DURATION OF MITOTIC CYCLE IN BRAIN CELLS OF THE MOSQUITO, AEDES DORSALIS

1969 ◽  
Vol 11 (3) ◽  
pp. 673-676 ◽  
Author(s):  
Asit B. Mukherjee ◽  
Don M. Rees
Keyword(s):  
Cell Cycle ◽  
High Resolution ◽  
Mitotic Cycle ◽  
Brain Cells ◽  
Duration Of Mitosis ◽  
High Resolution Autoradiography

Duration of the mitotic cycle and its various phases in the dividing brain cells of Aedes dorsalis larvae has been determined by high-resolution autoradiography. The length of the cell cycle is 10 hours. The duration of G1 is about 1 hour and 15 minutes, DNA synthetic period (S) is approximately 7 hours, G2 is 1 hour and the duration of mitosis (M) is about 45 minutes.

ESTIMATION OF THE MITOTIC CYCLE IN LARVAL BRAIN CELLS OF THE HOUSE FLY

1970 ◽  
Vol 12 (4) ◽  
pp. 779-784 ◽  
Author(s):  
K. Y. Jan ◽  
J. W. Boyes
Keyword(s):  
Cell Cycle ◽  
Mitotic Cycle ◽  
House Fly ◽  
Total Cell ◽  
Brain Cells ◽  
Theoretical Expectation ◽  
Larval Brain ◽  
Third Instar Larvae

An attempt to estimate the mitotic cycle in brain cells of the house fly was made by injecting thymidine-methyl-H3 into third instar larvae. The G2 period plus prophase was about 1.5 hours for some of the XX and XY cells. The graph of the percentages of metaphases labelled deviated considerably from the theoretical expectation, preventing a valid estimation of the duration of G1, S, mitosis and total cell cycle. The probable causes of such deviation have been discussed.

Mise en évidence du rôle, dans la régénération des Amphibiens, d'une glycoprotéine sécrétée par la cape apicale: étude cytochimique et autoradiographique en microscopie électronique

Development ◽  
1974 ◽  
Vol 32 (1) ◽  
pp. 133-145
Author(s):  
Par Claude Chapron
Keyword(s):  
High Resolution ◽  
Epithelial Cells ◽  
Limb Regeneration ◽  
Target Cells ◽  
Silver Particles ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
High Resolution Autoradiography

Evidence for the role of an apical cap glycoprotein in amphibian regeneration: cytochemical and autoradiographic electron-microscopic studies Early during limb regeneration in the newt, an ectodermal apical cap covering a mesodermal blastema is formed. High-resolution autoradiography of these tissues has been carried out after incorporation of [3H]fucose, which is a precursor of glycoproteins. Autoradiography shows that silver particles are located at first on epithelial cells, then on mesenchymatous cells. This observation is consistent with a hypothesis in which the apical cap would elaborate a glycoprotein acting on the blastema. Substructural autoradiography and cytochemistry also show the importance of cellular surfaces for both cells producing glycoprotein and those which are target cells.

scholarly journals The structure of the yeast Ctf3 complex

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Stephen M Hinshaw ◽  
Andrew N Dates ◽  
Stephen C Harrison
Keyword(s):  
Electron Microscopy ◽  
Cell Cycle ◽  
High Resolution ◽  
Atomic Model ◽  
Kinetochore Assembly ◽  
Cryo Electron Microscopy ◽  
Molecular Interpretation ◽  
Spindle Microtubules ◽  
And Function ◽  
Assembly Site

Kinetochores are the chromosomal attachment points for spindle microtubules. They are also signaling hubs that control major cell cycle transitions and coordinate chromosome folding. Most well-studied eukaryotes rely on a conserved set of factors, which are divided among two loosely-defined groups, for these functions. Outer kinetochore proteins contact microtubules or regulate this contact directly. Inner kinetochore proteins designate the kinetochore assembly site by recognizing a specialized nucleosome containing the H3 variant Cse4/CENP-A. We previously determined the structure, resolved by cryo-electron microscopy (cryo-EM), of the yeast Ctf19 complex (Ctf19c, homologous to the vertebrate CCAN), providing a high-resolution view of inner kinetochore architecture (Hinshaw and Harrison, 2019). We now extend these observations by reporting a near-atomic model of the Ctf3 complex, the outermost Ctf19c sub-assembly seen in our original cryo-EM density. The model is sufficiently well-determined by the new data to enable molecular interpretation of Ctf3 recruitment and function.

scholarly journals Cell cycle analysis of brain cells as a growth index in larval cod at different feeding conditions and temperatures

2007 ◽  
Vol 71 (3) ◽  
pp. 485-497 ◽  
Author(s):  
Rafael González-Quirós ◽  
Iyziar Munuera ◽  
Arild Folkvord
Keyword(s):  
Cell Cycle ◽  
Growth Index ◽  
Cell Cycle Analysis ◽  
Brain Cells

High‐Resolution Cytometry for High‐Content Cell Cycle Analysis

2014 ◽  
Vol 70 (1) ◽  
Author(s):  
Laura Furia ◽  
Piergiuseppe Pelicci ◽  
Mario Faretta
Keyword(s):  
Cell Cycle ◽  
High Resolution ◽  
Cell Cycle Analysis

scholarly journals Structures of GapR reveal a central channel which could accommodate B-DNA

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Michael J. Tarry ◽  
Christoph Harmel ◽  
James A. Taylor ◽  
Gregory T. Marczynski ◽  
T. Martin Schmeing
Keyword(s):  
Cell Cycle ◽  
High Resolution ◽  
Dna Binding ◽  
Central Channel ◽  
Biological Functions ◽  
Dna Mutation ◽  
Density Maps ◽  
Lysine Residues ◽  
Α Helix ◽  
Positively Charged

Abstract GapR is a nucleoid-associated protein required for the cell cycle of Caulobacter cresentus. We have determined new crystal structures of GapR to high resolution. As in a recently published structure, a GapR monomer folds into one long N-terminal α helix and two shorter α helices, and assembles into a tetrameric ring with a closed, positively charged, central channel. In contrast to the conclusions drawn from the published structures, we observe that the central channel of the tetramer presented here could freely accommodate B-DNA. Mutation of six conserved lysine residues lining the cavity and electrophoretic mobility gel shift experiments confirmed their role in DNA binding and the channel as the site of DNA binding. Although present in our crystals, DNA could not be observed in the electron density maps, suggesting that DNA binding is non-specific, which could be important for tetramer-ring translocation along the chromosome. In conjunction with previous GapR structures we propose a model for DNA binding and translocation that explains key published observations on GapR and its biological functions.

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