Results 251 to 260 of about 319,110 (303)
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Biosynthesis of peptide–nucleobase hybrids in ribosomal peptides
Nature Chemical BiologyThe main biopolymers in nature are oligonucleotides and polypeptides. However, naturally occurring peptide-nucleobase hybrids are rare. Here we report the characterization of the founding member of a class of peptide-nucleobase hybrid natural products with a pyrimidone motif from a widely distributed ribosomally synthesized and post-translationally ...
Zeng-Fei Pei +4 more
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Combinatorial Biosynthesis of Non-Ribosomal Peptides
Combinatorial Chemistry & High Throughput Screening, 2003Non-ribosomal peptide synthetases (NRPS) are modular assembly lines catalysing the synthesis of many small peptides in microbes. Genetic replacements of domains or modules in NRPS encoded by gene clusters in Bacillus sp. with corresponding domains or modules from foreign NRPS have led in several cases to the in vivo synthesis of peptides with predicted
Ullrich, Keller, Florian, Schauwecker
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Nonribosomal biosynthesis of backbone-modified peptides
Nature Chemistry, 2017Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here that an L-Phe-specific module of an archetypal nonribosomal peptide synthetase can be reprogrammed to ...
David L. Niquille +5 more
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Biosynthesis and distribution of opioid peptides
Journal of Endocrinological Investigation, 1983Group III opioid peptides are derived from proenkephalin B. The processing of this precursor peptide is still only partly understood and we still do not know how many final products come from proenkephalin B and whether Leu-enkephalin is produced from Group III peptides.
H, Imura +10 more
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Peptide Hormone Biosynthesis — Recent Developments
1985The biosynthesis of peptide hormones is now recognized to be a highly ordered series of events. These biosynthetic events can frequently be localized to a particular subcellular organelle (Fig.1). Each organelle will be discussed in turn, to emphasize the sequential nature of the maturation process.
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Biosynthesis of Cardiac Natriuretic Peptides
2009Cardiac-derived peptide hormones were identified more than 25 years ago. An astonishing amount of clinical studies have established cardiac natriuretic peptides and their molecular precursors as useful markers of heart disease. In contrast to the clinical applications, the biogenesis of cardiac peptides has only been elucidated during the last decade ...
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Biosynthesis of Neuronal Peptides
1977The general acceptance of the idea that peptides represent a new class of intercellular messengers in the nervous system (i.e., neurotransmitters and neuromodulators) naturally raises the question whether the biosynthetic mechanisms for peptides in “peptidergic” neurons (i.e., neurons that synthesize peptides for release as intercellular messengers ...
Harold Gainer, Y. Peng Loh, Yosef Sarne
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In Situ Biosynthesis of Peptide Arrays
2009Polypeptide and protein arrays enable high-throughput screening capabilities for studying molecular interactions and profiling of biomarkers, and provide a powerful functional screening tool for peptidomics. To overcome the limitations of conventional arraying methods, we have exploited cell-free systems for generating arrays of polypeptides by direct ...
Mingyue, He, Oda, Stoevesandt
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Biosynthesis of antibiotic peptides with isoleucine stereoisomers
Archives of Biochemistry and Biophysics, 1972Abstract Streptomyces antibioticus normally synthesizes an actinomycin mixture which contains N -methyl- l -valine and d -valine in the antibiotic peptides. Amino acid analyses indicate that trace amounts of isoleucine and, possibly, N -methylalloisoleucine are present also in actinomycin molecules. S.
T, Yajima, M A, Grigg, E, Katz
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On the biosynthesis of peptide ergot alkaloids
Experientia, 1974Futterung vonl-Valyl-(1-14C)-l-valyl-l-prolin anClaviceps purpurea und Abbau des erhaltenen Ergocornins und Ergokryptins zeigt, dass dieses Tripeptid, ebenso wie andere fruher untersuchte Peptide, sehr wahrscheinlich kein freies Zwischenprodukt in der Biogenese der Mutterkornalkaloide vom Peptidtyp ist.
H G, Floss +3 more
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