Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.
about
Antimutator variants of DNA polymerasesYeast Dun1 Kinase Regulates Ribonucleotide Reductase Small Subunit Localization in Response to Iron Deficiency.Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.The Cell Killing Mechanisms of HydroxyureaIxr1 is required for the expression of the ribonucleotide reductase Rnr1 and maintenance of dNTP poolsDif1 controls subcellular localization of ribonucleotide reductase by mediating nuclear import of the R2 subunitNormally lethal amino acid substitutions suppress an ultramutator DNA Polymerase δ variantConserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesisRibonucleotide reductase metallocofactor: assembly, maintenance and inhibition.Evaluation of bendamustine in combination with fludarabine in primary chronic lymphocytic leukemia cells.Natural polymorphism in BUL2 links cellular amino acid availability with chronological aging and telomere maintenance in yeast.Yeast Dun1 kinase regulates ribonucleotide reductase inhibitor Sml1 in response to iron deficiencyThe ribonucleotide reductase inhibitor, Sml1, is sequentially phosphorylated, ubiquitylated and degraded in response to DNA damageMechanisms of mutagenesis in vivo due to imbalanced dNTP pools.Genome-wide single-cell-level screen for protein abundance and localization changes in response to DNA damage in S. cerevisiae.Ribosome synthesis-unrelated functions of the preribosomal factor Rrp12 in cell cycle progression and the DNA damage response.Increased Rrm2 gene dosage reduces fragile site breakage and prolongs survival of ATR mutant mice.dNTP pool levels modulate mutator phenotypes of error-prone DNA polymerase ε variants.Regulation of ribonucleotide reductase in response to iron deficiency.Endogenous DNA replication stress results in expansion of dNTP pools and a mutator phenotypeDampening DNA damage checkpoint signalling via coordinated BRCT domain interactions.Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1Mutations in the Non-Catalytic Subunit Dpb2 of DNA Polymerase Epsilon Affect the Nrm1 Branch of the DNA Replication Checkpoint.MEK2 regulates ribonucleotide reductase activity through functional interaction with ribonucleotide reductase small subunit p53R2.S phase block following MEC1ATR inactivation occurs without severe dNTP depletion.Telomere length homeostasis responds to changes in intracellular dNTP pools.RAD53 is limiting in double-strand break repair and in protection against toxicity associated with ribonucleotide reductase inhibitionProfiling DNA damage-induced phosphorylation in budding yeast reveals diverse signaling networksChromosome Duplication in Saccharomyces cerevisiae.Molecular basis of the essential s phase function of the rad53 checkpoint kinase.Spd1 accumulation causes genome instability independently of ribonucleotide reductase activity but functions to protect the genome when deoxynucleotide pools are elevated.Cytoplasmic localization of Hug1p, a negative regulator of the MEC1 pathway, coincides with the compartmentalization of Rnr2p-Rnr4p.The Intra-S Checkpoint Responses to DNA Damage.Eukaryotic DNA damage checkpoint activation in response to double-strand breaks.Surviving chromosome replication: the many roles of the S-phase checkpoint pathway.The DNA damage checkpoint response to replication stress: A Game of Forks.DNA damage response: three levels of DNA repair regulation.P53 suppresses ribonucleotide reductase via inhibiting mTORC1.S-phase checkpoint regulations that preserve replication and chromosome integrity upon dNTP depletion.The available SRL3 deletion strain of Saccharomyces cerevisiae contains a truncation of DNA damage tolerance protein Mms2: Implications for Srl3 and Mms2 functions.
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P2860
Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@ast
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@en
type
label
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@ast
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@en
prefLabel
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@ast
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@en
P2093
P2860
P1433
P1476
Dif1 is a DNA-damage-regulated ...... for ribonucleotide reductase.
@en
P2093
Joanne Stubbe
Stephen J Elledge
Yang David Lee
P2860
P356
10.1016/J.MOLCEL.2008.08.018
P577
2008-10-01T00:00:00Z