Results 141 to 150 of about 417,703 (296)

Time after time – circadian clocks through the lens of oscillator theory

open access: yesFEBS Letters, EarlyView.
Oscillator theory bridges physics and circadian biology. Damped oscillators require external drivers, while limit cycles emerge from delayed feedback and nonlinearities. Coupling enables tissue‐level coherence, and entrainment aligns internal clocks with environmental cues.
Marta del Olmo   +2 more
wiley   +1 more source

Multiple ETS family transcription factors bind mutant p53 via distinct interaction regions

open access: yesFEBS Letters, EarlyView.
Mutant p53 gain‐of‐function is thought to be mediated by interaction with other transcription factors. We identify multiple ETS transcription factors that can bind mutant p53 and found that this interaction can be promoted by a PXXPP motif. ETS proteins that strongly bound mutant p53 were upregulated in ovarian cancer compared to ETS proteins that ...
Stephanie A. Metcalf   +6 more
wiley   +1 more source

The newfound relationship between extrachromosomal DNAs and excised signal circles

open access: yesFEBS Letters, EarlyView.
Extrachromosomal DNAs (ecDNAs) contribute to the progression of many human cancers. In addition, circular DNA by‐products of V(D)J recombination, excised signal circles (ESCs), have roles in cancer progression but have largely been overlooked. In this Review, we explore the roles of ecDNAs and ESCs in cancer development, and highlight why these ...
Dylan Casey, Zeqian Gao, Joan Boyes
wiley   +1 more source

Author Correction: A PIP2 substitute mediates voltage sensor-pore coupling in KCNQ activation. [PDF]

open access: yesCommun Biol, 2022
Liu Y   +17 more
europepmc   +1 more source

Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets

open access: yesFEBS Letters, EarlyView.
Cryptochrome and PAS/LOV proteins play intricate roles in circadian clocks where they act as both sensors and mediators of protein–protein interactions. Their ubiquitous presence in signaling networks has positioned them as targets for small‐molecule therapeutics. This review provides a structural introduction to these protein families.
Eric D. Brinckman   +2 more
wiley   +1 more source

CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting

open access: yeseLife
We present near-atomic-resolution cryoEM structures of the mammalian voltage-gated potassium channel Kv1.2 in open, C-type inactivated, toxin-blocked and sodium-bound states at 3.2 Å, 2.5 Å, 3.2 Å, and 2.9 Å.
Yangyu Wu   +6 more
doaj   +1 more source

Pore opening, not voltage sensor movement, underpins the voltage-dependence of facilitation by a hERG blocker. [PDF]

open access: yesMol Pharmacol, 2022
Furutani K   +6 more
europepmc   +1 more source

An upstream open reading frame regulates expression of the mitochondrial protein Slm35 and mitophagy flux

open access: yesFEBS Letters, EarlyView.
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva   +5 more
wiley   +1 more source

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