Results 231 to 240 of about 3,446,513 (355)

BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma

open access: yesFEBS Open Bio, EarlyView.
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

Analysis of amino acid residues affecting the transcriptional activity of nuclear factor Ya. [PDF]

open access: yesMol Biol Res Commun
Tao D   +11 more
europepmc   +1 more source

Plasma levels of amino acids and osteoporosis: a cross-sectional study [PDF]

open access: gold
Chaoho Ouyang   +6 more
openalex   +1 more source

Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control

open access: yesFEBS Open Bio, EarlyView.
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

Amino Acid Metabolism

open access: yesAnnual Review of Plant Physiology, 1977
Miflin, B. J., Lea, P. J.
openaire   +1 more source

Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes

open access: yesFEBS Open Bio, EarlyView.
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

C2α‐carbanion‐protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2‐hydroxyacyl‐CoA lyase

open access: yesFEBS Open Bio, EarlyView.
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

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