Morning report for all: a qualitative study of disseminating case conferences via podcasting.

BACKGROUND: Despite its long-established importance, diagnostic reasoning (DR) education has suffered uneven implementation in medical education. The Clinical Problem Solvers (CPSolvers) podcast has emerged as a novel strategy to help teach DR through case conferences with expert diagnosticians and trainees. CPSolvers has 25,000 listeners in 147 countries. The aim of this study was to evaluate the podcast by eliciting the developers' goals of the podcast, then determining to what extent they aligned with the listeners' actual usage habits, features they valued, and perceptions of the podcast. METHODS: We conducted semi-structured interviews with 3 developers and 8 listeners from April-May 2020, followed by qualitative thematic analysis. RESULTS: Three major developer goals with sub-goals resulted: 1. To teach diagnostic reasoning in a case-based format by (1a) teaching schemas, (1b) modeling expert diagnostic reasoning, (1c) teaching clinical knowledge, and (1d) teaching diagnostic reasoning terminology. 2. To change the culture of medicine by (2a) promoting diversity, (2b) modeling humility and promoting psychological safety, and (2c) creating a fun, casual way to learn. 3. To democratize the teaching of diagnostic reasoning by leveraging technology. Listeners' usage habits, valued features, and perceptions overall strongly aligned with all these aspects, except for (1c) clinical knowledge, and (1d) diagnostic reasoning terminology. Listeners identified (1a) schemas, and (2c) promotion of psychological safety as the most valuable features of the podcast. CONCLUSION: CPSolvers has been perceived as a highly effective and novel way to disseminate DR education in the form of case conferences, serving as an alternative to traditional in-person case conferences suspended during COVID-19. CPSolvers combines many known benefits of in-person case conferences with a compassionate and entertaining teaching style, plus advantages of the podcasting medium - democratizing morning report for listeners around the world.

Left Ventricular Compression and Hypotension Due to Acute Colonic Pseudo-Obstruction.

Acute colonic pseudo-obstruction is a postsurgical dilatation of the colon that presents with abdominal distension, pain, nausea, vomiting, constipation, or diarrhea and may lead to colonic ischemia and bowel perforation.

Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.

Hematopoietic tyrosine phosphatase (HePTP) is one of three members of the kinase interaction motif (KIM) phosphatase family which also includes STEP and PCPTP1. The KIM-PTPs are characterized by a 15 residue sequence, the KIM, which confers specific high-affinity binding to their only known substrates, the MAP kinases Erk and p38, an interaction which is critical for their ability to regulate processes such as T cell differentiation (HePTP) and neuronal signaling (STEP). The KIM-PTPs are also characterized by a unique set of residues in their PTP substrate binding loops, where 4 of the 13 residues are differentially conserved among the KIM-PTPs as compared to more than 30 other class I PTPs. One of these residues, T106 in HePTP, is either an aspartate or asparagine in nearly every other PTP. Using multiple techniques, we investigate the role of these KIM-PTP specific residues in order to elucidate the molecular basis of substrate recognition by HePTP. First, we used NMR spectroscopy to show that Erk2-derived peptides interact specifically with HePTP at the active site. Next, to reveal the molecular details of this interaction, we solved the high-resolution three-dimensional structures of two distinct HePTP-Erk2 peptide complexes. Strikingly, we were only able to obtain crystals of these transient complexes using a KIM-PTP specific substrate-trapping mutant, in which the KIM-PTP specific residue T106 was mutated to an aspartic acid (T106D). The introduced aspartate side chain facilitates the coordination of the bound peptides, thereby stabilizing the active dephosphorylation complex. These structures establish the essential role of HePTP T106 in restricting HePTP specificity to only those substrates which are able to interact with KIM-PTPs via the KIM (e.g., Erk2, p38). Finally, we describe how this interaction of the KIM is sufficient for overcoming the otherwise weak interaction at the active site of KIM-PTPs.