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Article ; Online: Management of Patients Undergoing CAR-T Cell Therapy in Germany.

Penack, Olaf / Dreger, Peter / Ajib, Salem / Ayuk, Francis / Baermann, Ben-Niklas / Bug, Gesine / Kriege, Oliver / Jentzsch, Madlen / Kobbe, Guido / Koenecke, Christian / Lutz, Mathias / Martin, Sonja / Schlegel, Paul-Gerhard / Schroers, Roland / von Tresckow, Bastian / Vucinic, Vladan / Subklewe, Marion / Bethge, Wolfgang / Wolff, Daniel

Oncology research and treatment

2024 Volume 47, Issue 3, Page(s) 65–75

Abstract: Introduction: Chimeric antigen receptor positive T cell (CAR-T cell) treatment became standard therapy for relapsed or refractory hematologic malignancies, such as non-Hodgkin's lymphoma and multiple myeloma. Owing to the rapidly progressing field of ... ...

Abstract	Introduction: Chimeric antigen receptor positive T cell (CAR-T cell) treatment became standard therapy for relapsed or refractory hematologic malignancies, such as non-Hodgkin's lymphoma and multiple myeloma. Owing to the rapidly progressing field of CAR-T cell therapy and the lack of generally accepted treatment guidelines, we hypothesized significant differences between centers in the prevention, diagnosis, and management of short- and long-term complications. Methods: To capture the current CAR-T cell management among German centers to determine the medical need and specific areas for future clinical research, the DAG-HSZT (Deutsche Arbeitsgemeinschaft für Hämatopoetische Stammzelltransplantation und Zelluläre Therapie; German Working Group for Hematopoietic Stem Cell Transplantation and Cellular Therapy) performed a survey among 26 German CAR-T cell centers. Results: We received answers from 17 centers (65%). The survey documents the relevance of evidence in the CAR-T cell field with a homogeneity of practice in areas with existing clinical evidence. In contrast, in areas with no - or low quality - clinical evidence, we identified significant variety in management in between the centers: management of cytokine release syndrome, immune effector cell-related neurotoxicity syndrome, IgG substitution, autologous stem cell backups, anti-infective prophylaxis, and vaccinations. Conclusion: The results indicate the urgent need for better harmonization of supportive care in CAR-T cell therapies including clinical research to improve clinical outcome.
MeSH term(s)	Humans ; Receptors, Chimeric Antigen ; Immunotherapy, Adoptive ; Germany ; Patients ; Cell- and Tissue-Based Therapy
Chemical Substances	Receptors, Chimeric Antigen
Language	English
Publishing date	2024-01-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2760274-6
ISSN	2296-5262 ; 2296-5270
ISSN (online)	2296-5262
ISSN	2296-5270
DOI	10.1159/000536201
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Article ; Online: PTCy versus ATG as graft-versus-host disease prophylaxis in mismatched unrelated stem cell transplantation.

Penack, Olaf / Abouqateb, Mouad / Peczynski, Christophe / Boreland, William / Gülbas, Zafer / Gedde-Dahl, Tobias / Castilla-Llorente, Cristina / Kröger, Nicolaus / Eder, Mathias / Rambaldi, Alessandro / Bonifazi, Francesca / Blau, Igor Wolfgang / Stelljes, Matthias / Dreger, Peter / Moiseev, Ivan / Schoemans, Hélène / Koenecke, Christian / Peric, Zinaida

Blood cancer journal

2024 Volume 14, Issue 1, Page(s) 45

Abstract: There is an increased risk of GVHD and of non-relapse mortality (NRM) after allogeneic stem cell transplantations (alloSCT) when mismatched unrelated donors (MMUD) are used. In Europe, it is standard practice to use rabbit anti-thymocyte globulin (rATG) ... ...

