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At least 325 records · Page 18Linked to original sources
PubMed1997

Special considerations in the athletic throwing shoulder.

Overhead athletes are susceptible to a number of shoulder problems due to the repetitive nature and force needed to perform at a competitive level. Frequently, the rotator cuff becomes injured due to primary or secondary impingement. In young athletes, subtle instability is often the cause of rotator cuff tendinitis, but will frequently respond to a coordinated rehabilitation program. Older athletes are more likely to have rotator cuff injuries due to anatomic changes in the coracoacromial arch. This article outlines the mechanism of injury to the rotator cuff and our approach in dealing with shoulder problems in the overhead athlete.

Biomechanical Phenomena↗
PubMed1998

The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2.

The three-dimensional structures of the class II anticoagulant phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5 from the, Australian tiger snake, Notechis scutatus scutatus, were determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are monomeric and consist of 121 and 119 residues, respectively. A comparison of ten class I/II PLA2 structures showed, among other differences, that the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less twisted in class I than in class II PLA2s. This, along with the insertion of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the anticoagulant and (presynaptic) neurotoxic properties between the two classes of PLA2. It seems apparent from sequence and structural comparisons that the toxic site of PLA2 responsible for the strong anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free for intermolecular interactions. These lysines differ between the two classes of PLA2.

Amino Acid Sequence↗
PubMed2003

PNA and LNA throw light on DNA.

In some aspects, homogeneous (all-in-solution) nucleic acid hybridization assays are superior to the traditionally used heterogeneous (solution-to-surface) alternatives. Profluorescent probes, which reveal fluorescence enhancement or fluorescence polarization upon their binding to DNA and RNA targets, are a paradigm for the real-time sequence-specific homogeneous detection of nucleic acids. A variety of such DNA or RNA-derived probes of different constructs has already been developed with numerous applications. However, the recent additions to the field - locked nucleic acids (LNAs) and peptide nucleic acids (PNAs) - significantly increase the potential of profluorescent probes and provide a robust impulse for their new uses.

Base Pair Mismatch↗
PubMed2002

Thermal capsular shrinkage in the throwing athlete.

The role of thermal capsular shrinkage in treating various forms of pathology continues to evolve. The addition of thermal capsular shrinkage to the treatment regimen of standard pathologies in the thrower's shoulder has increased the rate of return to play even at the highest levels. Our data indicate an approximate 20% improvement in the rate of return to play with the addition of thermal capsular shrinkage to traditional treatments. These data represent relatively short-term follow-up. Longer duration of follow-up and increased numbers of patients will further enable us to make recommendations regarding the future use of this technology. As our understanding of the pathology that occurs in the thrower's shoulder continues to improve, so too will our understanding of the effect of applying thermal energy to the joint capsule.

Arthroscopy↗
PubMed1997

Throw that epidemiologist out of the emergency room! Using the television series ER as a vehicle for teaching methodologists about medical issues.

BACKGROUND: Epidemiology and biostatistics graduate students have diverse backgrounds, but many have little prior training in medicine or biology. This lack of content knowledge in future health researchers has recently been raised as a concern. METHODS: As part of a graduate course on the epidemiology of major diseases, the television series ER was used as a vehicle for learning more about diseases in general, and to become familiar with medical terminology and the ICD-10 by practicing coding on the patients seen. Furthermore, we wanted to provide human faces to the type of disease data students usually work with. RESULTS: In this article, the authors discuss how the ER sessions were organized and the problems that were encountered. The course evaluation concluded that the students found the exercise to be an interesting break from regular teaching.

Adult↗
PubMed1999

Throwing the switch in bacterial chemotaxis.

In Escherichia coli chemotaxis, the switch from counterclockwise to clockwise rotation of the flagella occurs as a result of binding of the phosphorylated CheY protein to the base of the flagellum. Analysis of CheY variants has provided a picture of the surface of CheY that undergoes conformational shifts, as a result of phosphorylation, to interact directly with the flagellum. Whether phospho-CheY binding and flagellar switching are sequential steps or can occur in a concerted fashion has yet to be determined.

Bacterial Proteins↗
PubMed1996

Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.

BACKGROUND: Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin, emitting yellow-green light. The reaction proceeds through activation of the substrate to form an adenylate intermediate. Firefly luciferase shows extensive sequence homology with a number of enzymes that utilize ATP in adenylation reactions. RESULTS: We have determined the crystal structure of firefly luciferase at 2.0 A resolution. The protein is folded into two compact domains. The large N-terminal domain consists of a beta-barrel and two beta-sheets. The sheets are flanked by alpha-helices to form an alphabetaalphabetaalpha five-layered structure. The C-terminal portion of the molecule forms a distinct domain, which is separated from the N-terminal domain by a wide cleft. CONCLUSIONS: Firefly luciferase is the first member of a superfamily of homologous enzymes, which includes acyl-coenzyme A ligases and peptide synthetases, to have its structure characterized. The residues conserved within the superfamily are located on the surfaces of the two domains on either side of the cleft, but are too far apart to interact simultaneously with the substrates. This suggests that the two domains will close in the course of the reaction. Firefly luciferase has a novel structural framework for catalyzing adenylate-forming reactions.

Adenosine↗