These data suggest that TaTME for rectal cancer is feasible with an acceptable pathological outcome and morbidity profile. Further data on functional and long-term survival outcomes are required.
Parasitic leiomyomas (PL) are rare intra-abdominal tumors usually found in young women and are considered a type of uterine leiomyomas. They are usually reported in women who underwent laparoscopic morcellation of fibroids and frequently present with symptoms such as abdominal pain and distention. Treatment usually involves en bloc removal of the mass after dividing its blood supply from the host organ. In this case report, we describe the case of a middle-aged female who developed high-grade small bowel obstruction due to compression from a large PL with blood supply from the greater omentum. The patient underwent operative resection of the PL and subsequently fared very well. Meticulous attention to blood supply and attachments of PL to host organs is necessary for safe resection.
Finding why protein-protein interactions (PPIs) are so specific can provide a valuable tool in a variety of fields. Statistical surveys of so-called transient complexes (like those relevant for signal transduction mechanisms) have shown a tendency of polar residues to participate in the interaction region. Following this scheme, residues in the unbound partners have to compete between interacting with water or interacting with other residues of the protein. On the other hand, several works have shown that the notion of active site electrostatic preorganization can be used to interpret the high efficiency in enzyme reactions. This preorganization can be related to the instability of the residues important for catalysis. In some enzymes, in addition, conformational changes upon binding to other proteins lead to an increase in the activity of the enzymatic partner. In this article the linear response approximation version of the semimacroscopic protein dipoles Langevin dipoles (PDLD/S-LRA) model is used to evaluate the stability of several residues in two phosphate hydrolysis enzymes upon complexation with their activating partners. In particular, the residues relevant for PPI and for phosphate hydrolysis in the CDK2/Cyclin A and Ras/GAP complexes are analyzed. We find that the evaluation of the stability of residues in these systems can be used to identify not only active site regions but it can also be used as a guide to locate "hot spots" for PPIs. We also show that conformational changes play a major role in positioning interfacing residues in a proper "energetic" orientation, ready to interact with the residues in the partner protein surface. Thus, we extend the preorganization theory to PPIs, extrapolating the results we obtained from the above-mentioned complexes to a more general case. We conclude that the correlation between stability of a residue in the surface and the likelihood that it participates in the interaction can be a general fact for transient PPIs.
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