2017
DOI: 10.1016/j.biocel.2017.06.001
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Targeting proteins to RNA transcription and processing sites within the nucleus

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Cited by 4 publications
(4 citation statements)
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“…ALP, being a promiscuous ectoenzyme on the cell membrane, can enable the ENS of a wide range of substrates for many innovative applications, such as the patching of lipid rafts, as reported by Zhang et al 444 As shown in Figure 69, the authors used the metal complex Ru(II)(bpy) 3 as a threedimensional (3D) core to conjugate with the D-phosphotetrapeptide (Nap-ffk p y 263 ) to generate a metal complex (186) as the substrate of ALP. The authors, after confirming that ALP converted the solution of 186 to a hydrogel, incubated 186 with HeLa, HS-5, Ect1/E6E7, and A375 cells.…”
Section: Peri/intracellular Ensmentioning
confidence: 99%
See 1 more Smart Citation
“…ALP, being a promiscuous ectoenzyme on the cell membrane, can enable the ENS of a wide range of substrates for many innovative applications, such as the patching of lipid rafts, as reported by Zhang et al 444 As shown in Figure 69, the authors used the metal complex Ru(II)(bpy) 3 as a threedimensional (3D) core to conjugate with the D-phosphotetrapeptide (Nap-ffk p y 263 ) to generate a metal complex (186) as the substrate of ALP. The authors, after confirming that ALP converted the solution of 186 to a hydrogel, incubated 186 with HeLa, HS-5, Ect1/E6E7, and A375 cells.…”
Section: Peri/intracellular Ensmentioning
confidence: 99%
“…Recent advances suggest that many enzymes act within NSs to facilitate the regulation of gene expression. , The best known molecular mechanism of nuclear speckle localization is a phosphorylation/dephosphorylation cycle of the arginine/serine repeat (RS) domain of serine rich (SR) proteins. Although it is generally believed that RS domain phosphorylation drives SR proteins from NSs to the nucleoplasm, a recent study reveals that synergistic interplay between PP1 and two splicing kinases (SRPK1 and CLK1) regulate the location of SR proteins, such as SRSF1 . Adams et al reported that SRSF1 binds to PP1 through the RRM1 domain and represses the catalytic activity of PP1 through an allosteric mechanism.…”
Section: Enzymatic Noncovalent Synthesis In Naturementioning
confidence: 99%
“…NB are made up of RNA and proteins, and hold their structure by the interactions existing between them: RNA-protein or protein-protein. These proteins are constantly exchanged with the nucleoplasm regulated by post-translational modifications like phosphorylation and SUMOylation [38], there being proteins common to different NB and others specific of a certain type of NB [3,29,39,47; https://www.ebi.ac.uk/QuickGO/term/]. With respect to the formation of NB, three models are considered: The first is the model of stochastic assembly where the components of the NB are grouped without a defined order; the assembly is random.…”
Section: Introductionmentioning
confidence: 99%
“…Nuclear bodies. It's shown the percentages in which the different nuclear bodies were mentioned in the selected articles[1,5,7,9,11,12,17,20,23,24,26,29,30,32,33,35,36,39,42,43,45,47,51,52,53,55] …”
mentioning
confidence: 99%