BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma
The schematic illustrates BMI‐1 phosphorylation during M phase, which triggers its translocation from the nucleus to the cytoplasm. In cycling cells, BMI‐1 functions within the PRC1 complex to mediate H2A K119 monoubiquitination. Following PTC596‐induced M phase arrest, phosphorylated BMI‐1 dissociates from PRC1 and is exported to the cytoplasm via its
Banlanjo Umaru +6 more
wiley +1 more source
Discovery of ultrafast myosin, its amino acid sequence, and structural features. [PDF]
Haraguchi T +9 more
europepmc +1 more source
Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control
Damaged rDNA accumulates at a specific perinuclear interface that couples nucleolar escape with nuclear envelope association. Nuclear pores at this site help inhibit Fob1‐induced rDNA instability. This spatial organization of damage handling supports a functional link between nuclear architecture, rDNA stability, and replicative lifespan in yeast.
Yamato Okada +5 more
wiley +1 more source
Calling the amino acid sequence of a protein/peptide from the nanospectrum produced by a sub-nanometer diameter pore. [PDF]
Liu X, Dong Z, Timp G.
europepmc +1 more source
Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes
We analyzed over 50 published proteomics datasets to explore the relationship between protein levels and ubiquitination changes across multiple experimental conditions and biological systems. Although ubiquitination is often associated with protein degradation, our analysis shows that changes in ubiquitination do not globally correlate with changes in ...
Nerea Osinalde +3 more
wiley +1 more source
Targeted modulation of protein liquid-liquid phase separation by evolution of amino-acid sequence. [PDF]
Lichtinger SM +3 more
europepmc +1 more source
The amino acid sequence around the active-site cysteine and histidine residues, and the buried cysteine residues in ficin [PDF]
S. Shaukat Husain, Gordon Lowe
openalex +1 more source
Enzymes of the 2‐hydroxyacyl‐CoA lyase group catalyze the condensation of formyl‐CoA with aldehydes or ketones. Thus, by structural adaptation of active sites, practically any pharmaceutically and industrially important 2‐hydroxyacid could be biotechnologically synthesized. Combining crystal structure analysis, active site mutations and kinetic assays,
Michael Zahn +4 more
wiley +1 more source
Taxonomy of Mitochondrial Cytochrome B Proteins of the Same Amino Acid Sequence Length. [PDF]
Zamyatnin AA +2 more
europepmc +1 more source

