Literature DB >> 15788783

Rapid motif-based prediction of circular permutations in multi-domain proteins.

January Weiner1, Geraint Thomas, Erich Bornberg-Bauer.   

Abstract

MOTIVATION: Rearrangements of protein domains and motifs such as swaps and circular permutations (CPs) can produce erroneous results in searching sequence databases when using traditional methods based on linear sequence alignments. Circular permutations are also of biological relevance because they can help to better understand both protein evolution and functionality.
RESULTS: We have developed an algorithm, RASPODOM, which is based on the classical recursive alignment scheme. Sequences are represented as strings of domains taken from precompiled resources of domain (motif) databases such as ProDom. The algorithm works several orders of magnitude faster than a reimplementation of the existing CP detection algorithm working on strings of amino acids, produces virtually no false positives and allows the discrimination of true CPs from 'intermediate' CPs (iCPs). Several true CPs which have not been reported in literature so far could be identified from Swiss-Prot/TrEMBL within minutes.

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Year:  2005        PMID: 15788783     DOI: 10.1093/bioinformatics/bti085

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  11 in total

1.  Detecting evolutionary relationships across existing fold space, using sequence order-independent profile-profile alignments.

Authors:  Lei Xie; Philip E Bourne
Journal:  Proc Natl Acad Sci U S A       Date:  2008-04-02       Impact factor: 11.205

Review 2.  From local structure to a global framework: recognition of protein folds.

Authors:  Agnel Praveen Joseph; Alexandre G de Brevern
Journal:  J R Soc Interface       Date:  2014-04-16       Impact factor: 4.118

3.  Deciphering the preference and predicting the viability of circular permutations in proteins.

Authors:  Wei-Cheng Lo; Tian Dai; Yen-Yi Liu; Li-Fen Wang; Jenn-Kang Hwang; Ping-Chiang Lyu
Journal:  PLoS One       Date:  2012-02-16       Impact factor: 3.240

4.  Circular permutation in proteins.

Authors:  Spencer Bliven; Andreas Prlić
Journal:  PLoS Comput Biol       Date:  2012-03-29       Impact factor: 4.475

5.  CPred: a web server for predicting viable circular permutations in proteins.

Authors:  Wei-Cheng Lo; Li-Fen Wang; Yen-Yi Liu; Tian Dai; Jenn-Kang Hwang; Ping-Chiang Lyu
Journal:  Nucleic Acids Res       Date:  2012-06-11       Impact factor: 16.971

6.  Domain similarity based orthology detection.

Authors:  Tristan Bitard-Feildel; Carsten Kemena; Jenny M Greenwood; Erich Bornberg-Bauer
Journal:  BMC Bioinformatics       Date:  2015-05-13       Impact factor: 3.169

7.  Function-selective domain architecture plasticity potentials in eukaryotic genome evolution.

Authors:  Viktorija Linkeviciute; Owen J L Rackham; Julian Gough; Matt E Oates; Hai Fang
Journal:  Biochimie       Date:  2015-05-15       Impact factor: 4.079

8.  iSARST: an integrated SARST web server for rapid protein structural similarity searches.

Authors:  Wei-Cheng Lo; Che-Yu Lee; Chi-Ching Lee; Ping-Chiang Lyu
Journal:  Nucleic Acids Res       Date:  2009-05-06       Impact factor: 16.971

9.  CPDB: a database of circular permutation in proteins.

Authors:  Wei-Cheng Lo; Chi-Ching Lee; Che-Yu Lee; Ping-Chiang Lyu
Journal:  Nucleic Acids Res       Date:  2008-10-08       Impact factor: 16.971

10.  CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships.

Authors:  Wei-Cheng Lo; Ping-Chiang Lyu
Journal:  Genome Biol       Date:  2008-01-18       Impact factor: 13.583

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