[With the tooth salvage box the tooth has a chance. Dentists recommend: Tooth salvage box belongs in the home emergency kit].
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Emergency Medical Services↗
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Results for “Boxing”
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Cigar box to personality box.
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Achievement↗
[A dental hygiene audio-visual box--the HAS box].
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Audiovisual Aids↗
All internal promoter elements of Neurospora crassa 5 S rRNA and tRNA genes, including the A boxes, are functionally gene-specific.
The internal control elements of Neurospora crassa 5 S genes include an A box and a C box as in Xenopus and Saccharomyces cerevisiae, plus a novel element, the Ribo box at position +18 to +34. The Ribo box is also found in the 40 S rRNA promoter and a ribosomal protein gene but is absent from tRNA genes in N. crassa. The 5 S A box diverges from the tRNA A box consensus at two positions. We tested whether replacement of the 5 S A box with a tRNALeu A box sequence would increase 5 S gene transcription in vitro or would remove the requirement for the Ribo box. The 5 S gene with the tRNALeu A box was transcribed poorly, and the Ribo box and the C box are still required for transcription. We tested the function of the Ribo box and 5 S A box in a tRNA-like transcription unit by constructing hybrids between a 5 S gene and a tRNALeu gene. In the tRNA-like context, the 5 S A box supported a lower level of transcription than the tRNA A box, and the Ribo box was not required at all. Therefore, in N. crassa, all of the 5 S internal control elements are gene-specific. In particular, the 5 S and tRNA A box sequences are not functionally interchangeable and may bind different transcription factors. Transcription of the hybrids was initiated at the 5 S initiation site, suggesting that the mechanism of initiation site selection is the same in the 5 S and tRNA genes. Competition experiments with the tRNA B box suggested that the N. crassa 5 S and tRNA genes require at least one common transcription factor such as TFIIIC.
Base Sequence↗
Effect of an odor eliminator on feline litter box behavior.
Decreasing litter box odor may be an important treatment component in addressing feline inappropriate elimination. A three-phase study was conducted to determine if the use of Zero Odor litter box spray increases the preference of litter boxes to cats, presumably by its odor-eliminating quality. In the first phase, cats were given a litter box preference test between a litter box sprayed with Zero Odor and one without. In the second phase, the number of occurrences of behaviors indicative of a cat's dissatisfaction with the litter box (scratching at the sides of the box, floor or wall, hesitating when entering the litter box, balancing on the side of the box and eliminating outside of the litter box) was compared before and after the use of Zero Odor. Last, the frequency of eliminations that occurred outside the litter box was measured during a baseline phase and a test phase, in which Zero Odor was sprayed into all litter boxes in the home. Significantly fewer behaviors associated with feline litter box dissatisfaction and fewer undesirable eliminations were observed in phases 2 and 3, respectively. These findings suggest that use of Zero Odor litter box spray appears to decrease litter box odor and increases the attractiveness of litter box to cats.
Aerosols↗
An E-box region within the prostaglandin endoperoxide synthase-2 (PGS-2) promoter is required for transcription in rat ovarian granulosa cells.
The prostaglandin endoperoxide synthase-2 (PGS-2) gene encodes an isoform of prostaglandin synthase that is transiently induced by protein kinase A (luteinizing hormone/cAMP) and protein kinase C (gonadotropin-releasing hormone) agonists in granulosa cells of ovulating follicles. The promoter of the rat PGS-2 gene contains a CAAT enhancer-binding protein consensus site (CAAT box) which can confer hormone inducibility to a PGS-2.CAT reporter gene, as well as a putative E-box region. To determine if the E-box region was involved in hormone induced trans-activation of the rat PGS-2 gene, constructs with the CAAT box and E-box regions (-192 PGS-2.CAT), only the putative E-box (-110 PGS-2.CAT), or neither region (-52 PGS-2.CAT) were transiently transfected into rat granulosa cell cultures. CAT activity was induced in both the -192 and -110 PGS-2*CAT vectors by luteinizing hormone (10-fold) and gonadotropin-releasing hormone (6-fold), whereas CAT activity of the -52 PGS-2.CAT construct did not differ from the promoterless vector (pCAT-Basic). Deletion of 1 base pair from the E-box within the -110 PGS-2.CAT construct, as well as point mutations within the CAAT box, E-box, or both regions of the -192 PGS-2.CAT construct, demonstrated that the E-box is critical for basal transcription, and that regions, in addition to the CAAT box, are involved in hormone induction of the PGS-2 gene. An oligonucleotide spanning the rat PGS-2 E-box bound two specific protein complexes which were supershifted in the presence of antibody specific for the upstream stimulatory factor. Thus, in rat granulosa cells, the PGS-2 E-box region appears to interact with upstream cis-acting elements other than the CAAT box to confer hormonal regulation of the gene. The E-box region of the rat PGS-2 promoter does not contain ATF/CRE activity found in the human and mouse PGS-2 promoters, but is critical for basal transcription of the PGS-2 gene in rat granulosa cells and binds the upstream stimulatory factor (as do E-box regions of other genes regulated in the ovary).
