Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases.
about
N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognitionBiotin and biotinidase deficiencyBiotinK12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts.Biotin regulates the expression of holocarboxylase synthetase in the miR-539 pathway in HEK-293 cells.Functional requirements driving the gene duplication in 12 Drosophila species.Feeding Drosophila a biotin-deficient diet for multiple generations increases stress resistance and lifespan and alters gene expression and histone biotinylation patternsHolocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeatsEpigenetic regulation of chromatin structure and gene function by biotin: are biotin requirements being met?Repression of transposable elements by histone biotinylation.Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.Biotinyl-methyl 4-(amidomethyl)benzoate is a competitive inhibitor of human biotinidase.Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes.The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylationK16-biotinylated histone H4 is overrepresented in repeat regions and participates in the repression of transcriptionally competent genes in human Jurkat lymphoid cellsNitric oxide signaling depends on biotin in Jurkat human lymphoma cells.Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation.
P2860
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P2860
Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
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2007年论文
@zh-cn
name
Susceptibility to heat stress ...... histones, not of carboxylases.
@ast
Susceptibility to heat stress ...... histones, not of carboxylases.
@en
type
label
Susceptibility to heat stress ...... histones, not of carboxylases.
@ast
Susceptibility to heat stress ...... histones, not of carboxylases.
@en
prefLabel
Susceptibility to heat stress ...... histones, not of carboxylases.
@ast
Susceptibility to heat stress ...... histones, not of carboxylases.
@en
P2093
P2860
P356
P1433
P1476
Susceptibility to heat stress ...... histones, not of carboxylases.
@en
P2093
Gabriela Camporeale
Janos Zempleni
Joel C Eissenberg
P2860
P304
P356
10.1093/JN/137.4.885
P407
P577
2007-04-01T00:00:00Z