Results 201 to 210 of about 3,349,066 (314)

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

Fuel-Switching Capability [PDF]

open access: yes
Bousquet, Alain, Ladoux, Norbert
core  

Dihydroorotate dehydrogenase (DHODH) regulates trophoblast syncytialization through organelle stress–induced cellular senescence

open access: yesFEBS Open Bio, EarlyView.
The inhibition of mitochondrial dihydroorotate dehydrogenase (DHODH) impairs syncytialization and induces cellular senescence via mitochondrial and endoplasmic reticulum stress in human trophoblast stem cells, elevating sFlt1/PlGF levels, a hallmark of placental dysfunction in hypertensive disorders of pregnancy.
Kanoko Yoshida   +6 more
wiley   +1 more source

Anchorage‐independent and faster growth in clonal population from UV‐irradiated NER‐deficient cells

open access: yesFEBS Open Bio, EarlyView.
UV‐irradiated cells expressing a DDB2 mutant protein unable to interact with PCNA (DDB2PCNA‐) form clones able to grow without anchorage. Different experimental approaches reveal heterogeneity in cell cycle regulation and drug response within these clones, emphasizing the crucial role of the DDB2‐PCNA interaction in preventing cellular transformation ...
Paola Perucca   +6 more
wiley   +1 more source

Healthcare professionals' beliefs on promoting physical activity in oncology: a COM-B framework analysis. [PDF]

open access: yesSupport Care Cancer
Carraça EV   +7 more
europepmc   +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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