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Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. TheExpand
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The Future of Peptide‐based Drugs
The suite of currently used drugs can be divided into two categories – traditional ‘small molecule’ drugs with typical molecular weights of <500 Da but with oral bioavailability, and much largerExpand
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Conopeptide characterization and classifications: an analysis using ConoServer.
Cone snails are carnivorous marine gastropods that have evolved potent venoms to capture their prey. These venoms comprise a rich and diverse cocktail of peptide toxins, or conopeptides, whose highExpand
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Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.
Several macrocyclic peptides ( approximately 30 amino acids), with diverse biological activities, have been isolated from the Rubiaceae and Violaceae plant families over recent years. We haveExpand
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ConoServer: updated content, knowledge, and discovery tools in the conopeptide database
ConoServer (http://www.conoserver.org) is a database specializing in the sequences and structures of conopeptides, which are toxins expressed by marine cone snails. Cone snails are carnivorousExpand
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Low-molecular-weight peptidic and cyclic antagonists of the receptor for the complement factor C5a.
Activation of the human complement system of plasma proteins during immunological host defense can result in overproduction of potent proinflammatory peptides such as the anaphylatoxin C5a. ExcessiveExpand
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ConoServer, a database for conopeptide sequences and structures
SUMMARY ConoServer is a new database dedicated to conopeptides, a large family of peptides found in the venom of marine snails of the genus Conus. These peptides have an exceptional diversity ofExpand
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Protein disulfide isomerase: the structure of oxidative folding.
Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, aExpand
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Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
The three-dimensional solution structure of the 40 residue amyloid beta-peptide, Abeta(1-40), has been determined using NMR spectroscopy at pH 5.1, in aqueous sodium dodecyl sulfate (SDS) micelles.Expand
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Novel ω-Conotoxins from Conus catus Discriminate among Neuronal Calcium Channel Subtypes*
ω-Conotoxins selective for N-type calcium channels are useful in the management of severe pain. In an attempt to expand the therapeutic potential of this class, four new ω-conotoxins (CVIA–D) haveExpand
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