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Paper Details

Characterizing and explaining the impact of disease-associated mutations in proteins without known structures or structural homologs.
Brief Bioinform
14
2022
CATH families, Pfam families, functional sites, human
Author NameAffiliation
Neeladri SenInstitute of Structural and Molecular Biology, University College London
Ivan AnishchenkoUniversity of Washington
Ivan AnishchenkoInstitute for Protein Design, University of Washington
Ivan AnishchenkoUniversity of Washington
Ivan AnishchenkoInstitute for Protein Design, University of Washington
Ian SillitoeInstitute of Structural and Molecular Biology, University College London
Ian SillitoeInstitute of Structural and Molecular Biology, University College London
Sameer VelankarEuropean Bioinformatics Institute (EMBL-EBI)
Sameer VelankarEuropean Bioinformatics Institute (EMBL-EBI)
David BakerUniversity of Washington
David BakerHoward Hughes Medical Institute, University of Washington
David BakerInstitute for Protein Design, University of Washington
David BakerUniversity of Washington
David BakerInstitute for Protein Design, University of Washington
David BakerHoward Hughes Medical Institute, University of Washington
Christine OrengoInstitute of Structural and Molecular Biology, University College London
Christine OrengoInstitute of Structural and Molecular Biology, University College London
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Datasets

Dataset
Description
Source Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
Release 1.2