Results 151 to 160 of about 17,972 (261)

The effects of the histone chaperone and histone modifications on nucleosome structure

open access: yes, 2016
The nucleosome, composed of 147-bp DNA and a histone octamer, is the basic unit of chromatin in eukaryotes, which is considered as a barrier for all DNA dependent processes. Understanding how nucleosome structure is regulated provides new insights into pivotal cellular processes.
Wang, Tao, author   +4 more
openaire   +1 more source

DIA2 genetically interacts with genes encoding histone chaperones and histone H3–H4 lysine mutants with defects in nucleosome assembly.

open access: yes, 2012
(A) Dia2 functions in parallel with known H3–H4 histone chaperones in transcriptional silencing at the silent HMR locus. Cells of the indicated genotype were assessed for HMR silencing as described in Figure 1A–1B.
Zhiguo Zhang (147197)   +4 more
core   +1 more source

Anemia‐associated mutations disrupt the CDIN1‐Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA‐I) disease

open access: yesThe FEBS Journal, EarlyView.
Congenital dyserythropoietic anemia type I (CDA‐I) arises from mutations in Codanin1 and CDIN1. Using quantitative biophysical approaches, we show that disease‐associated mutations disrupt the CDIN1‐Codanin1 complex. Our findings provide critical insights into the molecular mechanism that links protein dysfunction to disturbing chromatin arrangement ...
Martin Stojaspal   +8 more
wiley   +1 more source

Contributions of DNA, histone chaperones and chromatin remodeling enzymes to nucleosome positioning. [PDF]

open access: yes, 2009
The eukaryotic genome is packaged by wrapping ~147 bp units of DNA around histone octamers to form chains of nucleosomes. The packaging of the DNA within a nucleosome reduces access of the DNA to most transcription factors and polymerases.
Partensky, Peretz
core  

Proteostasis of organelles in aging and disease

open access: yesThe FEBS Journal, EarlyView.
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi   +5 more
wiley   +1 more source

Resistance‐exercise‐induced stress intervenes in TGF‐β signaling by cooperatively downregulating nuclear αB‐crystallin and SMAD4 in human skeletal muscle fibers

open access: yesThe FEBS Journal, EarlyView.
Alpha‐crystallin B chain (CRYAB) has been reported to stabilize mothers against decapentaplegic homolog 4 (SMAD4) in transforming growth factor‐β (TGF‐β) signaling, enabling target gene transcription. We show nuclear CRYAB–SMAD4 interaction for the first time in human skeletal muscle fibers and its regulation by exercise.
Kirill Schaaf   +7 more
wiley   +1 more source

Biogenesis of TNF‐α‐insights into proteostasis and inflammation

open access: yesThe FEBS Journal, EarlyView.
TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar   +3 more
wiley   +1 more source

Histone chaperone regulates replication

open access: yesThe Journal of Cell Biology, 2008
Histone supply and demand are tightly coupled at the replication fork by a chaperone, according to Genevieve Almouzni (Curie Institute, Paris, France) and colleagues. The chaperone, Asf1, passes histones from parental to daughter DNA strands and unwinds just enough DNA to match its transfer activities.
openaire   +2 more sources

The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity

open access: yes, 2011
Histones are highly positively charged proteins that wrap our genome. Their surface properties also make them prone to nonspecific interactions and aggregation.
Ladurner, Andreas G.   +3 more
core   +1 more source

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