Results 71 to 80 of about 10,903 (206)

Inhibition of histone deacetylase as a treatment for cardiac hypertrophy [PDF]

open access: yes, 2005
The present invention provides for methods of treating and preventing cardiac hypertrophy. Class II HDACs, which are known to participate in regulation of chromatin structure and gene expression, have been shown to have beneficial effects on cardiac ...
Bristow, Michael R.   +3 more
core   +1 more source

Synthesis of szentiamide, a depsipeptide from entomopathogenic Xenorhabdus szentirmaii with activity against Plasmodium falciparum

open access: yesBeilstein Journal of Organic Chemistry, 2012
The synthesis of the recently characterized depsipeptide szentiamide (1), which is produced by the entomopathogenic bacterium Xenorhabdus szentirmaii, is described. Whereas no biological activity was previously identified for 1, the material derived from
Friederike I. Nollmann   +6 more
doaj   +1 more source

Structure and Antibacterial Activity of Ambobactin, a New Telomycin-Like Cyclic Depsipeptide Antibiotic Produced by Streptomyces ambofaciens F3

open access: yesMolecules, 2015
A new telomycin-like cyclic depsipeptide, ambobactin (1), was isolated from the metabolites of Streptomyces ambofaciens F3, an endophyte of Platycladus orientalis.
Shaopeng Wei, Wenhao Zhang, Zhiqin Ji
doaj   +1 more source

How endo- is endo-?: surface sterilization of delicate samples: a Bryopsis (Bryopsidales, Chlorophyta) case study [PDF]

open access: yes, 2010
In the search for endosymbiotic bacteria, elimination of ectosymbionts is a key point of attention. Commonly, the surface of the host itself or the symbiotic structures are sterilized with aggressive substances such as chlorine or mercury derivatives ...
De Clerck, Olivier   +3 more
core   +2 more sources

depsipeptides

open access: yes, 2014
Citation: 'depsipeptides' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.D01604 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms. Requests for commercial
openaire   +1 more source

Acyl depsipeptide (ADEP) resistance in Streptomyces

open access: yesMicrobiology, 2011
ADEP, a molecule of the acyl depsipeptide family, has an antibiotic activity with a unique mode of action. ADEP binding to the ubiquitous protease ClpP alters the structure of the enzyme. Access of protein to the ClpP proteolytic chamber is therefore facilitated and its cohort regulatory ATPases (ClpA, ClpC, ClpX) are not required.
Myriam, Gominet   +2 more
openaire   +2 more sources

Resistance after chronic application of the HDAC-inhibitor valproic acid is associated with elevated Akt activation in renal cell carcinoma in vivo [PDF]

open access: yes, 2013
Targeted drugs have significantly improved the therapeutic options for advanced renal cell carcinoma (RCC). However, resistance often develops, negating the benefit of these agents.
Bartsch, Georg   +6 more
core   +2 more sources

Determination of Diketopiperazine Formation During the Solid‐Phase Synthesis of C‐Terminal Acid Peptides

open access: yesChemistry–Methods, Volume 5, Issue 11, November 2025.
Diketopiperazine formation (DKP) is one of the most serious side reactions during peptide synthesis. An accurate method to determine the DKP formation in peptide synthesis on Wang resin is reported. Furthermore, the strategies to minimize this side reaction and side products lacking C‐terminal amino acids are described. Diketopiperazine formation (DKP)
Mani Kaushal   +7 more
wiley   +1 more source

A macrolactonization approach to the total synthesis of the antimicrobial cyclic depsipeptide LI-F04a and diastereoisomeric analogues

open access: yesBeilstein Journal of Organic Chemistry, 2012
The cyclic peptide core of the antifungal and antibiotic cyclic depsipeptide LI-F04a was synthesised by using a modified Yamaguchi macrolactonization approach.
James R. Cochrane   +3 more
doaj   +1 more source

Chromopeptide A, a highly cytotoxic depsipeptide from the marine sediment-derived bacterium Chromobacterium sp. HS-13-94

open access: yesActa Pharmaceutica Sinica B, 2015
A bicyclic depsipeptide, chromopeptide A (1), was isolated from a deep-sea-derived bacterium Chromobacterium sp. HS-13-94. Its structure was determined by extensive spectroscopic analysis and by comparison with a related known compound.
Zhenfang Zhou   +9 more
doaj   +1 more source

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