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Linear Motif Discovery

Data from Neduva et al, PLoS Biol., 2005. DILIMOT server for Discovery of Linear Motifs. Protein linear motifs describe short (3-8 residue), common stretches of polypeptide chains that are associated with a specific function. They include phosphoarylation sites, other post-translational modifications, targetting signals for cellular compartments, protein cleavage sites and protein interaction modules. They are similar to protein domains. They are also non- globular. This prompted us in 2002 to start the ...

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Linear Motif Discovery | lmd.russelllab.org Reviews
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Data from Neduva et al, PLoS Biol., 2005. DILIMOT server for Discovery of Linear Motifs. Protein linear motifs describe short (3-8 residue), common stretches of polypeptide chains that are associated with a specific function. They include phosphoarylation sites, other post-translational modifications, targetting signals for cellular compartments, protein cleavage sites and protein interaction modules. They are similar to protein domains. They are also non- globular. This prompted us in 2002 to start the ...
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Linear Motif Discovery | lmd.russelllab.org Reviews

https://lmd.russelllab.org

Data from Neduva et al, PLoS Biol., 2005. DILIMOT server for Discovery of Linear Motifs. Protein linear motifs describe short (3-8 residue), common stretches of polypeptide chains that are associated with a specific function. They include phosphoarylation sites, other post-translational modifications, targetting signals for cellular compartments, protein cleavage sites and protein interaction modules. They are similar to protein domains. They are also non- globular. This prompted us in 2002 to start the ...

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Systematic discovery of peptides mediating protein interaction networks

http://lmd.russelllab.org/lmd/plos.html

These pages relate to: V. Neduva, R. Linding, I. Su-Angrand, A. Stark, F. de Massi, T.J. Gibson, J. Lewis, L. Serrano, R.B. Russell, Systematic discovery of peptides mediating protein interaction networks PLoS Biology. High confidence, pre-computed motif sets. Or if they interact with proteins sharing a common domain ( 'domain' set. And its occurence in a particular number of sequences (n) within a set of M sequences. A score which encapsulates probability of the motif and it conservation. The S. However...

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Services offered by Protein Evolution

http://www.russelllab.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

landscape.syscilia.org landscape.syscilia.org

Services offered by Protein Evolution

http://www.landscape.syscilia.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

mechismo.russelllab.org mechismo.russelllab.org

Services offered by Protein Evolution

http://www.mechismo.russelllab.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

pepsite2.russelllab.org pepsite2.russelllab.org

PepSite

http://pepsite2.russelllab.org/webservice

Run PepSite on a PDB structure. Run PepSite on your own PDB file. This PepSite web server can be accessed programmatically via a simple RESTful interface. Currently, the only implemented method is. Which queries an input peptide sequence against a protein surface identified via a PDB/chain code. Output format (see below). Web page with matches, scores, and molecular visualization. Plain text output with list of matches and scores. Match coordinates in pdb format. P-value of the best match in plain text.

3drepertoire.russelllab.org 3drepertoire.russelllab.org

Services offered by Protein Evolution

http://www.3drepertoire.russelllab.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

pepsite2.russelllab.org pepsite2.russelllab.org

PepSite

http://pepsite2.russelllab.org/examples

Run PepSite on a PDB structure. Run PepSite on your own PDB file. RNEDD4 WWIII domain from Rattus norvegicus. WW domains bind [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs. The PDB file with id 1i5h. Is a RNEDD4 WWIII domain bound to a ENaC peptide. For more information, please refer to the Kanelis et al (2011). You run PepSite on the bound structure by specifying PDB code 1i5h. Chain W, and peptide sequence GTPPPNYDSL (see results. 74 kDa type IV collagenase from Homo sapiens.

pepsite2.russelllab.org pepsite2.russelllab.org

PepSite

http://pepsite2.russelllab.org/about

Run PepSite on a PDB structure. Run PepSite on your own PDB file. PepSite was originally described in the following article:. Accurate prediction of peptide binding sites on protein surfaces. Petsalaki E, Stark A, García-Urdiales E, and Russell RB. Contributors to PepSite software development. V10 and original webserver). V2x and current webserver). Technical information about the PepSite webserver. Matches calculated with PepSite v2.2.20. Hot spots pre-calculated with PepSite v2.2.20.

dilimot.russelllab.org dilimot.russelllab.org

Services offered by Protein Evolution

http://www.dilimot.russelllab.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

proust2.russelllab.org proust2.russelllab.org

Services offered by Protein Evolution

http://www.proust2.russelllab.org/services.shtml

This tool lets you interrogate data from our collaborative project on the Ciliary proteome, where we identified nearly 5000 interactions and over 50 complexes, involving more than 1000 proteins in the cilia. From Boldt, van Reeuwijk, Lu, Koutroumpas et al Nat Commun. From Betts et al, Nucl Acids Res. A database of protein-chemical interactions predicted by structure superimpositions: if you are interested in chemicals that might bind a particular protein or vice versa, then check it out. From Stark et al...

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Linear Motif Discovery

Data from Neduva et al, PLoS Biol., 2005. DILIMOT server for Discovery of Linear Motifs. Protein linear motifs describe short (3-8 residue), common stretches of polypeptide chains that are associated with a specific function. They include phosphoarylation sites, other post-translational modifications, targetting signals for cellular compartments, protein cleavage sites and protein interaction modules. They are similar to protein domains. They are also non- globular. This prompted us in 2002 to start the ...

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