3 Search Results for "Lenhof, Hans-Peter"

Document
DOI: 10.4230/LIPIcs.STACS.2025.64
Cluster Editing on Cographs and Related Classes

Authors: Manuel Lafond, Alitzel López Sánchez, and Weidong Luo

Published in: LIPIcs, Volume 327, 42nd International Symposium on Theoretical Aspects of Computer Science (STACS 2025)

Abstract
In the Cluster Editing problem, sometimes known as (unweighted) Correlation Clustering, we must insert and delete a minimum number of edges to achieve a graph in which every connected component is a clique. Owing to its applications in computational biology, social network analysis, machine learning, and others, this problem has been widely studied for decades and is still undergoing active research. There exist several parameterized algorithms for general graphs, but little is known about the complexity of the problem on specific classes of graphs. Among the few important results in this direction, if only deletions are allowed, the problem can be solved in polynomial time on cographs, which are the P₄-free graphs. However, the complexity of the broader editing problem on cographs is still open. We show that even on a very restricted subclass of cographs, the problem is NP-hard, W[1]-hard when parameterized by the number p of desired clusters, and that time n^o(p/log p) is forbidden under the ETH. This shows that the editing variant is substantially harder than the deletion-only case, and that hardness holds for the many superclasses of cographs (including graphs of clique-width at most 2, perfect graphs, circle graphs, permutation graphs). On the other hand, we provide an almost tight upper bound of time n^O(p), which is a consequence of a more general n^O(cw⋅p) time algorithm, where cw is the clique-width. Given that forbidding P₄s maintains NP-hardness, we look at {P₄, C₄}-free graphs, also known as trivially perfect graphs, and provide a cubic-time algorithm for this class.
Cite as

Manuel Lafond, Alitzel López Sánchez, and Weidong Luo. Cluster Editing on Cographs and Related Classes. In 42nd International Symposium on Theoretical Aspects of Computer Science (STACS 2025). Leibniz International Proceedings in Informatics (LIPIcs), Volume 327, pp. 64:1-64:21, Schloss Dagstuhl – Leibniz-Zentrum für Informatik (2025)

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@InProceedings{lafond_et_al:LIPIcs.STACS.2025.64,
  author =	{Lafond, Manuel and L\'{o}pez S\'{a}nchez, Alitzel and Luo, Weidong},
  title =	{{Cluster Editing on Cographs and Related Classes}},
  booktitle =	{42nd International Symposium on Theoretical Aspects of Computer Science (STACS 2025)},
  pages =	{64:1--64:21},
  series =	{Leibniz International Proceedings in Informatics (LIPIcs)},
  ISBN =	{978-3-95977-365-2},
  ISSN =	{1868-8969},
  year =	{2025},
  volume =	{327},
  editor =	{Beyersdorff, Olaf and Pilipczuk, Micha{\l} and Pimentel, Elaine and Thắng, Nguy\~{ê}n Kim},
  publisher =	{Schloss Dagstuhl -- Leibniz-Zentrum f{\"u}r Informatik},
  address =	{Dagstuhl, Germany},
  URL =		{https://drops.dagstuhl.de/entities/document/10.4230/LIPIcs.STACS.2025.64},
  URN =		{urn:nbn:de:0030-drops-228895},
  doi =		{10.4230/LIPIcs.STACS.2025.64},
  annote =	{Keywords: Cluster editing, cographs, parameterized algorithms, clique-width, trivially perfect graphs}
}
Document
DOI: 10.4230/OASIcs.GCB.2013.56
Efficient Interpretation of Tandem Mass Tags in Top-Down Proteomics

Authors: Anna Katharina Hildebrandt, Ernst Althaus, Hans-Peter Lenhof, Chien-Wen Hung, Andreas Tholey, and Andreas Hildebrandt

Published in: OASIcs, Volume 34, German Conference on Bioinformatics 2013

Abstract
Mass spectrometry is the major analytical tool for the identification and quantification of proteins in biological samples. In so-called top-down proteomics, separation and mass spectrometric analysis is performed at the level of intact proteins, without preparatory digestion steps. It has been shown that the tandem mass tag (TMT) labeling technology, which is often used for quantification based on digested proteins (bottom-up studies), can be applied in top-down proteomics as well. This, however, leads to a complex interpretation problem, where we need to annotate measured peaks with their respective generating protein, the number of charges, and the a priori unknown number of TMT-groups attached to this protein. In this work, we give an algorithm for the efficient enumeration of all valid annotations that fulfill available experimental constraints. Applying the algorithm to real-world data, we show that the annotation problem can indeed be efficiently solved. However, our experiments also demonstrate that reliable annotation in complex mixtures requires at least partial sequence information and high mass accuracy and resolution to go beyond the proof-of-concept stage.
Cite as

Anna Katharina Hildebrandt, Ernst Althaus, Hans-Peter Lenhof, Chien-Wen Hung, Andreas Tholey, and Andreas Hildebrandt. Efficient Interpretation of Tandem Mass Tags in Top-Down Proteomics. In German Conference on Bioinformatics 2013. Open Access Series in Informatics (OASIcs), Volume 34, pp. 56-67, Schloss Dagstuhl – Leibniz-Zentrum für Informatik (2013)

