@inproceedings{MultiLoc_GCB05,
title = {Using N-terminal targeting sequences, amino acid composition, and sequence motifs for predicting protein subcellular localization},
author = {Annette Höglund and Pierre Dönnes and Torsten Blum and Hans-Werner Adolph and Oliver Kohlbacher},
editor = {Matthias Rarey Andrew Torda Stefan Kurtz},
url = {MultiLoc_2005.pdf},
year = {2005},
date = {2005-01-01},
booktitle = {Proceedings of the German Conference on Bioinformatics (GCB 2005)},
pages = {45--59},
publisher = {GI},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@article{RefMat,
title = {Reference methods and materials in standardisation and quality assurance},
author = {Christoph L Klein and Oliver Kohlbacher and Christian Huber and Knut Reinert},
year = {2005},
date = {2005-01-01},
journal = {FEBS J.},
volume = {272},
number = {S1},
note = {in press},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{NRPSPred,
title = {Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using Transductive Support Vector Machines (TSVM)},
author = {Christian Rausch and Tilmann Weber and Oliver Kohlbacher and Wolfgang Wohlleben and Daniel Huson},
url = {http://www.pubmedcentral.gov/articlerender.fcgi?tool=pubmed&pubmedid=16221976},
year = {2005},
date = {2005-01-01},
journal = {Nucl. Acids Res.},
volume = {33},
number = {18},
pages = {5799-5808},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@book{CLS2005b,
title = {Computational Life Sciences},
author = {Michael Berthold and Robert Glen and Kay Diederichs and Oliver Kohlbacher and Ingrid Fischer},
url = {http://www.springeronline.com/3-540-29104-0},
year = {2005},
date = {2005-01-01},
volume = {3695},
publisher = {Springer Lecture notes in Bioinformatics},
keywords = {},
pubstate = {published},
tppubtype = {book}
}
@inproceedings{InproceedingsReference.2006-01-19.8468200784,
title = {BALLView - An Open Source Tool for Molecular Modeling and Visualization},
author = {Andreas Moll and Andreas Hildebrandt and Andreas Kerzmann and Hans-Peter Lenhof and Oliver Kohlbacher},
editor = {Klumpp D D. Spath K. Haasis},
year = {2005},
date = {2005-01-01},
booktitle = {Tagungsband zum doIT Software-Forschungstag 2005},
pages = {203--214},
publisher = {MFG Stiftung},
address = {Stuttgart},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@article{lokeroref,
title = {From prediction of subcellular localization to functional classification: Discrimination of DNA-packing and other nuclear proteins},
author = {A Höglund and P Dönnes and HW Adolph and O Kohlbacher},
url = {http://www.comcen.com.au/~journals/dnapackingabs2005.htm},
year = {2005},
date = {2005-01-01},
journal = {Online Journal of Bioinformatics},
volume = {6},
number = {1},
pages = {51-64},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{WAPP,
title = {Integrated modelling of the major events in the MHC class I antigen processing pathway},
author = {Pierre Dönnes and Oliver Kohlbacher},
url = {http://dx.doi.org/10.1110/ps.051352405},
year = {2005},
date = {2005-01-01},
journal = {Protein Sci.},
volume = {14},
number = {8},
pages = {2132-2140},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{SNEP,
title = {SNEP: SNP-derived Epitope Prediction program for minor H antigens.},
author = {Mathias M Schuler and Pierre Dönnes and Maria-Dorothea Nastke and Oliver Kohlbacher and Hans-Georg Rammensee and Stefan Stevanovic},
url = {http://www.springerlink.com/openurl.asp?genre=article&id=doi:10.1007/s00251-005-0054-5},
year = {2005},
date = {2005-01-01},
journal = {Immunogenetics},
volume = {57},
number = {11},
pages = {816-820},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
SNEP: SNP-derived Epitope Prediction program for minor H antigens
Kabelitz, Dietrich (Ed.): Joint Annual Meeting of the German and Scandinavian Societies of Immunology, 21-24 September 2005, Kiel, Germany, pp. 361-622, Immunobiology 210(6-8), 2005.
