about
Quantitative Characterization of E-selectin Interaction with Native CD44 and P-selectin Glycoprotein Ligand-1 (PSGL-1) Using a Real Time Immunoprecipitation-based Binding Assay.Structural basis for proofreading during replication of the Escherichia coli chromosomeReplisome speed determines the efficiency of the Tus-Ter replication termination barrierThioredoxin suppresses microscopic hopping of T7 DNA polymerase on duplex DNA.Structure of the theta subunit of Escherichia coli DNA polymerase III in complex with the epsilon subunitPeptide ligands specific to the oxidized form of Escherichia coli thioredoxinReal-time single-molecule observation of rolling-circle DNA replication.Phosphate steering by Flap Endonuclease 1 promotes 5'-flap specificity and incision to prevent genome instability.Two modes of interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complexTiming, coordination, and rhythm: acrobatics at the DNA replication fork.DNA primase acts as a molecular brake in DNA replication.Dynamic DNA helicase-DNA polymerase interactions assure processive replication fork movement.Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase.Exchange of DNA polymerases at the replication fork of bacteriophage T7.The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunitTwo mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex.Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase IIIA direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesisDissecting the interactions of SERRATE with RNA and DICER-LIKE 1 in Arabidopsis microRNA precursor processingMotors, switches, and contacts in the replisome.Single-molecule FRET unveils induced-fit mechanism for substrate selectivity in flap endonuclease 1.Primer initiation and extension by T7 DNA primaseHydrolysis of the 5'-p-nitrophenyl ester of TMP by the proofreading exonuclease (epsilon) subunit of Escherichia coli DNA polymerase III.Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase.Essential residues in the C terminus of the bacteriophage T7 gene 2.5 single-stranded DNA-binding protein.Inadequate inhibition of host RNA polymerase restricts T7 bacteriophage growth on hosts overexpressing udk.Hydrolysis of the 5'-p-nitrophenyl ester of TMP by oligoribonucleases (ORN) from Escherichia coli, Mycobacterium smegmatis, and human.What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments.Characterization of Recombinant Thermococcus kodakaraensis (KOD) DNA Polymerases Produced Using Silkworm-Baculovirus Expression Vector System.Sequential and multistep substrate interrogation provides the scaffold for specificity in human flap endonuclease 1.Initial state of DNA-Dye complex sets the stage for protein induced fluorescence modulationPreliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase IIIThe C-terminal residues of bacteriophage T7 gene 4 helicase-primase coordinate helicase and DNA polymerase activitiesSingle-molecule studies of fork dynamics in Escherichia coli DNA replicationStructure of the processive human Pol δ holoenzymeMicrofluidics-based super-resolution microscopy enables nanoscopic characterization of blood stem cell rollingFunctional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domainFusion of the Cas9 endonuclease and the VirD2 relaxase facilitates homology-directed repair for precise genome engineering in rice
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Samir M. Hamdan
@ast
Samir M. Hamdan
@en
Samir M. Hamdan
@es
Samir M. Hamdan
@sl
type
label
Samir M. Hamdan
@ast
Samir M. Hamdan
@en
Samir M. Hamdan
@es
Samir M. Hamdan
@sl
prefLabel
Samir M. Hamdan
@ast
Samir M. Hamdan
@en
Samir M. Hamdan
@es
Samir M. Hamdan
@sl
P106
P1153
7004659263
P21
P31
P496
0000-0001-5192-1852