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Cindy L. White

Researcher at Colorado State University

Publications -  6
Citations -  1482

Cindy L. White is an academic researcher from Colorado State University. The author has contributed to research in topics: Nucleosome & Histone octamer. The author has an hindex of 6, co-authored 6 publications receiving 1357 citations.

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Book ChapterDOI

Reconstitution of Nucleosome Core Particles from Recombinant Histones and DNA

TL;DR: The cloning strategies for the construction of plasmids containing multiple repeats of defined DNA sequences, and the subsequent large-scale isolation of defined sequence DNA for nucleosome reconstitution are described.
Journal ArticleDOI

Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions.

TL;DR: The crystal structure of the nucleosome core particle from Saccharomyces cerevisiae reveals that the structure and function of this fundamental complex is conserved between single‐cell organisms and metazoans, consistent with the idea that much of the yeast genome remains constitutively open during much of its life cycle.
Journal ArticleDOI

Crystal Structures of Nucleosome Core Particles in Complex with Minor Groove DNA-binding Ligands

TL;DR: It is suggested that twist diffusion occurs over long distances through tightly bound nucleosomal DNA, which may be relevant to the mechanism of ATP-dependent and spontaneous nucleosome translocation, and to the effect of bound factors on nucleosomes dynamics.
Journal ArticleDOI

Crystal structures of histone Sin mutant nucleosomes reveal altered protein–DNA interactions

TL;DR: The number of lost protein–DNA interactions correlates directly with an increased propensity of the histone octamer to reposition with respect to the DNA, and with an overall destabilization of the nucleosome.
Journal ArticleDOI

Nucleosome Core Particles Containing a Poly(dA.dT) Sequence Element Exhibit a Locally Distorted DNA Structure.

TL;DR: Fluorescence resonance energy transfer showed that the interactions between the nucleosomal DNA ends and the histone octamer were destabilized in A16 NCP, consistent with previous in vivo and in vitro observations that poly(dA.dT) elements cause only modest changes in DNA accessibility and modest increases in steady-state transcription levels.