Animals↗
[Determination of human RHD gene rhesus box and its significance].
The aim was to determine RHD zygosity, further to investigate genetic structure of RHD gene, and to predict hemolytic disease of newborn (HDN). The upstream box, downstream box, and hybrid box of RHD gene were determined by PCR-SSP with 4 primers under the same conditions. The results showed that only hybrid box could be determined in RHD(-)/RHD(-) homozygosity. All the upstream box, downstream box, and hybrid box could be determined in RHD(+)/RHD(-) heterozygosity, while upstream box and downstream box except hybrid box could be determined in RHD(+)/RHD(+) homozygosity. Out of 50 cases of RhD(+), 5 cases (10%) were RHD(+)/RHD(-) heterozygosity, and the others (90%) were RHD(+)/RHD(+) homozygosity. 54 cases (55.1%), 36 cases (36.7%) and 8 cases (8.2%) were RHD(-)/RHD(-) homozygosity, RHD(+)/RHD(-) heterozygosity, and RHD(+)/RHD(+) homozygosity respectively in 98 unrelated cases of RhD(-) Chinese Hans. 2 cases of weak D were proved to be RHD(+)/RHD(-) heterozygosity. Out of 16 D(el) types, the upstream box, downstream box, and hybrid box could be determined in 10 cases (37.5%) and the upstream box and downstream box except hybrid box could be determined in 6 cases. Results detecting of RHD 10 exons in above samples proved the correctness of the method. It is concluded that the method is suitable for clinical application with its simplicity and veracity. There are many noneffective RHD genes (44.9%) in Chinese Hans with RhD(-) phenotype.
Genotype↗
A comprehensive set of DnaA-box mutations in the replication origin, oriC, of Escherichia coli.
We probed the complex between the replication origin, oriC, and the initiator protein DnaA using different types of mutations in the five binding sites for DnaA, DnaA boxes R1-R4 and M: (i) point mutations in individual DnaA boxes and combinations of them; (ii) replacement of the DnaA boxes by a scrambled 9 bp non-box motif; (iii) positional exchange; and (iv) inversion of the DnaA boxes. For each of the five DnaA boxes we found at least one type of mutation that resulted in a phenotype. This demonstrates that all DnaA boxes in oriC have a function in the initiation process. Most mutants with point mutations retained some origin activity, and the in vitro DnaA-binding capacity of these origins correlated well with their replication proficiency. Inversion or scrambling of DnaA boxes R1 or M inactivated oriC-dependent replication of joint replicons or minichromosomes under all conditions, demonstrating the importance of these sites. In contrast, mutants with inverted or scrambled DnaA boxes R2 or R4 could not replicate in wild-type hosts but gave transformants in host strains with deleted or compromised chromosomal oriC at elevated DnaA concentrations. We conclude that these origins require more DnaA per origin for initiation than does wild-type oriC. Mutants in DnaA box R3 behaved essentially like wild-type oriC, except for those in which the low-affinity box R3 was replaced by the high-affinity box R1. Apparently, initiation is possible without DnaA binding to box R3, but high-affinity DnaA binding to DnaA box R3 upsets the regulation. Taken together, these results demonstrate that there are finely tuned DnaA binding requirements for each of the individual DnaA boxes for optimal build-up of the initiation complex and replication initiation in vivo.
Bacterial Proteins↗
Genetic mechanisms of Rhesus box variation.
