A prominent β-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.
about
Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaTUnwinding and rewinding: double faces of helicase?Single-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding.Structure of the RecQ C-terminal domain of human Bloom syndrome proteinCrystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changesHuman RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structuresThe structural biology of CRISPR-Cas systemsMutations in RECQL Gene Are Associated with Predisposition to Breast CancerBorrowing nuclear DNA helicases to protect mitochondrial DNA.Catalytic strand separation by RECQ1 is required for RPA-mediated response to replication stress.RECQL5 has unique strand annealing properties relative to the other human RecQ helicase proteins.DNA repair and replication fork helicases are differentially affected by alkyl phosphotriester lesion.The Q motif of Fanconi anemia group J protein (FANCJ) DNA helicase regulates its dimerization, DNA binding, and DNA repair function.Human RecQ helicases in DNA repair, recombination, and replication.DNA-conjugated gold nanoparticles based colorimetric assay to assess helicase activity: a novel route to screen potential helicase inhibitorsInteraction of T4 UvsW helicase and single-stranded DNA binding protein gp32 through its carboxy-terminal acidic tail.Superfamily 2 helicasesHuman RECQ1 promotes restart of replication forks reversed by DNA topoisomerase I inhibition.A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.Probing Genome Maintenance Functions of human RECQ1.Molecular mechanism of double Holliday junction dissolution.Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding.The Human RecQ4 Helicase Contains a Functional RecQ C-terminal Region (RQC) That Is Essential for Activity.The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains.Fork sensing and strand switching control antagonistic activities of RecQ helicases.The Q Motif Is Involved in DNA Binding but Not ATP Binding in ChlR1 Helicase.On BLM helicase in recombination-mediated telomere maintenance.RecQ and Fe-S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions.Structural and functional aspects of winged-helix domains at the core of transcription initiation complexes.New Insights Into DNA Helicases as Druggable Targets for Cancer TherapySingle molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB
P2860
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P2860
A prominent β-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
A prominent β-hairpin structur ...... inding and oligomer formation.
@en
type
label
A prominent β-hairpin structur ...... inding and oligomer formation.
@en
prefLabel
A prominent β-hairpin structur ...... inding and oligomer formation.
@en
P2093
P2860
P50
P356
P1476
A prominent β-hairpin structur ...... winding and oligomer formation
@en
P2093
Alessandro Vindigni
Bojana Lucic
Frank H Niesen
Matteo Berti
Nicola A Burgess-Brown
Ramiro Mendoza-Maldonado
Ying Zhang
P2860
P304
P356
10.1093/NAR/GKQ1031
P577
2010-11-08T00:00:00Z