Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A survey of 123 subjects (dental students) was performed to evaluate quantitative data that may be of value in the incidence and treatment of myofacial pain. Social statistics, subjective and objective symptoms, and the influence of occlusal interferences on these symptoms were quantitated and recorded. The data indicated that, 123 subjects, 26% had maximum intercuspation of the teeth at terminal hinge closure, 42% had maximum intercuspation of the teeth with the condyles located symmetrically anterior to terminal hinge, and 32.5% had maximum intercuspation of the teeth with assymmetric variations of the condyles anterior to terminal hinge. Averages were obtained for the maximum intercuspal open, the condylar inclination, and the distance anterior from the terminal hinge of both condyles in symmetrical and asymmetrical variations. The location of the transverse (terminal hinge) axis from the external auditory meatus was measured on the ala-tragus line. These latter averages indicate that a significant occlusal discrepancy can result from prevailing techniques of locating an arbitrary hinge axis 10 to 13 mm anterior from the external auditory meatus. The results showed that most subjects demonstrated, both subjectively and clinically, symptoms of neuromuscular dysfunction without occlusal interferences. Therefore, it may be concluded that treatment modalities considered within the first 6 weeks should be conservative and reversible to eliminate or decrease myofascial trigger zones and their areas of referred pain. Alteration of the existing occlusion and maxillomandibular relations may be adjusted with caution, if necessary.
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PMID:A study of occlusal relationships and the incidence of myofacial pain. 695 40

The asymmetrical face bow with internal hinge was successfully employed in the treatment of all examined patients. It finds application as an individual appliance, in combination with removable appliances, and in conjunction with the fixed appliance technique. The major advantage of the face bow is that during a check-up visit, because it is already in place, it presents itself as a proven means for the treatment of asymmetries by adding a hinge on the side not to be distalized and by shortening the external arm on the same side. It is not necessary to employ a new, special face bow or even to change the orthodontic bands. In addition, in the case of an intermaxillary midline correction, no anchorage loss occurs. In the case of more extensive molar rotations, a pretreatment with a palatal archwire is recommended to rotate the molars. Because in 4% of the patients a cross bite or a cross bite tendency arises on the side distally treated, at the beginning of treatment the use of bands with attachments for palatal archwires should be considered. Relatively sizable distal forces in the range of 2:1 to 4:1 are exerted on the molar. This should be taken into account when selecting the forces of the external arm. It is recommended to apply on each of both sides a distal force of no more than 4 to 5 N. Decoupling of forces and movements through the internal hinge makes it possible for the practitioners to check the asymmetrical effect of the face bow by pulling out carefully the lingual archwire from the right or left tube. As long as the hinge still folds down, when the face bow is applied, the geometrics of the face bow should be altered. The following procedures can be recommended: 1. Further shortening of the already shortened arm; 2. outward bending of the long external arm; 3. use of an additional stop tube at the lingual archwire on the side that must be distalized. During the use of related low-pulls, the molars are subjected to diverse forces as a result of preferred sleeping positions, head bearings, and extensive friction, To avoid these non-calculable asymmetries, it is recommended to use gliding low-pulls. Because of the excellent results achieved throughout the use of the asymmetrical headgear with the lingual archwire, it can be recommended that it become a standard appliance in clinical practice.
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PMID:[How effective is asymmetrical headgear in practical use?]. 865 5

Single-photon radioluminescence (SPR), the excitation of fluorophores by short-range beta-decay electrons, was developed for the measurement of submicroscopic distances. The cytoplasmic domain of band 3 (cdb3) is the primary, multisite anchorage for the erythrocyte skeleton. To begin to define the membrane arrangement of the highly asymmetrical cdb3 structure, the distance from the bilayer of Cys-201 next to the "hinge" of cdb3 was measured by both SPR and resonance energy transfer (RET). cdb3 was labeled at Cys-201 with fluorescein maleimide. For SPR measurements, the bilayer was labeled with [3H]oleic acid. The corrected cdb3-specific SPR signal was 98 +/- 2 cps microCi-1 [mumol band 3]-1. From this and the signal from a parallel sample in which 3H2O was substituted for [3H]oleic acid to create uniform geometry between 3H and the fluorophores, a Cys-201-to-bilayer separation of 39 +/- 7 A was calculated. Confirmatory distances of 40 and 43 A were obtained by RET between fluorescein on Cys-201 and eosin and rhodamine B lipid probes, respectively. This distance indicates that Cys-201 lies near band 3's vertical axis of symmetry and that the subdomain of cdb3 between the hinge and the membrane is not significantly extended. In addition, these results validate SPR as a measure of molecular distances in biological systems.
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PMID:Distance between Cys-201 in erythrocyte band 3 and the bilayer measured by single-photon radioluminescence. 891 2