Abstract	There is an increased risk of GVHD and of non-relapse mortality (NRM) after allogeneic stem cell transplantations (alloSCT) when mismatched unrelated donors (MMUD) are used. In Europe, it is standard practice to use rabbit anti-thymocyte globulin (rATG) to reduce the high NRM and GVHD risks after MMUD alloSCT. As an alternative to rATG, post-transplantation Cyclophosphamide (PTCy) is in increasing clinical use. It is currently impossible to give general recommendations regarding preference for one method over another since comparative evidence from larger data sets is lacking. To improve the evidence base, we analyzed the outcome of rATG vs. PTCy prophylaxis in adult patients with hematologic malignancies undergoing first peripheral blood alloSCT from MMUD (9/10 antigen match) between Jan 2018 and June 2021 in the database of the European Society for Blood and Marrow Transplantation (EBMT). We performed multivariate analyses using the Cox proportional-hazards regression model. We included 2123 patients in the final analyses (PTCy, n = 583; rATG, n = 1540). p values and hazard ratios (HR) presented here are multivariate outcomes. Two years after alloSCT we found a lower NRM in the PTCy group of 18% vs. 24.9% in the rATG group; p = 0.028, HR 0.74. Overall survival in the PTCy cohort was higher with 65.7% vs. 55.7% in the rATG cohort; p < 0.001, HR 0.77. Progression-free survival was also better in the PTCy patients with 59.1% vs. 48.8% when using rATG; p = 0.001, 0.78. The incidences of chronic GVHD and acute GVHD were not significantly different between the groups. We found significantly lower NRM as well as higher survival in recipients of peripheral blood alloSCTs from MMUD receiving PTCy as compared to rATG. The results of the current analysis suggest an added value of PTCy as GVHD prophylaxis in MMUD alloSCT.
MeSH term(s)	Adult ; Humans ; Neoplasm Recurrence, Local/drug therapy ; Hematopoietic Stem Cell Transplantation/adverse effects ; Hematopoietic Stem Cell Transplantation/methods ; Cyclophosphamide/therapeutic use ; Graft vs Host Disease/etiology ; Graft vs Host Disease/prevention & control ; Antilymphocyte Serum/therapeutic use ; Unrelated Donors ; Retrospective Studies
Chemical Substances	Cyclophosphamide (8N3DW7272P) ; Antilymphocyte Serum
Language	English
Publishing date	2024-03-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2600560-8
ISSN	2044-5385 ; 2044-5385
ISSN (online)	2044-5385
ISSN	2044-5385
DOI	10.1038/s41408-024-01032-8
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Article: Emerging strategies in mass-spectrometry based proteomics.

Dreger, Mathias

European journal of biochemistry

2002 Volume 270, Issue 4, Page(s) 569

MeSH term(s)	Animals ; Humans ; Mass Spectrometry/methods ; Proteomics
Language	English
Publishing date	2002-08-09
Publishing country	England
Document type	Editorial
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1046/j.1432-1033.2003.03439.x
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Article: Subcellular proteomics.

Dreger, Mathias

Mass spectrometry reviews

2003 Volume 22, Issue 1, Page(s) 27–56

Abstract: The step from the analysis of the genome to the analysis of the proteome is not just a matter of numerical complexity in terms of variants of gene products that can arise from a single gene. A significant further level of complexity is introduced by the ... ...

Abstract	The step from the analysis of the genome to the analysis of the proteome is not just a matter of numerical complexity in terms of variants of gene products that can arise from a single gene. A significant further level of complexity is introduced by the supramolecular organization of gene products because of protein-protein interactions or targeting of proteins to specific subcellular structures. There is currently no single proteome analysis strategy that can sufficiently address all levels of the organization of the proteome. To approach an appropriate analytical complement for the interrogation of the proteome at all of the levels at which it is organized, there emerges the need for a whole arsenal of proteomics strategies. The proteome analysis at the level of subcellular structures (that can be enriched by subcellular fractionation) represents an analytical strategy that combines classic biochemical fractionation methods and tools for the comprehensive identification of proteins. Among the key potentials of this strategy is the capability to screen not only for previously unknown gene products but also to assign them, along with other known, but poorly characterized gene products, to particular subcellular structures. Furthermore, the analysis at the subcellular level is a prerequisite for the detection of important regulatory events such as protein translocation in comparative studies. This review is meant to give an overview on recent key studies in the field of proteome analysis at the level of subcellular structures, and to highlight potentials and requirements.
MeSH term(s)	Animals ; Cells/cytology ; Cells/metabolism ; Humans ; Organelles/physiology ; Proteome ; Proteomics/methods ; Subcellular Fractions
Chemical Substances	Proteome
Language	English
Publishing date	2003-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1491946-1
ISSN	1098-2787 ; 0277-7037
ISSN (online)	1098-2787
ISSN	0277-7037
DOI	10.1002/mas.10047
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Article: Proteome analysis at the level of subcellular structures.

