SCOP: a structural classification of proteins database for the investigation of sequences and structures.
By Alexey G. Murzin, Steven E. Brenner, Tim J. P. Hubbard, Cyrus Chothia. 1995
Subfields: Evaluation & Benchmarks, Computational Biology & Bioinformatics
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In Evaluation & Benchmarks
- Johannes Söding
- Liisa Holm
- Nick V. Grishin
- Kuo-Chen Chou
- Pierre Baldi
- Björn Wallner
- Yang Zhang
- Julian Gough
In Computational Biology & Bioinformatics
- Yang Zhang
- Jinbo Xu
- Sheng Wang
- David T. Jones
- Johannes Söding
- Burkhard Rost
- Arne Elofsson
- Björn Wallner
Citations in the corpus
- ECOD: An Evolutionary Classification of Protein Domains (2014, background): “Currently, the two leading structure classifications are SCOP (Structural Classification of Proteins) [4] and CATH (Class, Architecture, Topology, Homology) [5], both of which are widely used in analyzing protein sequence, structure, function, and evolution and in developing various bioinformatics t”
- Improvement of molecular-replacement models with Sculptor (2011, methodology): “A preliminary study suite containing four target structures was selected from the benchmark suite (one from each SCOP class) and used to explore the effect of algorithm parameters Acta Cryst.”
- Learning protein sequence embeddings using information from structure (2019, background): “Methods for finding proteins with related structure directly from sequence are of considerable interest, but the problem is challenging, because sequence similarity and structural similarity are only loosely related [1, 2, 3, 4], e.”
- DeepSF: deep convolutional neural network for mapping protein sequences to folds (2017, methodology): “The protein sequences for each SCOP domain were cleaned according to the observed residues in the atomic structures [2].”
- MRFalign: Protein Homology Detection through Alignment of Markov Random Fields (2014, methodology): “In total we use a set of 1400 protein pairs as the training and validation data, which covers 458 SCOP folds [30].”
- SCOPe: Structural Classification of Proteins—extended, integrating SCOP and ASTRAL data and classification of new structures (2013, methodology): “The SCOP database was first released in December 1994 and contained all 3091 entries in the PDB at that time (1).”
- TM-align: a protein structure alignment algorithm based on the TM-score (2005, positive): “For example, many authors use SCOP (1) or CATH (2) as the gold standard and assess the structural alignments based on the fold classi-fications in these databases (23–25).”
- The Pfam protein families database (2007, methodology): “The domain boundaries used are currently those defined by the SCOP database (6) and a new web-based tool allows direct cross-linking from domains on the SCOP web site to the corresponding Pfam families.”
- The Pfam protein families database (2011, methodology): “The domain boundaries used are currently those defined by the SCOP database ( 6 ) and a new web-based tool allows direct cross-linking from domains on the SCOP web site to the corresponding Pfam families.”
- MMseqs2: sensitive protein sequence searching for the analysis of massive data sets (2017, background): “tural domains [19] with 25% maximal pairwise sequence identity.”
- The HHpred interactive server for protein homology detection and structure prediction (2005, background): “The N-terminal domain has two significant hits in SCOP at rank 1 and 3.”
- Continuous Distributed Representation of Biological Sequences for Deep Proteomics and Genomics (2015, neutral): “In another study, researchers used motifs from protein interactions for detecting Structural Classification of Proteins (SCOP) [19] families for 368 proteins, and obtained a classification accuracy of 75% at sensitivity of 10% [20].”
- Data growth and its impact on the SCOP database: new developments (2007, neutral): “The Structural Classification of Proteins (SCOP) is a database of known structural and evolutionary relationships amongst proteins of known structure (1).”
- P2Rank: machine learning based tool for rapid and accurate prediction of ligand binding sites from protein structure (2018, background): “A non-redundant dataset designed in a way so that every SCOP family [77] has at most one typical representative and to minimize the number of unannotated binding sites (by superimposing ligands from very close homologs).”
- Template-based protein structure modeling using the RaptorX web server (2012, background): “Current methods do, however, become unreliable when there are no homologs with solved structures in PDB or when templates under consideration are distant homologs 16 .”