Ushiroyama T, Tanigawa Y, Tsuchiya M, Matsuura R, Ueki M, Sugimoto O, Shimoyama M: Amino acid sequence of histone H1 at the ADP-ribose-accepting site and ADP-ribose histone-H1 adduct as an inhibitor of cyclic-AMP-dependent phosphorylation. Eur J Biochem 151: 173–177, 1985...
To determine which isomer causes the +105.0215 Da mass shift, we first determined whether the pan anti- Kbzantibody recognises the above three isomers. We designed and synthesised four peptides based on the histone H4 amino acid sequence containing the lysine with a + 105.0215 Da ma...
A nucleosome is a fundamental unit of chromatin composed of 147 base pairs of DNA and an octamer of core histone proteins, two copies each of histones H2A, H2B, H3, and H4. Histone proteins are basic and conserved from archaea to humans based on the amino acid sequence.29,30Histone underg...
The specificity of chromatin acetylation has been attempted to be explained primarily by one of the following two models: (1) a TF binding to a specific DNA sequence specifies the chromatin sites where its partner acetyltransferase (complex) acetylates, or (2) an acetyltransferase (complex) bindin...
The nuclear protein NONO is highly conserved in humans and mice, and shares 98% amino acid sequence similarity [7, 8]. To further assess the role of NONO in regulating mammary tumor progression in vivo, we constructed a spontaneous mammary tumor mouse line in which NONO was specifically knocke...
(a nonencoded amino acid) bypeptidylarginine deiminases(PADs).PAD4is involved in histonecitrullinationduring NETosis in vitro, and chemical orgeneticremoval of PAD4 lessensNETformation (Knight et al., 2013; Knight et al., 2015; Lewis et al., 2015;Li, Li, Lindberg, Kennett, Xiong, & Wang...
Recombinant Histone H3.3 - biotinylated, Human, corresponds to the native histone sequence of mammalian histone H3 variant H3.3 and does not contain any amino acid substitutions or residue analogs. Histone H3.3 is known to be important for gene regulation. Recombinant Histone H3.3 - biotinylated, ...
arginine (MMA), symmetrical dimethylarginine (SDMA), or asymmetrical dimethylarginine (ADMA), and the sites of methylation include H3R2, H3R8, H3R17, H3R26, and H4R3[59]. The methylation of these amino acid residues increases the hydrophobicity via the reduction in hydrogen bonding capacity. ...
The amino-acid sequence of the PHD finger in SIZ1 demonstrated that C162 is in an α-helix, whereas C117 and C134 are not (Fig. 1c). It is probable that substitution of C162 to serine severely affects SIZ1 function. Fig. 1: Mutation in the plant homeodomain (PHD) finger of SIZ1...
The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues. BMC Evol. Biol. 9, 31 (2009). Article CAS PubMed PubMed Central Google Scholar Faast, R. et al. ...