Background: Surgical resection of arteriovenous malformations (AVMs) in eloquent areas is significantly associated with greater surgical morbidity. We describe a functional approach for surgical treatment of these lesions Methods: A total of 20 patients with AVMs in eloquent areas were surgically treated and retrospectively analyzed. Individualized functional approach, using brain mapping and/or neurophysiological monitoring was performed in each case according to every case specific features and location. Seventeen patients underwent surgery under assleep conditions and 3 -patients underwent awake intraoperative mapping Results: There was no mortality. Four patients had hemorrhagic complications (20%). Ten (50%) presented neurological immediate postoperative worsening. Eight of them achieved complete recovery in follow up and 2 showed a permanent deficit. At 6 months follow up all the patients (100%) had good clinical outcome (mRS less than 2). There were no intraoperative seizures but 5 patients (26.3%) developed postoperative seizures. Fifteen patients (75%) had total AVM resection. Language and/or motor function were identified in all but one patient (95%). Each case required changes in surgical strategy to preserve the motor and/or language functions during surgery. Conclusions: Intraoperative monitoring and brain mapping are valuable and safe for the treatment of eloquent AVMs by indentifying and protecting motor and language function during resection.

Proteolytic studies have enabled two of the three putative domains of the fibrinolytic protein streptokinase to be isolated and characterized (Conejero-Lara F et al., 1996, Protein Sci 5:2583–2591). The N-terminal domain, however, could not be isolated in these experiments because of its susceptibility to proteolytic cleavage. To complete the biophysical characterization of the domain structure of streptokinase we have overexpressed, purified, and characterized the N-terminal region of the protein, residues 1–146. The results show this is cooperatively folded with secondary structure content and overall stability closely similar to those of the equivalent region in the intact protein.