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Depsipeptide Dendrimers

Chemistry - A European Journal, 2000
The convergent synthesis of a new class of chiral dendrimers is described. Owing to their structural resemblance to depsipeptides they are called depsipeptide dendrimers. The ex-chiral pool synthesis starts from (R,R)-, (S,S)-, and meso-tartaric acid as branching units and dipeptides or tripeptides consisting of glycine, (L)-alanine, and (L)-leucine as
J, Kress, A, Rosner, A, Hirsch
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Depsipeptide Synthesis

ChemInform, 2007
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Maciej, Stawikowski, Predrag, Cudic
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Antimitotic Peptides and Depsipeptides

Current Medicinal Chemistry-Anti-Cancer Agents, 2012
Tubulin is the target for an ever increasing number of unusual peptides and depsipeptides that were originally isolated from a wide variety of organisms. Since tubulin is the major component of cellular microtubules, which maintain cell shape in interphase and form the mitotic spindle, most of these compounds are highly toxic to mammalian cells.
Ernest, Hamel, David G, Covell
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The cyclization of peptides and depsipeptides

Journal of Peptide Science, 2003
AbstractConstricting the peptide backbone into a more defined conformational form through cyclization is an activity evolved in nature and in synthetic work, the latter straddling only the most recent decades. The resulting conformational constraints increase the probability of an optimum response with bio‐receptors.
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Recent Developments in Depsipeptide Research

Current Medicinal Chemistry, 2002
This review focuses on the major developments in depsipeptide research since 1995. Depsipeptides are bio-oligomers composed of hydroxy and amino acids linked by amide and ester bonds. Many depsipeptides show very promising biological activities, including anticancer, antibacterial, antiviral, antifungal, anti-inflammatory, and anti-clotting or anti ...
C E, Ballard, H, Yu, B, Wang
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Biosynthesis of depsipeptide mycotoxins in Fusarium

European Journal of Plant Pathology, 2002
The cyclic hexadepsipeptide enniatin is known as a phytopathogenic compound from Fusaria causing necrosis and wilt. The molecule consists of three alternating residues each of a branched chain amino acid and D-hydroxyisovaleric acid (D-Hiv). Enniatins are synthesized by a 347kDa multienzyme (enniatin synthetase) via a thiol template mechanism.
Till Hornbogen   +2 more
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