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2 research outcomes, page 1 of 1
- publication . Article . 2018Open Access EnglishAuthors:Maria Loressa Uson; Ayala Carl; Yehuda Goldgur; Stewart Shuman;doi: 10.1093/nar/gky238pmc: PMC5934675pmid: 29635474Publisher: Oxford University PressProject: NIH | Pixel Array Detector for ... (1S10RR029205-01), NIH | NE-CAT Center for Advance... (4P41GM103403-14), NIH | MOUSE GENETICS (2P30CA008748-43), NIH | DNA Ligases in Mycobacter... (5R01AI064693-03)
Abstract Mycobacterium smegmatis FenA is a nucleic acid phosphodiesterase with flap endonuclease and 5′ exonuclease activities. The 1.8 Å crystal structure of FenA reported here highlights as its closest homologs bacterial FEN-family enzymes ExoIX, the Pol1 exonuclease ...
- publication . Article . 2020Open Access EnglishAuthors:Shreya Ghosh; Yehuda Goldgur; Stewart Shuman;doi: 10.1093/nar/gkaa075pmc: PMC7102940pmid: 32034423Publisher: Oxford University PressProject: NIH | Pixel Array Detector for ... (1S10RR029205-01), NIH | NE-CAT Center for Advance... (4P41GM103403-14), NIH | MOUSE GENETICS (2P30CA008748-43), NIH | Mechanisms of DNA and RNA... (1R35GM126945-01), NIH | DNA Ligases in Mycobacter... (5R01AI064693-03)
<jats:title>Abstract</jats:title> <jats:p>Mycobacterial Pol1 is a bifunctional enzyme composed of an N-terminal DNA flap endonuclease/5′ exonuclease domain (FEN/EXO) and a C-terminal DNA polymerase domain (POL). Here we document additional functions of Pol1: FEN activit...
2 research outcomes, page 1 of 1