Background: Geometry is fundamental in the comprehension of local flap design. The purpose of this study was to discuss the differences between the V-Y advancement flap and other local flaps, understand its geometry, and analyze its clinical applications.
Methods: The analysis was based on qualitative measurements of an injury, taking into consideration the following dimensions: largest diameter, shortest diameter, and depth. Standardization of the flap design consisted of directing its advancement over the shortest diameter and making the V base match the size of the largest diameter. The flap was analyzed in two planes: the horizontal plane includes the V-Y design and the vertical plane includes the flap pedicle. The height of the flap can be obtained by simple trigonometry, taking into consideration the largest diameter and alpha angle in the horizontal plane. In the vertical plane, where the pedicle and pivot plane are positioned, for known shortest diameter and depth, the final depth of the pivot plane can be calculated using Pythagoras' principles.
Results: This analysis was applied to 25 patients with adequate skin coverage at follow-up. A correction factor was added to reduce the overdeepening of the vertical plane calculations. The final concepts for clinical application in the classic deep pedicle V-Y flap design are to calculate the length of the V by modifying the alpha angle and to move the pivot plane deeper to accomplish optimal flap movement.
Conclusions: Using these principles, tension-free closure of the Y and appropriate advancement of the flap are obtained.
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http://dx.doi.org/10.1097/01.prs.0000160693.82527.d4 | DOI Listing |
Alzheimers Dement
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Stem Cells and Regenerative Medicine Laboratory, Li Ka Shing Institute of Health Sciences, The Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, PR China.
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View Article and Find Full Text PDFACS Infect Dis
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Department of Chemistry, Brandeis University, Waltham, Massachusetts 02454, United States.
Inosine 5'-monophosphate dehydrogenase (IMPDH) is a promising antibiotic target. This enzyme catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is the rate-limiting step in guanine nucleotide biosynthesis. Bacterial IMPDH-specific inhibitors have been developed that bind to the NAD site.
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