about
Reconstitution of hyperacetylated, DNase I-sensitive chromatin characterized by high conformational flexibility of nucleosomal DNA.Mobilization of hyperacetylated mononucleosomes by purified yeast ISW2 in vitro.A simple and cost-effective solid-phase protein nano-assay using polyacrylamide-coated glass plates.DNA-protein interactions and spatial organization of DNA.A motif within SET-domain proteins binds single-stranded nucleic acids and transcribed and supercoiled DNAs and can interfere with assembly of nucleosomes.A monomeric derivative of the cellular transcription factor CREB functions as a constitutive activator.On the role of inter-nucleosomal interactions and intrinsic nucleosome dynamics in chromatin function.SET domains of histone methyltransferases recognize ISWI-remodeled nucleosomal species.Interaction of SET domains with histones and nucleic acid structures in active chromatin.Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains.Yeast Isw1a and Isw1b exhibit similar nucleosome mobilization capacities for mononucleosomes, but differently mobilize dinucleosome templates.A composite agarose-polyacrylamide matrix as two-dimensional hard support for solid-phase protein assays.Comparison of the Isw1a, Isw1b, and Isw2 nucleosome disrupting activities.Remodeling of nucleosome-dimer particles with yIsw2 promotes their association with ALL-1 SET domain in vitro.Evidence for the nucleosome-disruption process regulated by phosphorylation of 120 kDa protein complex in Drosophila embryo cell-free system.Relationship between chromatin high-order folding and nucleosomal linker twist in nuclei of human HeLa s3 cells.A simple and reproducible method for analysis of chromatin condensationAcetylation of core histones causes the unfolding of 30 nm chromatin fiber: analysis by agarose gel electrophoresisFlexibility of DNA within transcriptionally active nucleosomes: analysis by circular dichroism measurementsDynamics of unfolded nucleosomal fiber"Direct" and "Indirect" Effects of Histone Modifications: Modulation of Sterical Bulk as a Novel Source of Functionality
P50
Q35871435-6FE29294-A26B-45E7-A186-6E865A081A0BQ38809877-16F27BEA-4F11-4ABE-BAD9-6DF1DBE7F1F7Q40239124-E9831AC2-6E30-446C-B082-EC64298A659FQ40717886-8DB5164F-B297-454C-BB15-C965B524061DQ41098354-7DD9348F-BBE9-44DF-91B6-2295E2858DA6Q41431643-4ACD61B0-982E-433C-AD38-63902B89EF2DQ41683197-8FB0BECF-1F3A-4257-ADB9-B0C86EF5D38AQ41980667-216A413F-1C80-415C-BFDC-DFF79737C101Q42182620-6ACBE117-1CF2-4C94-9D1B-63F5E36A392EQ42982373-341BDD86-DE78-4567-9F29-C1C0266A7C12Q45150660-320AFC91-7B0D-4E3E-B4BF-F6917E264AE5Q50542486-FC940FB3-3366-4304-A050-AFCB97188463Q50720852-E62FDA3A-55E3-44CB-8EC1-34F8DC3E9671Q51783083-F4C4F594-E0F8-4BA4-A3F9-6DC8EA73A119Q51970726-8DC57DBD-31CA-40A2-A184-AF931475C287Q64889040-43A788AB-97CC-44F4-8976-D324F9EB60A2Q70742045-F6F8415B-9D66-40AA-9760-0A74CE982B5CQ72547199-B6D7AD46-DE2E-43C1-A113-D9B714C0F959Q72894177-4FF45D7B-ED6A-4399-9A60-B13148764E27Q72894180-0CFA6EBD-3642-4FB1-9206-A4FBD0107BC4Q91723418-8CA90235-326F-4A91-BC4B-39020A3A58B6
P50
description
Pools onderzoeker
@nl
researcher
@en
name
Krajewski WA
@nl
Wladyslaw A. Krajewski
@en
Władysław Krajewski
@ast
Władysław Krajewski
@ca
Władysław Krajewski
@cs
Władysław Krajewski
@es
Władysław Krajewski
@gl
Władysław Krajewski
@hr
Władysław Krajewski
@hsb
Władysław Krajewski
@it
type
label
Krajewski WA
@nl
Wladyslaw A. Krajewski
@en
Władysław Krajewski
@ast
Władysław Krajewski
@ca
Władysław Krajewski
@cs
Władysław Krajewski
@es
Władysław Krajewski
@gl
Władysław Krajewski
@hr
Władysław Krajewski
@hsb
Władysław Krajewski
@it
altLabel
Krajewski WA
@en
prefLabel
Krajewski WA
@nl
Wladyslaw A. Krajewski
@en
Władysław Krajewski
@ast
Władysław Krajewski
@ca
Władysław Krajewski
@cs
Władysław Krajewski
@es
Władysław Krajewski
@gl
Władysław Krajewski
@hr
Władysław Krajewski
@hsb
Władysław Krajewski
@it
P106
P1412
P1559
Władysław Krajewski
@pl
P21
P27
P31
P496
0000-0002-9669-5614