Dreger, Mathias

European journal of biochemistry

2002 Volume 270, Issue 4, Page(s) 589–599

Abstract: The targeting of proteins to particular subcellular sites is an important principle of the functional organization of cells at the molecular level. In turn, knowledge about the subcellular localization of a protein is a characteristic that may provide a ... ...

Abstract	The targeting of proteins to particular subcellular sites is an important principle of the functional organization of cells at the molecular level. In turn, knowledge about the subcellular localization of a protein is a characteristic that may provide a hint as to the function of the protein. The combination of classic biochemical fractionation techniques for the enrichment of particular subcellular structures with the large-scale identification of proteins by mass spectrometry and bioinformatics provides a powerful strategy that interfaces cell biology and proteomics, and thus is termed 'subcellular proteomics'. In addition to its exceptional power for the identification of previously unknown gene products, the analysis of proteins at the subcellular level is the basis for monitoring important aspects of dynamic changes in the proteome such as protein transloction. This review summarizes data from recent subcellular proteomics studies with an emphasis on the type of data that can retrieved from such studies depending on the design of the analytical strategy.
MeSH term(s)	Animals ; Computational Biology ; Humans ; Mass Spectrometry ; Peptide Mapping ; Proteins/analysis ; Proteome/analysis ; Proteomics ; Subcellular Fractions/chemistry
Chemical Substances	Proteins ; Proteome
Language	English
Publishing date	2002-08-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1046/j.1432-1033.2003.03426.x
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Article ; Online: Are meaningful predictions of toxicological outcomes in clinical trials based on in vitro diagnostics of preclinical drug candidates possible?

Kroll, Friedrich / Dreger, Mathias

Future medicinal chemistry

2010 Volume 2, Issue 11, Page(s) 1613–1617

MeSH term(s)	Clinical Trials as Topic ; Drug Discovery ; Drug Evaluation, Preclinical ; Drug-Related Side Effects and Adverse Reactions ; Genomics ; Humans ; Metabolomics ; Models, Molecular ; Pharmaceutical Preparations/metabolism ; Proteins/chemistry ; Proteins/metabolism ; Proteomics ; Toxicology ; Treatment Outcome
Chemical Substances	Pharmaceutical Preparations ; Proteins
Language	English
Publishing date	2010-11
Publishing country	England
Document type	Editorial
ISSN	1756-8927
ISSN (online)	1756-8927
DOI	10.4155/fmc.10.245
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Article ; Online: Autologous transplant of follicular lymphoma in the era of rituximab.

Witzens-Harig, Mathias / Dreger, Peter

Leukemia & lymphoma

2010 Volume 51, Issue 6, Page(s) 967–974

Abstract: In advanced follicular lymphoma (FL), autologous stem cell transplant (ASCT) has been studied extensively in an attempt to prolong remission duration and, possibly, achieve ultimate cure. However, increasing evidence of the benefit of rituximab and ... ...