@inproceedings{InproceedingsReference.2006-01-03.7145695050,
title = {SNEP: SNP-derived Epitope Prediction program for minor H antigens},
author = {Mathias Schuler and Pierre Dönnes and Maria Nastke and Oliver Kohlbacher and H-G Rammensee and Stefan Stevanovic},
editor = {Dietrich Kabelitz},
year = {2005},
date = {2005-01-01},
booktitle = {Joint Annual Meeting of the German and Scandinavian Societies of Immunology, 21-24 September 2005, Kiel, Germany},
pages = {361-622},
publisher = {Immunobiology 210(6-8)},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
Istrail, Sorin; Florea, Liliana; Halldorsson, Bjarni V; Kohlbacher, Oliver; Schwartz, Russell S; Yap, Von Bing; Yewdell, Jonathan W; Hoffman, Stephen L
Comparative Immuno-Peptidomics of Humans and their Pathogens
Proc. Natl. Acad. Sci. USA, 101 (36), pp. 13268, 2004.
@article{PNASPeptidomics,
title = {Comparative Immuno-Peptidomics of Humans and their Pathogens},
author = {Sorin Istrail and Liliana Florea and Bjarni V Halldorsson and Oliver Kohlbacher and Russell S Schwartz and Von Bing Yap and Jonathan W Yewdell and Stephen L Hoffman},
url = {http://www.pnas.org/cgi/reprint/0404740101},
year = {2004},
date = {2004-01-01},
journal = {Proc. Natl. Acad. Sci. USA},
volume = {101},
number = {36},
pages = {13268},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{CAP.FASEBJ.2004,
title = {Integrative analysis of cancer-related data using CAP},
author = {Pierre Dönnes and Annette Höglund and Marc Sturm and Nicole Comtesse and Christina Backes and Eckart Meese and Oliver Kohlbacher and Hans-Peter Lenhof},
url = {http://www.fasebj.org/cgi/content/abstract/04-1797fjev1},
year = {2004},
date = {2004-01-01},
journal = {FASEB Journal},
volume = {18},
number = {12},
pages = {1465-1467},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{LocationReview,
title = {Predicting Protein Subcellular Localization: Past, Present, and Future},
author = {Pierre Dönnes and Annette Höglund},
url = {https://www.ncbi.nlm.nih.gov/pubmed/15901249},
year = {2004},
date = {2004-01-01},
journal = {Genomics Proteomics Bioinformatics},
volume = {2},
number = {4},
pages = {209--215},
abstract = {Functional characterization of every single protein is a major challenge of the post-genomic era. The large-scale analysis of a cell's proteins, proteomics, seeks to provide these proteins with reliable annotations regarding their interaction partners and functions in the cellular machinery. An important step on this way is to determine the subcellular localization of each protein. Eukaryotic cells are divided into subcellular compartments, or organelles. Transport across the membrane into the organelles is a highly regulated and complex cellular process. Predicting the subcellular localization by computational means has been an area of vivid activity during recent years. The publicly available prediction methods differ mainly in four aspects: the underlying biological motivation, the computational method used, localization coverage, and reliability, which are of importance to the user. This review provides a short description of the main events in the protein sorting process and an overview of the most commonly used methods in this field.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Functional characterization of every single protein is a major challenge of the post-genomic era. The large-scale analysis of a cell's proteins, proteomics, seeks to provide these proteins with reliable annotations regarding their interaction partners and functions in the cellular machinery. An important step on this way is to determine the subcellular localization of each protein. Eukaryotic cells are divided into subcellular compartments, or organelles. Transport across the membrane into the organelles is a highly regulated and complex cellular process. Predicting the subcellular localization by computational means has been an area of vivid activity during recent years. The publicly available prediction methods differ mainly in four aspects: the underlying biological motivation, the computational method used, localization coverage, and reliability, which are of importance to the user. This review provides a short description of the main events in the protein sorting process and an overview of the most commonly used methods in this field.
