about
Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosisA role for Saccharomyces cerevisiae histone H2A in DNA repair.A novel Rad24 checkpoint protein complex closely related to replication factor C.Repression of G1/S transcription is mediated via interaction of the GTB motifs of Nrm1 and Whi5 with Swi6.Checkpoint activation in response to double-strand breaks requires the Mre11/Rad50/Xrs2 complexThe RSF1 histone-remodelling factor facilitates DNA double-strand break repair by recruiting centromeric and Fanconi Anaemia proteinsSite-specific phosphorylation of the DNA damage response mediator rad9 by cyclin-dependent kinases regulates activation of checkpoint kinase 1Regulation of the DNA damage response and gene expression by the Dot1L histone methyltransferase and the 53Bp1 tumour suppressorMobility and distribution of replication protein A in living cells using fluorescence correlation spectroscopy.Genetic evidence for single-strand lesions initiating Nbs1-dependent homologous recombination in diversification of Ig v in chicken B lymphocytes.Differential Response of Mouse Thymic Epithelial Cell Types to Ionizing Radiation-Induced DNA Damage.Rational design and validation of a Tip60 histone acetyltransferase inhibitor.Sensing and responding to DNA damage.Dynamics of Rad9 chromatin binding and checkpoint function are mediated by its dimerization and are cell cycle-regulated by CDK1 activityATR-ATRIP kinase complex triggers activation of the Fanconi anemia DNA repair pathway.Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damageThe MRN complex: coordinating and mediating the response to broken chromosomes.The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its functionBinding specificity of the G1/S transcriptional regulators in budding yeastModification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulatedThe switch from survival responses to apoptosis after chromosomal breaks.Transcriptional response of Candida parapsilosis following exposure to farnesol.DNA repair: the importance of phosphorylating histone H2AX.BRCA1 Is Required for Maintenance of Phospho-Chk1 and G2/M Arrest during DNA Cross-Link Repair in DT40 CellsChromatin modulation and the DNA damage response.Co-mutation of histone H2AX S139A with Y142A rescues Y142A-induced ionising radiation sensitivity.Autofluorescent proteins.A role for the p53 tumour suppressor in regulating the balance between homologous recombination and non-homologous end joining.53BP1: function and mechanisms of focal recruitment.MRN and the race to the break.Chromatin assembly and signalling the end of DNA repair requires acetylation of histone H3 on lysine 56.Eukaryotic DNA damage checkpoint activation in response to double-strand breaks.Mesenchymal stromal cells: radio-resistant members of the bone marrow.ATR activates the S-M checkpoint during unperturbed growth to ensure sufficient replication prior to mitotic onset.Multiple facets of the DNA damage response contribute to the radioresistance of mouse mesenchymal stromal cell lines.An investigation into 53BP1 complex formation.Genetic dissection of vertebrate 53BP1: a major role in non-homologous end joining of DNA double strand breaks.Correction for Travesa et al., "Repression of G1/S Transcription Is Mediated via Interaction of the GTB Motifs of Nrm1 and Whi5 with Swi6"Enhanced protein detection using a trapping mode on a hybrid quadrupole linear ion trap (Q-Trap).The MRN complex.
P50
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description
Professor of Biochemistry
@en
hulumtues
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wetenschapper
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հետազոտող
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name
Noel F. Lowndes
@ast
Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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type
label
Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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prefLabel
Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
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Noel F. Lowndes
@nl
Noel F. Lowndes
@sl
P108
P106
P1153
7004013873
P21
P31
P496
0000-0002-3216-4427