Radiographic changes of chronic recurrent multifocal osteomyelitis that persisted into adulthood.

Chronic recurrent multifocal osteomyelitis (CRMO) is a rare non-infectious autoinflammatory disorder typically seen in young women. We describe the case of a young man who presented at 13 years of age with pain in the tibia, humerus, clavicle and hip. Worsening of the condition through clinical presentation and radiographic imaging was observed over 10 years.

Outcomes of anterior cruciate ligament reconstruction in patients older than 50 years of age.

Background: Anterior cruciate ligament reconstruction (ACLR) has traditionally been reserved for young patients with functional instability. As the aging population continues to grow and embrace a more active lifestyle, it is important to determine if favorable outcomes of ACLR can be achieved in older adults.

Methods: Patients greater than 50 years of age undergoing ACLR between January 2001 and September 2006 were identified.

An epidermal inclusion cyst mimicking chronic prepatellar bursitis: a case report.

Soft tissue lesions are common to the prepatellar region, often due to acute or chronic trauma, and most frequently include prepatellar bursitis, lipomas, and ganglion cysts. We report a case of a posttraumatic prepatellar epidermal inclusion cyst to highlight the diagnostic complexities that can arise with soft tissue lesions in this location. On the basis of our case report, treating orthopaedic surgeons should consider the possibility of an epidermal inclusion cyst in patients who present with atypical anterior soft tissue masses with a history of trauma to the anterior knee.

Diversity of Eukaryotic Translational Initiation Factor eIF4E in Protists.

The greatest diversity of eukaryotic species is within the microbial eukaryotes, the protists, with plants and fungi/metazoa representing just two of the estimated seventy five lineages of eukaryotes. Protists are a diverse group characterized by unusual genome features and a wide range of genome sizes from 8.2 Mb in the apicomplexan parasite Babesia bovis to 112,000-220,050 Mb in the dinoflagellate Prorocentrum micans.

Characterization of mammalian eIF4E-family members.

The translational factor eukaryotic initiation factor 4E (eIF4E) is a central component in the initiation and regulation of translation in eukaryotic cells. Through its interaction with the 5' cap structure of mRNA, eIF4E functions to recruit mRNAs to the ribosome. The accumulation of expressed sequence tag sequences has allowed the identification of three different eIF4E-family members in mammals termed eIF4E-1, eIF4E-2 (4EHP, 4E-LP) and eIF4E-3, which differ in their structural signatures, functional characteristics and expression patterns.

Two zebrafish eIF4E family members are differentially expressed and functionally divergent.

Eukaryotic translation initiation factor 4E (eIF4E) is an essential component of the translational machinery that binds m(7)GTP and mediates the recruitment of capped mRNAs by the small ribosomal subunit. Recently, a number of proteins with homology to eIF4E have been reported in plants, invertebrates, and mammals. Together with the prototypical translation factor, these constitute a new family of structurally related proteins.

Characterization of rainbow trout and zebrafish eukaryotic initiation factor 2alpha and its response to endoplasmic reticulum stress and IPNV infection.

The cDNAs of rainbow trout and zebrafish eIF2alpha have been isolated and found to encode proteins of similar molecular weight and isoelectric point to the alpha-subunit of the human translational initiation factor, eIF2. The rainbow trout (36.0kDa) and zebrafish (36.

Yeast "knockout-and-rescue" system for identification of eIF4E-family members possessing eIF4E-activity.

Evidence from several laboratories and sequencing projects has revealed that many eukaryotes contain multiple proteins related in sequence to the human mRNA-cap binding translation initiation factor 4E (eIF4E-1). Although some have been shown to bind cap-analogues, whether all eIF4E-family members function as translation initiation factors is unclear Furthermore, the existence of proteins related to eIF4E complicates the identification of the translation factor by sequence-based approaches. Methods to assess the functionality of eIF4E are limited.