BACKGROUND: The RHD gene is flanked by two highly homologous DNA segments of approximately 9000 bp, the upstream and downstream Rhesus boxes. In haplotypes with an RHD deletion, the fusion of the two Rhesus boxes generates the single-hybrid Rhesus box, the detection of which has been applied for RHD zygosity determination. Aberrant Rhesus boxes can confound this application and appear to be frequent among African individuals. STUDY DESIGN AND METHODS: A total of 5850 bp of the upstream and of the downstream Rhesus boxes were sequenced in 18 samples that were representative for all four D clusters and of the hybrid Rhesus boxes in four samples that were mistyped in assays for the hybrid Rhesus box. RESULTS: The known differences between upstream and downstream Rhesus boxes were in part restricted to subsets of RHD alleles. Forty-six additional polymorphisms were detected and caused by single-nucleotide substitutions, short insertions, or deletions. Gene conversions were found in the upstream Rhesus boxes of RHDpsi, DAU-1, and DAU-3 and in the downstream Rhesus boxes of Ccdes, weak D type 4.1, type 4.2 (DAR), and DAU-0. Recombinations between haplotypes were likely in several alleles like DIII type 4. Four nonstandard hybrid Rhesus boxes were suggestive of multiple RHD deletion events. CONCLUSION: There is considerable variation of Rhesus box sequences associated with distinct RHD alleles. RHD zygosity diagnostics in African persons is best based on quantitative polymerase chain reaction or amplification of the full-length hybrid Rhesus box. Because aberrant Rhesus boxes were observed among European persons, use of more than one method for hybrid Rhesus box detection may even be advisable in European persons.
Africa↗
[Study of rat control by using bait box].
This study examines the feasibility of using bait boxes for permanent rat control in Taiwan. During the test period between October 1988 and March 1989, 37 bait boxes made of PVC pipes were placed at various baiting sites in public markets, near restaurants and food stands in several communities known to be infested by rats. Each of the 37 boxes was baited with non-toxic rice powder to determine how well these boxes were accepted, the time needed for rats to use the boxes and eat the bait, and to do preliminary census on the relative densities of rat populations at these different places. The results showed that 27 of 29 (93.1%) bait boxes that had not been vandalized, disturbed or moved away and could be monitored continuously were used by rats. Of these 27 bait boxes, 13 (48.1%) were used the day after the boxes were set, and 25 (92.6%) were used within a week after the boxes were set. The amount of bait eaten per day for each bait box varied greatly, from less than 5 g to more than 300 g. After the bait in each bait box was taken regularly, half of the bait boxes with good bait acceptance were pulse-baited with 0.005% brodifacoum coated rice powder, and the other half of the bait boxes with good bait acceptance were baited with non toxic rice powder for comparison. The result of treatment indicated that rat control by using bait boxes is effective. However, the cooperation of the local people and the location of bait boxes have a great influence over the success of this control method.
Animals↗
Medical and safety reforms in boxing.
The continued existence of boxing as an accepted sport in civilized society has been long debated. The position of the American Medical Association (AMA) has evolved from promoting increased safety and medical reform to recommending total abolition of both amateur and professional boxing. In response to the AMA opposition to boxing, the boxing community has attempted to increase the safeguards in amateur and professional boxing.The United States of America Amateur Boxing Federation, which is the national regulatory agency for all amateur boxing in the United States, has taken several actions to prevent the occurrence of acute brain injury and is currently conducting epidemiologic studies to assess the long-term neuropsychologic consequences of amateur boxing. In professional boxing, state regulatory agencies such as the New York State Athletic Commission have introduced several medical interventions to prevent and reduce neurologic injury. The lack of a national regulatory agency to govern professional boxing has stimulated the formation of the Association of Boxing Commissions and potential legislation for the federal regulation of professional boxing by a federally chartered organization called the United States Boxing Commission. The AMA's opposition to boxing and the medical and safety reforms implemented by the proponents of boxing are discussed.
American Medical Association↗
Identification of substrates for F-box proteins.
F-box proteins serve as specificity factors for a family of ubiquitin protein ligases composed of Skp1, Cu11, and Rbx1. In SCF complexes, Cu11 serves as a scaffold for assembly of the catalytic components composed of Rbx1 and a ubiquitin-conjugating enzyme and the specificity module composed of Skp1 and an F-box protein. F-box proteins interact with Skp1 through the F-box motif and with ubiquitination substrates through C-terminal protein interaction domains such as WD40 repeats. The human genome contains approximately 68 F-box proteins, which fall into three major classes: Fbws containing WD40 repeats, Fbls containing leucine-rich repeats, and Fbxs containing other types of domains. Most often, F-box proteins interact with their targets in a phosphorylation-dependent manner. The interaction of F-box proteins with substrates typically involves a phosphodegron, a small peptide motif containing specific phosphorylation events whose sequence is complementary to the F-box protein. The identification of substrates of F-box proteins is frequently a challenge because of the relatively weak affinity of substrates for the requisite F-box protein. Here we describe approaches for the identification of substrates of F-box proteins. Approaches include stabilization of ubiquitination targets by Cu11-dominant negatives, the use of shRNA hairpins to disrupt F-box protein expression, and the use of collections of F-box proteins as biochemical reagents to identify interacting proteins that may be substrates. In addition, we describe approaches for the use of immobilized phosphopeptides to identify F-box proteins that recognize particular phosphodegrons.
