Dynamics and biological relevance of epigenetic N6-methyladenine DNA modification in eukaryotic cells

It is now clear that eukaryotic cells produce many thousands of non-coding RNAs. The least well-studied of these are longer than 200 nt and are known as lncRNAs (long non-coding RNAs). These loci are of particular interest as their biological relevance remains uncertain. Sequencing projects have identified thousands of these loci in a variety of species, from flies to humans. Genome-wide scans for functionality, such as evolutionary and expression analyses, suggest that many of these molecules have functional roles to play in the cell. Nevertheless, only a handful of lncRNAs have been experimentally investigated, and most of these appear to possess roles in regulating gene expression at a variety of different levels. Several lncRNAs have also been implicated in cancer. This evidence suggests that lncRNAs represent a new class of non-coding gene whose importance should become clearer upon further experimental investigation.

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Radiation-Induced DNA Lesions in Eukaryotic Cells, Their Repair and Biological Relevance

Biological Effects and Physics of Solar and Galactic Cosmic Radiation ◽

10.1007/978-1-4615-2918-7_1 ◽

1993 ◽

pp. 1-31 ◽

Cited By ~ 3

Author(s):

M. Frankenberg-Schwager

Keyword(s):

Dna Lesions ◽

Eukaryotic Cells ◽

Biological Relevance ◽

Radiation Induced

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Inertial focusing with sub-micron resolution for separation of bacteria

Lab on a Chip ◽

10.1039/c9lc00080a ◽

2019 ◽

Vol 19 (7) ◽

pp. 1257-1266 ◽

Cited By ~ 20

Author(s):

Javier Cruz ◽

Tiscar Graells ◽

Mats Walldén ◽

Klas Hjort

Keyword(s):

Eukaryotic Cells ◽

Inertial Focusing ◽

Biological Relevance ◽

Curved Channels

Inertial focusing in curved channels is demonstrated for particles between 0.5 and 2.0 μm in diameter; a range of biological relevance since it comprises a multitude of bacteria and organelles of eukaryotic cells.

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DNA-Modification of Eukaryotic Cells

Small ◽

10.1002/smll.201201852 ◽

2012 ◽

Vol 9 (2) ◽

pp. 255-262 ◽

Cited By ~ 19

Author(s):

Katrin Vogel ◽

Maximilian Glettenberg ◽

Hendrik Schroeder ◽

Christof M. Niemeyer

Keyword(s):

Eukaryotic Cells ◽

Dna Modification

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Induction, repair and biological relevance of radiation-induced DNA lesions in eukaryotic cells

Radiation and Environmental Biophysics ◽

10.1007/bf01210408 ◽

1990 ◽

Vol 29 (4) ◽

pp. 273-292 ◽

Cited By ~ 139

Author(s):

M. Frankenberg-Schwager

Keyword(s):

Dna Lesions ◽

Eukaryotic Cells ◽

Biological Relevance ◽

Radiation Induced

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

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100122964 ◽

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.

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Structure of clathrin cages and coats in ice

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010014213x ◽

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.

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The Hierarchic Order of Intermediate Filament Structure and Assembly

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100120308 ◽

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.

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