Literature DB >> 19785006

MPEx: a tool for exploring membrane proteins.

Craig Snider1, Sajith Jayasinghe, Kalina Hristova, Stephen H White.   

Abstract

Hydropathy plot methods form a cornerstone of membrane protein research, especially in the early stages of biochemical and structural characterization. Membrane Protein Explorer (MPEx), described in this article, is a refined and versatile hydropathy-plot software tool for analyzing membrane protein sequences. MPEx is highly interactive and facilitates the characterization and identification of favorable protein transmembrane regions using experiment-based physical and biological hydrophobicity scales. Besides allowing the consequences of sequence mutations to be examined, it provides tools for aiding the design of membrane-active peptides. MPEx is freely available as a Java Web Start application from our web site at http://blanco.biomol.uci.edu/mpex.

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Year:  2009        PMID: 19785006      PMCID: PMC2821280          DOI: 10.1002/pro.256

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  24 in total

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Authors:  S Jayasinghe; K Hristova; S H White
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

2.  Toward genomic identification of beta-barrel membrane proteins: composition and architecture of known structures.

Authors:  William C Wimley
Journal:  Protein Sci       Date:  2002-02       Impact factor: 6.725

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Authors:  A S Ladokhin; S H White
Journal:  J Mol Biol       Date:  2001-06-08       Impact factor: 5.469

4.  The progress of membrane protein structure determination.

Authors:  Stephen H White
Journal:  Protein Sci       Date:  2004-07       Impact factor: 6.725

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Journal:  Nucleic Acids Res       Date:  1991-04-25       Impact factor: 16.971

6.  Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule.

Authors:  G von Heijne
Journal:  J Mol Biol       Date:  1992-05-20       Impact factor: 5.469

7.  Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues.

Authors:  G von Heijne
Journal:  Nature       Date:  1989-10-05       Impact factor: 49.962

8.  Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability.

Authors:  W C Wimley; K Gawrisch; T P Creamer; S H White
Journal:  Proc Natl Acad Sci U S A       Date:  1996-04-02       Impact factor: 11.205

9.  A simple method for displaying the hydropathic character of a protein.

Authors:  J Kyte; R F Doolittle
Journal:  J Mol Biol       Date:  1982-05-05       Impact factor: 5.469

10.  Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides.

Authors:  W C Wimley; T P Creamer; S H White
Journal:  Biochemistry       Date:  1996-04-23       Impact factor: 3.162

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6.  Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66.6.

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Journal:  J Virol       Date:  2013-12-11       Impact factor: 5.103

7.  A peptide for transcellular cargo delivery: Structure-function relationship and mechanism of action.

Authors:  Alexander Komin; Maxim I Bogorad; Ran Lin; Honggang Cui; Peter C Searson; Kalina Hristova
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Authors:  Anukriti Mathur; Shouya Feng; Jenni A Hayward; Chinh Ngo; Daniel Fox; Ines I Atmosukarto; Jason D Price; Kristina Schauer; Erwin Märtlbauer; Avril A B Robertson; Gaetan Burgio; Edward M Fox; Stephen H Leppla; Nadeem O Kaakoush; Si Ming Man
Journal:  Nat Microbiol       Date:  2018-12-10       Impact factor: 17.745

9.  Detecting the functional complexities between high-density lipoprotein mimetics.

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10.  Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region.

Authors:  Gilad Ofek; Krisha McKee; Yongping Yang; Zhi-Yong Yang; Jeff Skinner; F Javier Guenaga; Richard Wyatt; Michael B Zwick; Gary J Nabel; John R Mascola; Peter D Kwong
Journal:  J Virol       Date:  2009-12-30       Impact factor: 5.103

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