3DM: Systematic analysis of heterogeneous superfamily data to discover protein functionalities
- 23 March 2010
- journal article
- research article
- Published by Wiley in Proteins: Structure, Function, and Bioinformatics
- Vol. 78 (9), 2101-2113
- https://doi.org/10.1002/prot.22725
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Structure and Function of 2,3-Dimethylmalate Lyase, a PEP Mutase/Isocitrate Lyase Superfamily MemberJournal of Molecular Biology, 2009
- Correlated mutation analyses on super‐family alignments reveal functionally important residuesProteins, 2009
- Database resources of the National Center for Biotechnology InformationNucleic Acids Research, 2009
- Data Deposition and Annotation at the Worldwide Protein Data BankMolecular Biotechnology, 2008
- The Use of in Vitro Peptide Binding Profiles and in Silico Ligand-Receptor Interaction Profiles to Describe Ligand-Induced Conformations of the Retinoid X Receptor α Ligand-Binding DomainMolecular Endocrinology, 2007
- Induced refolding of a temperature denatured llama heavy‐chain antibody fragment by its antigenProteins, 2005
- Isolation of Llama Antibody Fragments for Prevention of Dandruff by Phage Display in ShampooApplied and Environmental Microbiology, 2005
- The Universal Protein Resource (UniProt)Nucleic Acids Research, 2004
- A Family-based Approach Reveals the Function of Residues in the Nuclear Receptor Ligand-binding DomainJournal of Molecular Biology, 2004
- Collecting and harvesting biological data: the GPCRDB and NucleaRDB information systemsNucleic Acids Research, 2001