An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. - Wikidata - wikimedia - TriplyDB

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

http://www.wikidata.org/entity/Q43077852

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MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity Mechanism and evolution of DNA primases Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease The role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseases Structure of the DNA Repair Helicase XPD Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase Crystal structure of the C-terminal domain of human DNA primase large subunit Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore Mechanism for priming DNA synthesis by yeast DNA Polymerase α Structures of human primase reveal design of nucleotide elongation site and mode of Pol tethering A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast.A conserved motif in the C-terminal tail of DNA polymerase α tethers primase to the eukaryotic replisome.Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis.The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species.Identification of vital and dispensable sulfur utilization factors in the Plasmodium apicoplast The Cell Killing Mechanisms of Hydroxyurea Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes DNA polymerases at the eukaryotic fork-20 years later DNA polymerase δ and ζ switch by sharing accessory subunits of DNA polymerase δ Genetic instability in budding and fission yeast-sources and mechanisms The first cellular models based on frataxin missense mutations that reproduce spontaneously the defects associated with Friedreich ataxia A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster Redox Signaling through DNA Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome Altered gene expression and DNA damage in peripheral blood cells from Friedreich's ataxia patients: cellular model of pathology.An iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ε.The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain.Functional genomics analysis of the Saccharomyces cerevisiae iron responsive transcription factor Aft1 reveals iron-independent functions.DNA-mediated charge transport in redox sensing and signaling The C-terminal domain of the DNA polymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complex Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2.Parasites FeS up: iron-sulfur cluster biogenesis in eukaryotic pathogens.White spot syndrome virus protein kinase 1 defeats the host cell's iron-withholding defense mechanism by interacting with host ferritin.Global phylogenomic analysis disentangles the complex evolutionary history of DNA replication in archaea.Crystal structure of the human primase Essential role of the iron-sulfur cluster binding domain of the primase regulatory subunit Pri2 in DNA replication initiation.Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.

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P2860

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

http://www.wikidata.org/entity/Q43077852

description

2007 nî lūn-bûn

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name

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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type

label

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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prefLabel

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

@en

An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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Nature Structural & Molecular Biology

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An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis.

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Joseph D Maman

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Luca Pellegrini

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Sebastian Klinge

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P2860

Affinity labeling of the active center and ribonucleoside triphosphate binding site of yeast DNA primase.

Expression, purification, and characterization of the two human primase subunits and truncated complexes from Escherichia coli

Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit.

Structure of the heterodimeric core primase.

A single essential gene, PRI2, encodes the large subunit of DNA primase in Saccharomyces cerevisiae.

A DNA primase activity associated with DNA polymerase alpha from Drosophila melanogaster embryos.

Isolation of an intact DNA polymerase-primase from embryos of Drosophila melanogaster

The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus.

Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication.

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