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Anthony T. Yeung
Researcher at Fox Chase Cancer Center
Publications - 84
Citations - 4117
Anthony T. Yeung is an academic researcher from Fox Chase Cancer Center. The author has contributed to research in topics: DNA & UvrABC endonuclease. The author has an hindex of 31, co-authored 74 publications receiving 3989 citations. Previous affiliations of Anthony T. Yeung include University of Washington.
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Journal ArticleDOI
High-Throughput Screening for Induced Point Mutations
Trenton Colbert,Bradley J. Till,Rachel Tompa,Steve H. Reynolds,Michael N. Steine,Anthony T. Yeung,Claire M. McCallum,Luca Comai,Steven Henikoff +8 more
TL;DR: Adaptations of the targeting induced local lesions in genomes are reported, which help to understand gene function and effective reverse genetic strategies are increasingly in demand.
Journal ArticleDOI
Mutation detection using a novel plant endonuclease
TL;DR: The results indicate that CEL I mutation detection is a highly sensitive method for detecting both polymorphisms and disease-causing mutations in DNA fragments as long as 1120 bp in length.
Journal Article
Enhanced cisplatin cytotoxicity by disturbing the nucleotide excision repair pathway in ovarian cancer cell lines.
TL;DR: It is suggested that it is possible to substantially enhance the cisPlatin cytotoxicity by disturbing the NER pathway in cisplatin-resistant cell lines and to enhance the survival capacity of mice in an ovarian cancer xenograft model.
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MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1.
Alfonso Bellacosa,Lucia Cicchillitti,Filippo Schepis,Antonio Riccio,Anthony T. Yeung,Yoshihiro Matsumoto,Erica A. Golemis,Maurizio Genuardi,Giovanni Neri +8 more
TL;DR: It is suggested that MED1 is a novel human DNA repair protein that may be involved in MMR and, as such, may be a candidate eukaryotic homologue of the bacterial MMR endonuclease, MutH.
Journal ArticleDOI
Biphasic Kinetics of the Human DNA Repair Protein MED1 (MBD4), a Mismatch-specific DNA N-Glycosylase
Fiorella Petronzelli,Fiorella Petronzelli,Antonio Riccio,George D. Markham,Steven H. Seeholzer,Jay Stoerker,Maurizio Genuardi,Anthony T. Yeung,Yoshihiro Matsumoto,Alfonso Bellacosa,Alfonso Bellacosa +10 more
TL;DR: It is shown that MED1 functions as a mismatch-specific DNA N-glycosylase active on thymine, uracil, and 5-fluorouracil when these bases are opposite to guanine, and that the 5-methylcytosine binding domain and methylation of the mismatched CpG site are not required for efficient catalysis.