Peptide Deformylase As Novel Drug Target (Paperback)
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Von Händler/Antiquariat, BuySomeBooks [52360437], Las Vegas, NV, U.S.A.
Paperback. 168 pages. Dimensions: 8.7in. x 5.9in. x 0.4in.Peptide deformylase (PDF) was originally viewed as unique only to the prokaryotes and lacking from the eukaryotes. In bacteria, PDF is the enzyme that catalyzes the removal of the N-formyl moiety from the initiator methionine residue during protein translation and is essential. Inhibitors that target its reaction mechanism are also potent against bacterial growth. This property makes PDF an attractive novel drug target. Recent genomic sequencing has also revealed PDF homologs in eukaryotes. This book, therefore, provides evidence and insight into two PDF homologs found in the malaria-causing organism, Plasmodium falciparum, and human. Both eukaryotic PDFs are enzymatically active but localized in the cellular organelles and raise the concern of the effectiveness of PDF as an antimicrobial drug target. However, the rational design of a novel class of PDF inhibitors demonstrates specificity toward the bacterial and the eukaryotic counterparts. The evidence and study presented in this book should help shed some light on the forefront of the much needed, novel antimicrobial drug target and discovery field. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN.

Von Händler/Antiquariat, BuySomeBooks [52360437], Las Vegas, NV, U.S.A.
This item is printed on demand. Paperback. Peptide deformylase (PDF) was originally viewed as unique only to the prokaryotes and lacking from the eukaryotes. In bacteria, PDF is the enzyme that catalyzes the removal of the N-formyl moiety from the initiator methionine residue during protein translation and is essential. Inhibitors that target its reaction mechanism are also potent against bacterial growth. This property makes PDF an attractive novel drug target. Recent genomic sequencing has also revealed PDF homologs in eukaryotes. This book, therefore, provides evidence and insight into two PDF homologs found in the malaria-causing organism, Plasmodium falciparum, and human. Both eukaryotic PDFs are enzymatically active but localized in the cellular organelles and raise the concern of the effectiveness of PDF as an antimicrobial drug target. However, the rational design of a novel class of PDF inhibitors demonstrates specificity toward the bacterial and the eukaryotic counterparts. The evidence and study presented in this book should help shed some light on the forefront of the much needed, novel antimicrobial drug target and discovery field. This item ships from La Vergne,TN.

Von Händler/Antiquariat, AHA-BUCH GmbH [51283250], Einbeck, Germany.
This item is printed on demand - Print on Demand Titel. Neuware - Peptide deformylase (PDF) was originally viewed as unique only to the prokaryotes and lacking from the eukaryotes. In bacteria, PDF is the enzyme that catalyzes the removal of the N-formyl moiety from the initiator methionine residue during protein translation and is essential. Inhibitors that target its reaction mechanism are also potent against bacterial growth. This property makes PDF an attractive novel drug target. Recent genomic sequencing has also revealed PDF homologs in eukaryotes. This book, therefore, provides evidence and insight into two PDF homologs found in the malaria-causing organism, Plasmodium falciparum, and human. Both eukaryotic PDFs are enzymatically active but localized in the cellular organelles and raise the concern of the effectiveness of PDF as an antimicrobial drug target. However, the rational design of a novel class of PDF inhibitors demonstrates specificity toward the bacterial and the eukaryotic counterparts. The evidence and study presented in this book should help shed some light on the forefront of the much needed, novel antimicrobial drug target and discovery field. 168 pp. Englisch.

Von Händler/Antiquariat, The Book Depository EURO [60485773], London, United Kingdom.
Language: English Brand New Book ***** Print on Demand *****.Peptide deformylase (PDF) was originally viewed as unique only to the prokaryotes and lacking from the eukaryotes. In bacteria, PDF is the enzyme that catalyzes the removal of the N-formyl moiety from the initiator methionine residue during protein translation and is essential. Inhibitors that target its reaction mechanism are also potent against bacterial growth. This property makes PDF an attractive novel drug target. Recent genomic sequencing has also revealed PDF homologs in eukaryotes. This book, therefore, provides evidence and insight into two PDF homologs found in the malaria-causing organism, Plasmodium falciparum, and human. Both eukaryotic PDFs are enzymatically active but localized in the cellular organelles and raise the concern of the effectiveness of PDF as an antimicrobial drug target. However, the rational design of a novel class of PDF inhibitors demonstrates specificity toward the bacterial and the eukaryotic counterparts. The evidence and study presented in this book should help shed some light on the forefront of the much needed, novel antimicrobial drug target and discovery field.

Von Händler/Antiquariat, English-Book-Service - A Fine Choice [1048135], Mannheim, Germany.
This item is printed on demand for shipment within 3 working days.

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