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Corresponding Regions (corresponding + regions)
Selected AbstractsUser-Controllable Color TransferCOMPUTER GRAPHICS FORUM, Issue 2 2010Xiaobo An This paper presents an image editing framework where users use reference images to indicate desired color edits. In our approach, users specify pairs of strokes to indicate corresponding regions in both the original and the reference image that should have the same color "style". Within each stroke pair, a nonlinear constrained parametric transfer model is used to transfer the reference colors to the original. We estimate the model parameters by matching color distributions, under constraints that ensure no visual artifacts are present in the transfer result. To perform transfer on the whole image, we employ optimization methods to propagate the model parameters defined at each stroke location to spatially-close regions of similar appearance. This stroke-based formulation requires minimal user effort while retaining the high degree of user control necessary to allow artistic interpretations. We demonstrate our approach by performing color transfer on a number of image pairs varying in content and style, and show that our algorithm outperforms state-of-the-art color transfer methods on both user-controllability and visual qualities of the transfer results. [source] Identification and analysis of Lydia, a LTR retrotransposon from Lymantria disparINSECT MOLECULAR BIOLOGY, Issue 4 2000T. A. Pfeifer Abstract Degenerative PCR primers to conserved amino acid motifs were used to identify an LTR retrotransposon from Lymantria dispar. The isolated retrotransposon, Lydia, is 6655 base pairs (bp) in length and contains perfect 300 bp terminal repeats. The identified gag and pol related ORFs have a high degree of similarity to the corresponding regions of the retrotransposon Ted from Trichoplusia ni, although several reading frameshifts and missense mutations are evident. The high degree of similarity between Lydia and Ted LTRs lends support for a family of lepidopteran retrotransposons. Southern blot analysis of individuals from two geographically distinct gypsy moth populations demonstrates that Lydia is found in both populations and the position of this element within the genome of these isolated populations is variable. [source] Amino acids outside of the loops that define the agonist binding site are important for ligand binding to insect nicotinic acetylcholine receptorsJOURNAL OF NEUROCHEMISTRY, Issue 1 2008Zewen Liu Abstract Nicotinic acetylcholine (ACh) receptors (nAChRs) are the targets of several kinds of insecticides. Based on the mutagenesis studies of Torpedo californica nAChRs and solved structure of a molluscan, glial-derived soluble ACh-binding protein, a model of the agonist site was constructed with contributing amino acids from three distinct loops (A, B, and C) of the , subunits and another three loops (D, E, and F) of the non-, subunits. According to this model, most insect nAChR subunits can form the functional heteromeric or homomeric receptors. Actually, insect subunits themselves did not form any functional receptor at various combinations as yet, and only part of them can form the functional receptors with vertebrate non-, subunits. These findings suggested that the agonist binding for insect nAChRs was not only contributed by those key amino acids in six loops, but also some unidentified amino acids from other regions. In our previous studies on nAChRs for Nilaparvata lugens, a target-site mutation (Y151S) was found within two , subunits (Nl,1 and Nl,3). In Drosophila S2 cells and Xenopus oocytes, Nl,1 can form functional receptors with rat ,2 subunit. However, the same thing was not observed in Nl,3. In the present paper, by exchanging the corresponding regions between Nl,1 and Nl,3 to generate different chimeras, amino acid residues or residue clusters in the regions outside the six loops were found to play essential roles in agonist binding, especially for the amino acid clusters between loop B and C. This result indicated that the residues in the six loops could be necessary, but not enough for the activity of agonist binding. [source] Glutamate levels and transport in cat (Felis catus) area 17 during cortical reorganization following binocular retinal lesionsJOURNAL OF NEUROCHEMISTRY, Issue 6 2003Ann Massie Abstract Glutamate is known to play a crucial role in the topographic reorganization of visual cortex after the induction of binocular central retinal lesions. In this study we investigated the possible involvement of the glial high-affinity Na+/K+ -dependent glutamate transporters in cortical plasticity using western blotting and intracortical microdialysis. Basal extracellular glutamate levels and the re-uptake activity for glutamate have been determined by comparing the extracellular glutamate concentration before and during the blockage of glutamate removal from the synaptic cleft with the potent transporter inhibitor l - trans -pyrrolidine-3,4-dicarboxylic acid. In cats with central retinal lesions we observed increased basal extracellular glutamate concentrations together with a decreased re-uptake activity in non-deprived, peripheral area 17, compared with the sensory-deprived, central cortex of the same animal as well as the topographically