Protein Dual Targeting
Mostrando 1-12 de 44 artigos, teses e dissertações.
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1. Simultaneously expressed miR-424 and miR-381 synergistically suppress the proliferation and survival of renal cancer cells---Cdc2 activity is up-regulated by targeting WEE1
OBJECTIVES: MiRNAs are intrinsic RNAs that interfere with protein translation. Few studies on the synergistic effects of miRNAs have been reported. Both miR-424 and miR-381 have been individually reported to be involved in carcinogenesis. They share a common putative target, WEE1, which is described as an inhibitor of G2/M progression. Here, we studied the
Clinics. Publicado em: 2013-06
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2. Identificação de interatores putativos envolvidos na localização de proteínas de duplo direcionamento em Arabidopsis thaliana / Identification of putative interactors involved in the localization of dual-targeted proteins in Arabidopsis thaliana
Most organellar proteins are nuclear encoded, synthesized in the cytosol and then targeted to their destination. Specific subcellular targeting is conducted by a complex machinery for the specific localization of the proteins, which includes targeting sequences, cytosolic proteins and specific organelar receptors. However, little is known about the process t
Publicado em: 2011
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3. Estudos sobre o duplo direcionamento de proteínas de plantas / Studies on the dual targeting of plant proteins
Compartimentalization of the metabolic processes in organelles, each one having a characteristic protein pool and distinct functions, is a property of eukaryote cells. A highly specific cellular system directs proteins, which are synthesized in the cytosol, to the proper organelles. However, due to functional overlaps between organelles, a given protein may
Publicado em: 2008
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4. Subcellular localization of sugarcane (Sccharum spp.) proteins : in silico characterization and functional evaluation / Localização subcelular de proteinas de cana-de-açucar (Sccharum spp.) : caracterização in silico e avaliação funcional
Plant cells are highly organized and many biological processes are associated with specialized subcellular structures. Subcellular localization is a key feature of proteins, since it is related to biological function. The determination of subcellular localization using computational prediction is a highly desirable strategy because experimental approaches ar
Publicado em: 2008
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5. Dual-Domain, Dual-Targeting Organellar Protein Presequences in Arabidopsis Can Use Non-AUG Start Codons
The processes accompanying endosymbiosis have led to a complex network of interorganellar protein traffic that originates from nuclear genes encoding mitochondrial and plastid proteins. A significant proportion of nucleus-encoded organellar proteins are dual targeted, and the process by which a protein acquires the capacity for both mitochondrial and plastid
American Society of Plant Biologists.
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6. Dual Targeting of Osh1p, a Yeast Homologue of Oxysterol-binding Protein, to both the Golgi and the Nucleus-Vacuole Junction
Oxysterol binding protein (OSBP) is the only protein known to bind specifically to the group of oxysterols with potent effects on cholesterol homeostasis. Although the function of OSBP is currently unknown, an important role is implicated by the existence of multiple homologues in all eukaryotes so far examined. OSBP and a subset of homologues contain p
The American Society for Cell Biology.
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7. Membrane Trafficking of Heterotrimeric G Proteins via the Endoplasmic Reticulum and Golgi
Membrane targeting of G-protein αβγ heterotrimers was investigated in live cells by use of Gα and Gγ subunits tagged with spectral mutants of green fluorescent protein. Unlike Ras proteins, Gβγ contains a single targeting signal, the CAAX motif, which directed the dimer to the endoplasmic reticulum. Endomembrane localization of farnesylated Gγ1, but
The American Society for Cell Biology.
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8. Determinants of membrane-targeting and transmembrane translocation during bacterial protein export.
We have separately analyzed membrane-targeting and membrane translocation of an exported bacterial protein. The precursor of the outer membrane protein LamB of Escherichia coli was synthesized in vitro and translocated into inverted plasma membrane vesicles under co- and post-translational conditions. The translation/translocation products of LamB were subse
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9. Signal Peptide-Dependent Targeting of a Rice α-Amylase and Cargo Proteins to Plastids and Extracellular Compartments of Plant Cells1
α-Amylases are important enzymes for starch degradation in plants. However, it has been a long-running debate as to whether α-amylases are localized in plastids where starch is stored. To study the subcellular localization of α-amylases in plant cells, a rice (Oryza sativa) α-amylase, αAmy3, with or without its own signal peptide (SP) was expressed in t
American Society of Plant Biologists.
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10. Targeting of a Tail-anchored Protein to Endoplasmic Reticulum and Mitochondrial Outer Membrane by Independent but Competing Pathways
Many mitochondrial outer membrane (MOM) proteins have a transmembrane domain near the C terminus and an N-terminal cytosolic moiety. It is not clear how these tail-anchored (TA) proteins posttranslationally select their target, but C-terminal charged residues play an important role. To investigate how discrimination between MOM and endoplasmic reticulum
The American Society for Cell Biology.
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11. Inhibition of HIV-1 multiplication by antisense U7 snRNAs and siRNAs targeting cyclophilin A
Human immunodeficiency virus 1 (HIV-1) multiplication depends on a cellular protein, cyclophilin A (CyPA), that gets integrated into viral particles. Because CyPA is not required for cell viability, we attempted to block its synthesis in order to inhibit HIV-1 replication. For this purpose, we used antisense U7 small nuclear RNAs (snRNAs) that disturb CyPA p
Oxford University Press.
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12. Import Pathways of Chloroplast Interior Proteins and the Outer-Membrane Protein OEP14 Converge at Toc75
Most chloroplast outer-membrane proteins are synthesized at their mature size without cleavable targeting signals. Their insertion into the outer membrane is insensitive to thermolysin pretreatment of chloroplasts and does not require ATP. It has therefore been assumed that insertion of outer-membrane proteins proceeds through a different pathway from import
American Society of Plant Biologists.