Michael G. Weller

Federal Institute For Materials Research and Testing

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Reinhard Nießner

Technical University of Munich

U. Leiterer

German Meteorological Service

Georg Tscheuschner

Federal Institute For Materials Research and Testing

Martin Paul

Innovations for High Performance Microelectronics

Ulrich Pöschl

Max Planck Institute for Chemistry

Rudolf J. Schneider

Federal Institute For Materials Research and Testing

Ulrich Panne

Federal Institute For Materials Research and Testing

Timm Schwaar

Federal Institute For Materials Research and Testing

Knut Rurack

Federal Institute For Materials Research and Testing

Jule L. Völzke

Federal Institute For Materials Research and Testing

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Federal Institute For Materials Research and Testing

109

Technical University of Munich

Humboldt-Universität zu Berlin

University of Zurich

Freie Universität Berlin

University Hospital of Zurich

Charité - Universitätsmedizin Berlin

Istituti di Ricovero e Cura a Carattere Scientifico

University of Tübingen

Max Planck Institute for Chemistry

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Development of a Direct Competitive Microcystin Immunoassay of Broad Specificity

Analytical Sciences (2001)

Michael G. Weller Anne Zeck Anja Eikenberg Satoshi Nagata Yoshio Ueno

10.2116/analsci.17.1445

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Citations (34)

Characterization of a monoclonal TNT-antibody by measurement of the cross-reactivities of nitroaromatic compounds

Fresenius Journal of Analytical Chemistry (1999)

Anne Zeck Michael G. Weller Reinhard Nießner

Trinitrotoluene

Reactivity

Cross-reactivity

10.1007/s002160051309

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Citations (72)

Comprehensive evaluation of peptide de novo sequencing tools for monoclonal antibody assembly

Briefings in Bioinformatics (2022)

Denis Beslic Georg Tscheuschner Bernhard Y. Renard Michael G. Weller Thilo Muth

Abstract Monoclonal antibodies are biotechnologically produced proteins with various applications in research, therapeutics and diagnostics. Their ability to recognize and bind to specific molecule structures makes them essential research tools and therapeutic agents. Sequence information of antibodies is helpful for understanding antibody–antigen interactions and ensuring their affinity and specificity. De novo protein sequencing based on mass spectrometry is a valuable method to obtain the amino acid sequence of peptides and proteins without a priori knowledge. In this study, we evaluated six recently developed de novo peptide sequencing algorithms (Novor, pNovo 3, DeepNovo, SMSNet, PointNovo and Casanovo), which were not specifically designed for antibody data. We validated their ability to identify and assemble antibody sequences on three multi-enzymatic data sets. The deep learning-based tools Casanovo and PointNovo showed an increased peptide recall across different enzymes and data sets compared with spectrum-graph-based approaches. We evaluated different error types of de novo peptide sequencing tools and their performance for different numbers of missing cleavage sites, noisy spectra and peptides of various lengths. We achieved a sequence coverage of 97.69–99.53% on the light chains of three different antibody data sets using the de Bruijn assembler ALPS and the predictions from Casanovo. However, low sequence coverage and accuracy on the heavy chains demonstrate that complete de novo protein sequencing remains a challenging issue in proteomics that requires improved de novo error correction, alternative digestion strategies and hybrid approaches such as homology search to achieve high accuracy on long protein sequences.

Sequence assembly

Protein methods

Sequence (biology)

10.1093/bib/bbac542

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Citations (38)

Referee Report 06 March 2017

Michael G. Weller

This article is a valuable and welcome contribution to the ongoing discussion of antibody quality. The suggestion of a two-tier approach is helpful to distinguish between simple descriptive data and the validation of an antibody for a specified application.

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A heterogeneous immunoassay for the determination of triazine herbicides in water

Fresenius Journal of Analytical Chemistry (1991)

L. Weil Rudolf J. Schneider O. Sch�fer Petra Ulrich Michael G. Weller

Triazine

10.1007/bf00323800

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Citations (16)

Tetranuclear Cu(I) thiolate complexes in relation to the metal bonding site of yeast copperthionein

Inorganica Chimica Acta (1983)

Margot Linss Michael G. Weller Ulrich Weser

Cubane

Perchlorate

Adamantane

10.1016/s0020-1693(00)91283-0

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Citations (6)

Ferric Nitrilotriacetate: An Active Centre Analogue of Pyrocatechase

Springer eBooks (1983)

Michael G. Weller

Catechol

Cleavage (geology)

Muconic acid

FERRIC IRON

10.1007/978-94-009-7049-6_24

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Citations (1)

Trendbericht Analytische Chemie 2000/2001

Nachrichten aus der Chemie (2002)

Reinhard Nießner J. A. C. Broekaert Jürgen W. Einax Hendrik Emons W. Engewald

Abstract Enzymatische und immunchemische Verfahren sowie Chemo‐ und Biosensoren präsentiert der abschließende Teil des Trendberichts zur den wichtigsten Fortschritten in der Analytik der vergangenen zwei Jahre, Teil 1 beginnt auf Seite 455.

10.1002/nadc.20020500418

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Citations (1)

Jeanette M. Van Emon (Ed.): Immunoassay and other bioanalytical techniques

Analytical and Bioanalytical Chemistry (2007)

Michael G. Weller

Bioanalysis

10.1007/s00216-007-1591-6

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Digging into the Sequential Space of Thiolactone Precision Polymers: A Combinatorial Strategy to Identify Functional Domains

Angewandte Chemie International Edition (2018)

Sensu Celasun Dario Remmler Timm Schwaar Michael G. Weller Filip Du Prez

Functional sequences of precision polymers based on thiolactone/Michael chemistry are identified from a large one-bead one-compound library. Single-bead readout by MALDI-TOF MS/MS identifies sequences that host m-THPC that is a second generation photo-sensitizer drug. The corresponding Tla/Michael-PEG conjugates make m-THPC available in solution and drug payload as well as drug release kinetics can be fine-tuned by the precision segment.

Digging

Thiolactone

10.1002/anie.201810393

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Citations (46)