BLM unfolds G-quadruplexes in different structural environments through different mechanisms
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Title
BLM unfolds G-quadruplexes in different structural environments through different mechanisms
Authors
Keywords
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Journal
NUCLEIC ACIDS RESEARCH
Volume 43, Issue 9, Pages 4614-4626
Publisher
Oxford University Press (OUP)
Online
2015-04-21
DOI
10.1093/nar/gkv361
References
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Related references
Note: Only part of the references are listed.- Molecular mechanism of G-quadruplex unwinding helicase: sequential and repetitive unfolding of G-quadruplex by Pif1 helicase
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- TRF1 negotiates TTAGGG repeat-associated replication problems by recruiting the BLM helicase and the TPP1/POT1 repressor of ATR signaling
- (2014) Michal Zimmermann et al. GENES & DEVELOPMENT
- G quadruplexes are genomewide targets of transcriptional helicases XPB and XPD
- (2014) Lucas T Gray et al. Nature Chemical Biology
- G-quadruplex conformation and dynamics are determined by loop length and sequence
- (2014) Ramreddy Tippana et al. NUCLEIC ACIDS RESEARCH
- RecQ-core of BLM unfolds telomeric G-quadruplex in the absence of ATP
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- Regulation of gene expression by the BLM helicase correlates with the presence of G-quadruplex DNA motifs
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- Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures
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- Pif1 family helicases suppress genome instability at G-quadruplex motifs
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- Srs2 prevents Rad51 filament formation by repetitive motion on DNA
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- Replication Protein A Unfolds G-Quadruplex Structures with Varying Degrees of Efficiency
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- BLM helicase measures DNA unwound before switching strands and hRPA promotes unwinding reinitiation
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