about
Human single-stranded DNA binding proteins are essential for maintaining genomic stabilityHSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage responseSingle-stranded DNA-binding protein hSSB1 is critical for genomic stabilityConformational flexibility revealed by the crystal structure of a crenarchaeal RadANucleophosmin: from structure and function to disease developmentChemotherapeutic compounds targeting the DNA double-strand break repair pathways: the good, the bad, and the promisingStructure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricusThe structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricusBRCA1 is an essential mediator of vinorelbine-induced apoptosis in mesothelioma.Genome stability pathways in head and neck cancersRodent blood-stage Plasmodium survive in dendritic cells that infect naive mice.Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis.Phosphorylation of Exo1 modulates homologous recombination repair of DNA double-strand breaks.Identification of a BRCA1-mRNA splicing complex required for efficient DNA repair and maintenance of genomic stabilityBRCA1 deficiency exacerbates estrogen-induced DNA damage and genomic instabilityHuman single-stranded DNA binding protein 1 (hSSB1/NABP2) is required for the stability and repair of stalled replication forks.hSSB1 rapidly binds at the sites of DNA double-strand breaks and is required for the efficient recruitment of the MRN complex.WT1 interacts with MAD2 and regulates mitotic checkpoint functionContribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.ATM mediated phosphorylation of CHD4 contributes to genome maintenance.Generation and characterisation of cisplatin-resistant non-small cell lung cancer cell lines displaying a stem-like signature.hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity.Recent advances in cancer therapy targeting proteins involved in DNA double-strand break repair.Vascular endothelial growth factor is an autocrine growth factor, signaling through neuropilin-1 in non-small cell lung cancer.Néstor-Guillermo Progeria Syndrome: a biochemical insight into Barrier-to-Autointegration Factor 1, alanine 12 threonine mutationINT6/EIF3E interacts with ATM and is required for proper execution of the DNA damage response in human cellsNovel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexeshSSB1 associates with and promotes stability of the BLM helicaseInvolvement of Exo1b in DNA damage-induced apoptosisINTS3 controls the hSSB1-mediated DNA damage responseSex Hormone Binding Globulin Modifies Testosterone Action and Metabolism in Prostate Cancer CellsCirculating tumour cells, their role in metastasis and their clinical utility in lung cancer.Functions and therapeutic roles of exosomes in cancer.The role of DNA repair pathways in cisplatin resistant lung cancer.Kruppel-associated Box (KRAB)-associated co-repressor (KAP-1) Ser-473 phosphorylation regulates heterochromatin protein 1β (HP1-β) mobilization and DNA repair in heterochromatin.A novel corepressor, BCoR-L1, represses transcription through an interaction with CtBP.Substrate recognition and catalysis by the Holliday junction resolving enzyme Hje.Antiproton induced DNA damage: proton like in flight, carbon-ion like near rest.Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase.[Modeling 5-FU clearance during a chronomodulated infusion]
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description
onderzoeker
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researcher
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հետազոտող
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name
Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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label
Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
@nl
Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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Derek J. Richard
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P106
P1153
7102203579
P31
P496
0000-0002-4839-8471