about
The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairsStructure and regulatory targets of SCO3201, a highly promiscuous TetR-like regulator of Streptomyces coelicolor M145Structural analysis and knock-out of a Burkholderia pseudomallei homolog of the eukaryotic transcription coactivator PC4C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding siteFunctional analysis of the TFIID-specific yeast TAF4 (yTAF(II)48) reveals an unexpected organization of its histone-fold domainDimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine ProteaseThe histone fold is a key structural motif of transcription factor TFIID.Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIIDIdentification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.Assignment strategies and analysis of cross-peak patterns and intensities in the three-dimensional homonuclear TOCSY-NOESY of RNA.Identification of the ssDNA-binding protein of bacteriophage T5: Implications for T5 replication.Correction: Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease.Production and isotope labeling of antimicrobial peptides in Escherichia coli by means of a novel fusion partner that enables high-yield insoluble expression and fast purification.High-affinity DNA binding by the C-terminal domain of the transcriptional coactivator PC4 requires simultaneous interaction with two opposing unpaired strands and results in helix destabilization.Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coliStructural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold
P50
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P50
description
biomedical researcher
@en
wetenschapper
@nl
name
Sebastiaan Werten
@en
Werten B
@nl
type
label
Sebastiaan Werten
@en
Werten B
@nl
prefLabel
Sebastiaan Werten
@en
Werten B
@nl
P106
P31
P496
0000-0003-2244-9688