1996
DOI: 10.1016/0161-5890(95)00125-5
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Characterization of an endonuclease activity which preferentially cleaves the G-rich immunoglobulin switch repeat sequences

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Cited by 17 publications
(10 citation statements)
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“…In an effort to identify a novel nuclease activity involved in immunoglobulin isotype switch recombination, work from our laboratory identified Endo-SR, which preferentially cleaved DNA within switch recombination sequences (Lyon et al, 1996;Lyon and Aguilera, 1997). Furthermore, Endo-SR exhibited an acid pH optimum and functioned independently of divalent cations.…”
Section: Identification and Characterization Of The Mammalian Dnase Imentioning
confidence: 98%
See 1 more Smart Citation
“…In an effort to identify a novel nuclease activity involved in immunoglobulin isotype switch recombination, work from our laboratory identified Endo-SR, which preferentially cleaved DNA within switch recombination sequences (Lyon et al, 1996;Lyon and Aguilera, 1997). Furthermore, Endo-SR exhibited an acid pH optimum and functioned independently of divalent cations.…”
Section: Identification and Characterization Of The Mammalian Dnase Imentioning
confidence: 98%
“…Furthermore, Endo-SR exhibited an acid pH optimum and functioned independently of divalent cations. Endo-SR was subsequently purified to homogeneity from bovine spleen and subjected to peptide microsequencing (Lyon et al, 1996;Lyon, 1997;Lyon and Aguilera, 1997). Three separate peptide sequences were obtained from this analysis and compared to database sequences.…”
Section: Identification and Characterization Of The Mammalian Dnase Imentioning
confidence: 99%
“…Consistent with a generalized role in DNA degradation and an acidic pH optima, DNase II enzymes exhibit a ubiquitous tissue distribution and are localized within lysosomes [1,3]. While DNase II enzymes can degrade DNA substrates to completion, they also exhibit cleavage preferences that are site-and speciesspecific [1,[4][5][6].…”
Section: Introductionmentioning
confidence: 95%
“…By using a biochemical approach, Lion et al (43,44) isolated and purified a protein with endonuclease activity (Endo-SR) from murine and bovine spleen that could specifically recognize and cleave GC-rich switch region DNA sequences. The human analog of Endo-SR has not been described and the cloning of the gene encoding Endo-SR has not yet been reported.…”
Section: Other Candidate Proteins In Csrmentioning
confidence: 99%