Torsten Schwede - Selected Publications#

Bibliometric Statistics:
h-index: 61 (39 since 2017)
i10-index: 95 (80 since 2017)
Relative Citation Ratio (iCite RCR) Max: 296.40 Mean: 11.43 Median: 1.95

Selected publications:

Arnold, K., Bordoli, L., Kopp, J. and Schwede, T. (2006) ‘The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling’, Bioinformatics, Vol. 22, H. 2, pp. 195–201.

Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T. A. P., Rempfer, C., Bordoli, L., Lepore, R. and Schwede, T. (2018) ‘SWISS-MODEL: homology modelling of protein structures and complexes’, Nucleic acids research, 46(W1), pp. W296-W303.

Pereira, J. and Schwede, T. (2021) ‘Interactomes in the era of deep learning’, Science, 374(6573), 1319–1320.

Kryshtafovych, A., Schwede, T., Topf, M., Fidelis, K. and Moult, J. (2021) ‘Critical assessment of methods of protein structure prediction (CASP)-Round XIV’, Proteins, 89(12), pp. 1607–1617.

Robin, X., Haas, J., Gumienny, R., Smolinski, A., Tauriello, G. and Schwede, T. (2021) ‘Continuous Automated Model Evaluation (CAMEO)-Perspectives on the future of fully automated evaluation of structure prediction methods’, Proteins: Structure, Function, and Bioinformatics , 89(12), pp. 1977–1986.

Studer, G., Rempfer, C., Waterhouse, A. M., Gumienny, R., Haas, J. and Schwede, T. (2019) ‘QMEANDisCo - Distance Constraints Applied on Model Quality Estimation’, Bioinformatics, 36(6), pp. 1765–1771.

Studer, G., Tauriello, G., Bienert, S., Waterhouse, A. M., Bertoni, M., Bordoli, L., Schwede, T. and Lepore, R. (2019) ‘Modeling of Protein Tertiary and Quaternary Structures Based on Evolutionary Information’, Methods in Molecular Biology, 1851, pp. 301–316.

Bertoni, M., Kiefer, F., Biasini, M., Bordoli, L. and Schwede, T. (2017) ‘Modeling protein quaternary structure of homo- and hetero-oligomers beyond binary interactions by homology’, Scientific Reports, 7(1), p. 10480.

Schwede, T. (2013) ‘Protein modeling: what happened to the “protein structure gap”?’, Structure: with folding and design, Vol. 21, H. 9, pp. 1531–1540.

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