DMT and Dissociation: Opening the Window of Tolerance to Embodiment; Development of a Method

Dissociative symptoms show in many different types of diagnoses, and dance/movement therapists have the skill set to introduce embodiment as a distress tolerance and regulatory skill. The current literature regarding effective dance/movement therapy as a tool for working with dissociative symptoms does not include the intersection of those that hold a queer identity. Inclusion of dissociative symptoms with trans* (any person who is not cisgender) identity allows for empowerment of recovery. The discussed development of a method is designed to contribute to the strengths and limitations dance/movement therapy holds in relation to dissociative symptoms, specifically working within the window of tolerance trauma model and with trans* individuals where the intersection of dissociation can be aligned with gender dysphoria. This method was implemented with queer adults at a partial hospitalization program, and it was observed that the intervention of active embodiment in the relationship to regulating dissociative symptoms led to activation in itself. Individual validation and specific mention of systemic discrimination in regard to trans* people’s lived experience with dissociation was also observed. Future research should examine a more specific practice of embodiment that focus around the queer identity as empowerment and expression. Dance/movement therapists should continue to explore how the integration of dance/movement therapy tools for regulation of dissociative symptoms can be best applied to trans* clients

Clinical relevance of soluble c-erbB-2 for patients with metastatic breast cancer predicting the response to second-line hormone or chemotherapy

Concentrations of soluble c-erbB-2 were determined in the sera of 64 patients with distant metastasis from advanced breast cancer receiving second-line hormone or chemotherapy in comparison to 35 breast cancer patients without detectable recurrent disease and 17 healthy blood donors. The sera of non-metastatic breast cancer patients contained s-erbB-2 concentrations similar to those of healthy blood donors. Patients with distant metastasis from advanced breast cancer had significantly higher values of s-erbB-2 in comparison to patients with non-disseminated disease (mean: 59.6 vs. 11.6 U/ml; p = 0.022). A significant correlation was observed between s-erbB-2 serum levels and serum LDH concentrations (p < 0.001), levels of alkaline phosphatase (p < 0.001), and the presence of hepatic metastasis (p = 0.001). Time to tumor progression was significantly shorter in patients with s-erbB-2 levels above 40 U/ml (mean: 23.4 vs. 56.7 months; p = 0.002). Furthermore, breast cancer patients with hepatic metastasis and those with elevated s-erbB-2 serum levels above 40 U/ml had limited response to hormone or chemotherapy. Non-responders had significantly higher s-erbB-2 levels (mean: 270.3, range: 42-500 U/ml;) compared with the responder group (mean: 23.1, range: 0-149 U/ml; p < 0.001). Logistic regression analysis indicated that elevated s-erbB-2 serum levels above 40 U/ml independently predicted an unfavorable response to second-line hormone or chemotherapy in patients with advanced metastatic breast cancer. Copyright (C) 2002 S. KargerAG, Basel

Dynamic architecture of the peroxisomal import receptor Pex5p

AbstractThe majority of peroxisomal matrix proteins are recognized by the import receptor Pex5p. The receptor is dynamic in terms of its overall architecture and association with the peroxisomal membrane. It participates in different protein complexes during the translocation of cargos from the cytosol to the peroxisomal matrix. Its sequence comprises two structurally and functionally autonomous parts. The N-terminal segment interacts with several peroxins that assemble into distinct protein complexes during cargo translocation. Despite evidence for α-helical binding motifs for some of these components (Pex13p, Pex14p) its overall appearance is that of a molten globule and folding/unfolding transitions may play a critical role in its function. In contrast, most of the C-terminal part of the receptor folds into a ring-like α-helical structure and binds folded and functionally intact peroxisomal targets that bear a C-terminal peroxisomal targeting signal type-1. Some of these targets also bind to secondary binding sites of the receptor

Crystallization and structure solution at 4 Å resolution of the recombinant synthase domain of N(5′-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue

The recombinant synthase domain of the bifunctional enzyme N-(5″-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli has been crystallized, and the structure has been solved at 4 Å resolution. Two closely related crystal forms grown from ammonium sulphate diffract to 2 Å resolution. One form (space group R32, a = 163 Å, α = 29.5°) contains the unliganded synthase domain; the second crystal form (space group P6322, a = 144 Å, c = 158 Å) is co-crystallized with the substrate analogue N-(5′-phosphoribit-1-yl)anthranilate. The structure of the synthase-inhibitor complex has been solved by the molecular replacement method. This achievement represents the first successful use of a (βα)g-barrel monomer as a trial model. The recombinant synthase domain associates as a trimer in the crystal, the molecules being related by a pseudo-crystallographic triad. The interface contacts between the three domains are mediated by those residues that are also involved in the domain interface of the bifunctional enzyme. This system provides a model for an interface which is used in both intermolecular and intramolecular domain contact