Global ETD Search
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Showing 1 to 20 of 46 for “"Ripps"”.
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Biosynthetic and bioinformatic investigation of RiPPs with radical SAM-installed crosslinks
… and post translationally modified peptides (RiPPs) are an expanding class of natural products containing new chemical modalities and bioactive molecules. Although with diverse biological functions, significant research has been focused on investigating RiPPs with antibacterial activity due to …
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Biomolecular NMR studies of the structure and biosynthesis of RiPP natural products
… and Posttranslationally modified Peptides (RiPPs) are a particularly intriguing class. These compounds begin as a genetically encoded precursor, which is translated into a short (~50) residue peptide. This precursor peptide is then modified by genetically co-located enzymes to generate a …
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Expanding the structural diversity of the RiPP class of natural products
… and post-translationally modified peptides (RiPPs) are a diverse and rapidly expanding class of natural products. Despite starting out as linear chains of amino acids, RiPP natural products acquire structural diversity ranging from small molecules like microcin C7 to 48-mer polytheonamides …
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Mechanistic interrogations of ribosomal and non-ribosomal natural product enzymes
… and post-translationally modified peptides (RiPPs), with a particular emphasis on the thiopeptide subclass of RiPPs. Additionally, characterization of an off-loading enzyme involved in hybrid polyketide/non-ribosomal peptide (PK-NRP) natural product biosynthesis is described.
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Characterization of Cyclopropyl Synthases Involved in the Maturation of Ribosomally Synthesized and Posttranslationally Modified Peptides
… and post-translationally modified peptides (RiPPs) are a large class of natural products with significant human health implications. RiPPs are synthesized from a genetically encoded precursor peptide that undergoes significant modifications by maturing enzymes, or maturases. Recently, …
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On the biosynthesis and discovery of ribosomally synthesized and post-translationally modified peptides
… and post-translationally modified peptides (RiPPs) that all contain thiazole and oxazole heterocycles derived from cysteine, serine, and threonine residues, respectively. The thiazole/oxazole heterocycle is installed over two distinct steps. First, the cyclodehydratase cyclizes an unmodified …
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Functional and mechanistic elucidation of peptide backbone thioamidation
… and post-translationally modified peptides (RiPPs) and are critical for their biological functions. In addition to RiPPs, thioamide has also been observed as a post-translational modification in two essential protein complexes: methyl-coenzyme M reductase (MCR) and the ribosome. Genetic …
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Exploring and understanding lantibiotic biosynthesis
… and post-translationally modified peptides (RiPPs). The biosynthetic machinery of RiPPs offers a new platform for the discovery and engineering of peptidic natural products. Although rapid advances have been made in elucidating biosynthetic pathways generating various RiPPs, investigations …
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Discovery and characterization of ribosomally synthesized and post-translationally modified peptide natural products
… Once genome mining has been used to select RiPPs gene clusters, chemical and microbiological techniques are employed to characterize the structure, biosynthesis, antibiotic activity, and mode of action of newly discovered RiPPs. Plantazolicin (PZN) is a RiPP natural product with a rigid, …
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Elucidation and control of substrate recognition during RiPP biosynthesis
… and posttranslationally modified peptides (RiPPs) are a rapidly growing class of natural products. RiPP precursor peptides can undergo extensive enzymatic tailoring to yield structurally and functionally diverse products. Cyclodehydratases are a type of RiPP modifying enzyme that catalyze …
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Design of Post-Translationally Modified Peptides by Combining Enzymes from Diverse Pathways
… and post-translationally modified peptides (RiPPs) have emerged as both therapeutically-relevant and engineerable, two traits previously unobserved together in a natural product class. Their biosynthesis is modular: a precursor peptide recruits enzymes that bind one region of the peptide and …
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Investigations into the molecular basis of enzyme-catalyzed reactions in natural product biosynthesis
… and post-translationally modified peptides (RiPPs). The chemical modifications found in these peptide natural products further distinguish each them into specific types. The borosins constitute a class of RiPPs that are characterized by a cyclized N-C structure with methylations on the amide …
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Structural and biochemical studies on tailoring enzymes involved in ribosomal peptides biosynthesis
… and post-translationally modified peptides (RiPPs). Precursor peptides and tailoring enzymes for post-translational modifications (PTMs) are encoded in the same gene cluster, which is efficient in producing peptide variants providing different precursor sequences. The peptides are first …
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New chemical and biosynthetic methodologies for the study of lanthipeptides
… and posttranslationally modified peptides (RiPPs). One of the largest classes of RiPPs is the lanthionine-containing peptides (lanthipeptides), which are characterized by intramolecular thioether crosslinks dubbed lanthionine (Lan) and methyllanthionine (MeLan). The evolvability and brevity …
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Biosynthesis and engineering of lanthipeptide natural products for novel applications
… and post-translationally modified peptides (RiPPs) have recently been recognized as a major class of natural products as a result of the genome sequencing efforts. The post-translational modifications endow them with diverse and rigid structures such as polycylic or macrocyclic scaffolds, …
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Engineering of the microviridin post-translational modification enzymes for the production of synthetic protease inhibitors
… and post-translationally modified peptides (RiPPs) are a group of natural products generated by the action of post-translationally modifying enzymes on precursor peptides translated from mRNA by ribosomes. The great substrate promiscuity exhibited by many of the enzymes from RiPP biosynthetic …
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Biosynthesis and engineering of lanthipeptides
… and post-translational modified peptides (RiPPs). Lanthipeptides are a class of RiPPs with pharmaceutically valuable properties including antimicrobial activity against clinically-relevant bacterial pathogens, even including drug-resistant strains. These peptides are characterized by …
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Exploration of the biosynthesis of lanthipeptides
… synthesized and post-translationally modified (RiPPs). Lanthipeptides, which possess (methyl)lanthionine structures, are a class of intensively studied RiPPs. Based on the biosynthesis enzymes that introduce the thioether motifs, lanthipeptides are classified into four classes. Class I …
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Investigating and engineering the post-translational modifications in RiPP natural product biosynthesis (I) Thiopeptides (II) Sactipeptides
… and post-translationally modified peptides (RiPPs) have been attracting interest as one such source of untapped potential. Owing to the unique “promiscuous-yet-specific” biosynthetic paradigm that RiPPs offer, this class of natural products have been an area of intense research. Chapter 1 …
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Discovery and structural characterization of lanthipeptides from soil and rumen bacteria
… modified peptide natural products (RiPPs), lanthipeptides possess myriad structural diversity and potential for discovery using genome-guided approaches. Biological activities of interest embedded within lanthipeptide structures include antimicrobial, antiviral, and morphogenetic …
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