Animals↗
Evolution and divergence of the MADS-box gene family based on genome-wide expression analyses.
MADS-box genes encode transcription factors involved in various important aspects of development and differentiation in land plants, metazoans, and other organisms. Three types of land plant MADS-box genes have been reported. MIKCC- and MIKC*-type genes both contain conserved MADS and K domains but have different exon/intron structures. M-type genes lack a K domain. Most MADS-box genes previously analyzed in land plants are expressed in the sporophyte (diploid plant body); few are expressed in the gametophyte (haploid plant body). Land plants are believed to have evolved from a gametophyte (haploid)-dominant ancestor without a multicellular sporophyte (diploid plant body); most genes expressed in the sporophyte probably originated from those used in the gametophyte during the evolution of land plants. To analyze the evolution and diversification of MADS-box genes in land plants, gametophytic MADS-box genes were screened using macroarray analyses for 105 MADS-box genes found in the Arabidopsis genome. Eight MADS-box genes were predominantly expressed in pollen, the male gametophyte; all but one of their expression patterns was confirmed by Northern analyses. Analyses of the exon/intron structure of these seven genes revealed that they included two MIKCC-type, one M-type, and four MIKC*-type MADS-box genes. Previously, MIKC*-type genes have been reported only from a moss and a club moss, and this is the first record in seed plants. These genes can be used to investigate the unknown ancestral functions of MADS-box genes in land plants. The macroarray analyses did not detect expression of 56 of 61 M-type MADS-box genes in any tissues examined. A phylogenetic tree including all three types of Arabidopsis MADS-box genes with representative genes from other organisms showed that M-type genes were polyphyletic and that their branch lengths were much longer than for the other genes. This finding suggests that most M-type genes are pseudogenes, although further experiments are necessary to confirm this possibility. Our global phylogenetic analyses of MADS-box genes did not support the previous classification of MADS-box genes into type I and II groups, based on smaller scale analyses. An evolutionary scenario for the evolution of MADS-box genes in land plants is discussed.
Arabidopsis↗
BOX DNA: a novel regulatory element related to embryonal carcinoma cell differentiation.
BOX DNA was previously isolated from the DNA sequence inserted in the enhancer B domain of mutant polyomavirus (fPyF9) DNA. We also reported that BOX DNA functioned negatively on DNA replication and transcription of another polyomavirus mutant (PyhrN2) in F9-28 cells, a subclone of mouse F9 embryonal carcinoma (EC) cells expressing the polyomavirus large T antigen. In this study, we demonstrate that BOX DNA enhances transcription from the thymidine kinase (TK) promoter in various EC cells. One or three copies of BOX DNA, linked to the bacterial chloramphenicol acetyltransferase gene under the control of the herpes simplex virus TK promoter, activated promoter activity in F9, P19, and ECA2 cells. Band shift assays using BOX DNA as a probe revealed that specific binding proteins were present in all EC cells examined; the patterns of BOX DNA-protein complexes were the same among them. A mutation introduced within BOX DNA abolished enhancer activity as well as the formation of specific DNA-protein complexes. In non-EC cells, including L and BALB/3T3 cells, the enhancer activity of BOX DNA on the TK promoter was not observed, although binding proteins specific to the sequence exist. In band shift assays, the patterns of the DNA-protein complexes of either L or BALB/3T3 cells were different from those of EC cells. Furthermore, the enhancer activity of BOX DNA decreased upon differentiation induction in all EC cells examined, of different origins and distinct differentiation ability. In parallel with the loss of enhancer activity, the binding proteins specific for BOX DNA decreased in these cells. Moreover, we cloned a genomic DNA of F9, termed BOXF1, containing BOX DNA sequence approximately 400 bp upstream from the RNA start site of the gene. BOXF1, containing a TATA-like motif and the binding elements for Sp1 and Oct in addition to BOX DNA, possessed promoter activity deduced by a BOXF1-chloramphenicol acetyltransferase construct. Deletion analyses of the construct revealed that the transcription of BOXF1 gene is regulated by BOX DNA, preferentially in undifferentiated EC cells versus differentiated cells. Hence, BOX DNA is probably a novel transcriptional element related to EC cell differentiation.
