scholarly journals In Vitro Binding of Agrobacterium tumefaciens to Plant Cells from Suspension Culture

1979 ◽  
Vol 63 (2) ◽  
pp. 382-387 ◽  
Author(s):  
Kanji Ohyama ◽  
Lawrence E. Pelcher ◽  
Angelika Schaefer ◽  
Larry C. Fowke
2019 ◽  
Author(s):  
Filip Fratev ◽  
Denisse A. Gutierrez ◽  
Renato J. Aguilera ◽  
suman sirimulla

AKT1 is emerging as a useful target for treating cancer. Herein, we discovered a new set of ligands that inhibit the AKT1, as shown by in vitro binding and cell line studies, using a newly designed virtual screening protocol that combines structure-based pharmacophore and docking screens. Taking together with the biological data, the combination of structure based pharamcophore and docking methods demonstrated reasonable success rate in identifying new inhibitors (60-70%) proving the success of aforementioned approach. A detail analysis of the ligand-protein interactions was performed explaining observed activities.<br>


2004 ◽  
Vol 385 (1) ◽  
pp. 309-317 ◽  
Author(s):  
Zhefeng ZHAO ◽  
Joanna GRUSZCZYNSKA-BIEGALA ◽  
Anna ZOLKIEWSKA

The extracellular domain of integrin α7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 skeletal muscle cells. The effect of ADP-ribosylation on the structure or function of integrin α7β1 has not been explored. In the present study, we show that ADP-ribosylation of integrin α7 takes place exclusively in differentiated myotubes and that this post-translational modification modulates the affinity of α7β1 dimer for its ligand, laminin. ADP-ribosylation in the 37-kDa ‘stalk’ region of α7 that takes place at micromolar NAD+ concentrations increases the binding of the α7β1 dimer to laminin. Increased in vitro binding of integrin α7β1 to laminin after ADP-ribosylation of the 37-kDa fragment of α7 requires the presence of Mn2+ and it is not observed in the presence of Mg2+. In contrast, ADP-ribosylation of the 63-kDa N-terminal region comprising the ligand-binding site of α7 that occurs at approx. 100 μM NAD+ inhibits the binding of integrin α7β1 to laminin. Furthermore, incubation of C2C12 myotubes with NAD+ increases the expression of an epitope on integrin β1 subunit recognized by monoclonal antibody 9EG7. We discuss our results based on the current models of integrin activation. We also hypothesize that ADP-ribosylation may represent a mechanism of regulation of integrin α7β1 function in myofibres in vivo when the continuity of the membrane is compromised and NAD+ is available as a substrate for ecto-ADP-ribosylation.


2016 ◽  
Vol 12 ◽  
pp. P144-P144
Author(s):  
Zhizhen Zeng ◽  
Patricia J. Miller ◽  
Brett M. Connolly ◽  
Stacey S. O’Malley ◽  
Idriss Bennacef ◽  
...  

Life Sciences ◽  
1988 ◽  
Vol 42 (21) ◽  
pp. 2097-2104 ◽  
Author(s):  
Thomas Brücke ◽  
Yuan Feen Tsai ◽  
Catherine McLellan ◽  
Weerachai Singhanyom ◽  
Hank F. Kung ◽  
...  

Synapse ◽  
2005 ◽  
Vol 56 (2) ◽  
pp. 100-104 ◽  
Author(s):  
Subroto Ghose ◽  
Masahiro Fujita ◽  
Paul Morrison ◽  
George Uhl ◽  
Dennis L. Murphy ◽  
...  

1984 ◽  
Vol 9 (Supplement 1) ◽  
pp. 98-99 ◽  
Author(s):  
Leslie M. Shaw ◽  
Roy Altman ◽  
Bernard C. Thompson ◽  
Leona Fields

1991 ◽  
Vol 69 (4) ◽  
pp. 822-830 ◽  
Author(s):  
Ulisses G. Batista ◽  
Verna J. Higgins

The production and distribution of the phytoalexin falcarindiol in tomato foliage infected with leaf mold was examined to determine how the fungus Cladosporium fulvum is able to colonize and sporulate in an apparently antifungal environment. In a compatible interaction (cv. Potentate – C. fulvum race 2.3), by 12 and 15 days after inoculation, solvent-extractable falcarindiol and two other phytoalexins from tomato, compound 2 (probably falcarinol) and compound 3 (unidentified), reached concentrations considerably in excess of ED50 values for inhibition of the fungus. In contrast, intercellular (apoplastic) fluids obtained from similarly infected leaflets contained only traces of falcarindiol. ED50 values for germination and germ-tube growth of C. fulvum increased as the incubation time was extended, suggesting that adaptation or recovery was possible at the concentrations tested. In in vitro experiments, C. fulvum appeared to readily metabolize falcarindiol, as did a Lycopersicon cell suspension culture. Binding of falcarindiol to living and dead fungal and plant cells was also observed. Falcarindiol, injected into tomato leaflets, decreased rapidly and was only recovered in trace amounts by 24 h. The results suggest that falcarindiol and probably the two other phytoalexins do not reach sufficient concentrations in the apoplast of an infected susceptible leaf to have an effect on growth and sporulation of C. fulvum. Key words: leaf mold, Fulvia fulva, falcarindiol, falcarinol.


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