Detecting local structural similarity in proteins by maximizing number of equivalent residues
By Daron M. Standley, Hiroyuki Toh, Haruki Nakamura. 2004
27 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Kazutaka Katoh
- Daron M. Standley
- John Rozewicki
- Karlou Mar Amada
- Songling Li
- Akira R. Kinjo
- Haruki Nakamura
- Torsten Schwede
In Molecular Biology
- Daron M. Standley
- Kazutaka Katoh
- John Rozewicki
- Karlou Mar Amada
- Songling Li
- Akira R. Kinjo
- Haruki Nakamura
- B. Faircloth
Citations in the corpus
- MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability (2013, methodology): “The residue-level equivalences, which form the basis of all ASH alignments, provide a convenient route for combining MAFFT and ASH.”
- Advances and pitfalls of protein structural alignment. (2009, unknown): “i1⁄41 e ðdi=4Þ 2 Differentiable GASH [58], RASH [66]”
- Protein Data Bank Japan (PDBj): maintaining a structural data archive and resource description framework format (2011, background): “org/ash (23,29,30) MAFTTash Integrated multiple sequence/structure alignment pdbj.”
- MAFFT-DASH: integrated protein sequence and structural alignment (2019, methodology): “For benchmark sets which included structure files (Mattbench, HomFam) two additional scores were calculated, iRMSD (29) and Aligned Number of Equivalent Residues (NER) (30). iRMSD is a measurement developed to evaluate the quality of MSAs when structures are known.”