Iterated profile searches with PSI-BLAST--a tool for discovery in protein databases.
By Stephen F. Altschul, Eugene V. Koonin. 1998
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The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Sheng Wang
- Jinbo Xu
- Yang Zhang
- David T. Jones
- Daniel W. A. Buchan
- Liam J. McGuffin
- Han Zhang
- Yoshua Bengio
Citations in the corpus
- Biological structure and function emerge from scaling unsupervised learning to 250 million protein sequences (2019, background): “To do well at this prediction task, the learned representations must encode the underlying factors that influence sequence variation in the data.”
- A simple and fast secondary structure prediction method using hidden neural networks (2005, methodology): “All involved secondary structure prediction methods were tested on the same PSI-BLAST results to make the comparison as unbiased as possible.”
- Evolution of proteins and proteomes: a phylogenetics approach (2005, methodology): “The sensitivity of such homology searches has been more than doubled (Park, et al 1998) by profi le-based methods such as PSI-BLAST (Altschul and Koonin 1998, Altschul, et al 1997) or hidden markov models (Baldi, et al 1994, Eddy 1998).”
- Predicting protein contact map using evolutionary and physical constraints by integer programming (2013, methodology): “…using the following input features: EPAD (a context-specific distance-based statistical potential) (Zhao and Xu, 2012), PSIBLAST sequence profile (Altschul and Koonin, 1998), secondary structure predicted by PSIPRED (Jones, 1999), pairwise contact score and contrastive MI (CMI) derived from…”
- Ortholog identification in the presence of domain architecture rearrangement (2011, background): “Each functional or structural domain can then be used as a starting point to identify homologs in sequence databases such as UniProt [62] using BLAST, PSI-BLAST [63] or related tools.”
- CPHmodels-3.0—remote homology modeling using structure-guided sequence profiles (2010, methodology): “This includes a PsiBlast search against a reduced non-redundant protein sequence database (nr), profile-profile alignment including predicted local structure information obtained from NetSurfP (7), and a double-sided Z -score evaluation.”
- Prediction of the human membrane proteome (2010, methodology): “Sequence profiles were assembled for each query sequence with the position specific iterative basic local alignment search tool [29] using the complete UniProtKB/ Swiss-Prot [30] sequence set (release 14.8) as database and allowing a maximum of two iterations with an e -value cut-off of 1e (cid:2) 5.”
- Application of protein structure alignments to iterated hidden Markov model protocols for structure prediction (2006, methodology): “Casbon and Saqi tested a profile-to-pro-file approach relying on a hybrid PSI-BLAST/HMM protocol [26].”
- Bioinformatics Original Paper Integrating Multi-attribute Similarity Networks for Robust Representation of the Protein Space (unknown): “For sequence based components of the similarity network, we choose two widely used sequence comparison methods, PSI-Blast (Altschul and Koonin, 1998), and HMMer (Eddy, 1998) on the SUPERFAMILY database (Gough, 2002) (HMMer is referred to as HMM throughout the paper).”
- Saccharomyces Genome Database (SGD) provides tools to identify and analyze sequences from Saccharomyces cerevisiae and related sequences from other organisms (2004, methodology): “Each protein sequence in SGD is used as a query for the PSI-BLAST (Position-Specific Iterated BLAST) program ( 4 ) against the most recent version of the nonredundant (nr) protein sequence data set (5) at NCBI (6).”
- Scalable web services for the PSIPRED Protein Analysis Workbench (2013, methodology): “For each method, a list of the best scoring PDB chains is compiled, and a homology model is built for each. pGenTHREADER and HHSearch natively output models, whereas MODELLER (14) is used to build models against the PSIBLAST results.”
- The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data (2004, methodology): “The sequence of each enzyme which has been manually annotated was taken from the PDB sequences repository held at EBI (pdb_aa.fasta, available from the MSD group FTP site at ftp://ftp.ebi.ac.uk/pub/databases/msd/) and subjected to PSI-BLAST (6) analysis (using a cut-off of <0.0005 for inclusion in t”