10.1002/anie.200704178
10.1002/anie.200704178 · doi-reference
10.1073/pnas.1111252108
10.1073/pnas.1111252108 · doi-reference
10.1038/nprot.2009.86
10.1038/nprot.2009.86 · doi-reference
10.1093/protein/gzq042
10.1093/protein/gzq042 · doi-reference
10.1093/bioinformatics/btn353
10.1093/bioinformatics/btn353 · doi-reference
CUPSAT: prediction of protein stability upon point mutations
10.1093/nar/gkl190 · doi-reference
Integrated prediction of the effect of mutations on multiple protein characteristics
10.1002/prot.22870 · doi-reference
10.1093/bioinformatics/btr254
10.1093/bioinformatics/btr254 · doi-reference
10.1186/1471-2105-12-151
10.1186/1471-2105-12-151 · doi-reference
10.1093/nar/gkr363
10.1093/nar/gkr363 · doi-reference
MuD: an interactive web server for the prediction of non-neutral substitutions using protein structural data
10.1093/nar/gkq528 · doi-reference
Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site
10.1093/bioinformatics/btr576 · doi-reference
10.1093/bioinformatics/btp370
10.1093/bioinformatics/btp370 · doi-reference
iPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations
10.1093/bioinformatics/btm100 · doi-reference
10.1002/prot.20810
10.1002/prot.20810 · doi-reference
I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure
10.1093/nar/gki375 · doi-reference
10.1093/bioinformatics/btm344
10.1093/bioinformatics/btm344 · doi-reference
10.1371/journal.pcbi.1000002
10.1371/journal.pcbi.1000002 · doi-reference
In the light of directed evolution: pathways of adaptive protein evolution
10.1073/pnas.0901522106 · doi-reference
Ordered conformational change in the protein backbone: prediction of conformationally variable positions from sequence and low-resolution structural data
10.1002/prot.21899 · doi-reference
10.1016/j.str.2008.09.012
10.1016/j.str.2008.09.012 · doi-reference
10.1016/j.str.2005.10.007
10.1016/j.str.2005.10.007 · doi-reference
10.1002/prot.20052
10.1002/prot.20052 · doi-reference
10.1002/prot.22654
10.1002/prot.22654 · doi-reference
10.1021/bi802191b
10.1021/bi802191b · doi-reference
10.1073/pnas.0909150106
10.1073/pnas.0909150106 · doi-reference
10.1038/nchem.1244
10.1038/nchem.1244 · doi-reference
A method for the analysis of domain movements in large biomolecular complexes
10.1002/prot.22339 · doi-reference
Database of ligand-induced domain movements in enzymes
10.1186/1472-6807-9-13 · doi-reference
10.1002/(sici)1097-0134(19980201)30:23.0.co;2-n
10.1002/(sici)1097-0134(19980201)30:2<144::aid-prot4>3.0.co;2-n · doi-reference
HingeProt: automated prediction of hinges in protein structures
10.1002/prot.21613 · doi-reference
10.1093/bioinformatics/btp304
10.1093/bioinformatics/btp304 · doi-reference
WEBnm@: a web application for normal mode analyses of proteins
10.1186/1471-2105-6-52 · doi-reference
ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
10.1093/nar/gkh368 · doi-reference
High-throughput modeling and analysis of protein structural dynamics
10.1093/bib/bbm014 · doi-reference
10.1016/j.theochem.2008.09.024
10.1016/j.theochem.2008.09.024 · doi-reference
10.1016/s0006-3495(01)76033-x
10.1016/s0006-3495(01)76033-x · doi-reference
10.1016/s1359-0278(97)00024-2
10.1016/s1359-0278(97)00024-2 · doi-reference
Coarse-grained (multiscale) simulations in studies of biophysical and chemical systems
10.1146/annurev-physchem-032210-103335 · doi-reference
10.1016/j.sbi.2005.08.007
10.1016/j.sbi.2005.08.007 · doi-reference
