The SWISS-MODEL Repository: new features and functionalities

The SWISS-MODEL Repository is a database of annotated 3D protein structure models generated by the SWISS-MODEL homology-modelling pipeline. As of September 2005, the repository contained 675 000 models for 604 000 different protein sequences of the UniProt database. Regular updates ensure that the content of the repository reflects the current state of sequence and structure databases, integrating new or modified target sequences, and making use of new template structures. Each Repository entry consists of one or more 3D models accompanied by detailed information about the target protein and the model building process: functional annotation, a detailed template selection log, target-template alignment, summary of the model building and model quality assessment. The SWISS-MODEL Repository is freely accessible at http://swissmodel.expasy.org/repositor

The SWISS‐MODEL Repository of annotated three‐dimensional protein structure homology models

The SWISS‐MODEL Repository is a database of annotated three‐dimensional comparative protein structure models generated by the fully automated homology‐modelling pipeline SWISS‐MODEL. The Repository currently contains about 300 000 three‐dimensional models for sequences from the Swiss‐Prot and TrEMBL databases. The content of the Repository is updated on a regular basis incorporating new sequences, taking advantage of new template structures becoming available and reflecting improvements in the underlying modelling algorithms. Each entry consists of one or more three‐dimensional protein models, the superposed template structures, the alignments on which the models are based, a summary of the modelling process and a force field based quality assessment. The SWISS‐MODEL Repository can be queried via an interactive website at http://swissmodel.expasy. org/repository/. Annotation and cross‐linking of the models with other databases, e.g. Swiss‐Prot on the ExPASy server, allow for seamless navigation between protein sequence and structure information. The aim of the SWISS‐MODEL Repository is to provide access to an up‐to‐date collection of annotated three‐dimensional protein models generated by automated homology modelling, bridging the gap between sequence and structure database

On the theory of social innovations: Tarde's neglected contribution to the development of a sociological innovation theory

The term 'social innovation' is currently becoming increasingly significant in social and political discourse. However, so far there is still no theoretically grounded, practicable concept of social innovation. Through recourse to the social theory of Gabriel Tarde, with its focus on social inventions and social practices of imitation, social innovation can be identified as a specific mechanism of change, and hence the analytical perspective can be directed towards society as a locus of innovation. This provides valuable input for an integrative theory of innovation, and for the analysis and shaping of social transformation processes

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Motivation: Homology models of proteins are of great interest for planning and analysing biological experiments when no experimental three-dimensional structures are available. Building homology models requires specialized programs and up-to-date sequence and structural databases. Integrating all required tools, programs and databases into a single web-based workspace facilitates access to homology modelling from a computer with web connection without the need of downloading and installing large program packages and databases. Results: SWISS-MODEL workspace is a web-based integrated service dedicated to protein structure homology modelling. It assists and guides the user in building protein homology models at different levels of complexity. A personal working environment is provided for each user where several modelling projects can be carried out in parallel. Protein sequence and structure databases necessary for modelling are accessible from the workspace and are updated in regular intervals. Tools for template selection, model building and structure quality evaluation can be invoked from within the workspace. Workflow and usage of the workspace are illustrated by modelling human Cyclin A1 and human Transmembrane Protease 3. Availability: The SWISS-MODEL workspace can be accessed freely at Contact: [email protected] Supplementary information: Supplementary data are available at Bioinformatics onlin

SWISS-MODEL: an automated protein homology-modeling server

SWISS-MODEL (http://swissmodel.expasy.org) is a server for automated comparative modeling of three-dimensional (3D) protein structures. It pioneered the field of automated modeling starting in 1993 and is the most widely-used free web-based automated modeling facility today. In 2002 the server computed 120 000 user requests for 3D protein models. SWISS-MODEL provides several levels of user interaction through its World Wide Web interface: in the ‘first approach mode' only an amino acid sequence of a protein is submitted to build a 3D model. Template selection, alignment and model building are done completely automated by the server. In the ‘alignment mode', the modeling process is based on a user-defined target-template alignment. Complex modeling tasks can be handled with the ‘project mode' using DeepView (Swiss-PdbViewer), an integrated sequence-to-structure workbench. All models are sent back via email with a detailed modeling report. WhatCheck analyses and ANOLEA evaluations are provided optionally. The reliability of SWISS-MODEL is continuously evaluated in the EVA-CM project. The SWISS-MODEL server is under constant development to improve the successful implementation of expert knowledge into an easy-to-use serve

Neue Perspektiven betrieblicher Personalentwicklung

Wie können Fachkräfte in der globalisierten Wirtschaft kontinuierlich und vor allem effizient (weiter-)qualifiziert werden? Die Autoren gehen dieser Frage nach und stellen Leitlinien für eine betriebsnahe Weiterbildung vor, welche die Mitarbeiterpotentiale in den Unternehmen besser entwickeln und nutzen hilft. (IAB2

The versatility of the free osteocutaneous fibula flap in the reconstruction of extremities after sarcoma resection

BACKGROUND: An understanding of the biology of bone and soft-tissue sarcomas, knowledge of adjuvant therapies and refinement in techniques of reconstructive surgery have allowed limb-sparing and limb salvage surgery to become a reality in the management of malignant tumors of the extremities. Functional limb salvage following radical resection has become a possibility in many resectable tumors by the use of alloplastic prostheses, homograft or autogenous bone for skeletal reconstitution combined with vascularized soft tissue coverage. Although the free fibula flap has been well described for reconstructions of the mandible and oral cavity, it has not been widely presented as an ideal tool to preserve extremities and to circumvent amputation. PATIENTS AND METHODS: We describe the complex surgical reconstruction in four patients with primary sarcomas of the extremities. The sarcomas (Ewing's sarcoma, osteosarcoma and epitheloid sarcoma) were resected radically and the massive bone and soft tissue defect was replaced by vascularized free fibula transfer. RESULTS: We present our experience with versatility of this osteocutaneous flap to allow reconstruction and salvage of extremitity sarcomas. There were no operative or postoperative complication and all the four patients had good limb function. The flap was found to be versatile as it could be used for either upper limb or lower limb and for large defects. The results were better in upper limb than in lower limb. CONCLUSIONS: Free fibular graft was found to be effective for salvaging limb function where a massive bone defect resulted from wide tumor resection in the extremities

Von der Suche nach Rationalität zur Arbeit an Dilemmata und Paradoxen. Ansätze für eine Organisationsberatung in widersprüchlichen Kontexten

Kühl S. Von der Suche nach Rationalität zur Arbeit an Dilemmata und Paradoxen. Ansätze für eine Organisationsberatung in widersprüchlichen Kontexten. In: Howaldt J, Kopp R, eds. Sozialwissenschaftliche Organisationsberatung. Auf der Suche nach einem spezifischen Beratungsverständnis. Berlin: Edition Sigma; 1998: 303-322