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Search Publications by: Pawel Jaruga (Fed)

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Displaying 126 - 150 of 224

Copper oxide nanoparticle mediated DNA damage in terrestrial plant models

December 22, 2011
Author(s)
Bryant C. Nelson, Donald H. Atha, Elijah J. Petersen, Huanhua Wang, Danielle Cleveland, Richard D. Holbrook, Pawel Jaruga, M Miral Dizdar, Baoshan Xing
Engineered nanoparticles, due to their unique electrical, mechanical and catalytic properties, are presently found in many commercial products and will be intentionally or inadvertently released at increasing concentrations into the natural environment

Evidence for upregulated repair of oxidatively induced DNA damage in human colorectal cancer

September 15, 2011
Author(s)
M Miral Dizdar, Pawel Jaruga, Prasad T. Reddy, Guldal Kirkali, Didem Keles, Gulgun Oktay, Aras E. Canda
Molecular pathways that play a role in the development of colorectal cancer involve multiple genetic changes in cancer-related genes that may be caused by overproduction of oxygen-derived species including free radicals, which are capable of damaging DNA

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
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