@inproceedings{FHKSHI2003,
title = {Epitope Prediction Algorithms for Peptide based Vaccine Design},
author = {Liliana Florea and Bjarni Halldórsson and Oliver Kohlbacher and Russell Schwartz and Stephen Hoffman and Sorin Istrail},
url = {http://csdl.computer.org/comp/proceedings/csb/2003/2000/00/20000017abs.htm},
year = {2003},
date = {2003-01-01},
booktitle = {Proceedings of the 2nd IEEE Computer Society Conference on Bioinformatics},
pages = {17-26},
publisher = {IEEE Computer Society},
note = {PMID: 16826643},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@preprint{NonlocalESPreprint,
title = {Using nonlocal electrostatics for solvation free energy computations: ions and small molecules},
author = {Andreas Hildebrandt and Oliver Kohlbacher and Ralf Blossey and Hans-Peter Lenhof},
url = {http://arXiv.org/abs/physics/0212074},
year = {2003},
date = {2003-01-01},
keywords = {},
pubstate = {published},
tppubtype = {preprint}
}
@article{AKLM2002,
title = {A Combinatorial Approach to Protein Docking with Flexible Side-Chains},
author = {Ernst Althaus and Oliver Kohlbacher and Hans Peter Lenhof and Peter Müller},
doi = {https://doi.org/10.1089/106652702760277336},
year = {2002},
date = {2002-01-01},
journal = {J. Comput. Biol.},
volume = {9},
number = {4},
pages = {597-612},
abstract = {Rigid-body docking approaches are not sufficient to predict the structure of a protein complex from the unbound (native) structures of the two proteins. Accounting for side chain flexibility is an important step towards fully flexible protein docking. This work describes an approach that allows conformational flexibility for the side chains while keeping the protein backbone rigid. Starting from candidates created by a rigid-docking algorithm, we demangle the side chains of the docking site, thus creating reasonable approximations of the true complex structure. These structures are ranked with respect to the binding free energy. We present two new techniques for side chain demangling. Both approaches are based on a discrete representation of the side chain conformational space by the use of a rotamer library. This leads to a combinatorial optimization problem. For the solution of this problem, we propose a fast heuristic approach and an exact, albeit slower, method that uses branch-and-cut techniques. As a test set, we use the unbound structures of three proteases and the corresponding protein inhibitors. For each of the examples, the highest-ranking conformation produced was a good approximation of the true complex structure.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rigid-body docking approaches are not sufficient to predict the structure of a protein complex from the unbound (native) structures of the two proteins. Accounting for side chain flexibility is an important step towards fully flexible protein docking. This work describes an approach that allows conformational flexibility for the side chains while keeping the protein backbone rigid. Starting from candidates created by a rigid-docking algorithm, we demangle the side chains of the docking site, thus creating reasonable approximations of the true complex structure. These structures are ranked with respect to the binding free energy. We present two new techniques for side chain demangling. Both approaches are based on a discrete representation of the side chain conformational space by the use of a rotamer library. This leads to a combinatorial optimization problem. For the solution of this problem, we propose a fast heuristic approach and an exact, albeit slower, method that uses branch-and-cut techniques. As a test set, we use the unbound structures of three proteases and the corresponding protein inhibitors. For each of the examples, the highest-ranking conformation produced was a good approximation of the true complex structure.
@inproceedings{NKK2002,
title = {Modelling the sugar-lectin interaction by computer simulated docking},
author = {Dirk Neumann and Andreas Kerzmann and Oliver Kohlbacher},
year = {2002},
date = {2002-01-01},
booktitle = {Abstracts of the 20th Interlec Meeting},
pages = {116},
publisher = {University of Copenhagen, Copenhagen, Denmark},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@article{SSEKKBL2002,
title = {BioMiner - modeling, analysing, and visualizing biochemical pathways and networks},
author = {Marite Sirava and Thomas Schäfer and Markus Eiglsperger and Michael Kaufmann and Oliver Kohlbacher and Erich Bornberg-Bauer and Hans-Peter Lenhof},
url = {http://bioinformatics.oupjournals.org/cgi/reprint/18/suppl_2/S219},
year = {2002},
date = {2002-01-01},
journal = {Bioinformatics},
volume = {19},
number = {10},
pages = {S219-230},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{SVMHC,
title = {Prediction of MHC class I binding peptides, using SVMHC},
author = {Pierre Dönnes and Arne Elofsson},
url = {http://www.biomedcentral.com/1471-2105/3/25},
year = {2002},
date = {2002-01-01},
journal = {BMC Bioinformatics},
volume = {3},
number = {25},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
@article{articleKBM2001,
title = {Structure prediction of protein complexes by a NMR-based protein docking algorithm},
author = {Oliver Kohlbacher and Andreas Burchardt and Andreas Moll and Andreas Hildebrandt and Peter Bayer and Hans-Peter Lenhof},
url = {https://link.springer.com/article/10.1023/A:1011216130486},
year = {2001},
date = {2001-01-01},
journal = {J. Biomol. NMR},
volume = {20},
pages = {15-21},
