Calcium phosphate–mediated transfection of eukaryotic cells

2005 ◽  
Vol 2 (4) ◽  
pp. 319-320 ◽  
Keyword(s):  
Calcium Phosphate ◽  
Eukaryotic Cells

Calcium Phosphate-Mediated Transfection of Eukaryotic Cells with Plasmid DNAs

2019 ◽  
Vol 2019 (10) ◽  
pp. pdb.prot095430 ◽  
Author(s):  
Priti Kumar ◽  
Arvindhan Nagarajan ◽  
Pradeep D. Uchil
Keyword(s):  
Calcium Phosphate ◽  
Eukaryotic Cells ◽  
Plasmid Dnas

Calcium-phosphate-mediated Transfection of Eukaryotic Cells with Plasmid DNAs

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.prot3871 ◽  
Author(s):  
Joseph Sambrook ◽  
David W. Russell
Keyword(s):  
Calcium Phosphate ◽  
Eukaryotic Cells ◽  
Plasmid Dnas

DNA passage to nuclei: role of endo-lysosomal circuit in eukaryotic Dictyostelium

2009 ◽  
Vol 55 (5) ◽  
pp. 617-621
Author(s):  
Bhavesh Vats ◽  
Harish Padh
Keyword(s):  
Calcium Phosphate ◽  
Recombinant Protein ◽  
Recombinant Protein Production ◽  
Protein Production ◽  
Fluid Phase ◽  
Eukaryotic Cells ◽  
Dna Nanoparticles ◽  
Recombinant Cells ◽  
Foreign Genes

The understanding of DNA passage in eukaryotic cells is still very ambiguous. The route to the nucleus is difficult owing to the barriers, metabolic as well as membranous, posed by the eukaryotic cells. Endocytosis appears to be the most likely process responsible for the transport but is also the major culprit of low transfection efficiencies. Here, we report a study on a eukaryotic amoeba, Dictyostelium discoideum , where by disruption of the endocytic process at the opportune moment, the transformant number increased. We have observed that by disruption of fluid-phase uptake of calcium phosphate DNA nanoparticles, the number of clones increased with the probable increase in number of foreign genes integrating in the host genome. The method described here leads to the possibility of safe and inexpensive methods for transfer of genes required for heterologous recombinant protein production as well as generating therapeutic recombinant cells.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

The Hierarchic Order of Intermediate Filament Structure and Assembly

1985 ◽  
Vol 43 ◽  
pp. 722-725
Author(s):  
U. Aebi ◽  
E.C. Glavaris ◽  
R. Eichner
Keyword(s):  
Tissue Specificity ◽  
Structural Model ◽  
Eukaryotic Cells ◽  
Cdna Sequencing ◽  
Filament Structure ◽  
Keratin Filaments ◽  
Isoelectric Points ◽  
Immunological Crossreactivity

Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.

Calcium Phosphate Bone Cements: A Comprehensive Review

2003 ◽  
Vol 13 (1) ◽  
pp. 8 ◽  
Author(s):  
Denton D. Weiss ◽  
Matthew A. Sachs ◽  
Charles R. Woodard
Keyword(s):  
Calcium Phosphate ◽  
Bone Cements ◽  
Comprehensive Review
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