Results 1 to 10 of about 28,191 (215)
Chromatin gels are auxetic due to cooperative nucleosome assembly and disassembly dynamics [PDF]
We study "chromatin gels", model systems for chromatin, to theoretically predict the conditions, under which such gels show negative Poisson's ratios. A chromatin gel shows phase separation due to an instability arising from the disassembly of nucleosomes by RNA polymerases during transcription.
Yamamoto, T., Schiessel, H.
core +8 more sources
Epigenetics and Chromatin: Interactions and processes Boston, MA, USA. 11-13 March 2013. Abstracts. [PDF]
The Eukaryotic genome is packaged together with histone proteins to form the nucleoprotein structure called chromatin. This packaging of DNA into chromatin is critical to prevent inappropriate access to the DNA in order to enable the fundamental processes of the genome, such as gene expression, DNA repair and DNA replication, to be highly regulated ...
Jessica K. Tyler
europepmc +7 more sources
At blocked replication forks, homologous recombination mediates the nascent strands to switch template in order to ensure replication restart, but faulty template switches underlie genome rearrangements in cancer cells and genomic disorders. Recombination occurs within DNA packaged into chromatin that must first be relaxed and then restored when ...
Pietrobon, Violena+6 more
doaj +8 more sources
Replication-Coupled Chromatin Remodeling: An Overview of Disassembly and Assembly of Chromatin during Replication [PDF]
The doubling of genomic DNA during the S-phase of the cell cycle involves the global remodeling of chromatin at replication forks. The present review focuses on the eviction of nucleosomes in front of the replication forks to facilitate the passage of replication machinery and the mechanism of replication-coupled chromatin assembly behind the ...
Céline Duc, Christophe Thiriet
semanticscholar +8 more sources
Regulation of Chromatin Assembly/Disassembly by Rtt109p, a Histone H3 Lys56-specific Acetyltransferase, in Vivo [PDF]
Rtt109p, a histone acetyltransferase, associates with active genes and acetylates lysine 56 on histone H3 in Saccharomyces cerevisiae. However, the functional role of Rtt109p or H3 Lys(56) acetylation in chromatin assembly/disassembly (and hence gene expression) immediately switching transcription on or off has not been clearly elucidated in vivo. Here,
Geetha Durairaj+5 more
semanticscholar +6 more sources
Chromatin Assembly and Disassembly During Genomic Processes
Chromatin assembly and disassembly has long been acknowledged to accompany the process of DNA replication. Accordingly, we previously discovered a key histone chaperone involved in the assembly of chromatin during DNA replication, termed Asf1 (Tyler et al., Nature 1999).
Jessica K. Tyler+3 more
semanticscholar +4 more sources
Chromatin Assembly and Disassembly
The eukaryotic genome is packaged together with histone proteins to form the nucleoprotein structure called chromatin. This packaging of DNA into chromatin is critical to prevent inappropriate access to the DNA in order to enable the fundamental processes of the genome, such as gene expression, DNA repair and DNA replication, to be highly regulated ...
Jessica K. Tyler
semanticscholar +3 more sources
The role of the host—Neutrophil biology
Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple+4 more
wiley +1 more source
Assembly/Disassembly of the Nuclear Envelope Membrane [PDF]
Assembly and disassembly of the nucleus at mitosis in eukaryotes involves the reversible interaction of chromatin with the nuclear membrane. Previously we have shown that this interaction is regulated by the antagonistic activities of a kinase and a phosphatase. The kinase promotes membrane release while the phosphatase stimulates binding.
John Newport, Rupert Pfaller
openaire +3 more sources
Post‐Translational Modifications in Cilia and Ciliopathies
This review synthesizes current understanding of post‐translational modifications (PTMs) in ciliary proteins and emphasizes their roles in ciliary formation, homeostasis, and signaling. This review also discusses the implication of PTM dysregulation in ciliopathies and explores therapeutic strategies targeting PTM‐modifying enzymes.
Jie Ran, Jun Zhou
wiley +1 more source