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Unique Domain (unique + domain)
Selected AbstractsDeficiency of Myo18B in mice results in embryonic lethality with cardiac myofibrillar aberrationsGENES TO CELLS, Issue 10 2008Rieko Ajima Myo18B is an unconventional myosin family protein expressed predominantly in muscle cells. Although conventional myosins are known to be localized on the A-bands and function as a molecular motor for muscle contraction, Myo18B protein was localized on the Z-lines of myofibrils in striated muscles. Like Myo18A, another 18th class of myosin, the N-terminal unique domain of the protein and not the motor domain and the coiled-coil tail is critical for its localization to F-actin in myocytes. Myo18B expression was induced by myogenic differentiation through the binding of myocyte-specific enhancer factor-2 to its promoter. Deficiency of Myo18B caused an embryonic lethality in mice accompanied by disruption of myofibrillar structures in cardiac myocytes at embryonic day 10.5. Thus, Myo18B is a unique unconventional myosin that is predominantly expressed in myocytes and whose expression is essential for the development and/or maintenance of myofibrillar structure. [source] Epitope mapping of canine distemper virus phosphoprotein by monoclonal antibodiesMICROBIOLOGY AND IMMUNOLOGY, Issue 12 2009Akihiro Sugai ABSTRACT The gene for phosphoprotein (P) of CDV encodes three different proteins, P, V, and C. The P protein is involved in viral gene transcription and replication. In the present study, we produced MAbs against a unique domain of the CDV-P protein, from aa 232 to 507, and determined their antigenic sites. By immunizing BALB/c mice with the recombinant P protein-specific fragment, we obtained six MAbs. Competitive binding inhibition assays revealed that they recognized two distinct regions of the P protein. Western blot analysis and immunofluorescence assays using deletion mutants of the unique C-terminus of the CDV-P protein revealed that all MAbs recognized a central short region (aa 233,303) of the CDV-P protein. In addition, linear and conformational epitopes have been determined, and at least four antigenic sites exist in the P protein central region. Furthermore, four of the MAbs were found to react with the P protein of recent Japanese field isolates but not with that of the older CDV strains, including a vaccine strain. Thus, these MAbs could be clinically useful for quick diagnosis during the CDV outbreaks. [source] How Do Mothers Feel About Their Very Low Birth Weight Infants?INFANT MENTAL HEALTH JOURNAL, Issue 2 2006Development of a New Measure The early relationship between a mother and her very low birth weight (VLBW; <1.5 kg) infant may be difficult to evaluate. Therefore, we aimed to develop a useful and practical method to describe a mother's early relationship with her VLBW infant. Mothers (mean age=27 years, 46% married) of 119 singleton VLBW infants (mean BW=1,056 g, mean GA=28 weeks) admitted to the neonatal ICU at Rainbow Babies and Children's Hospital completed a novel questionnaire regarding their feelings about their infant at 3 weeks' postnatal age, and at 35 weeks', 40 weeks' (term), and 4 months' postmenstrual ages. Factor analysis of initial interview data was used to construct subscales to measure unique domains hypothesized to underpin the beginning maternal,infant relationship. Three subscales were identified: (a) The Worry subscale focuses on the mother's concerns about her infant's current medical condition and future development, (b) the Enjoyment subscale examines the mother's positive feelings about and responsiveness to her infant, and (c) the Separation Anxiety subscale examines the mother's mental anxiety about being physically separated from her infant. Statistical and clinical validation of the subscales produced positive supporting evidence that the subscales are a meaningful measure of the mother,infant relationship. We have developed a unique and practical measure for describing the early mother,VLBW infant relationship. [source] Evolutionary constraints on structural similarity in orthologs and paralogs,PROTEIN SCIENCE, Issue 6 2009Mark E. Peterson Abstract Although a quantitative relationship between sequence similarity and structural similarity has long been established, little is known about the impact of orthology on the relationship between protein sequence and structure. Among homologs, orthologs (derived by speciation) more frequently have similar functions than paralogs (derived by duplication). Here, we hypothesize that an orthologous pair will tend to exhibit greater structural similarity than a paralogous pair at the same level of sequence similarity. To test this hypothesis, we used 284,459 pairwise structure-based alignments of 12,634 unique domains from SCOP as well as orthology and paralogy assignments from OrthoMCL DB. We divided the comparisons by sequence identity and determined whether the sequence-structure relationship differed between the orthologs and paralogs. We found that at levels of sequence identity between 30 and 70%, orthologous domain pairs indeed tend to be significantly more structurally similar than paralogous pairs at the same level of sequence identity. An even larger difference is found when comparing ligand binding residues instead of whole domains. These differences between orthologs and paralogs are expected to be useful for selecting template structures in comparative modeling and target proteins in structural genomics. [source] | ||||||||||