Kaur / Sharma | Bacterial Enzymes as Targets for Drug Discovery | Buch | 978-0-443-22222-1 | www.sack.de

Buch, Englisch, 496 Seiten, Format (B × H): 193 mm x 234 mm, Gewicht: 1002 g

Kaur / Sharma

Bacterial Enzymes as Targets for Drug Discovery

Meeting the Challenges of Antibiotic Resistance
Erscheinungsjahr 2024
ISBN: 978-0-443-22222-1
Verlag: Elsevier Science

Meeting the Challenges of Antibiotic Resistance

Buch, Englisch, 496 Seiten, Format (B × H): 193 mm x 234 mm, Gewicht: 1002 g

ISBN: 978-0-443-22222-1
Verlag: Elsevier Science


Bacterial Enzymes as Targets for Drug Discovery: Meeting the Challenges of Antibiotic Resistance addresses the gap between medical microbiology, structural biology, and genomic science in the development of new antibacterial drug development. This book consolidates detailed profiling of bacterial target enzyme families for the drug discovery process and methodologies for use and validation of the potential drug targets. The contents cover the foundations of the antibiotic drug discovery process and focus on bacterial enzymes as drug targets, building across these disciplines to provide a comprehensive resource in bacterial structural biology and genomics. This is the ideal reference for antibiotic drug discovery researchers in the pharma industry and academia. Biochemists, microbiologists, and medicinal chemists will also benefit from this books’ content.

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Weitere Infos & Material


Part I Primer of antibiotic discovery process
1. Antibacterial drug discovery: A Silent Pandemic
2. Current scenario and future prospective of drug discovery and development against bacterial enzymes
3. Clinical diagnostics of bacterial infections and their resistance to Antibiotics - Current State and Novel Enabling Technologies Implementation Perspectives
4. An Odyssey into Phylogenetic Functional Conservation of Novel Antibacterial Targets in Human Pathogens
5. Validation of drug targets using molecular methodologies and enzymatic activity assays for validation of inhibitory potential
6. Computational tools to identify potential drug targets in bacteria
7. Antimicrobial drug resistance and bypassing strategies
Part II Bacterial enzyme as drug targets
8. Designing Tomorrow's Antibiotics: Cutting-Edge Strategies and Technologies
9. Inhibiting the replication by targeting topoisomerases
10. Role of beta lactamases in antibiotic drug discovery
11. Selective vs broad spectrum inhibition of novel outer membrane targets in Gram negatives
12. Ribosomal binding antibacterial agents
13. RNA polymerase: A key target for Novel Antimicrobial Therapeutic Strategies
14. Colistin resistance and strategies against superbug, where we are?
15. Deoxythymidine pathway enzymes as an antibacterial target
16. Arresting the peptidoglycan synthesis to kill the bacteria
17. Clp protease complex as a therapeutic target for tuberculosis
18. PlaF: a bacterial Lands cycle phospholipase A mediating membrane phospholipid degradation and virulence adaptation
19. Bacterial TIR domain-containing proteins as drug targets
20. Drug Repurposing: Tackling the antibiotic resistance with existing therapeutics


Kaur, Punit
Dr. Kaur's specialties include Bioinformatics, Structural Biology, X-ray Crystallography, and Rational Structure-Based Drug Design. Her research focuses on clinically relevant bacterial pathogens where a multidisciplinary approach is adopted to understand the antibacterial resistance mechanisms and design of novel inhibitory molecules. She has published more than 240 original publications, reviews and chapters in the field of bioinformatics, biophysical enzymatic activity and structural biology.

Sharma, Priyanka
Dr. Priyanka Sharma is a postdoctoral student with the biomedical Informatics department at the ICMR. Her work focuses on the field of computational biology involving structural bioinformatics and genomics of bacterial pathogens. She has published widely in the field of clinical bacteriology and is the author of over 30 research papers, reviews and chapters. She has work experience in field of antimicrobial resistance due to enzymatic mutations.



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