abstract = {Protein docking algorithms can be used to study the driving forces and reaction mechanisms of docking processes. They are also able to speed up the lengthy process of experimental structure elucidation of protein complexes by proposing potential structures. In this paper, we are discussing a variant of the protein-protein docking problem, where the input consists of the tertiary structures of proteins A and B plus an unassigned one-dimensional 1H-NMR spectrum of the complex AB. We present a new scoring function for evaluating and ranking potential complex structures produced by a docking algorithm. The scoring function computes a `theoretical' 1H-NMR spectrum for each tentative complex structure and subtracts the calculated spectrum from the experimental one. The absolute areas of the difference spectra are then used to rank the potential complex structures. In contrast to formerly published approaches (e.g. [Morelli et al. (2000) Biochemistry, 39, 2530–2537]) we do not use distance constraints (intermolecular NOE constraints). We have tested the approach with four protein complexes whose three-dimensional structures are stored in the PDB data bank [Bernstein et al. (1977)] and whose 1H-NMR shift assignments are available from the BMRB database. The best result was obtained for an example, where all standard scoring functions failed completely. Here, our new scoring function achieved an almost perfect separation between good approximations of the true complex structure and false positives.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Protein docking algorithms can be used to study the driving forces and reaction mechanisms of docking processes. They are also able to speed up the lengthy process of experimental structure elucidation of protein complexes by proposing potential structures. In this paper, we are discussing a variant of the protein-protein docking problem, where the input consists of the tertiary structures of proteins A and B plus an unassigned one-dimensional 1H-NMR spectrum of the complex AB. We present a new scoring function for evaluating and ranking potential complex structures produced by a docking algorithm. The scoring function computes a `theoretical' 1H-NMR spectrum for each tentative complex structure and subtracts the calculated spectrum from the experimental one. The absolute areas of the difference spectra are then used to rank the potential complex structures. In contrast to formerly published approaches (e.g. [Morelli et al. (2000) Biochemistry, 39, 2530–2537]) we do not use distance constraints (intermolecular NOE constraints). We have tested the approach with four protein complexes whose three-dimensional structures are stored in the PDB data bank [Bernstein et al. (1977)] and whose 1H-NMR shift assignments are available from the BMRB database. The best result was obtained for an example, where all standard scoring functions failed completely. Here, our new scoring function achieved an almost perfect separation between good approximations of the true complex structure and false positives.
@inproceedings{procTur2001,
title = {Visualization Challenges for a New Cyberpharmaceutical Computing Paradigm},
author = {Russell J Turner and Kabir Chaturvedi and Nathan J Edwards and Daniel Fasulo and Aaron L Halpern and Daniel H Huson and Karin A Remington and Russell Schwartz and Brian Walenz and Shibu Yooseph and Sorin Istrail},
year = {2001},
date = {2001-01-01},
booktitle = {Proceedings of the IEEE Symposium on Parallel and Large-Data Visualization and Graphics (PVG2001)},
pages = {7--18},
address = {San Diego, USA,},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
A NMR-spectra-based scoring function for protein docking
Sankoff, David; Lengauer, Thomas (Ed.): RECOMB 2001, Proceedings of the Fifth Annual International Conference on Computational Molecular Biology, pp. 169-177, ACM press, 2001.
@inproceedings{KBHMBL2000,
title = {A NMR-spectra-based scoring function for protein docking},
author = {Oliver Kohlbacher and Andreas Burchardt and Andreas Hildebrandt and Andreas Moll and Peter Bayer and Hans-Peter Lenhof},
editor = {David Sankoff and Thomas Lengauer},
url = {http://portal.acm.org/citation.cfm?doid=369133.369194},
year = {2001},
date = {2001-01-01},
booktitle = {RECOMB 2001, Proceedings of the Fifth Annual International Conference on Computational Molecular Biology},
pages = {169-177},
publisher = {ACM press},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@inproceedings{procNKH2000,
title = {Modeling the Sugar Lectin Interaction by Computational Chemistry Relevant to Drug Design},
author = {Dirk Neumann and Oliver Kohlbacher and Eleonore Haltner and Hans-Peter Lenhof and Claus-Michael Lehr},
year = {2000},
date = {2000-01-01},
booktitle = {Proc. 3rd World Meeting on Pharmaceutics, Biopharmaceutics and Pharmaceutical Technology},
pages = {233},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@article{articleKL2000,
title = {BALL - Rapid Software Prototyping in Computational Molecular Biology},
author = {Oliver Kohlbacher and Hans-Peter Lenhof},
url = {https://www.ncbi.nlm.nih.gov/pubmed/11108704},
year = {2000},
date = {2000-01-01},
journal = {Bioinformatics},
volume = {16},
number = {9,},
pages = {815--824},
abstract = {MOTIVATION:
Rapid software prototyping can significantly reduce development times in the field of computational molecular biology and molecular modeling. Biochemical Algorithms Library (BALL) is an application framework in C++ that has been specifically designed for this purpose.
