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Phytochelatin synthase: of a protease a peptide polymerase made

Physiologia Plantarum, 2012
Of the mechanisms known to protect vascular plants and some algae, fungi and invertebrates from the toxic effects of non‐essential heavy metals such as As, Cd or Hg, one of the most sophisticated is the enzyme‐catalyzed synthesis of phytochelatins (PCs).
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Combinatorialization of Fungal Polyketide Synthase–Peptide Synthetase Hybrid Proteins

Journal of the American Chemical Society, 2014
The programming of the fungal polyketide synthase (PKS) is quite complex, with a simple domain architecture leading to elaborate products. An additional level of complexity has been found within PKS-based pathways where the PKS is fused to a single module nonribosomal peptide synthetase (NRPS) to synthesize polyketides conjugated to amino acids.
Thomas B, Kakule   +2 more
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Stimulation of endothelial nitric oxide synthase by proinsulin C-peptide

Nitric Oxide, 2003
There is increasing evidence for biological functions of human C-peptide. Recently, we have described that proinsulin C-peptide increases nutritive capillary blood flow and restores erythrocyte deformability in type 1 diabetic patients, whereas it has no such effect in non-diabetic subjects.
Thomas, Wallerath   +11 more
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Target Recognition of Apocalmodulin by Nitric Oxide Synthase I Peptides

Biochemistry, 2002
An increasing number of proteins are found that are regulated by the Ca(2+)-free state of calmodulin, apocalmodulin. Many of these targets harbor a so-called IQ motif within their primary sequence, but several target proteins of apocalmodulin lack this motif.
Petra, Censarek   +2 more
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The ATP Synthase ofTrypanosoma bruceiIs Developmentally Regulated by an Inhibitor Peptide

Archives of Biochemistry and Biophysics, 1996
The Trypanosoma brucei ATP synthase, like those of other organisms, is composed of two moieties, the membrane bound F0 and the catalytic F1 with each of these parts comprised of multiple subunits. In addition, an endogenous inhibitor peptide of the ATP synthase has been identified from a variety of sources.
T B, Chi, S Y, Choi, N, Williams
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The identification of thymidylate synthase peptide domains located in the interface region that bind thymidylate synthase mRNA

Biochemical and Biophysical Research Communications, 2002
Thymidylate synthase (TS) is a critical chemotherapeutic target and intracellular levels of TS are an important determinant of sensitivity to TS inhibitors. Translational autoregulation represents one cellular mechanism for controlling the level of expression of TS. This mechanism involves the binding of TS protein to its own messenger RNA (mRNA), thus,
Donna M, Voeller   +3 more
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Insect venom peptides as potent inhibitors of Escherichia coli ATP synthase

International Journal of Biological Macromolecules, 2020
Insect venom peptides (IVPs) eumenitin, lasiocepsin, lycosin1, mastoparanB, panurgine1, and protonectin possess antibacterial properties, and the ubiquitous enzyme ATP synthase has a peptide-binding site. In the present study, we studied the effect of IVPs on binding and inhibition of three Escherichia coli strains (wild type, mutant, and null) and ...
Amon, Amini   +4 more
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Internalization and Stability of a Thymidylate Synthase Peptide Inhibitor in Ovarian Cancer Cells

Journal of Medicinal Chemistry, 2014
Information on the cellular internalization and stability of the ovarian cancer cell growth inhibitor peptide, LSCQLYQR (LR), is vital for lead optimization. Ad-hoc-synthesized LR/fluorescent-probe conjugates were used to monitor the internalization of the peptide.
CANNAZZA, Giuseppe   +11 more
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Venom peptides as selective inhibitors of bacterial ATP synthase

The FASEB Journal, 2020
Background It is predicted that by the year 2050 world will face 10 million additional deaths per year due to antibiotic resistance. Misuse and overuse of antibiotics, is making microbes resistant to normally effective antibiotics.
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A connection between antimicrobial properties of venom peptides and microbial ATP synthase

International Journal of Biological Macromolecules, 2018
Venom peptides anoplin, cupiennin 1a, latarcin 1, latarcin 3a, latarcin 5, melittin, and pandinin 2 are known to have antibacterial properties. In the current study, we examined whether the antimicrobial properties of these venom peptides have any connection to the binding and inhibition of bacterial ATP synthase.
Hiba Syed   +2 more
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