01475nas a2200229   4500008004100000022001400041245005200055210005200107260001500159300000900174490000700183520087700190653001701067653002001084653001901104653001601123653001701139100001601156700001501172700001401187856004401201       2020                        eng d  a2072-665100aCentipede Venom Peptides Acting on Ion Channels0 aCentipede Venom Peptides Acting on Ion Channels  c05/04/2020  a1-180 v123 a<p>Centipedes are among the oldest venomous arthropods that use their venom to subdue the prey. The major components of centipede venom are a variety of low-molecular-weight peptide toxins that have evolved to target voltage-gated ion channels to interfere with the central system of prey and produce pain or paralysis for efficient hunting. Peptide toxins usually contain several intramolecular disulfide bonds, which confer chemical, thermal and biological stability. In addition, centipede peptides generally have novel structures and high potency and specificity and therefore hold great promise both as diagnostic tools and in the treatment of human disease. Here, we review the centipede peptide toxins with reported effects on ion channels, including Nav, Kv, Cav and the nonselective cation channel polymodal transient receptor potential vanilloid 1 (TRPV1).</p>
10aanimal toxin10acentipede venom10adrug discovery10aion channel10apeptide drug1 aChu, YanYan1 aQiu, PeiJu1 aYu, RiLei  uhttps://www.mdpi.com/2072-6651/12/4/23002624nas a2200229   4500008004100000022001400041245006100055210006100116260001500177300000900192490000800201520194600209653001902155653002702174653001802201653002302219653001902242100002002261700002402281700002202305856006702327       2020                        eng d  a0965-174800aDiversity and evolution of the P450 family in arthropods0 aDiversity and evolution of the P450 family in arthropods  c22/10/2020  a1-220 v1273 a<p>The P450 family (CYP genes) of arthropods encodes diverse enzymes involved in the metabolism of foreign compounds and in essential endocrine or ecophysiological functions. The P450 sequences (CYPome) from 40 arthropod species were manually curated, including 31 complete CYPomes, and a maximum likelihood phylogeny of nearly 3000 sequences is presented. Arthropod CYPomes are assembled from members of six CYP clans of variable size, the CYP2, CYP3, CYP4 and mitochondrial clans, as well as the CYP20 and CYP16 clans that are not found in Neoptera. CYPome sizes vary from two dozen genes in some parasitic species to over 200 in species as diverse as collembolans or ticks. CYPomes are comprised of few CYP families with many genes and many CYP families with few genes, and this distribution is the result of dynamic birth and death processes. Lineage-specific expansions or blooms are found throughout the phylogeny and often result in genomic clusters that appear to form a reservoir of catalytic diversity maintained as heritable units. Among the many P450s with physiological functions, six CYP families are involved in ecdysteroid metabolism. However, five so-called Halloween genes are not universally represented and do not constitute the unique pathway of ecdysteroid biosynthesis. The diversity of arthropod CYPomes has only partially been uncovered to date and many P450s with physiological functions regulating the synthesis and degradation of endogenous signal molecules (including ecdysteroids) and semiochemicals (including pheromones and defense chemicals) remain to be discovered. Sequence diversity of arthropod P450s is extreme, and P450 sequences lacking the universally conserved Cys ligand to the heme have evolved several times. A better understanding of P450 evolution is needed to discern the relative contributions of stochastic processes and adaptive processes in shaping the size and diversity of CYPomes.</p>
10aDetoxification10aEcdysteroid metabolism10aGene clusters10aOrthologous groups10aP450 Evolution1 aDermauw, Wannes1 aVan Leeuwen, Thomas1 aFeyereisen, René  uhttps://linkinghub.elsevier.com/retrieve/pii/S096517482030179X