scholarly journals Molecular composition of Ro small ribonucleoprotein complexes in human cells. Intracellular localization of the 60- and 52-kD proteins.

1994 ◽  
Vol 93 (4) ◽  
pp. 1637-1644 ◽  
Author(s):  
A Kelekar ◽  
M R Saitta ◽  
J D Keene
Keyword(s):  
Intracellular Localization ◽  
Human Cells ◽  
Molecular Composition ◽  
Ribonucleoprotein Complexes

scholarly journals Correction: Dependence of the Ce(iii)/Ce(iv) ratio on intracellular localization in ceria nanoparticles internalized by human cells

Nanoscale ◽  
2017 ◽  
Vol 9 (15) ◽  
pp. 5021-5021 ◽  
Author(s):  
Daniela Ferraro ◽  
Ilenia G. Tredici ◽  
Paolo Ghigna ◽  
Hiram Castillo-Michel ◽  
Andrea Falqui ◽  
...  
Keyword(s):  
Intracellular Localization ◽  
Human Cells ◽  
Ceria Nanoparticles

Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein

Microbiology ◽  
2000 ◽  
Vol 81 (1) ◽  
pp. 135-142 ◽  
Author(s):  
Rosario Bullido ◽  
Paulino Gómez-Puertas ◽  
Carmen Albo ◽  
Agustín Portela
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Fluorescent Protein ◽  
Intracellular Localization ◽  
Phosphorylation Site ◽  
Nuclear Accumulation ◽  
Systematic Analysis ◽  
Ribonucleoprotein Complexes ◽  
Cytoplasmic Transport ◽  
Green Fluorescent

A systematic analysis was carried out to identify the amino acid signals that regulate the nucleo-cytoplasmic transport of the influenza A virus nucleoprotein (NP). The analysis involved determining the intracellular localization of eight deleted recombinant NP proteins and 14 chimeric proteins containing the green fluorescent protein fused to different NP fragments. In addition, the subcellular distribution of NP derivatives that contained specific substitutions at serine-3, which is the major phosphorylation site of the A/Victoria/3/75 NP, were analysed. From the results obtained, it is concluded that the NP contains three signals involved in nuclear accumulation and two regions that cause cytoplasmic accumulation of the fusion proteins. One of the karyophilic signals was located at the N terminus of the protein, and the data obtained suggest that the functionality of this signal can be modified by phosphorylation at serine-3. These findings are discussed in the context of the transport of influenza virus ribonucleoprotein complexes into and out of the nucleus.

scholarly journals Analysis of the molecular composition of Ro ribonucleoprotein complexes

2000 ◽  
Vol 267 (9) ◽  
pp. 2778-2789 ◽  
Author(s):  
Gustav Fabini ◽  
Saskia A. Rutjes ◽  
Christof Zimmermann ◽  
Ger J. M. Pruijn ◽  
Günter Steiner
Keyword(s):  
Molecular Composition ◽  
Ribonucleoprotein Complexes ◽  
Ro Ribonucleoprotein

scholarly journals CRISPR prime editing with ribonucleoprotein complexes in zebrafish and primary human cells

2021 ◽  
Author(s):  
Karl Petri ◽  
Weiting Zhang ◽  
Junyan Ma ◽  
Andrea Schmidts ◽  
Hyunho Lee ◽  
...  
Keyword(s):  
Human Cells ◽  
Ribonucleoprotein Complexes ◽  
Primary Human Cells

scholarly journals Intracellular Localization of PNA in Human Cells upon its Introduction by Electroporation

2012 ◽  
Vol 7 (3) ◽  
pp. 1934578X1200700
Author(s):  
Eri Noguchi ◽  
Narumi Shigi ◽  
Makoto Komiyama
Keyword(s):  
Cell Division ◽  
Peptide Nucleic Acid ◽  
Intracellular Localization ◽  
Repeat Sequence ◽  
Human Cells ◽  
Time Dependent ◽  
Telomere Repeat ◽  
Dna Analogs ◽  
Coii Gene ◽  
Telomere Repeat Sequence

Peptide nucleic acid (PNA) is one of the most useful DNA analogs in a wide variety of gene analysis in human cells. In order to exhibit its maximal functions, PNA must be localized to a desired place (e.g., nucleus, cytoplasm and other organelles). Here, we introduced PNAs into HeLa cells by electroporation and examined their localization at various time points. The PNA which binds to the mitochondrial COII gene was initially accumulated in the nucleus, and thereafter mostly transferred to cytoplasm. This time-dependent intracellular localization of PNA is ascribed to the breakdown of the nuclear envelope in the cell division. On the other hand, another PNA that binds to telomere repeat sequence mostly remained in the nucleus, even after the cell division occurred. The retention of this PNA in the nucleus was further enhanced when it was conjugated with Cy3.

scholarly journals Author Correction: CRISPR prime editing with ribonucleoprotein complexes in zebrafish and primary human cells

2021 ◽  
Author(s):  
Karl Petri ◽  
Weiting Zhang ◽  
Junyan Ma ◽  
Andrea Schmidts ◽  
Hyunho Lee ◽  
...  
Keyword(s):  
Human Cells ◽  
Ribonucleoprotein Complexes ◽  
Primary Human Cells

scholarly journals Dependence of the Ce(iii)/Ce(iv) ratio on intracellular localization in ceria nanoparticles internalized by human cells

Nanoscale ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 1527-1538 ◽  
Author(s):  
Daniela Ferraro ◽  
Ilenia G. Tredici ◽  
Paolo Ghigna ◽  
Hiram Castillio-Michel ◽  
Andrea Falqui ◽  
...  
Keyword(s):  
Intracellular Localization ◽  
Human Cells ◽  
Ceria Nanoparticles

scholarly journals Intracellular Localization of 8-Oxo-dGTPase in Human Cells, with Special Reference to the Role of the Enzyme in Mitochondria

1995 ◽  
Vol 270 (24) ◽  
pp. 14659-14665 ◽  
Author(s):  
Dongchon Kang ◽  
Jun-ichi Nishida ◽  
Akihiro Iyama ◽  
Yusaku Nakabeppu ◽  
Masato Furuichi ◽  
...  
Keyword(s):  
Special Reference ◽  
Intracellular Localization ◽  
Human Cells
Sign in / Sign up

Export Citation Format

Share Document