Literature DB >> 18428766

Using Dali for structural comparison of proteins.

Liisa Holm1, Sakari Kääriäinen, Chris Wilton, Dariusz Plewczynski.   

Abstract

The Dali program is widely used for carrying out automatic comparisons of protein structures determined by X-ray crystallography or NMR. The most familiar version is the Dali server, which performs a database search comparing a query structure supplied by the user against the database of known structures (PDB) and returns the list of structural neighbors by e-mail. The more recently introduced DaliLite server compares two structures against each other and visualizes the result interactively. The Dali database is a structural classification based on precomputed all-against-all structural similarities within the PDB. The resulting hierarchical classification can be browsed on the Web and is linked to protein sequence classification resources. All Dali resources use an identical algorithm for structure comparison. Users may run Dali using the Web, or the program may be downloaded to be run locally on Linux computers.

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Year:  2006        PMID: 18428766     DOI: 10.1002/0471250953.bi0505s14

Source DB:  PubMed          Journal:  Curr Protoc Bioinformatics        ISSN: 1934-3396


  69 in total

1.  Novel role of 4-hydroxy-2-nonenal in AIFm2-mediated mitochondrial stress signaling.

Authors:  Sumitra Miriyala; Chadinee Thippakorn; Luksana Chaiswing; Yong Xu; Teresa Noel; Artak Tovmasyan; Ines Batinic-Haberle; Craig W Vander Kooi; Wang Chi; Ahmed Abdel Latif; Manikandan Panchatcharam; Virapong Prachayasittikul; D Allan Butterfield; Mary Vore; Jeffrey Moscow; Daret K St Clair
Journal:  Free Radic Biol Med       Date:  2015-12-09       Impact factor: 7.376

Review 2.  Nothing about protein structure classification makes sense except in the light of evolution.

Authors:  Ruben E Valas; Song Yang; Philip E Bourne
Journal:  Curr Opin Struct Biol       Date:  2009-04-24       Impact factor: 6.809

3.  Structure homology and interaction redundancy for discovering virus-host protein interactions.

Authors:  Benoît de Chassey; Laurène Meyniel-Schicklin; Anne Aublin-Gex; Vincent Navratil; Thibaut Chantier; Patrice André; Vincent Lotteau
Journal:  EMBO Rep       Date:  2013-09-06       Impact factor: 8.807

4.  TM0486 from the hyperthermophilic anaerobe Thermotoga maritima is a thiamin-binding protein involved in response of the cell to oxidative conditions.

Authors:  Zorah Dermoun; Amélie Foulon; Mitchell D Miller; Daniel J Harrington; Ashley M Deacon; Corinne Sebban-Kreuzer; Philippe Roche; Daniel Lafitte; Olivier Bornet; Ian A Wilson; Alain Dolla
Journal:  J Mol Biol       Date:  2010-05-13       Impact factor: 5.469

5.  Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase.

Authors:  Vincenzo Carbone; Linley R Schofield; Yanli Zhang; Carrie Sang; Debjit Dey; Ingegerd M Hannus; William F Martin; Andrew J Sutherland-Smith; Ron S Ronimus
Journal:  J Biol Chem       Date:  2015-07-14       Impact factor: 5.157

6.  The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily.

Authors:  David R Cooper; Katarzyna Grelewska; Chang-Yub Kim; Andrzej Joachimiak; Zygmunt S Derewenda
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-02-23

7.  Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling.

Authors:  Yan Yang; Peng Xie; Yarden Opatowsky; Joseph Schlessinger
Journal:  Proc Natl Acad Sci U S A       Date:  2010-01-11       Impact factor: 11.205

8.  Crystal structure of the variable domain of the Streptococcus gordonii surface protein SspB.

Authors:  Nina Forsgren; Richard J Lamont; Karina Persson
Journal:  Protein Sci       Date:  2009-09       Impact factor: 6.725

9.  The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain.

Authors:  Agnieszka Swiatek; Stuart A Macneill
Journal:  Biol Direct       Date:  2010-04-12       Impact factor: 4.540

10.  Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .

Authors:  Urszula Derewenda; Tomasz Boczek; Kelly L Gorres; Minmin Yu; Li-wei Hung; David Cooper; Andrzej Joachimiak; Ronald T Raines; Zygmunt S Derewenda
Journal:  Biochemistry       Date:  2009-09-15       Impact factor: 3.162

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