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Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joiningThe myosin X motor is optimized for movement on actin bundles.Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VIThe checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNAProto-oncogene TCL1: more than just a coactivator for AktThe TCL1A oncoprotein interacts directly with the NF-kappaB inhibitor IkappaB.Delineation of the Xrcc4-interacting region in the globular head domain of cernunnos/XLF.Force-producing ADP state of myosin bound to actin.Highly selective inhibition of myosin motors provides the basis of potential therapeutic applicationAn overview and online registry of microvillus inclusion disease patients and their MYO5B mutations.Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles.How actin initiates the motor activity of MyosinXLF and APLF bind Ku80 at two remote sites to ensure DNA repair by non-homologous end joiningStructural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseasesPlugged into the Ku-DNA hub: The NHEJ networkAutocyclized and oxidized forms of SCR7 induce cancer cell death by inhibiting nonhomologous DNA end joining in a Ligase IV dependent mannerUnraveling protein dynamics through fast spectral density mappingProper chromosome alignment depends on BRCA2 phosphorylation by PLK1
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description
hulumtuese
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հետազոտող
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name
Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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type
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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prefLabel
Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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Virginie Ropars
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P214
P106
P108
P21
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0000 0003 5702 9464
P214
P31
P496
0000-0002-3372-6030
P569
1980-01-01T00:00:00Z