Homework setting in cognitive behavioral therapy: A study of discursive strategies.

In recent years cognitive behavioral therapy (CBT), a form ofpsychotherapy, has risen to prominence due to a large number of studies attesting to its efficacy. A crucial part of the model of CBT is the use of the therapeutic strategy, homework, in which the client undertakes therapeutic tasks between sessions. The focus of this study is on how homework is implemented in sessions of CBT. This is undertaken through an analysis utilizing theme-orientated discourse analysis of video recorded sessions of CBT of one therapist and a client. Through tracking the focal theme of homework, the analysis focuses on homework as a face-threatening act (Brown and Levinson 1987) and how discursive strategies are employed to manage this issue. Other analytic themes include the use of frames (Goffman 1974) and constructed dialogue (Tannen 2007). It is the expertise of the therapist in putting into practice the therapeutic task of homework that is the subject of this study.

The negotiation of the problem statement in cognitive behavioural therapy.

Cognitive behavioural therapy (CBT) is a form of psychotherapy which is characterized by being highly structured, outcomes focused and time limited. The literature concerning CBT is extensive but it has primarily focused on the outcomes of therapy with limited qualitative studies investigating the process of CBT. In this present study we investigate how the CBT model is implemented in therapeutic interaction through a focus on the conversion of the client's problem into CBT terms and its ultimate articulation as the problem statement. The problem statement is an integral part of the form of CBT studied from which the subsequent therapy is derived. Drawing on theme-oriented discourse analysis we examine the first two sessions of the treatment of one client using a number of tools derived from discourse and conversation analysis. This case study was drawn from a larger corpus of the CBT treatment often clients. The expertise of the therapist in applying the generic CBT model of therapy to the client's particular problem is a focus of this study.

Persistent pain after hysteroscopic sterilization with microinserts.

BACKGROUND: Hysteroscopic sterilization using tubal microinsert devices is an increasingly common method of contraception. Postprocedure pain is typically minimal and brief, adding to the popularity of this method. This report describes a case of intractable pain after placement of microinserts, ultimately requiring removal of the inserts. CASE: A 31-year-old gravida 4 para 4 woman underwent an uncomplicated office hysteroscopic tubal occlusion for permanent birth control. Subsequent to the procedure, she had significant bilateral pelvic pain that failed all attempts at conservative management and required removal of the microinserts for pain relief. CONCLUSION: Hysteroscopic placement of tubal microinserts for sterilization may occasionally be associated with intractable pelvic pain requiring removal of the devices.

Structure of Escherichia coli uridine phosphorylase at 2.0 A.

The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 A model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated.

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.

The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.