Further study in larger sample size is required.”
“Introduction: Iatrogenic injury to the spleen is not an uncommon complication. Left nephrectomy has been reported as the second commonest

cause of Compound C price iatrogenic splenectomy with a reported incidence between 1.3 and 24%. Iatrogenic splenectomy is associated with significant morbidity and mortality. Aims: We reviewed the occurrence of iatrogenic splenectomy during left nephrectomy at our centre. Our aims were to determine the incidence of iatrogenic splenectomy within the Mid Yorkshire Hospitals NHS Trust in order to understand the nature of the splenic injury and the morbidity and mortality associated with it. Methods: All splenectomy and nephrectomy histology reports from January 2000 to December 2007 were reviewed retrospectively. Indications for splenectomy and nephrectomy were identified. Patients’ demographic data, tumour characteristics, operative details, length of hospital stay and any reported morbidity or mortality were collected. Results: A total of 447 nephrectomies were identified which included 234 left nephrectomies. Within the same period 136 cases of splenectomy were performed. Thirty-four cases

were iatrogenic this website splenectomies and 12 were caused by left nephrectomy. The incidence was 5.13%. The male to female ratio was 1: 1 with an average age of 66 years. Grade 2 and stage pT2 renal cancer were the commonest tumour characteristics. All iatrogenic injuries occurred LDK378 during mobilisation of the colon or division of adhesion. The average operative time was 4.7 h. Average length of hospital stay was 14 days. Five patients had postoperative complications and 1 died of respiratory failure and sepsis. Conclusion: Splenic injury

during left nephrectomy is a morbid complication. A good understanding of anatomy and surgical approach may reduce the incidence, morbidity and mortality of iatrogenic splenectomy during left nephrectomy. Copyright (C) 2011 S. Karger AG, Basel”
“Natural proteins often partake in several highly specific protein-protein interactions. They are thus subject to multiple opposing forces during evolutionary selection. To be functional, such multispecific proteins need to be stable in complex with each interaction partner, and, at the same time, to maintain affinity toward all partners. How is this multispecificity acquired through natural evolution? To answer this compelling question, we study a prototypical multispecific protein, calmodulin (CaM), which has evolved to interact with hundreds of target proteins. Starting from high-resolution structures of sixteen CaM-target complexes, we employ state-of-the-art computational methods to predict a hundred CaM sequences best suited for interaction with each individual CaM target.