RESULTS:
BALL provides an extensive set of data structures as well as classes for molecular mechanics, advanced solvation methods, comparison and analysis of protein structures, file import/export, and visualization. BALL has been carefully designed to be robust, easy to use, and open to extensions. Especially its extensibility which results from an object-oriented and generic programming approach distinguishes it from other software packages. BALL is well suited to serve as a public repository for reliable data structures and algorithms. We show in an example that the implementation of complex methods is greatly simplified when using the data structures and functionality provided by BALL.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
MOTIVATION:
Rapid software prototyping can significantly reduce development times in the field of computational molecular biology and molecular modeling. Biochemical Algorithms Library (BALL) is an application framework in C++ that has been specifically designed for this purpose.
RESULTS:
BALL provides an extensive set of data structures as well as classes for molecular mechanics, advanced solvation methods, comparison and analysis of protein structures, file import/export, and visualization. BALL has been carefully designed to be robust, easy to use, and open to extensions. Especially its extensibility which results from an object-oriented and generic programming approach distinguishes it from other software packages. BALL is well suited to serve as a public repository for reliable data structures and algorithms. We show in an example that the implementation of complex methods is greatly simplified when using the data structures and functionality provided by BALL.
@article{articleBKL2000,
title = {Rapid software prototyping in molecular modeling using the biochemical algorithms library (BALL)},
author = {N P Boghossian and O Kohlbacher and H P Lenhof},
year = {2000},
date = {2000-01-01},
journal = {J. Exp. Algorithmics},
volume = {5},
pages = {16},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Althaus, Ernst; Kohlbacher, Oliver; Lenhof, Hans-Peter; Müller, Peter
A Combinatorial Approach to Protein Docking with Flexible Side-Chains
Shamir, Ron; Miyano, Satoru; Istrail, Sorin; Pevzner, Pavel; Waterman, Michael (Ed.): RECOMB 2000 -- Proceedings of the Fourth Annual International Conference on Computational Molecular Biology, pp. 15–24, ACM press, 2000.
@inproceedings{procAKL2000,
title = {A Combinatorial Approach to Protein Docking with Flexible Side-Chains},
author = {Ernst Althaus and Oliver Kohlbacher and Hans-Peter Lenhof and Peter Müller},
editor = {Ron Shamir and Satoru Miyano and Sorin Istrail and Pavel Pevzner and Michael Waterman},
year = {2000},
date = {2000-01-01},
booktitle = {RECOMB 2000 -- Proceedings of the Fourth Annual International Conference on Computational Molecular Biology},
pages = {15--24},
publisher = {ACM press},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@techreport{AKLM2000,
title = {A branch and cut algorithm for the optimal solution of the side-chain placement problem},
author = {Ernst Althaus and Oliver Kohlbacher and Hans-Peter Lenhof and Peter Müller},
url = {http://domino.mpi-sb.mpg.de/internet/reports.nsf/NumberView/2000-1-001},
year = {2000},
date = {2000-01-01},
number = {MPI-I-2000-1-001},
address = {Stuhlsatzenhausweg 85, 66123 Saarbrücken, Germany},
institution = {Max-Planck-Institute für Informatik},
keywords = {},
pubstate = {published},
tppubtype = {techreport}
}
@inproceedings{procKL1999,
title = {Rapid Software Prototyping in Computational Molecular Biology},
author = {O Kohlbacher and H -P Lenhof},
year = {1999},
date = {1999-01-01},
booktitle = {Proceedings of the German Conference on Bioinformatics (GCB'99)},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@inproceedings{procNHL1998,
title = {Investigating the Sugar-Lectin Interaction by Computational Chemistry: Tunneling the Epithelial Barrier},
author = {Dirk Neumann and Elleonore Haltner and Claus-Michael Lehr and Oliver Kohlbacher and Hans-Peter Lenhof},
year = {1998},
date = {1998-01-01},
booktitle = {Abstracts of the 18th Interlec Meeting},
pages = {549},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
@article{Immel_Comms_Bio_2021,
title = {Genome-wide study of a Neolithic Wartberg grave community reveals distinct HLA variation and hunter-gatherer ancestry},
