Chin-up-induced bilateral anterior shoulder dislocation: a case report.

BACKGROUND: Simultaneous bilateral shoulder dislocations are extremely rare occurrences. OBJECTIVE: We present an unusual case where the patient suffered simultaneous bilateral anterior shoulder dislocations during chin-up exercises. To our knowledge, this mechanism has not been previously reported. CASE REPORT: A 44-year-old woman presented to the Emergency Department (ED) complaining of bilateral shoulder pain while doing chin-up exercises. She was completing her workout when she developed severe pain to both of her shoulders with associated parasthesias to both hands and the right forearm. The patient was found to have bilateral anterior shoulder dislocations; both were reduced using procedural sedation and traction-countertraction techniques. CONCLUSION: The mechanics of chin-up exercises places the glenohumeral joint in a position of instability, increasing the likelihood of dislocation.

A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site.

We identified UIC-94003, a nonpeptidic human immunodeficiency virus (HIV) protease inhibitor (PI), containing 3(R),3a(S),6a(R)-bis-tetrahydrofuranyl urethane (bis-THF) and a sulfonamide isostere, which is extremely potent against a wide spectrum of HIV (50% inhibitory concentration, 0.0003 to 0.0005 microM). UIC-94003 was also potent against multi-PI-resistant HIV-1 strains isolated from patients who had no response to any existing antiviral regimens after having received a variety of antiviral agents (50% inhibitory concentration, 0.0005 to 0.0055 microM). Upon selection of HIV-1 in the presence of UIC-94003, mutants carrying a novel active-site mutation, A28S, in the presence of L10F, M46I, I50V, A71V, and N88D appeared. Modeling analysis revealed that the close contact of UIC-94003 with the main chains of the protease active-site amino acids (Asp29 and Asp30) differed from that of other PIs and may be important for its potency and wide-spectrum activity against a variety of drug-resistant HIV-1 variants. Thus, introduction of inhibitor interactions with the main chains of key amino acids and seeking a unique inhibitor-enzyme contact profile should provide a framework for developing novel PIs for treating patients harboring multi-PI-resistant HIV-1.