scholarly journals antibacTR: dynamic antibacterial-drug-target ranking integrating comparative genomics, structural analysis and experimental annotation

BMC Genomics ◽  
2014 ◽  
Vol 15 (1) ◽  
pp. 36 ◽  
Author(s):  
Alejandro Panjkovich ◽  
Isidre Gibert ◽  
Xavier Daura
Keyword(s):  
Comparative Genomics ◽  
Structural Analysis ◽  
Drug Target ◽  
Antibacterial Drug ◽  
Experimental Annotation ◽  
Antibacterial Drug Target

scholarly journals Structural insights into stereochemical inversion by diaminopimelate epimerase: An antibacterial drug target

2006 ◽  
Vol 103 (23) ◽  
pp. 8668-8673 ◽  
Author(s):  
B. Pillai ◽  
M. M. Cherney ◽  
C. M. Diaper ◽  
A. Sutherland ◽  
J. S. Blanchard ◽  
...  
Keyword(s):  
Drug Target ◽  
Antibacterial Drug ◽  
Antibacterial Drug Target ◽  
Structural Insights

scholarly journals Peptide Deformylase as an Antibacterial Drug Target: Assays for Detection of Its Inhibition in Escherichia coli Cell Homogenates and Intact Cells

2001 ◽  
Vol 45 (4) ◽  
pp. 1053-1057 ◽  
Author(s):  
Christian M. Apfel ◽  
Stefan Evers ◽  
Christian Hubschwerlen ◽  
Wolfgang Pirson ◽  
Malcolm G. P. Page ◽  
...  
Keyword(s):  
Drug Target ◽  
Peptide Deformylase ◽  
Translation System ◽  
Antibacterial Drug ◽  
Bacterial Cells ◽  
Methionine Aminopeptidase ◽  
Intact Cells ◽  
Physiological Conditions ◽  
A Cell ◽  
Antibacterial Drug Target

ABSTRACT An assay was developed to determine the activity of peptide deformylase (PDF) inhibitors under conditions as close as possible to the physiological situation. The assay principle is the detection of N-terminal [35S]methionine labeling of a protein that contains no internal methionine. If PDF is active, the deformylation of the methionine renders the peptide a substrate for methionine aminopeptidase, resulting in the removal of the N-terminal methionine label. In the presence of a PDF inhibitor, the deformylation is blocked so that the N-formylated peptide is not processed and the label is detected. Using this assay, it is possible to determine the PDF activity under near-physiological conditions in a cell-free transcription-translation system as well as in intact bacterial cells.

scholarly journals Assessment of Pseudomonas aeruginosa N5,N10-Methylenetetrahydrofolate Dehydrogenase - Cyclohydrolase as a Potential Antibacterial Drug Target

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e35973 ◽  
Author(s):  
Thomas C. Eadsforth ◽  
Mary Gardiner ◽  
Fernando V. Maluf ◽  
Stuart McElroy ◽  
Daniel James ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Drug Target ◽  
Antibacterial Drug ◽  
Methylenetetrahydrofolate Dehydrogenase ◽  
Antibacterial Drug Target

scholarly journals Structural and functional investigations of Ureaplasma parvum UMP kinase - a potential antibacterial drug target

FEBS Journal ◽  
2007 ◽  
Vol 274 (24) ◽  
pp. 6403-6414 ◽  
Author(s):  
Louise Egeblad-Welin ◽  
Martin Welin ◽  
Liya Wang ◽  
Staffan Eriksson
Keyword(s):  
Drug Target ◽  
Antibacterial Drug ◽  
Ureaplasma Parvum ◽  
Ump Kinase ◽  
Antibacterial Drug Target ◽  
Kinase A

scholarly journals Mechanismen und Funktionen von bakteriellen AAA+­Entfaltungsmaschinen

BIOspektrum ◽  
2021 ◽  
Vol 27 (1) ◽  
pp. 22-24
Author(s):  
Axel Mogk
Keyword(s):  
Quality Control ◽  
Drug Target ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Stress Conditions ◽  
Misfolded Proteins ◽  
Antibacterial Drug ◽  
Protein Homeostasis ◽  
Antibacterial Drug Target

AbstractBacterial AAA+ proteins play crucial roles in proteostasis networks and ensure protein homeostasis during stress conditions. They function as ATP-dependent components of proteolytic complexes degrading misfolded proteins or as disaggregases reactivating aggregated proteins. AAA+ proteins generate an ATP-fueled threading force driving substrate unfolding and translocation. Their central functions in protein quality control qualify them as antibacterial drug target.

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