matching regions of area 17 in normal subjects. Western blotting experiments revealed a parallel decrease in the expression level of the glial glutamate transporter proteins GLT-1 and GLAST in non-deprived cortex compared with sensory-deprived cortex of lesion cats and the corresponding regions of area 17 of normal subjects. This study shows that partial sensory deprivation of the visual cortex affects the removal of glutamate from the synaptic cleft and implicates a role for glial,neuronal interactions in adult brain plasticity. [source] Helicobacter pylori and Campylobacter rectus share a common antigenMOLECULAR ORAL MICROBIOLOGY, Issue 2 2003S. Tanabe Aim: ,The aim of this study was to investigate the presence of antigens with immunological cross-reactivity in periodontopathogenic bacteria and Helicobacter pylori, the pathogen associated with gastritis and peptic ulcers in human. Materials and methods/Results: ,Among the putative periodontopathogens tested (Actinobacillus actinomycetemcomitans, Campylobacter rectus, Fusobacterium nucleatum, Porphyromonas gingivalis, Prevotella intermedia and Treponema denticola), cross-reactive bands were only detected in C. rectus by SDS,PAGE/Western immunoblotting analysis using a polyclonal antibody directed to H. pylori cells. One of these cross-reactive antigens, a 64-kDa band antigen, also reacted with a monoclonal antibody directed to the human heat shock protein (HSP) 60. The N -terminal amino acid sequence of this C. rectus protein revealed a high degree of homology with corresponding regions of other HSPs belonging to the HSP60 family, indicating that the 64-kDa antigen was a GroEL protein. The nucleotide sequence of the C. rectus GroEL protein coded for a 547 amino acid protein with a predicted size of 57.8 kDa. Comparison of the alignment of the deduced amino acid sequence of the GroEL protein of C. rectus with that of H. pylori showed a high degree of similarity throughout its length (76.8%). GroEL protein from C. rectus possessed the ability to stimulate production of IL-6 by a confluent monolayer of human gingival epithelial cells and was cytotoxic when used at a high concentration. Conclusions: ,This study reveals an immunological relationship between H. pylori and C. rectus, and clearly indicates that one of the shared antigens is a GroEL protein possessing a biological activity that might play a role in the initiation and progression of periodontal disease. [source] Secondary structure and dynamics of micelle bound ,- and ,-synucleinPROTEIN SCIENCE, Issue 5 2006Yoon-hui Sung Abstract We have used solution state NMR spectroscopy to characterize the secondary structure and backbone dynamics of the proteins ,- and ,-synuclein in their detergent micelle-bound conformations. Comparison of the results with those previously obtained for the Parkinson's disease-linked protein ,-synuclein shows that structural differences between the three homologous synuclein family members are directly related to variations in their primary amino acid sequences. An 11-residue deletion in the lipid-binding domain of ,-synuclein leads to the destabilization of an entire segment of the micelle-bound helical structure containing the deletion site. The acidic C-terminal tail region of ,-synuclein, which displays extensive sequence divergence, is more highly disordered than the corresponding regions in the other two family members. The observed structural differences are likely to mediate functional variations between the three proteins, with differences between ,- and ,-synuclein expected to revolve around their lipid interactions, while differences in ,-synuclein function are expected to result from different protein,protein interactions mediated by its unique C-terminal tail. [source] Hyperstability and crystal structure of cytochrome c555 from hyperthermophilic Aquifex aeolicusACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009Marii Obuchi In order to elucidate the relationship between the stability and the structure of the monohaem cytochrome c555 (AA c555) from the hyperthermophilic bacterium Aquifex aeolicus, chemical denaturation and crystal structure determination were carried out. AA c555 exhibited higher stability than the thermophilic Hydrogenobacter thermophilus cytochrome c552 (HT c552), which is one of the most stable cytochromes c. The three-dimensional crystal structure of AA c555, which was determined using the multiple anomalous dispersion technique at 1.15,Å resolution, included a unique 14-residue extra helix, while the side-chain interactions of several amino-acid residues responsible for the stability of HT c552 were conserved in AA c555. The side chain of the Met61 residue in the extra helix was aligned towards the haem, forming a coordination bond between the Met S and haem Fe atoms. In other cytochromes c the corresponding regions always form , loops which also include the haem-liganding Met residue and are known to be involved in the initial step in cytochrome c denaturation. The formation of the extra helix in AA c555 results in the highest helix content, 59.8%, among the monohaem cytochromes c. The extra helix should mainly contribute to the hyperstability of AA c555 and is presumed to be a novel strategy of cytochromes c for adaptation to a hyperthermophilic environment. [source] | |||||||||||||