Alamethicin is an alpha-helical channel-forming peptide, which inserts into lipid bilayers in a voltage-dependent, asymmetrical fashion. Nanosecond molecular dynamics simulations have been used to compare alamethicin conformation and dynamics in three different environments: 1) in water; 2) in methanol; and 3) inserted into a lipid (palmitoyl-oleoyl-phosphatidylcholine) bilayer to form a transmembrane helix. In the bilayer and in methanol, there was little change (Calpha RMSD approximately 0.2 nm over 2 ns and 1 ns) from the initial helical conformation of the peptide. In water there were substantial changes (Calpha RMSD approximately 0.4 nm over 1 ns), especially in the C-terminal segment of the peptide, which lost its alpha-helical conformation. In the bilayer and in methanol, the alamethicin molecule underwent hinge-bending motion about its central Gly-X-X-Pro sequence motif. Analysis of H-bonding interactions revealed that the polar C-terminal side chains of alamethicin provided an "anchor" to the bilayer/water interface via formation of multiple H-bonds that persisted throughout the simulation. This explains why the preferred mode of helix insertion into the bilayer is N-terminal, which is believed to underlie the asymmetry of voltage activation of alamethicin channels.
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PMID:Alamethicin helices in a bilayer and in solution: molecular dynamics simulations. 987 21

In this work, we present studies of the covalent structure of human IgG2 molecules. Detailed analysis showed that recombinant human IgG2 monoclonal antibody could be partially resolved into structurally distinct forms caused by multiple disulfide bond structures. In addition to the presently accepted structure for the human IgG2 subclass, we also found major structures that differ from those documented in the current literature. These novel structural isoforms are defined by the light chain constant domain (C(L)) and the heavy chain C(H)1 domain covalently linked via disulfide bonds to the hinge region of the molecule. Our results demonstrate the presence of three main types of structures within the human IgG2 subclass, and we have named these structures IgG2-A, -B, and -A/B. IgG2-A is the known classic structure for the IgG2 subclass defined by structurally independent Fab domains and hinge region. IgG2-B is a structure defined by a symmetrical arrangement of a (C(H)1-C(L)-hinge)(2) complex with both Fab regions covalently linked to the hinge. IgG2-A/B represents an intermediate form, defined by an asymmetrical arrangement involving one Fab arm covalently linked to the hinge through disulfide bonds. The newly discovered structural isoforms are present in native human IgG2 antibodies isolated from myeloma plasma and from normal serum. Furthermore, the isoforms are present in native human IgG2 with either kappa or lambda light chains, although the ratios differ between the light chain classes. These findings indicate that disulfide structural heterogeneity is a naturally occurring feature of antibodies belonging to the human IgG2 subclass.
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PMID:Human IgG2 antibodies display disulfide-mediated structural isoforms. 1833 24

Protein kinase A (PKA) is the main receptor for the universal cAMP second messenger. PKA is a tetramer with two catalytic (C) and two regulatory (R) subunits, each including two tandem cAMP binding domains, i.e. CBD-A and -B. Structural investigations of RIalpha have revealed that although CBD-A plays a pivotal role in the cAMP-dependent inhibition of C, the main function of CBD-B is to regulate the access of cAMP to site A. To further understand the mechanism underlying the cross-talk between CBD-A and -B, we report here the NMR investigation of a construct of R, RIalpha-(119-379), which unlike previous fragments characterized by NMR, spans in full both CBDs. Our NMR studies were also extended to two mutants, R209K and the corresponding R333K, which severely reduce the affinity of cAMP for CBD-A and -B, respectively. The comparative NMR analysis of wild-type RIalpha-(119-379) and of the two domain silencing mutations has led to the definition at an unprecedented level of detail of both intra- and interdomain allosteric networks, revealing several striking differences between the two CBDs. First, the two domains, although homologous in sequence and structure, exhibit remarkably different responses to the R/K mutations especially at the beta2-3 allosteric "hot spot." Second, although the two CBDs are reciprocally coupled at the level of local unfolding of the hinge, the A-to-B and B-to-A pathways are dramatically asymmetrical at the level of global unfolding. Such an asymmetric interdomain cross-talk ensures efficiency and robustness in both the activation and de-activation of PKA.
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PMID:Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations. 2020 31

Igs in vertebrates comprise equally sized H and L chains, with exceptions such as H chain-only Abs in camels or natural Ag receptors in sharks. In Reptilia, Igs are known as IgYs. Using immunoassays with isotype-specific mAbs, in this study we show that green turtles (Chelonia mydas) have a 5.7S 120-kDa IgY comprising two equally sized H/L chains with truncated Fc and a 7S 200-kDa IgY comprised of two differently sized H chains bound to L chains and apparently often noncovalently associated with an antigenically related 90-kDa moiety. Both the 200- and 90-kDa 7S molecules are made in response to specific Ag, although the 90-kDa molecule appears more prominent after chronic Ag stimulation. Despite no molecular evidence of a hinge, electron microscopy reveals marked flexibility of Fab arms of 7S and 5.7S IgY. Both IgY can be captured with protein G or melon gel, but less so with protein A. Thus, turtle IgY share some characteristics with mammalian IgG. However, the asymmetrical structure of some turtle Ig and the discovery of an Ig class indicative of chronic antigenic stimulation represent striking advances in our understanding of immunology.
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PMID:Green Turtles (Chelonia mydas) Have Novel Asymmetrical Antibodies. 2650 Mar 46