Literature DB >> 12490462

PoPMuSiC, rationally designing point mutations in protein structures.

J M Kwasigroch1, D Gilis, Y Dehouck, M Rooman.   

Abstract

PoPMuSiC is an efficient tool for rational computer-aided design of single-site mutations in proteins and peptides. Two types of queries can be submitted. The first option allows to estimate the changes in folding free energy for specific point mutations given by the user. In the second option, all possible point mutations in a given protein or protein region are performed and the most stabilizing or destabilizing mutations, or the neutral mutations with respect to thermodynamic stability, are selected. For each sequence position or secondary structure the deviation from the most stable sequence is moreover evaluated, which helps to identify the most suitable sites for the introduction of mutations.

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Year:  2002        PMID: 12490462     DOI: 10.1093/bioinformatics/18.12.1701

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


  17 in total

1.  Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases.

Authors:  Fan Wang; Wensi Song; Giovanna Brancati; Laura Segatori
Journal:  J Biol Chem       Date:  2011-10-17       Impact factor: 5.157

2.  Enhancing the stability and solubility of TEV protease using in silico design.

Authors:  Lisa D Cabrita; Dimitri Gilis; Amy L Robertson; Yves Dehouck; Marianne Rooman; Stephen P Bottomley
Journal:  Protein Sci       Date:  2007-09-28       Impact factor: 6.725

3.  Genetic determinants involved in p-aminosalicylic acid resistance in clinical isolates from tuberculosis patients in northern China from 2006 to 2012.

Authors:  Xiaobing Zhang; Liguo Liu; Yan Zhang; Guangming Dai; Hairong Huang; Qi Jin
Journal:  Antimicrob Agents Chemother       Date:  2014-11-24       Impact factor: 5.191

4.  Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein.

Authors:  Helen M Saunders; Dimitri Gilis; Marianne Rooman; Yves Dehouck; Amy L Robertson; Stephen P Bottomley
Journal:  Protein Sci       Date:  2011-08-18       Impact factor: 6.725

5.  A dual mechanism for I(Ks) current reduction by the pathogenic mutation KCNQ1-S277L.

Authors:  Jerri Chen; Michael Weber; Sung Yon Um; Christine A Walsh; Yingying Tang; Thomas V McDonald
Journal:  Pacing Clin Electrophysiol       Date:  2011-09-02       Impact factor: 1.976

6.  Rational-Design Engineering to Improve Enzyme Thermostability.

Authors:  Vinutsada Pongsupasa; Piyanuch Anuwan; Somchart Maenpuen; Thanyaporn Wongnate
Journal:  Methods Mol Biol       Date:  2022

7.  Molecular genetics of para-aminosalicylic acid resistance in clinical isolates and spontaneous mutants of Mycobacterium tuberculosis.

Authors:  Vanessa Mathys; René Wintjens; Philippe Lefevre; Julie Bertout; Amit Singhal; Mehdi Kiass; Natalia Kurepina; Xiao-Ming Wang; Barun Mathema; Alain Baulard; Barry N Kreiswirth; Pablo Bifani
Journal:  Antimicrob Agents Chemother       Date:  2009-02-23       Impact factor: 5.191

8.  An Italian cohort study identifies four new pathologic mutations in the ARSA gene.

Authors:  Daniela Galla; Paola de Gemmis; Laura Anesi; Silvia Berto; Diego Dolcetta; Uroš Hladnik
Journal:  J Mol Neurosci       Date:  2013-04-05       Impact factor: 3.444

Review 9.  Candidate gene association studies: a comprehensive guide to useful in silico tools.

Authors:  Radhika Patnala; Judith Clements; Jyotsna Batra
Journal:  BMC Genet       Date:  2013-05-09       Impact factor: 2.797

10.  Machine learning integration for predicting the effect of single amino acid substitutions on protein stability.

Authors:  Ayşegül Ozen; Mehmet Gönen; Ethem Alpaydan; Türkan Haliloğlu
Journal:  BMC Struct Biol       Date:  2009-10-19
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