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Structural Mechanisms of Hexameric Helicase Loading, Assembly, and UnwindingStructure of Shroom domain 2 reveals a three-segmented coiled-coil required for dimerization, Rock binding, and apical constrictionStructure of a highly conserved domain of Rock1 required for Shroom-mediated regulation of cell morphologyExome sequencing reveals MCM8 mutation underlies ovarian failure and chromosomal instabilityMCM9 mutations are associated with ovarian failure, short stature, and chromosomal instabilityAssembly of the bacteriophage T4 primosome: single-molecule and ensemble studiesArchitecture of the bacteriophage T4 primosome: electron microscopy studies of helicase (gp41) and primase (gp61).Dynamic protein interactions in the bacteriophage T4 replisome.The dynamic processivity of the T4 DNA polymerase during replicationSteric exclusion and wrapping of the excluded DNA strand occurs along discrete external binding paths during MCM helicase unwinding.Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics.Crystal Structure of a Transcribing RNA Polymerase II Complex Reveals a Complete Transcription Bubble.Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.Biochemical Characterization of the Human Mitochondrial Replicative Twinkle Helicase: SUBSTRATE SPECIFICITY, DNA BRANCH MIGRATION, AND ABILITY TO OVERCOME BLOCKADES TO DNA UNWINDING.DNA Interactions Probed by Hydrogen-Deuterium Exchange (HDX) Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Confirm External Binding Sites on the Minichromosomal Maintenance (MCM) Helicase.Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transferThe excluded DNA strand is SEW important for hexameric helicase unwinding.Mechanistic insights into how CMG helicase facilitates replication past DNA roadblocks.Biochemistry: Molecular hurdles cleared with ease.Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme.Protein-protein interactions in the bacteriophage T4 replisome. The leading strand holoenzyme is physically linked to the lagging strand holoenzyme and the primosome.Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme.On the solution structure of the T4 sliding clamp (gp45).Assembly and distributive action of an archaeal DNA polymerase holoenzyme.Coordination and Substitution of DNA Polymerases in Response to Genomic Obstacles.'Screw-cap' clamp loader proteins that thread.Molecular biology: the loader of the rings.Bacterial DnaB helicase interacts with the excluded strand to regulate unwinding.MCM forked substrate specificity involves dynamic interaction with the 5'-tail.Dissociative properties of the proteins within the bacteriophage T4 replisome.The application of a minicircle substrate in the study of the coordinated T4 DNA replication.A clamp-like biohybrid catalyst for DNA oxidation.Strand annealing and terminal transferase activities of a B-family DNA polymerase.Control of Hexamerization, Assembly, and Excluded Strand Specificity for the Sulfolobus solfataricus MCM HelicaseOrganization of the archaeal MCM complex on DNA and implications for the helicase mechanismFine-tuning of the replisome: Mcm10 regulates fork progression and regressionAmidst multiple binding orientations on fork DNA, MCM helicase proceeds N-first for unwindingNovel interaction of the bacterial-Like DnaG primase with the MCM helicase in archaea
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Michael Trakselis
@ast
Michael Trakselis
@en
Michael Trakselis
@es
Michael Trakselis
@nl
Michael Trakselis
@sl
type
label
Michael Trakselis
@ast
Michael Trakselis
@en
Michael Trakselis
@es
Michael Trakselis
@nl
Michael Trakselis
@sl
prefLabel
Michael Trakselis
@ast
Michael Trakselis
@en
Michael Trakselis
@es
Michael Trakselis
@nl
Michael Trakselis
@sl
P106
P1153
6602117168
P21
P31
P496
0000-0001-7054-8475