Literature DB >> 16928737

MMM: a sequence-to-structure alignment protocol.

Brajesh K Rai1, Carlos J Madrid-Aliste, J Eduardo Fajardo, András Fiser.   

Abstract

MOTIVATION: Accurate alignment of a target sequence to a template structure continues to be a bottleneck in producing good quality comparative protein structure models.
RESULTS: Multiple Mapping Method (MMM) is a comparative protein structure modeling server with an emphasis on a novel alignment optimization protocol. MMM takes inputs from five profile-to-profile based alignment methods. The alternatively aligned regions from the input alignment set are combined according to their fit in the structural environment of the template structure. The resulting, optimally spliced MMM alignment is used as input to an automated comparative modeling module to produce a full atom model. AVAILABILITY: The MMM server is freely accessible at http://www.fiserlab.org/servers/mmm

Mesh:

Year:  2006        PMID: 16928737     DOI: 10.1093/bioinformatics/btl449

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


  24 in total

1.  A biochemical mechanism for the oncogenic potential of the p110beta catalytic subunit of phosphoinositide 3-kinase.

Authors:  Hashem A Dbouk; Huan Pang; Andras Fiser; Jonathan M Backer
Journal:  Proc Natl Acad Sci U S A       Date:  2010-10-28       Impact factor: 11.205

2.  Computational Redesign of PD-1 Interface for PD-L1 Ligand Selectivity.

Authors:  Rojan Shrestha; Sarah C Garrett; Steven C Almo; Andras Fiser
Journal:  Structure       Date:  2019-03-28       Impact factor: 5.006

3.  Residues in the eighth transmembrane domain of the proton-coupled folate transporter (SLC46A1) play an important role in defining the aqueous translocation pathway and in folate substrate binding.

Authors:  Srinivas Aluri; Rongbao Zhao; Andras Fiser; I David Goldman
Journal:  Biochim Biophys Acta Biomembr       Date:  2017-08-09       Impact factor: 3.747

4.  The molecular evolution of cytochrome P450 genes within and between drosophila species.

Authors:  Robert T Good; Lydia Gramzow; Paul Battlay; Tamar Sztal; Philip Batterham; Charles Robin
Journal:  Genome Biol Evol       Date:  2014-04-20       Impact factor: 3.416

5.  A P425R mutation of the proton-coupled folate transporter causing hereditary folate malabsorption produces a highly selective alteration in folate binding.

Authors:  Daniel Sanghoon Shin; Rongbao Zhao; Enghui H Yap; Andras Fiser; I David Goldman
Journal:  Am J Physiol Cell Physiol       Date:  2012-02-15       Impact factor: 4.249

6.  Functional roles of the A335 and G338 residues of the proton-coupled folate transporter (PCFT-SLC46A1) mutated in hereditary folate malabsorption.

Authors:  Daniel Sanghoon Shin; Rongbao Zhao; Andras Fiser; David I Goldman
Journal:  Am J Physiol Cell Physiol       Date:  2012-07-25       Impact factor: 4.249

7.  Improved scoring function for comparative modeling using the M4T method.

Authors:  Dmitry Rykunov; Elliot Steinberger; Carlos J Madrid-Aliste; András Fiser
Journal:  J Struct Funct Genomics       Date:  2008-11-05

8.  The functional roles of the His247 and His281 residues in folate and proton translocation mediated by the human proton-coupled folate transporter SLC46A1.

Authors:  Ersin Selcuk Unal; Rongbao Zhao; Min-Hwang Chang; Andras Fiser; Michael F Romero; I David Goldman
Journal:  J Biol Chem       Date:  2009-04-23       Impact factor: 5.157

9.  Substituted-cysteine accessibility and cross-linking identify an exofacial cleft in the 7th and 8th helices of the proton-coupled folate transporter (SLC46A1).

Authors:  Srinivas Aluri; Rongbao Zhao; Andras Fiser; I David Goldman
Journal:  Am J Physiol Cell Physiol       Date:  2017-11-22       Impact factor: 4.249

10.  PCRPi: Presaging Critical Residues in Protein interfaces, a new computational tool to chart hot spots in protein interfaces.

Authors:  Salam A Assi; Tomoyuki Tanaka; Terence H Rabbitts; Narcis Fernandez-Fuentes
Journal:  Nucleic Acids Res       Date:  2009-12-11       Impact factor: 16.971

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