author = {Alexander Immel and Federicia Perini and Christoph Rinne and John Meadows and Rodrigo Barquera and Andras Szolek and Julian SUsat and Lisa Böhme and Janina Dose and Joanna Bonczarowska and Clara Drummer and Katharina Fuchs and David Ellinghaus and Jan-Christian Kässens and Martin Furholt and Oliver Kohlbacher and Sabine Schade-Lindig and Andre Franke and Stefan Schreiber and Johannes Krause and Johannes Müller and Tobias L. Lenz and Almut Nebel and Ben Krause-Kyora},
journal = {Communications Biology},
abstract = {The Wartberg culture (WBC, 3500-2800 BCE) dates to the Late Neolithic period, a time of
important demographic and cultural transformations in western Europe. We performed
genome-wide analyses of 42 individuals who were interred in a WBC collective burial in
Niedertiefenbach, Germany (3300-3200 cal. BCE). The results showed that the farming
population of Niedertiefenbach carried a surprisingly large hunter-gatherer ancestry component
(34–58%). This component was most likely introduced during the cultural transformation
that led to the WBC. In addition, the Niedertiefenbach individuals exhibited a distinct
human leukocyte antigen gene pool, possibly reflecting an immune response that was geared
towards detecting viral infections.},
keywords = {},
pubstate = {forthcoming},
tppubtype = {article}
}
The Wartberg culture (WBC, 3500-2800 BCE) dates to the Late Neolithic period, a time of
important demographic and cultural transformations in western Europe. We performed
genome-wide analyses of 42 individuals who were interred in a WBC collective burial in
Niedertiefenbach, Germany (3300-3200 cal. BCE). The results showed that the farming
population of Niedertiefenbach carried a surprisingly large hunter-gatherer ancestry component
(34–58%). This component was most likely introduced during the cultural transformation
that led to the WBC. In addition, the Niedertiefenbach individuals exhibited a distinct
human leukocyte antigen gene pool, possibly reflecting an immune response that was geared
towards detecting viral infections.
@article{EVComp_Nat_Comm_2021,
title = { Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences},
author = {Anna Green and Hadeer Elhabashy and Kelly Brock and Rohan Maddamsetti and Oliver Kohlbacher and Debora S. Marks},
journal = {Nat. Commun.},
abstract = {Increasing numbers of protein interactions have been identified in high-throughput experiments, but only a small proportion have solved structures. Recently, sequence coevolution-based approaches have led to a breakthrough in predicting monomer protein structures and protein interaction interfaces. Here we address the challenges of large-scale interaction prediction at residue resolution with a fast alignment concatenation method and a probabilistic score for the interaction of residues. Importantly, this method (EVcomplex2) is able to assess the likelihood of a protein interaction, as we show here applied to large-scale experimental datasets where the pairwise interactions are unknown. We predict 504 interactions de novo in the E. coli membrane proteome, including 243 that are newly discovered. While EVcomplex2 does not require available structures, coevolving residue pairs can be used to produce structural models of protein interactions, as done here for membrane complexes including the Flagellar Hook-Filament Junction and the Tol/Pal complex.
Increasing numbers of protein interactions have been identified in high-throughput experiments, but only a small proportion have solved structures. Recently, sequence coevolution-based approaches have led to a breakthrough in predicting monomer protein structures and protein interaction interfaces. Here we address the challenges of large-scale interaction prediction at residue resolution with a fast alignment concatenation method and a probabilistic score for the interaction of residues. Importantly, this method (EVcomplex2) is able to assess the likelihood of a protein interaction, as we show here applied to large-scale experimental datasets where the pairwise interactions are unknown. We predict 504 interactions de novo in the E. coli membrane proteome, including 243 that are newly discovered. While EVcomplex2 does not require available structures, coevolving residue pairs can be used to produce structural models of protein interactions, as done here for membrane complexes including the Flagellar Hook-Filament Junction and the Tol/Pal complex.
@article{EVComplex_NatComm_2020,
title = {Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences},
author = {Anna Green and Hadeer Elhabashy and Kelly Brock and Rohan Maddamsetti and Oliver Kohlbacher and Debora S. Marks},
journal = {Nat. Commun.},
keywords = {},
pubstate = {forthcoming},
tppubtype = {article}
}
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