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Displaying 76 - 100 of 123

Stable isotope-labeling of DNA repair proteins, and their purification and characterization

July 1, 2011
Author(s)
M Miral Dizdar, Pawel Jaruga, Prasad T. Reddy, Bryant C. Nelson, Mark S. Lowenthal
Reduced DNA repair capacity is associated with increased risk for a variety of disease processes including carcinogenesis. Thus, DNA repair proteins have the potential to be used as important predictive, prognostic and therapeutic biomarkers in cancer and

A Major Role for Non-Enzymatic Antioxidant Processes in the Radioresistance of Halobacterium salinarum

April 1, 2011
Author(s)
M Miral Dizdar, Pawel Jaruga, Courtney K. Robinson, Kim Webb, Amardeep Kaur, Nitin S. Baliga, Allen Place, Jocelyne DiRuggiero
Oxidative stress occurs when the generation of reactive oxygen species (ROS) exceeds the capacity of the cell’s endogenous systems to neutralize them. We analyzed the oxidative stress responses and cellular damage of the archaeon Halobacterium salinarum

The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo

March 16, 2010
Author(s)
Minin Liu, Viswanath Bandaru, Jeffrey Bond, Pawel Jaruga, Xiaobei Zhao, Plamen P. Christov, Cynthia Burrows, Carmelo J. Rizzo, Miral M. Dizdar, Susan Wallace
To protect cells from oxidative DNA damage and mutagenesis, organisms possess multiple glycosylases to recognize the damaged bases and to initiate the Base Excision Repair (BER) pathway. Recently, three DNA glycosylases were identified in mammals that are

The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate specificities from their Escherichia coli counterparts

February 4, 2010
Author(s)
Yin Guo, Viswanath Bandaru, Pawel Jaruga, Xiaobei Zhao, Cynthia Burrows, Shigenori Iwai, Miral M. Dizdar, Jeffrey Bond, Susan Wallace
The DNA glycosylases function in the first step of the base excision repair process that is responsible for removing endogenous oxidative purine and pyrimidine damages from DNA. The DNA glycosylases that remove oxidized DNA bases fall into two general

Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase

September 1, 2009
Author(s)
Viktoriya Sidorenko, Arthur P. Grollman, Pawel Jaruga, Miral M. Dizdar, Dmitry Zharhov
Human 8-oxoguanine-DNA-glycosylase (OGG1) efficiently removes mutagenic 8-oxoguanine (8-oxoGua) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) when paired with cytosine in damaged DNA. Excision of 8-oxoGua mispaired with adenine may lead to GT

Plant and fungal Fpg homologs are formamidopyrimidine DNA glycosylases but not 8-oxoguanine DNA glycosylases

May 1, 2009
Author(s)
Scott D. Kathe, Ramiro Barrantes-Reynolds, Pawel Jaruga, Michael Newton, Cynthia Burrows, Viswanath Bandaru, Miral M. Dizdar, Jeffrey Bond, Susan Wallace
Formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) share an overall common three dimensional structure and primary amino acid sequence in conserved structural motifs but have different substrate specificities, with bacterial Fpg proteins

Measurement of formamidopyrimidines in DNA

December 15, 2008
Author(s)
Pawel Jaruga, Guldal Kirkali, Miral M. Dizdar
Formamidopyrimidines, 4,6-diamino-5-formamidopyrimidine (FapyAde) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua), are among major lesions in DNA generated by hydroxyl radical attack, UV radiation or photosensitization in vitro and in vivo

Structural alterations in breast stromal and epithelial DNA: the influence of 8,5'-cyclo-2'-deoxyadenosine

June 1, 2006
Author(s)
K. M. Anderson, Pawel Jaruga, C. R. Ramsey, N. K. Gilman, V. M. Green, S. W. Rostad, J. T. Emerman, M Miral Dizdar, D. C. Malins
(5'S)-8,5'-Cyclo-2'-deoxyadenosine (S-cdA), which arises from the reaction of the hydroxyl radical (*OH) with 2'-deoxyadenosine in DNA, is a lesion comprising a base-sugar linkage that distorts the DNA backbone. This structure impedes transcription and

Repair of Formamidopyrimidines in DNA Involves Different Glycosylases - Role of the OGG1, NTH1, and NEIL1 Enzymes

December 9, 2005
Author(s)
J Hu, N de Souza-Pinto, K Haraguchi, Barbara A. Hogue, Pawel Jaruga, M M. Greenberg, Miral M. Dizdar, V. Bohr
2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino-5-formamidopyrimidine (FapyA), are formed abundantly in DNA of cultured cells or tissues exposed to ionizing radiation or to other free radical-generating systems. We show here that FapyG

Oxidative DNA Damage: Induction, Repair and Significance

September 1, 2004
Author(s)
M D. Evans, Miral M. Dizdar, M S. Cooke
The generation of reactive oxygen species may be both beneficial to cells, performing a function in inter- and intra-cellular signaling, and detrimental, modifying cellular bimolecules, accumulation of which has been associated with numerous diseases. Of
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