Cox K

References (3)

Title : Genome assembly with in vitro proximity ligation data and whole-genome triplication in lettuce - Reyes-Chin-Wo_2017_Nat.Commun_8_14953
Author(s) : Reyes-Chin-Wo S , Wang Z , Yang X , Kozik A , Arikit S , Song C , Xia L , Froenicke L , Lavelle DO , Truco MJ , Xia R , Zhu S , Xu C , Xu H , Xu X , Cox K , Korf I , Meyers BC , Michelmore RW
Ref : Nat Commun , 8 :14953 , 2017
Abstract : Lettuce (Lactuca sativa) is a major crop and a member of the large, highly successful Compositae family of flowering plants. Here we present a reference assembly for the species and family. This was generated using whole-genome shotgun Illumina reads plus in vitro proximity ligation data to create large superscaffolds; it was validated genetically and superscaffolds were oriented in genetic bins ordered along nine chromosomal pseudomolecules. We identify several genomic features that may have contributed to the success of the family, including genes encoding Cycloidea-like transcription factors, kinases, enzymes involved in rubber biosynthesis and disease resistance proteins that are expanded in the genome. We characterize 21 novel microRNAs, one of which may trigger phasiRNAs from numerous kinase transcripts. We provide evidence for a whole-genome triplication event specific but basal to the Compositae. We detect 26% of the genome in triplicated regions containing 30% of all genes that are enriched for regulatory sequences and depleted for genes involved in defence.
ESTHER : Reyes-Chin-Wo_2017_Nat.Commun_8_14953
PubMedSearch : Reyes-Chin-Wo_2017_Nat.Commun_8_14953
PubMedID: 28401891
Gene_locus related to this paper: lacsa-a0a2j6jnd3 , lacsa-a0a2j6l6y4 , lacsa-a0a2j6mjs5 , lacsa-a0a2j6mk82 , lacsa-a0a2j6k5z4 , lacsa-a0a2j6mk08 , lacsa-a0a2j6mhc5 , lacsa-a0a2j6m8d0 , lacsa-a0a2j6mdb6 , lacsa-a0a2j6mdh6 , lacsa-a0a2j6jnf0 , lacsa-a0a2j6mji4 , lacsa-a0a2j6ke81 , lacsa-a0a2j6jip3 , lacsa-a0a2j6jir5 , lacsa-a0a2j6ksa7 , lacsa-a0a2j6l4a3

Title : Three hydrolases and a transferase: comparative analysis of active-site dynamics via the BioSimGrid database - Tai_2007_J.Mol.Graph.Model_25_896
Author(s) : Tai K , Baaden M , Murdock S , Wu B , Ng MH , Johnston S , Boardman R , Fangohr H , Cox K , Essex JW , Sansom MS
Ref : J Mol Graph Model , 25 :896 , 2007
Abstract : Comparative molecular dynamics (MD) simulations enable us to explore the conformational dynamics of the active sites of distantly related enzymes. We have used the BioSimGrid (http://www.biosimgrid.org) database to facilitate such a comparison. Simulations of four enzymes were analyzed. These included three hydrolases and a transferase, namely acetylcholinesterase, outer-membrane phospholipase A, outer-membrane protease T, and PagP (an outer-membrane enzyme which transfers a palmitate chain from a phospholipid to lipid A). A set of 17 simulations were analyzed corresponding to a total of approximately 0.1 micros simulation time. A simple metric for active-site integrity was used to demonstrate the existence of clusters of dynamic conformational behaviour of the active sites. Small (i.e. within a cluster) fluctuations appear to be related to the function of an enzymatically active site. Larger fluctuations (i.e. between clusters) correlate with transitions between catalytically active and inactive states. Overall, these results demonstrate the potential of a comparative MD approach to analysis of enzyme function. This approach could be extended to a wider range of enzymes using current high throughput MD simulation and database methods.
ESTHER : Tai_2007_J.Mol.Graph.Model_25_896
PubMedSearch : Tai_2007_J.Mol.Graph.Model_25_896
PubMedID: 17011806

Title : Muscarinic agonists and antagonists in the treatment of Alzheimer's disease - Greenlee_2001_Farmaco_56_247
Author(s) : Greenlee W , Clader J , Asberom T , McCombie S , Ford J , Guzik H , Kozlowski J , Li S , Liu C , Lowe D , Vice S , Zhao H , Zhou G , Billard W , Binch H , Crosby R , Duffy R , Lachowicz J , Coffin V , Watkins R , Ruperto V , Strader C , Taylor L , Cox K
Ref : Farmaco , 56 :247 , 2001
Abstract : Alzheimer's disease (AD) is a neurodegenerative disease characterized by cognitive impairment and personality changes. The development of drugs for the treatment of the cognitive deficits of AD has focused on agents which counteract loss in cholinergic activity. Although symptoms of AD have been successfully treated with acetylcholinesterase inhibitors (tacrine, donepezil. rivastigmine, galanthamine), limited success has been achieved with direct M1 agonists, probably due to their lack of selectivity versus other muscarinic receptor subtypes. Muscarinic M2 antagonists have been reported to increase synaptic levels of acetylcholine after oral administration to rats (e.g. BIBN-99, SCH-57790), but their selectivity versus other muscarinic receptor subtypes is modest. Exploration of a series of piperidinylpiperidines has yielded the potent and selective M2 antagonist SCH-217443. This antagonist has excellent bioavailability in rats and dogs and shows activity in a rat model of cognition.
ESTHER : Greenlee_2001_Farmaco_56_247
PubMedSearch : Greenlee_2001_Farmaco_56_247
PubMedID: 11421251