Alan P. Wolffe

TL;DR: A cluster of basic residues within the globular domain of H10, a somatic linker histone variant from Xenopus laevis, are examined and it is shown that these residues do not play an essential role in the structure-specific binding of a linker Histone to the nucleosome.

TL;DR: The results provide insight into the molecular mechanisms of VEGF-A up-regulation during cancer development and show that endothelial PAS domain protein 1 (EPAS1) can efficiently bind to the endogenous HRE in U87MG cells but not in HEK293 cells in which the chromosomal HS-1100 is not accessible to DNase I.

TL;DR: In this article, the translational regulation of histone H4 mRNA when Xenopus laevis oocytes are induced to mature with progesterone was examined, and the potential role of nuleoplasmin in the remodeling of repressive ribonucleoprotein particles containing maternal mRNA was discussed.

TL;DR: It is demonstrated that acetylation of core histone tails does not significantly impair the ability of linker histones to bind preferentially and asymmetrically to a defined sequence mononucleosome core reconstituted in vitro, and a simple inhibition mechanism cannot explain models whereby acetylations is causal for the observed reduction in the linkerhistone content in chromatin.