Results 141 to 150 of about 1,195,384 (219)

Threonine 348 regulates the subcellular localization of PTEN

open access: yesFEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP‐ribosylating toxin AB to establish a persistent infection

open access: yesFEBS Open Bio, EarlyView.
The two catalytic subunits of typhoid toxin dissociate from the holotoxin in the ER of an intoxicated cell, but only CdtB exits the ER to generate immunosuppressive effects. PltA is retained in the ER and sequestered from its cytosolic target, thus allowing the anti‐inflammatory effects of CdtB to promote intestinal colonization.
Maria C. Zabala‐Rodriguez   +4 more
wiley   +1 more source

Retraction Note to: KLF5 regulated lncRNA RP1 promotes the growth and metastasis of breast cancer via repressing p27kip1 translation

open access: yesCell Death and Disease
Xiaoting Jia   +13 more
doaj   +1 more source

Ubiquitin receptor-mediated, ubiquitin-independent targeted protein degradation via 26<i>S</i> proteasomes. [PDF]

open access: yesSci Adv
Park SH   +11 more
europepmc   +1 more source

A minimal cellulosome‐like system in Cellulosilyticum lentocellum

open access: yesFEBS Open Bio, EarlyView.
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan   +2 more
wiley   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

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