Animals↗
The X boxes from promoters of HLA class II B genes at different loci do not complete for nuclear protein-specific binding.
Expression of HLA class II genes is coordinately regulated by cis-acting elements present in their promoter regions immediately upstream from the 5' end of their transcription start sites. Trans-acting factors from the nuclear proteins of the cell are able to positively or negatively regulate transcription of these genes by binding to highly conserved sequences, called boxes. After cloning the promoter regions of all the transcribed class II B genes present in the cell line Priess, we were able to identify certain protein-box complexes and to determine the affinity of these proteins for their respective boxes by comparing promoter boxes of each gene to those of the other genes. Different nuclear proteins seemed to bind to the X boxes of the different class II B genes tested. In the case of the Y box-protein complexes, the various Y boxes competed with similar affinities. The protein(s) which specifically bound to the DRB1-CCAAT box also bound to DPB1-CCAAT box, but completely failed to bind the homologous box from DQB1. Further, CCAAT box-specific protein(s) did not bind to the Y box of the same gene, excluding the possibility that these proteins just recognize the reverse CCAAT box (ATTGG) present within Y.
Amino Acid Sequence↗
Insights into the quality of DnaA boxes and their cooperativity.
Plasmids carrying the mioC promoter region with its two DnaA boxes are as efficient in titration of DnaA protein as plasmids carrying a replication-inactivated oriC region with its five DnaA boxes. The two DnaA boxes upstream of the mioC promoter were mutated in various ways to study the cooperativity between the DnaA boxes, and to study in vivo the in vitro-defined 9mer DnaA box consensus sequence (TT(A)/(T)TNCACA). The quality and cooperativity of the DnaA boxes were determined in two complementary ways: as titration of DnaA protein leading to derepression of the dnaA promoter, and as repression of the mioC promoter caused by the DnaA protein binding to the DnaA boxes. Titration of DnaA protein correlated with repression of the mioC promoter. The level of titration and repression with the normal promoter-proximal box (TTTTCCACA) depends strongly on the presence and the quality of a DnaA box in the promoter-distal position, whereas a promoter-proximal DnaA box with the sequence TTATCCACA titrated DnaA protein and caused significant repression of the mioC promoter without a promoter-distal DnaA box. The quality of the eight different consensus DnaA boxes located in the promoter-proximal position was determined: TTATCCACA had the highest affinity for DnaA protein. In the third position, A was better than T, and the four possibilities in the fifth position could be ranked as C >A >or=G >T. Parallel in vitro experiments using a purified DNA-binding domain of DnaA protein gave the same ranking of the binding affinities of the eight DnaA boxes.
Bacterial Proteins↗
The LAMB1 gene from the clubmoss, Lycopodium annotinum, is a divergent MADS-box gene, expressed specifically in sporogenic structures.
Transcription factors encoded by the large MADS-box gene family have important developmental functions in angiosperms, the flowering plants. Mutations in certain MADS-box genes are known to cause homeotic alterations in floral organ identity, and the establishment of floral organ identity is the most well-studied developmental process in which MADS-box genes are known to function. Our interest is in the potential connection between the duplication history of this gene family and the evolutionary origin of the structures that the different MADS-box genes developmentally regulate in plants. Previous studies have demonstrated that the origin of the MADS-box genes that control floral organ identity predate the evolutionary origin of the flower itself, since gymnosperms have genes that are orthologous to angiosperm floral homeotic MADS-box genes, whereas ferns appear to lack such genes. Here we report on the isolation of a MADS-box gene from Lycopodium annotinum, which belongs to the clubmosses, the phylogenetic sister group to other vascular plants. The gene, LAMB1, in the sporophyte is expressed exclusively in the reproductive structure, the strobilus, during sporogenesis. LAMB1 is similar to other plant MADS-box genes in that it contains a MADS-box as well as a second conserved element, a K-box. However, it differs in length and in exon/intron structure in the region between the MADS- and K-box, and also in the length and structure of the C-terminal region. A phylogenetic analysis indicates that LAMB1 is not closely related to other plant-type MADS-box genes, and may represent one of the basal branches in the phylogenetic tree of plant MADS-box genes.
Amino Acid Sequence↗