Biofilm and Planktonic Bacteria Differentially Express a Small Molecule (<3kD), Heat‐Stable, Protease‐Resistant Factor that Affects Bovine Neutrophil Function in a NF‐Kappa β‐Independent Mechanism

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Joey Lockhart ◽  
Andre Buret ◽  
Douglas Morck
Keyword(s):  
Small Molecule ◽  
Differentially Express ◽  
Neutrophil Function ◽  
Heat Stable ◽  
Planktonic Bacteria ◽  
Independent Mechanism ◽  
Bovine Neutrophil

Effects of dexamethasone and Mycoplasma bovis on bovine neutrophil function in vitro

2015 ◽  
Vol 164 (1-2) ◽  
pp. 67-73 ◽  
Author(s):  
Hussain A. Alabdullah ◽  
Lawrence K. Fox ◽  
John M. Gay ◽  
George M. Barrington ◽  
Robert H. Mealey
Keyword(s):  
Neutrophil Function ◽  
Mycoplasma Bovis ◽  
Bovine Neutrophil

Taking aim at protein translation in AML

Blood ◽  
2009 ◽  
Vol 114 (8) ◽  
pp. 1458-1459 ◽  
Author(s):  
Martin Carroll
Keyword(s):  
Tumor Cells ◽  
Small Molecule ◽  
Translation Initiation ◽  
Protein Translation ◽  
Translation Control ◽  
Active Protein ◽  
Initiation Complex ◽  
Molecule Inhibitor ◽  
Growing Body ◽  
Independent Mechanism

Abstract In this issue of Blood, Tamburini and colleagues have studied the regulation of protein translation control in primary AML cells and describe a mTORC1-independent mechanism of regulation of the translation initiation complex that can be targeted with 4EGI-1, a small molecule inhibitor of translation, leading to death of the cells.1 This and other recent studies add to a growing body of evidence that AML cells have a critical dependence on active protein translation, which may provide an Achilles' heel for the tumor cells that can be targeted therapeutically.

Interactive effects of dexamethasone and opsonized Mycoplasma bovis on bovine neutrophil function in vitro

2018 ◽  
Vol 196 ◽  
pp. 18-21
Author(s):  
Hussain A. Alabdullah ◽  
Lawrence K. Fox ◽  
John M. Gay ◽  
George M. Barrington
Keyword(s):  
Neutrophil Function ◽  
Interactive Effects ◽  
Mycoplasma Bovis ◽  
Bovine Neutrophil

scholarly journals Improving the Thermostability of Raw-Starch-Digesting Amylase from a Cytophaga sp. by Site-Directed Mutagenesis

2003 ◽  
Vol 69 (4) ◽  
pp. 2383-2385 ◽  
Author(s):  
Rong-Jen Shiau ◽  
Hui-Chen Hung ◽  
Chii-Ling Jeang
Keyword(s):  
Amino Acids ◽  
Enzymatic Activity ◽  
Half Life ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Raw Starch ◽  
Heat Stable ◽  
Independent Mechanism

ABSTRACT A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65°C, the half-life of this mutant RSDA, which, compared with the wild-type RSDA, lacks amino acids R178 and G179, was increased 20-fold. While the wild type was inactivated completely at pH 3.0, the mutant RSDA still retained 41% of its enzymatic activity. The enhancement of RSDA thermostability was demonstrated to be via a Ca2+-independent mechanism.

scholarly journals FtsZ‐Independent Mechanism of Division Inhibition by the Small Molecule PC190723 inEscherichia coli

2019 ◽  
Vol 3 (11) ◽  
pp. 1900021 ◽  
Author(s):  
Somya Khare ◽  
Jen Hsin ◽  
Nohemy A. Sorto ◽  
Gabriella M. Nepomuceno ◽  
Jared T. Shaw ◽  
...  
Keyword(s):  
Small Molecule ◽  
Inescherichia Coli ◽  
Independent Mechanism
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