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1.
Nano Lett ; 24(2): 640-648, 2024 Jan 17.
Artículo en Inglés | MEDLINE | ID: mdl-38166209

RESUMEN

We demonstrate an important step toward on-chip integration of single-photon sources at room temperature. Excellent photon directionality is achieved with a hybrid metal-dielectric bullseye antenna, while back-excitation is permitted by placement of the emitter in a subwavelength hole positioned at its center. The unique design enables a direct back-excitation and very efficient front coupling of emission either to a low numerical aperture (NA) optics or directly to an optical fiber. To show the versatility of the concept, we fabricate devices containing either a colloidal quantum dot or a nanodiamond containing silicon-vacancy centers, which are accurately positioned using two different nanopositioning methods. Both of these back-excited devices display front collection efficiencies of ∼70% at NAs as low as 0.5. The combination of back-excitation with forward directionality enables direct coupling of the emitted photons into a proximal optical fiber without any coupling optics, thereby facilitating and simplifying future integration.

2.
Biol Direct ; 19(1): 41, 2024 May 29.
Artículo en Inglés | MEDLINE | ID: mdl-38812048

RESUMEN

The enzymes performing protein post-translational modifications (PTMs) form a critical post-translational regulatory circuitry that orchestrates literally all cellular processes in the organism. In particular, the balance between cellular stemness and differentiation is crucial for the development of multicellular organisms. Importantly, the fine-tuning of this balance on the genetic level is largely mediated by specific PTMs of histones including lysine methylation. Lysine methylation is carried out by special enzymes (lysine methyltransferases) that transfer the methyl group from S-adenosyl-L-methionine to the lysine residues of protein substrates. Set7/9 is one of the exemplary protein methyltransferases that however, has not been fully studied yet. It was originally discovered as histone H3 lysine 4-specific methyltransferase, which later was shown to methylate a number of non-histone proteins that are crucial regulators of stemness and differentiation, including p53, pRb, YAP, DNMT1, SOX2, FOXO3, and others. In this review we summarize the information available to date on the role of Set7/9 in cellular differentiation and tissue development during embryogenesis and in adult organisms. Finally, we highlight and discuss the role of Set7/9 in pathological processes associated with aberrant cellular differentiation and self-renewal, including the formation of cancer stem cells.


Asunto(s)
Diferenciación Celular , N-Metiltransferasa de Histona-Lisina , N-Metiltransferasa de Histona-Lisina/metabolismo , N-Metiltransferasa de Histona-Lisina/genética , Humanos , Animales , Procesamiento Proteico-Postraduccional , Metilación , Células Madre/metabolismo
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