human RAD51 recombinase”.
2014 Invited Speaker, Gordon Research conference. Medicinal Chemistry. ColbySawyer College, New London, NH, USA, “Small Molecule Inhibitors of the Homologous Recombination Proteins”.
2014 Invited Speaker, Temple University, Fels Institute, Philadelphia, PA, “RAD51 recombinase is the main genome guardian in humans: new mechanistic insights and development of anticancer therapies”.
2015 Invited Speaker, International RecA and chromosome biology conference, Taiwan, Taipei, “Novel pairing process promoted by human RAD52 protein”.
2015 Invited Speaker, Penn Genome Integrity Group, University of Pennsylvania, Philadelphia, PA, “RAD52 protein: genome guardian and therapeutic target”.
2015 Invited Speaker, Thomas Jefferson University, Molecular Biology and Genetics Group, Philadelphia, PA, “RAD52 protein: genome guardian and therapeutic target”.
2015 Invited Speaker, Sidney Kimmel Cancer Center Consortium Basic Scientific Retreat, Philadelphia, PA, “Targeting recombinational DNA repair with small molecule inhibitors”
2016 Invited Speaker, Thomas Jefferson University, Philadelphia, PA, “DNA double strand break repair: mechanisms and applications for cancer therapy”
2016 Invited Speaker, Clinical & Translational Research Institute Symposium, Philadelphia, PA, “Development of targeted therapy against BRCA-deficient familial breast cancer”.
2016 Invited Speaker, Thomas Jefferson University, Philadelphia, PA, “Enhancing DNA damage sensitivity of AML cells by inhibiting DNA repair proteins”
2016 Invited Speaker, Mechanisms of Genome Maintenance, International symposium, University of California, Davis, CA, “Driving RAD52 in inverse”.
2017 Invited Speaker, Clemson College, Clemson, SC, “RAD52 protein: genome guardian and therapeutic target”.
2017 Invited Speaker, Coulter-Drexel Board, Philadelphia, PA, “Development of targeted therapy against BRCA-deficient breast cancer and ovarian cancer”
2017 Invited Speaker, Thomas Jefferson University, Breast Cancer Group, Philadelphia, PA, “RAD52 protein as a therapeutic target for BRCA-deficient cancers”.
2017 Invited Speaker, Hengrui Corp, Princeton, NJ, “Targeting recombinational DNA repair with small molecule inhibitors”.
2017 Invited Speaker, University of Nebraska Medical Center, Omaha, NE, “RAD52 protein: genome guardian and therapeutic target”.
2018 Invited Speaker, Boston University School of Medicine, Boston, MA, “RAD52 protein: genome guardian and therapeutic target”.
2019 Invited Speaker, Georgia Institute of Technology, Atlanta, GA, “RAD52 protein: genome guardian and therapeutic target”.
2019 Invited Speaker, Blumberg Institute, Doylestown, PA, “RAD52 protein: genome guardian and therapeutic target”.
2019 Invited Speaker, Southern Illinois University Carbondale, Carbondale, IL, “RAD52 protein: genome guardian and therapeutic target”.
2019 Invited Speaker, Virtici, LLC, Seattle, WA “Development of RAD52 inhibitors”
2019 Invited Speaker, Jefferson University, Philadelphia, PA, “RAD52 protein: genome guardian and therapeutic target”.
2020 Invited Speaker, Cyteir Therapeutics, Lexington, MA, “RAD52 protein: genome guardian and therapeutic target”
2020 Invited Speaker, 28-7 Therapeutics, Cambridge, MA, “Development of RAD52 inhibitors against BRCA-deficient cancers”
2020 Invited Speaker, Rain Therapeutics, Newark, CA, “RAD52 protein: genome guardian and therapeutic target”
2020 Invited Speaker, University of Texas Health Science Center, San Antonio, TX, “RAD52 protein: genome guardian and therapeutic target”
2021 Invited Speaker, Thomas Jefferson University, Philadelphia, PA, “"Targeting DNA