Understanding protein structure: using scop for fold interpretation.
By Steven E. Brenner, Cyrus Chothia, Tim J. P. Hubbard, Alexey G. Murzin. 1996
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- John-Marc Chandonia
- Naomi Fox
- Antonina Andreeva
- Steven E. Brenner
- Tristan Bepler
- Bonnie Berger
- Ben M. Webb
- Cyrus Chothia
Citations in the corpus
- 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.”
- SCOP database in 2004: refinements integrate structure and sequence family data (2004, background): “The protein domains are classi®ed hierarchically into families, superfamilies, folds and classes, whose meaning has been discussed before (1,2).”
- Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores. (2000, unknown): “The basic unit of comparison: a pair of protein domains The protein domains that we studied were classi-fied by SCOP, a Structural Classification of Proteins (Murzin et al .”
- SCOP database in 2002: refinements accommodate structural genomics (2002, methodology): “Protein domains in SCOP are grouped according to species and hierarchically classified into families, superfamilies, folds and classes, whose meaning is described in the original articles (1,2).”
- SCOPe: Manual Curation and Artifact Removal in the Structural Classification of Proteins – extended Database (2016, methodology): “06, we curated structures from the 126 largest Pfam families not classified in SCOP, using the same principles previously employed by the SCOP curator to identify domains and classify them in the hierarchy [24].”