Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Tim R. Hebbes"'
Autor:
Stuart C H Allen, Tim R. Hebbes
Publikováno v:
FEBS Letters. 534:119-124
We have screened protein extracts from chicken blood cells for acetyltransferases. An in gel acetyltransferase assay revealed that a 32 kDa protein, which is more prevalent in whole blood when compared with erythrocyte cells, possessed an auto-acetyl
Autor:
Tim R. Hebbes, Stuart C H Allen
Publikováno v:
Journal of Biological Chemistry. 275:31347-31352
We have examined salt-soluble chromatin released by micrococcal nuclease from a 15-day-old chicken embryo erythrocyte nuclei for histone acetyltransferase (HAT) activities. This chromatin is enriched in transcriptionally active sequences from within
Publikováno v:
Molecular and Cellular Biology. 18:6281-6292
In chromosome translocations characteristic of Burkitt lymphomas (BL) and murine plasmacytomas, c-myc genes become juxtaposed to immunoglobulin heavy-chain (IgH) sequences, resulting in aberrant c-myc transcription. Translocated c-myc alleles that re
Publikováno v:
The EMBO Journal. 13:1823-1830
The distribution of core histone acetylation across the chicken beta-globin locus has been mapped in 15 day chicken embryo erythrocytes by immunoprecipitation of mononucleosomes with an antibody recognizing acetylated histones, followed by hybridizat
Publikováno v:
Nucleic Acids Research. 20:1017-1022
An affinity-purified antibody that recognises the epitope epsilon-acetyl lysine has been used to fractionate chicken erythrocyte mononucleosomes obtained from 5 and 15 day embryos. The antibody bound chromatin was enriched in multiply acetylated form
Chromatin immunoprecipitation (ChIP) is a technique widely used for determining the genomic location of modified histones and other chromatin-associated factors. Here we describe the methodology we have used in our laboratory for the immunoprecipitat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9590813fc163021a18b84929c331318f
https://doi.org/10.1385/1-59259-828-5:021
https://doi.org/10.1385/1-59259-828-5:021
Publisher Summary This chapter describes the use of chromatin immunoprecipitation assays in the acetylation mapping of higher eukaryotes. Acetylation of specific lysine residues in the N-terminal domains of core histones is a biochemical marker of ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2648845a9de2c8a3a4a6750e44ff4f81
https://doi.org/10.1016/s0076-6879(99)04031-8
https://doi.org/10.1016/s0076-6879(99)04031-8
Publikováno v:
Methods (San Diego, Calif.). 12(1)
Acetylation of specific lysine residues in the N-terminal domains of core histones is a biochemical marker of active genes. To determine the spatial and temporal distribution of this reversible posttranslational modification, affinity-purified polycl
Autor:
Tim R. Hebbes, Konstantin K. Ebralidse, Alan W. Thorne, Colyn Crane-Robinson, Alison L. Clayton
Publikováno v:
Nucleic acids research. 21(20)
Chemically induced histone-DNA crosslinking in nuclei is used to monitor structural changes in chromosomal domains containing hyperacetylated histones. Core particles harbouring the crosslinks are immunofractionated with antibodies specific for acety
Publikováno v:
The EMBO Journal. 7:1395-1402
An antiserum raised against chemically acetylated histone H4 was found to recognize the epitope epsilon-N-acetyl lysine. Affinity-purified antibodies were used to fractionate oligo- and mononucleosomal chromatin fragments from the nuclei of 15-day ch