Results 11 to 20 of about 253,651 (260)

Interaction of the pioneer transcription factor GATA3 with nucleosomes

open access: yesNature Communications, 2020
GATA 3 functions as a pioneer factor during cellular reprogramming. Here the authors delineate nucleosome positioning relative to GATA3 binding motifs and describe the structure of a GATA3–nucleosome complex; providing insight into how a pioneer factor ...
Hiroki Tanaka   +7 more
doaj   +1 more source

Internal modifications in the CENP-A nucleosome modulate centromeric dynamics

open access: yesEpigenetics & Chromatin, 2017
Background Posttranslational modifications of core histones are correlated with changes in transcriptional status, chromatin fiber folding, and nucleosome dynamics. However, within the centromere-specific histone H3 variant CENP-A, few modifications have
Minh Bui   +7 more
doaj   +1 more source

Telomeric chromatin structure

open access: yesCurrent Opinion in Structural Biology, 2022
Eukaryotic DNA is packaged into nucleosomes, which further condenses into chromosomes. The telomeres, which form the protective end-capping of chromosomes, play a pivotal role in ageing and cancer. Recently, significant advances have been made in understanding the nucleosomal and telomeric chromatin structure at the molecular level. In addition, recent
Aghil Soman   +2 more
openaire   +3 more sources

Structural basis for the inhibition of HTLV-1 integration inferred from cryo-EM deltaretroviral intasome structures

open access: yesNature Communications, 2021
Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism of novel integrase strand transfer inhibitor (INSTI) candidates to limit HTLV-1 infection.
Michal S. Barski   +10 more
doaj   +1 more source

Job Opening for Nucleosome Mechanic: Flexibility Required

open access: yesCells, 2020
The nucleus has been studied for well over 100 years, and chromatin has been the intense focus of experiments for decades. In this review, we focus on an understudied aspect of chromatin biology, namely the chromatin fiber polymer’s mechanical ...
Mary Pitman   +2 more
doaj   +1 more source

Unbiased high-throughput characterization of mussel transcriptomic responses to sublethal concentrations of the biotoxin okadaic acid [PDF]

open access: yesPeerJ, 2015
Background. Harmful Algal Blooms (HABs) responsible for Diarrhetic Shellfish Poisoning (DSP) represent a major threat for human consumers of shellfish. The biotoxin Okadaic Acid (OA), a well-known phosphatase inhibitor and tumor promoter, is the primary ...
Victoria Suarez-Ulloa   +7 more
doaj   +2 more sources

Structural Transition of the Nucleosome during Transcription Elongation

open access: yesCells, 2023
In eukaryotes, genomic DNA is tightly wrapped in chromatin. The nucleosome is a basic unit of chromatin, but acts as a barrier to transcription. To overcome this impediment, the RNA polymerase II elongation complex disassembles the nucleosome during ...
Tomoya Kujirai   +3 more
doaj   +1 more source

The cryo‐EM structure of full‐length RAD52 protein contains an undecameric ring

open access: yesFEBS Open Bio, 2023
The human RAD52 protein, which forms an oligomeric ring structure, is involved in DNA double‐strand break repair. The N‐terminal half of RAD52 is primarily responsible for self‐oligomerisation and DNA binding.
Chiaki Kinoshita   +5 more
doaj   +1 more source

Chromatin and nucleosome structure [PDF]

open access: yesNucleic Acids Research, 1976
Chromatin nucleosomes (mononucleosomes through pentanucleosomes) have been isolated by staphylococcal nuclease digestion of calf thymus nuclei. The peak value ellipticity is the same for all oligomers, 1900 deg cm2, mol-1 at 280-nm, 23 degrees C. The dh280/dT vs T show a progressive increase in Tm of the main thermal band (73.5 degrees C, monomer; 79 ...
R, Mandel, G D, Fasman
openaire   +2 more sources

A model for chromatin structure [PDF]

open access: yesNucleic Acids Research, 1975
A model for chromatin structure is presented. (a) Each of four histone species, H2A (IIbl or f2a2), H2B (IIb2 or f2b), H3 (III or f3) and H4 (IV or f2al) can form a parallel dimer. (b) These dimers can form two tetramers, (H2A)2(H2b)2 and (H3)2(H4)2. (C) These two tetramers bind a segment of DNA and condense it into a "C" segments.
openaire   +2 more sources

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