Results 1 - 10 of 7,105

SCOP: a structural classification of proteins database for the investigation of sequences and structures.

by Tim J P Hubbard , Bart Ailey , Steven E Brenner , Alexey G Murzin , Cyrus Chothia - J. Mol. Biol. , 1995
"... ABSTRACT The Structural Classification of Proteins (SCOP) database provides a detailed and comprehensive description of the relationships of all known proteins structures. The classification is on hierarchical levels: the first two levels, family and superfamily, describe near and far evolutionary ..."
Abstract - Cited by 1552 (24 self) - Add to MetaCart
ABSTRACT The Structural Classification of Proteins (SCOP) database provides a detailed and comprehensive description of the relationships of all known proteins structures. The classification is on hierarchical levels: the first two levels, family and superfamily, describe near and far evolutionary

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

by Jimmy K. Eng, Ashley L. Mccormack, John R. Yates - J. Am. Soc. Mass Spectrom , 1994
"... A method to correlate the uninterpreted tandem mass spectra of peptides produced under low energy (lo-50 eV) collision conditions with amino acid sequences in the Genpept database has been developed. In this method the protein database is searched to identify linear amino acid sequences within a mas ..."
Abstract - Cited by 944 (19 self) - Add to MetaCart
A method to correlate the uninterpreted tandem mass spectra of peptides produced under low energy (lo-50 eV) collision conditions with amino acid sequences in the Genpept database has been developed. In this method the protein database is searched to identify linear amino acid sequences within a

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.

by Stephen F Altschul , Thomas L Madden , Alejandro A Schäffer , Jinghui Zhang , Zheng Zhang , Webb Miller , David J Lipman - Nucleic Acids Res. , 1997
"... ABSTRACT The BLAST programs are widely used tools for searching protein and DNA databases for sequence similarities. For protein comparisons, a variety of definitional, algorithmic and statistical refinements described here permits the execution time of the BLAST programs to be decreased substantia ..."
Abstract - Cited by 8572 (88 self) - Add to MetaCart
ABSTRACT The BLAST programs are widely used tools for searching protein and DNA databases for sequence similarities. For protein comparisons, a variety of definitional, algorithmic and statistical refinements described here permits the execution time of the BLAST programs to be decreased

Pfam protein families database

by Robert D. Finn, John Tate, Jaina Mistry, Penny C. Coggill, Stephen John Sammut, Hans-rudolf Hotz, Goran Ceric, Kristoffer Forslund, Sean R. Eddy, Erik L. L. Sonnhammer, Alex Bateman - Nucleic Acids Research, 2008, 36(Database issue): D281–D288
"... Pfam is a comprehensive collection of protein domains and families, represented as multiple sequence alignments and as profile hidden Markov models. The current release of Pfam (22.0) contains 9318 protein families. Pfam is now based not only on the UniProtKB sequence database, but also on NCBI GenP ..."
Abstract - Cited by 771 (13 self) - Add to MetaCart
Pfam is a comprehensive collection of protein domains and families, represented as multiple sequence alignments and as profile hidden Markov models. The current release of Pfam (22.0) contains 9318 protein families. Pfam is now based not only on the UniProtKB sequence database, but also on NCBI Gen

The Pfam protein families database

by Alex Bateman, Lachlan Coin, Richard Durbin, Robert D. Finn, Volker Hollich, Ajay Khanna, Mhairi Marshall, Simon Moxon, Erik L. L. Sonnhammer, David J. Studholme, Corin Yeats, Sean R. Eddy - Nucleic Acids Res , 2002
"... Pfam is a large collection of protein families and domains. Over the past 2 years the number of families in Pfam has doubled and now stands at 6190 (version 10.0). Methodology improvements for searching the Pfam collection locally as well as via the web are described. Other recent innovations includ ..."
Abstract - Cited by 1070 (39 self) - Add to MetaCart
Pfam is a large collection of protein families and domains. Over the past 2 years the number of families in Pfam has doubled and now stands at 6190 (version 10.0). Methodology improvements for searching the Pfam collection locally as well as via the web are described. Other recent innovations

The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000

by Amos Bairoch, Rolf Apweiler - Nucleic Acids Res , 2000
"... SWISS-PROT is a curated protein sequence database which strives to provide a high level of annotation (such as the description of the function of a protein, its domains structure, post-translational modifications, variants, etc.), a minimal level of redundancy and high level of integration with othe ..."
Abstract - Cited by 773 (21 self) - Add to MetaCart
SWISS-PROT is a curated protein sequence database which strives to provide a high level of annotation (such as the description of the function of a protein, its domains structure, post-translational modifications, variants, etc.), a minimal level of redundancy and high level of integration

NCBI reference sequence (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins

by Kim D. Pruitt, Tatiana Tatusova, Donna R. Maglott - NUCLEIC ACIDS RES , 2005
"... ..."
Abstract - Cited by 605 (6 self) - Add to MetaCart
Abstract not found

The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999

by Amos Bairoch, Rolf Apweiler - Nucleic Acids Res , 1999
"... SWISS-PROT is a curated protein sequence database which strives to provide a high level of annotation (such as the description of the function of a protein, its domain structure, post-translational modifications, variants, etc.), a minimal level of redundancy and high level of integration with other ..."
Abstract - Cited by 624 (5 self) - Add to MetaCart
SWISS-PROT is a curated protein sequence database which strives to provide a high level of annotation (such as the description of the function of a protein, its domain structure, post-translational modifications, variants, etc.), a minimal level of redundancy and high level of integration

Hidden Markov models in computational biology: applications to protein modeling

by Anders Krogh, Michael Brown, I. Saira Mian, Kimmen Sjölander, David Haussler - JOURNAL OF MOLECULAR BIOLOGY , 1994
"... Hidden.Markov Models (HMMs) are applied t.0 the problems of statistical modeling, database searching and multiple sequence alignment of protein families and protein domains. These methods are demonstrated the on globin family, the protein kinase catalytic domain, and the EF-hand calcium binding moti ..."
Abstract - Cited by 655 (39 self) - Add to MetaCart
Hidden.Markov Models (HMMs) are applied t.0 the problems of statistical modeling, database searching and multiple sequence alignment of protein families and protein domains. These methods are demonstrated the on globin family, the protein kinase catalytic domain, and the EF-hand calcium binding

Arabidopsis nucleolar protein database (AtNoPDB

by John W. S. Brown, Peter J. Shaw, Paul Shaw, David F. Marshall - Nucleic Acids Res , 2005
"... The Arabidopsis Nucleolar Protein Database ..."
Abstract - Cited by 8 (0 self) - Add to MetaCart
The Arabidopsis Nucleolar Protein Database
Results 1 - 10 of 7,105