Publications by authors named "Safet Hatic"

Background: Approximately 1 in 4 adults will develop hallux valgus (HV). Up to 80% of adult Internet users reference online sources for health-related information. Overall, with the high prevalence of HV combined with the numerous treatment options, we believe patients are likely turning to Internet search engines for questions relevant to HV.

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Although discussed as an alternative to triple arthrodesis for hindfoot correction, the published data surrounding the medial double arthrodesis, or fusion of the subtalar and talonavicular joints, has not addressed the proximity of the anatomic structures at risk. A total of 10 cadaver specimens were used to examine the risk of damage to the neurovascular and tendinous structures of the posterior medial hindfoot when performing the medial double arthrodesis. The distance of the reviewed structures was measured in relation to the standardized point of the middle facet of the calcaneus (mean ± standard deviation and range).

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The plantar plate of the first metatarsophalangeal (MP) joint is a critical structure of the forefoot that has been identified as a major stabilizer within the capsuloligamentous complex. Many studies have clarified and documented the anatomy of the lesser toe MP plantar plates, but few have looked closely at the anatomy of the first MP joint. Ten cadaveric specimens were examined to identify and document the objective anatomic relationship of the plantar plate, tibial sesamoid, and surrounding osseus structures.

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Recurrent deformity in the adult flatfoot following previous tendon transfer represents a challenging treatment dilemma for even the most experienced foot and ankle surgeon. The evaluation must be comprehensive, resulting in a clear understanding of the extent to which previous surgical procedures either failed to address the deformity initially or led to progressive recurrence. Particularly in younger, more high-demand patients, every effort to preserve normal joint mechanics while alleviating pain and restoring functional alignment must be made.

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Yersinia enterocolitica produces a virulence-associated phospholipase A(2) (YplA) that is secreted via its flagellar type-III secretion apparatus. When the N-terminal 59 amino acids of YplA are removed (giving YplA(S)), it retains phospholipase activity; however, it is altered with respect to the apparent kinetics of hydrolysis using fluorescent phospholipid substrates in micellar form. To explore the physical properties of YplA more carefully, Langmuir phospholipid monolayers were used to study the association of YplA with biological membranes.

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The virulence-associated phospholipase of Yersinia enterocolitica (YplA), which is secreted by a flagellar type III secretion system, was cloned and purified for structure-function analysis using a His(6)-tag expression system. Two versions of YplA have been proposed on the basis of two potential initiating methionine residues. The longer derivative possesses 59 additional amino acids at its N-terminus and appears to represent the native form of YplA; however, the shorter recombinant protein possesses enhanced activity in vitro.

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