Faculty Bibliography

BACKGROUND: Failures of communication during the transfer of patient care errors. METHODS: We created a new format for written sign-out material, based on aviation industry practice and cognitive psychology theory, designed to improve interns' and senior medical students' communication during transfers of patient care responsibility. We carried out a randomized, blinded, crossover trial, comparing a new, narrative, written sign-out report to a usual written sign-out. Thirty-two interns and fourth-year medical students rated their confidence across various clinical tasks and answered clinical questions regarding hypothetical patients presented to them in written, new, narrative sign-out compared with the customary format. RESULTS: There was no statistical difference in confidence when interns and senior medical students received usual versus narrative sign-outs. CONCLUSIONS: Although a limited measure suggested some improvement in competence, the narrative format did not improve participants' self-rated confidence during patient-care transfer.

A series of 2,3-dihydro-1H-pyrrolo[1,2-a]indoles were prepared as analogs of the active intermediates of the natural products, mitomycin C and FR900482, and their reactions with various nucleophiles were studied

The small Ras-related GTP binding and hydrolyzing protein Ran has been implicated in a variety of processes, including cell cycle progression, DNA synthesis, RNA processing, and nuclear-cytosolic trafficking of both RNA and proteins. Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. One such putative effector, Ran-binding protein 1 (RanBP1), interacts selectively with Ran-GTP. Ran proteins contain a diagnostic short, acidic, carboxyl-terminal domain, DEDDDL, which, at least in the case of human Ran, is required for its role in cell cycle regulation. We show here that this domain is required for the interaction between Ran and RanBP1 but not for the interaction between Ran and a Ran guanine nucleotide exchange factor or between Ran and a Ran GTPase activating protein. In addition, Ran lacking this carboxyl-terminal domain functions normally in an in vitro nuclear protein import assay. We also show that RanBP1 interacts with the mammalian homolog of yeast protein RNA1, a protein involved in RNA transport and processing. These results are consistent with the hypothesis that Ran functions directly in at least two pathways, one, dependent on RanBP1, that affects cell cycle progression and RNA export, and another, independent of RanBP1, that affects nuclear protein import