Welcome!
Our laboratory consists of interacting scientists that are interested in improving our basic understanding
and manipulation of interactions between proteins, using a combination of computational and experimental
approaches.
This embraces different levels of resolution and scale: starting from the basic atom - level details of
interactions; continuing to prediction and characterization of specific interactions; and finally addressing
the ultimate question of their role within the context of a cell and a whole organism.
Our computational tools include the structure-based computational prediction and manipulation of specific
interactions using the Rosetta modeling framework, analysis of evolutionary signals hidden in sequences, and
large-scale integration of this data by machine-learning approaches.
Our ERC starting grant has made it possible for us to realize a dream and to open a wet lab. Our experimental
setup includes the characterization of interactions using biophysical methods such as ITC, as well as in
vitro selection with Yeast surface Display. In addition, we have embarked on the journey of characterizing
the functional role of proteins with repeated domains for the adaptability of yeast to environmental
changes.
Read More »
Positions available for PhD Students and PostDocs
News
(9/2017) PIPER-FlexPepDock is now online!
PIPER-FlexPepDock
is a fragment-based protocol for high-resolution global peptide-protein docking.
Selected Publications
Check out our
full publication list
Derived Peptides
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London N, Raveh B, Movshovitz-Attias D, Schueler-Furman O (2010).
Can self-inhibitory peptides be derived from the interfaces of globular protein-protein interactions?
Proteins 78(15):3140-9.
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Sedan, Marcu, Lyskov & Schueler-Furman (2016).
Peptiderive server: derive peptide inhibitors from protein-protein interactions. Nucleic Acids Res. 44(W1):W536-541.
Peptide-protein interactions within their context
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Dodson EJ, Fishbain-Yoskovitz V, Rotem-Bamberger S,
Schueler-Furman O (2015).
Versatile communication strategies among tandem WW domain repeats. Exp Biol Med 240:351-360.
Comprehensive Reviews on peptide-peptide docking and the
peptide-based inhibition of protein-protein interactions
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London, Raveh, Schueler-Furman (2013)
Peptide docking and structure-based characterization of peptide binding: from knowledge to know-how. Curr Opin
Struct Biol 23:894-902.
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London, Raveh, Schueler-Furman (2013)
Druggable protein-protein interactions-from hot spots to hot segments. Curr Opin Chem Biol 17:952-959.
Protein-protein association energy landscapes
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Kozakov, Li, Hall, Beglov, Zheng, Vakili,
Schueler-Furman, Paschalidis, Clore, Vajda (2014)
Encounter complexes and dimensionality reduction in protein-protein association. Elife 3:e01370.
Binding Specificity & Design
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Slutzki, Reshef, Barak, Haimovitz, Rotem-Bamberger,
Lamed, Bayer, Schueler-Furman (2015).
Crucial roles of single residues in binding affinity, specificity and promiscuity in the cellulosomal
cohesin-dockerin interface. JBC in press.
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Gao M, London N, Cheng K, Tamura R, Jin J,
Schueler-Furman O, Yin H. (2014).
Rationally Designed Macrocyclic Peptides as Synergistic Agonists of LPS-Induced Inflammatory Response.
Tetrahedron 70:7664-7668.
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London, Lamphear, Hougland, Fierke & Schueler-Furman
(2011).
Identification of a novel class of farnesylation targets by structure-based modeling of binding specificity.
PLoS Comput Biol 7:e1002170.
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Al-Quadan, Price, London, Schueler-Furman & Abukwaik
(2011).
Anchoring of bacterial effectors to host membranes through host-mediated lipidation by prenylation: a common
paradigm. Trends Microbiol. 19:573-579.
FlexPepDock
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London, Raveh, Cohen, Fathi & Schueler-Furman
(2011).
Rosetta FlexPepDock web server--high resolution modeling of peptide-protein interactions.Nucleic Acids Res
39(Web Server issue):W249-53.
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Raveh, London, Zimmerman & Schueler-Furman
(2011).
Rosetta FlexPepDock ab-initio: Simultaneous Folding, Docking and Refinement of Peptides onto
Their Receptors. PLoS One 6:e18934.
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Belitsky, Avshalom, Erental, Yelin, Kumar, London,
Sperber, Schueler-Furman & Engelberg-Kulka (2011).
The Escherichia coli extracellular death factor EDF induces the endoribonucleolytic activities of the
toxins MazF and ChpBK. Mol Cell 41:625-35.