Controlling cell morphology on amino acid-modified cellulose

Soft Matter ◽  
2008 ◽  
Vol 4 (5) ◽  
pp. 1059 ◽  
Author(s):  
Deepak M. Kalaskar ◽  
Julie E. Gough ◽  
Rein V. Ulijn ◽  
William W. Sampson ◽  
David J. Scurr ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Morphology ◽  
Modified Cellulose

Characterisation of amino acid modified cellulose surfaces using ToF-SIMS and XPS

Cellulose ◽  
2010 ◽  
Vol 17 (4) ◽  
pp. 747-756 ◽  
Author(s):  
D. M. Kalaskar ◽  
R. V. Ulijn ◽  
J. E. Gough ◽  
M. R. Alexander ◽  
D. J. Scurr ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tof Sims ◽  
Modified Cellulose

scholarly journals DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane.

1996 ◽  
Vol 16 (4) ◽  
pp. 1770-1776 ◽  
Author(s):  
H Hasegawa ◽  
E Kiyokawa ◽  
S Tanaka ◽  
K Nagashima ◽  
N Gotoh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Morphology ◽  
Tyrosine Kinases ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Nucleotide Exchange ◽  
Reading Frame ◽  
Guanine Nucleotide Exchange ◽  
Acid Protein

CRK belongs to a family of adaptor proteins that consist mostly of SH2 and SH3 domains. Far Western blotting with CRK SH3 has demonstrated that it binds to 135- to 145-, 160-, and 180-kDa proteins. The 135- to 145-kDa protein is C3G, a CRK SH3-binding guanine nucleotide exchange protein. Here, we report on the molecular cloning of the 180-kDa protein, which is designated DOCK180 (180-kDa protein downstream of CRK). The isolated cDNA contains a 5,598-bp open reading frame encoding an 1,866-amino-acid protein. The deduced amino acid sequence did not reveal any significant homology to known proteins, except that an SH3 domain was identified at its amino terminus. To examine the function of DOCK180, a Ki-Ras farnesylation signal was fused to the carboxyl terminus of DOCK180, a strategy that has been employed successfully for activation of adaptor-binding proteins in vivo. Whereas wild-type DOCK180 accumulated diffusely in the cytoplasm and did not have any effect on cell morphology, farnesylated DOCK180 was localized on the cytoplasmic membrane and changed spindle 3T3 cells to flat, polygonal cells. These results suggest that DOCK180 is a new effector molecule which transduces signals from tyrosine kinases through the CRK adaptor protein.

The Mode of Action of Thrombin

1958 ◽  
Vol 02 (03/04) ◽  
pp. 205-217 ◽  
Author(s):  
K Laki ◽  
Jules A. Gladner ◽  
J. E Folk ◽  
D. R Kominz
Keyword(s):  
Amino Acid ◽  
Active Center ◽  
Mode Of Action ◽  
Amino Acid Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Quantitative Amino Acid Analysis ◽  
Fibrinogen Molecule ◽  
Modified Cellulose

SummaryThe peptides liberated from fibrinogen by the action of thrombin have been isolated on modified cellulose adsorbents. These peptides have been characterized by sedimentation-diffusion measurements by quantitative amino acid analysis, and by C-terminal analysis. Both peptides were found to contain arginine as C-terminal amino acid. Thrombin thus splits specific arginyl-glycine bonds in the fibrinogen molecule. The specificity of thrombin is discussed in view of the finding that the active center of thrombin is similar to that of trypsin and chymotrypsin.

scholarly journals Amino Acid-Dependent Alterations in Cell Wall and Cell Morphology of Deinococcus indicus DR1

2019 ◽  
Vol 10 ◽  
Author(s):  
Deepika Chauhan ◽  
Pulkit Anupam Srivastava ◽  
Barbara Ritzl ◽  
Ragothaman M. Yennamalli ◽  
Felipe Cava ◽  
...  
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Cell Morphology

Amino acid modified cellulose whiskers

RSC Advances ◽  
2011 ◽  
Vol 1 (9) ◽  
pp. 1695 ◽  
Author(s):  
Carolina Andreia Cateto ◽  
Arthur Ragauskas
Keyword(s):  
Amino Acid ◽  
Cellulose Whiskers ◽  
Modified Cellulose

Cell morphology, volume, and surface area determinations from multilevel contouring within HVEM micrographs of serial sections and whole-cell mounts

1987 ◽  
Vol 45 ◽  
pp. 588-589
Author(s):  
M. Marko ◽  
A. Leith ◽  
D. Parsons
Keyword(s):  
Surface Area ◽  
Electron Micrographs ◽  
Cell Morphology ◽  
Individual Variation ◽  
Serial Section ◽  
Stereo Pair ◽  
Complex Structures ◽  
Serial Sections ◽  
Surface Areas ◽  
Computer Based

The use of serial sections and computer-based 3-D reconstruction techniques affords an opportunity not only to visualize the shape and distribution of the structures being studied, but also to determine their volumes and surface areas. Up until now, this has been done using serial ultrathin sections.The serial-section approach differs from the stereo logical methods of Weibel in that it is based on the Information from a set of single, complete cells (or organelles) rather than on a random 2-dimensional sampling of a population of cells. Because of this, it can more easily provide absolute values of volume and surface area, especially for highly-complex structures. It also allows study of individual variation among the cells, and study of structures which occur only infrequently.We have developed a system for 3-D reconstruction of objects from stereo-pair electron micrographs of thick specimens.

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