scholarly journals Posttranslational Influence of NADPH-Dependent Thioredoxin Reductase C on Enzymes in Tetrapyrrole Synthesis

2013 ◽  
Vol 162 (1) ◽  
pp. 63-73 ◽  
Author(s):  
Andreas S. Richter ◽  
Enrico Peter ◽  
Maxi Rothbart ◽  
Hagen Schlicke ◽  
Jouni Toivola ◽  
...  
2019 ◽  
Vol 15 (5) ◽  
pp. 369-383
Author(s):  
Rahul Balasaheb Aher ◽  
Kunal Roy

Tuberculosis, malaria, dengue, chikungunya, leishmaniasis etc. are a large group of neglected tropical diseases that prevail in tropical and subtropical countries, affecting one billion people every year. Minimal funding and grants for research on these scientific problems challenge many researchers to find a different way to reduce the extensive time and cost involved in the drug discovery cycle of these problems. Computer-aided drug design techniques have already been proved successful in the discovery of new molecules rationally by reducing the time and cost involved in the development of drugs. In the current minireview, we are highlighting on the molecular modeling studies published during 2010-2018 for target specific antitubercular agents. This review includes the studies of Structure-Based (SB) and Ligand-Based (LB) modeling and those involving Machine Learning (ML) techniques against different antitubercular targets such as dihydrofolate reductase (DHFR), enoyl Acyl Carrier Protein (ACP) reductase (InhA), catalase-peroxidase (KatG), enzyme antigen 85C, protein tyrosine phosphatases (PtpA and PtpB), dUTPase, thioredoxin reductase (MtTrxR), etc. The information presented in this review will help the researchers to get acquainted with the recent progress in the modeling studies of antitubercular agents.


1967 ◽  
Vol 242 (22) ◽  
pp. 5232-5236 ◽  
Author(s):  
Giuliana Zanetti ◽  
Charles H. Williams

2012 ◽  
Vol 58 (2) ◽  
pp. 206-211 ◽  
Author(s):  
Min-Sik Park ◽  
Hyeon-Jung Kim ◽  
A Rum Park ◽  
Kisup Ahn ◽  
Hye-Won Lim ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Amir Ata Saei ◽  
Christian M. Beusch ◽  
Pierre Sabatier ◽  
Juan Astorga Wells ◽  
Hassan Gharibi ◽  
...  

AbstractDespite the immense importance of enzyme–substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.


1967 ◽  
Vol 242 (5) ◽  
pp. 852-859
Author(s):  
Lars Thelander

1989 ◽  
Vol 264 (22) ◽  
pp. 12752-12753
Author(s):  
J Kuriyan ◽  
L Wong ◽  
M Russel ◽  
P Model

2021 ◽  
Vol 3 ◽  
pp. 100127
Author(s):  
Tendai J. Mafireyi ◽  
Jorge O. Escobedo ◽  
Robert M. Strongin

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