Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Viswanath Bandaru"'
Autor:
Peter Lipsky, Patrick T. Vallano, Jeffrey Smith, Walter Owens, Daniel Snider, Viswanath Bandaru, Yunfu Sun, Ross Wallingford, Joseph Duncan, Joshua Lewis, Jason Southall, Azeem Ansari, Hong Li
Publikováno v:
Frontiers in Pharmacology, Vol 12 (2021)
The objective of the current work was to demonstrate the equivalence of Mylan’s glatiramer acetate (GA) to that of the reference product Copaxone® (COP) using the four criteria for active pharmaceutical ingredient sameness as established by the US
Externí odkaz:
https://doaj.org/article/6c8856da14af4e719f4464db96b5733b
Autor:
Wendy J. Cannan, Susan S. Wallace, Viswanath Bandaru, Minmin Liu, April M. Averill, Alicia Holmes
Publikováno v:
Protein Expression and Purification. 84:130-139
Endonuclease VIII-like 3 (Neil3) is one of the five DNA glycosylases found in mammals that recognize and remove oxidized bases, and initiate the Base Excision Repair (BER) pathway. Previous attempts to express and purify the mouse and human orthologs
Autor:
Shigenori Iwai, Pawel Jaruga, Yin Guo, Cynthia J. Burrows, Jeffrey P. Bond, Viswanath Bandaru, Miral Dizdaroglu, Xiaobei Zhao, Susan S. Wallace
Publikováno v:
DNA Repair. 9:177-190
The DNA glycosylases that remove oxidized DNA bases fall into two general families: the Fpg/Nei family and the Nth superfamily. Based on protein sequence alignments, we identified four putative Fpg/Nei family members, as well as a putative Nth protei
Publikováno v:
Protein Expression and Purification. 65:230-237
A putative DNA glycosylase encoded by the Rv3297 gene (MtuNei2) has been identified in Mycobacterium tuberculosis. Our efforts to express this gene in Escherichia coli either by supplementing tRNAs for rare codons or optimizing the gene with preferre
Autor:
Viswanath Bandaru, Cynthia J. Burrows, Jeffrey P. Bond, Miral Dizdaroglu, Michael R. Newton, Ramiro Barrantes-Reynolds, Susan S. Wallace, Scott D. Kathe, Pawel Jaruga
Publikováno v:
DNA Repair. 8:643-653
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 pr
Publikováno v:
Structure. 17:703-712
SummaryAmong the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8-dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognize
Autor:
Ramiro Barrantes-Reynolds, Susan M. Robey-Bond, Jeffrey P. Bond, Viswanath Bandaru, Susan S. Wallace
Publikováno v:
Biochemistry. 47:7626-7636
During repair of damaged DNA, the oxidized base 8-oxoguanine (8-oxoG) is removed by 8-oxoguanine—DNA glycosylase (Ogg) in eukaryotes and most archaea, whereas in most bacteria it is removed by formamidopyrimidine—DNA glycosylase (Fpg). We report
Autor:
T. C. Wu, Chanjuan Shi, Craig N. Morrell, J. Stephen Dumler, Soo Chin Lee, Antony R. Parker, Li Hua, James R. Eshleman, Viswanath Bandaru
Publikováno v:
Journal of Antimicrobial Chemotherapy. 61:262-272
Several therapeutic strategies that target nucleic acids exist; however, most approaches target messenger RNA, rather than genomic DNA. We describe a novel oligonucleotide-based strategy, called anti-gene padlocks (AGPs), which eliminate Escherichia
Publikováno v:
DNA Repair. 2:441-453
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:1142-1144
DNA glycosylases repair oxidative DNA damage caused by free radicals. Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types