Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase
about
Structures to complement the archaeo-eukaryotic primases catalytic cycle description: What's next?Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primaseCrystal structure of the C-terminal domain of human DNA primase large subunitCryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactorsCrystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophoreStructures of human primase reveal design of nucleotide elongation site and mode of Pol tetheringInsights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA PrimaseStructural Basis for the Interaction of a Hexameric Replicative Helicase with the Regulatory Subunit of Human DNA Polymerase -PrimaseA primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primaseA photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur clusterMechanism of Concerted RNA-DNA Primer Synthesis by the Human PrimosomeAn iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ε.The C-terminal domain of the DNA polymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complexEssential functions of iron-requiring proteins in DNA replication, repair and cell cycle control.A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2.Crystal structure of the human primaseEssential role of the iron-sulfur cluster binding domain of the primase regulatory subunit Pri2 in DNA replication initiation.Insight into the Human DNA Primase Interaction with Template-Primer.Crystallization and preliminary X-ray diffraction analysis of human DNA primase.The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transportFlexible tethering of primase and DNA Pol α in the eukaryotic primosome.Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster.Crystal Structures of Bacterial (6-4) Photolyase Mutants with Impaired DNA Repair Activity.Novel Families of Archaeo-Eukaryotic Primases Associated with Mobile Genetic Elements of Bacteria and Archaea.The elemental role of iron in DNA synthesis and repair.A Prokaryotic (6-4) Photolyase with a DMRL Chromophore and an Iron-Sulfur Cluster
P2860
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P2860
Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@ast
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@en
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@nl
type
label
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@ast
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@en
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@nl
prefLabel
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@ast
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@en
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@nl
P2093
P2860
P1433
P1476
Shared Active Site Architectur ...... tic Primase and DNA Photolyase
@en
P2093
Joseph D Maman
Luca Pellegrini
Ludovic Sauguet
Rajika L Perera
Sebastian Klinge
P2860
P304
P356
10.1371/JOURNAL.PONE.0010083
P407
P577
2010-04-09T00:00:00Z