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@InProceedings{hildebrandt_et_al:OASIcs.GCB.2013.56,
  author =	{Hildebrandt, Anna Katharina and Althaus, Ernst and Lenhof, Hans-Peter and Hung, Chien-Wen and Tholey, Andreas and Hildebrandt, Andreas},
  title =	{{Efficient Interpretation of Tandem Mass Tags in Top-Down Proteomics}},
  booktitle =	{German Conference on Bioinformatics 2013},
  pages =	{56--67},
  series =	{Open Access Series in Informatics (OASIcs)},
  ISBN =	{978-3-939897-59-0},
  ISSN =	{2190-6807},
  year =	{2013},
  volume =	{34},
  editor =	{Bei{\ss}barth, Tim and Kollmar, Martin and Leha, Andreas and Morgenstern, Burkhard and Schultz, Anne-Kathrin and Waack, Stephan and Wingender, Edgar},
  publisher =	{Schloss Dagstuhl -- Leibniz-Zentrum f{\"u}r Informatik},
  address =	{Dagstuhl, Germany},
  URL =		{https://drops.dagstuhl.de/entities/document/10.4230/OASIcs.GCB.2013.56},
  URN =		{urn:nbn:de:0030-drops-42304},
  doi =		{10.4230/OASIcs.GCB.2013.56},
  annote =	{Keywords: Mass spectrometry, TMT labeling, Top-down Proteomics}
}
Document
DOI: 10.4230/DagSemProc.05471.8
Glycosylation Patterns of Proteins Studied by Liquid Chromatography-Mass Spectrometry and Bioinformatic Tools

Authors: Hansjörg Toll, Peter Berger, Andreas Hofmann, Andreas Hildebrandt, Herbert Oberacher, Hans Peter Lenhof, and Christian G. Huber

Published in: Dagstuhl Seminar Proceedings, Volume 5471, Computational Proteomics (2006)

Abstract
Due to their extensive structural heterogeneity, the elucidation of glycosylation patterns in glycoproteins such as the subunits of chorionic gonadotropin (CG), CG-alpha and CG-beta remains one of the most challenging problems in the proteomic analysis of posttranslational modifications. In consequence, glycosylation is usually studied after decomposition of the intact proteins to the proteolytic peptide level. However, by this approach all information about the combination of the different glycopeptides in the intact protein is lost. In this study we have, therefore, attempted to combine the results of glycan identification after tryptic digestion with molecular mass measurements on the intact glycoproteins. Despite the extremely high number of possible combinations of the glycans identified in the tryptic peptides by high-performance liquid chromatography-mass spectrometry (> 1000 for CG-alpha and > 10.000 for CG-beta), the mass spectra of intact CG-alpha and CG-beta revealed only a limited number of glycoforms present in CG preparations from pools of pregnancy urines. Peak annotations for CG-alpha were performed with the help of an algorithm that generates a database containing all possible modifications of the proteins (inclusive possible artificial modifications such as oxidation or truncation) and subsequent searches for combinations fitting the mass difference between the polypeptide backbone and the measured molecular masses. Fourteen different glycoforms of CG-alpha, including methionine-oxidized and N-terminally truncated forms, were readily identified. For CG-beta, however, the relatively high mass accuracy of ± 2 Da was still insufficient to unambiguously assign the possible combinations of posttranslational modifications. Finally, the mass spectrometric fingerprints of the intact molecules were shown to be very useful for the characterization of glycosylation patterns in different CG preparations.
Cite as

Hansjörg Toll, Peter Berger, Andreas Hofmann, Andreas Hildebrandt, Herbert Oberacher, Hans Peter Lenhof, and Christian G. Huber. Glycosylation Patterns of Proteins Studied by Liquid Chromatography-Mass Spectrometry and Bioinformatic Tools. In Computational Proteomics. Dagstuhl Seminar Proceedings, Volume 5471, pp. 1-6, Schloss Dagstuhl – Leibniz-Zentrum für Informatik (2006)

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@InProceedings{toll_et_al:DagSemProc.05471.8,
  author =	{Toll, Hansj\"{o}rg and Berger, Peter and Hofmann, Andreas and Hildebrandt, Andreas and Oberacher, Herbert and Lenhof, Hans Peter and Huber, Christian G.},
  title =	{{Glycosylation Patterns of Proteins Studied by Liquid Chromatography-Mass Spectrometry and Bioinformatic Tools}},
  booktitle =	{Computational Proteomics},
  pages =	{1--6},
  series =	{Dagstuhl Seminar Proceedings (DagSemProc)},
  ISSN =	{1862-4405},
  year =	{2006},
  volume =	{5471},
  editor =	{Christian G. Huber and Oliver Kohlbacher and Knut Reinert},
  publisher =	{Schloss Dagstuhl -- Leibniz-Zentrum f{\"u}r Informatik},
  address =	{Dagstuhl, Germany},
  URL =		{https://drops.dagstuhl.de/entities/document/10.4230/DagSemProc.05471.8},
  URN =		{urn:nbn:de:0030-drops-5431},
  doi =		{10.4230/DagSemProc.05471.8},
  annote =	{Keywords: Liquid chromatography, mass spectrometry, glycoproteins, glycosylation, peak annotation}
}
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