Results 201 to 210 of about 896,632 (275)

A dataset for geographical origin identification of tobacco leaves from multiple countries using near-infrared spectroscopy and chemometric analysis. [PDF]

open access: yesData Brief
Chen H   +16 more
europepmc   +1 more source

Differential regulation of ZFAS1 splice variants by endoplasmic reticulum stress in hepatocyte cell lines

open access: yesFEBS Open Bio, EarlyView.
ZFAS1 is a lncRNA promoting cell proliferation and migration, exhibiting high expression in various cancers. It is conserved, widely expressed, and produces multiple splice variants with unclear roles. We identified several splice variants in hepatocyte models, and found that inhibiting or suppressing regulators of the unfolded protein response (PERK ...
Sébastien Soubeyrand   +2 more
wiley   +1 more source

The cooperative regulation of miR‐221 by APE1 and AUF1 impacts p27Kip1 defining a miR signature relevant for cervical cancer

open access: yesFEBS Open Bio, EarlyView.
A regulatory axis involving APE1, AUF1, and miR‐221 is proposed. Pri‐miR‐221 is processed by DROSHA and DICER to generate mature miR‐221, which targets p27Kip1 mRNA. APE1 and AUF1 compete for pre‐miR‐221 binding. Reduced APE1/AUF1 levels impair miR‐221 biogenesis, decrease p27Kip1 mRNA degradation, and promote cell cycle progression, chemoresistance ...
Matilde Clarissa Malfatti   +3 more
wiley   +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

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

Advanced fractional soliton solutions of the Joseph-Egri equation via Tanh-Coth and Jacobi function methods. [PDF]

open access: yesSci Rep
Shakeel K   +6 more
europepmc   +1 more source

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