Results 41 to 50 of about 181,554 (237)
The human histone H3 complement anno 2011 [PDF]
Histones are highly basic, relatively small proteins that complex with DNA to form higher order structures that underlie chromosome topology. Of the four core histones H2A, H2B, H3 and H4, it is H3 that is most heavily modified at the post-translational level.
Ederveen, T.H.A.+2 more
openaire +3 more sources
Interactions With Histone H3 & Tools to Study Them [PDF]
Histones are an integral part of chromatin and thereby influence its structure, dynamics, and functions. The effects of histone variants, posttranslational modifications, and binding proteins is therefore of great interest. From the moment that they are deposited on chromatin, nucleosomal histones undergo dynamic changes in function of the cell cycle ...
William A. Scott+3 more
openaire +4 more sources
The protonated form of butyrate, as well as other short‐chain fatty acids (SCFAs), is membrane permeable. In acidic extracellular environments, this can lead to intracellular accumulation of SCFAs and cytosolic acidification. This phenomenon will be particularly relevant in acidic environments such as the large intestine or tumor microenvironments ...
Muwei Jiang+2 more
wiley +1 more source
A natural histone H2A variant lacking the Bub1 phosphorylation site and regulated depletion of centromeric histone CENP-A foster evolvability in Candida albicans. [PDF]
Eukaryotes have evolved elaborate mechanisms to ensure that chromosomes segregate with high fidelity during mitosis and meiosis, and yet specific aneuploidies can be adaptive during environmental stress.
Brimacombe, Cedric A+8 more
core +3 more sources
The complex mode of action of the topoisomerase II inhibitor etoposide in triggering apoptosis involves several mechanisms: overexpression of the mitochondrial protein VDAC1, leading to its oligomerization and formation of a large channel that mediates the release of pro‐apoptotic protein; and overexpression of the apoptosis regulators p53, Bax, and ...
Aditya Karunanithi Nivedita+1 more
wiley +1 more source
Uncoupling histone turnover from transcription-associated histone H3 modifications [PDF]
Transcription in eukaryotes is associated with two major changes in chromatin organization. Firstly, nucleosomal histones are continuously replaced by new histones, an event that in yeast occurs predominantly at transcriptionally active promoters. Secondly, histones become modified post-translationally at specific lysine residues.
Ferrari Paolo, Strubin Michel
openaire +4 more sources
NAD+ regeneration by mitochondrial complex I NADH dehydrogenase is important for cancer cell proliferation. Specifically, NAD+ is necessary for the activities of NAD+‐dependent deacetylases SIRT3 and SIRT7, which suppress the expression of p21Cip1 cyclin‐dependent kinase inhibitor, an antiproliferative molecule, at the translational and transcriptional
Masato Higurashi+5 more
wiley +1 more source
Phosphoserines on Maize CENTROMERIC HISTONE H3 and Histone H3 Demarcate the Centromere and Pericentromere during Chromosome Segregation [PDF]
We have identified and characterized a 17- to 18-kD Ser50-phosphorylated form of maize (Zea mays) CENTROMERIC HISTONE H3 (phCENH3-Ser50). Immunostaining in both mitosis and meiosis indicates that CENH3-Ser50 phosphorylation begins in prophase/diplotene, increases to a maximum at prometaphase-metaphase, and drops during anaphase.
Xiaolan Zhang+4 more
openaire +3 more sources
sNASP and ASF1A function through both competitive and compatible modes of histone binding [PDF]
Histone chaperones are proteins that interact with histones to regulate the thermodynamic process of nucleosome assembly. sNASP and ASF1 are conserved histone chaperones that interact with histones H3 and H4 and are found in a multi-chaperoning complex ...
Bowman, Andrew J.+6 more
core +1 more source
Presurgery 72‐h fasting in GB patients leads to adaptations of plasma lipids and polar metabolites. Fasting reduces lysophosphatidylcholines and increases free fatty acids, shifts triglycerides toward long‐chain TGs and increases branched‐chain amino acids, alpha aminobutyric acid, and uric acid.
Iris Divé+7 more
wiley +1 more source