Abstract	In advanced follicular lymphoma (FL), autologous stem cell transplant (ASCT) has been studied extensively in an attempt to prolong remission duration and, possibly, achieve ultimate cure. However, increasing evidence of the benefit of rituximab and various other new drugs has questioned the appropriate place of ASCT in the treatment algorithm of FL in recent years. The purpose of this overview is to propose a definition of the potential role of ASCT in the treatment armamentarium of FL in the light of these new treatment options. Taken together, the absence of an overall survival benefit, the risk of secondary malignancies, and the remarkably good prognosis of patients who receive rituximab and ASCT as salvage therapy in the relapse situation make the use of ASCT as initial therapy difficult to justify. In contrast, evidence is accumulating that, in eligible patients with relapsed FL, rituximab-based chemotherapy followed by ASCT might provide superior disease control in comparison to either modality alone, and has curative potential in a subset of patients. However, these considerations are largely based on retrospective analyses and should be confirmed in prospective randomized trials.
MeSH term(s)	Antibodies, Monoclonal/therapeutic use ; Antibodies, Monoclonal, Murine-Derived ; Combined Modality Therapy ; Disease-Free Survival ; Hematopoietic Stem Cell Transplantation/methods ; Humans ; Lymphoma, Follicular/therapy ; Prognosis ; Rituximab ; Salvage Therapy ; Transplantation, Autologous ; Treatment Outcome
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Monoclonal, Murine-Derived ; Rituximab (4F4X42SYQ6)
Language	English
Publishing date	2010-04-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1042374-6
ISSN	1029-2403 ; 1042-8194
ISSN (online)	1029-2403
ISSN	1042-8194
DOI	10.3109/10428191003793341
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Article ; Online: Profiling of methyltransferases and other S-Adenosyl-L-homocysteine-binding proteins by Capture Compound mass spectrometry.

Lenz, Thomas / Poot, Peter / Weinhold, Elmar / Dreger, Mathias

Methods in molecular biology (Clifton, N.J.)

2012 Volume 803, Page(s) 97–125

Abstract: There is a variety of approaches to reduce the complexity of the proteome on the basis of functional small molecule-protein interactions. We describe a generic approach based on trifunctional Capture Compounds, in which the initial equilibrium-driven ... ...

Abstract	There is a variety of approaches to reduce the complexity of the proteome on the basis of functional small molecule-protein interactions. We describe a generic approach based on trifunctional Capture Compounds, in which the initial equilibrium-driven interaction between a small molecule probe and target proteins is irreversibly fixed upon photo-crosslinking between an independent photo-activable reactivity function of the Capture Compound and the surface of the target protein(s). Subsequently, Capture Compound - protein conjugates are isolated from complex biological mixtures via the sorting function of the Capture Compound. Here, we describe the application of a trifunctional Capture Compound that carries the methyltransferase product inhibitor S-Adenosyl-L -homocysteine as the selectivity function for the isolation of methyltransferases from a complex lysate of Escherichia coli DH5α cells. Photo-activated crosslinking enhances yield and sensitivity of the experiment, and the specificity can be readily tested for in competition experiments using an excess of free S-Adenosyl-L -homocysteine.
MeSH term(s)	Automation ; Chromatography, Liquid ; Databases, Protein ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/enzymology ; Mass Spectrometry/methods ; Methyltransferases/metabolism ; Nanotechnology ; Peptides/chemistry ; Peptides/isolation & purification ; Protein Binding ; S-Adenosylhomocysteine/metabolism ; Silver Staining ; Trypsin/metabolism
Chemical Substances	Peptides ; S-Adenosylhomocysteine (979-92-0) ; Methyltransferases (EC 2.1.1.-) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-61779-364-6_8
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Book ; Online ; Thesis: Analyse posttranslationaler Modifikationen von Kernhüllenproteinen

Dreger, Mathias

1999

Author's details	vorgelegt von Mathias Dreger
Keywords	Phosphorylierung ; Tyrosin ; Proteine ; Kernhülle ; Photoionisationsmassenspektrometrie ; Matrix-unterstützte Laser-Desorption
Language	German
Size	Online-Ressource
Edition	[Elektronische Ressource]
Document type	Book ; Online ; Thesis
Thesis / German Habilitation thesis	Freie Univ., Diss--Berlin, 1999
Note	Dateiformat: zip, Dateien im PDF-Format
Database	Former special subject collection: coastal and deep sea fishing

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Article ; Online: Probing small molecule-protein interactions: A new perspective for functional proteomics.

Lenz, Thomas / Fischer, Jenny J / Dreger, Mathias

Journal of proteomics

2011 Volume 75, Issue 1, Page(s) 100–115

Abstract: The isolation of proteome subsets on the basis of the interactions of small molecules with proteins is an emerging paradigm in proteomics. Depending on the nature of the small molecule used as a bait, entire protein families can be monitored in ... ...

Abstract	The isolation of proteome subsets on the basis of the interactions of small molecules with proteins is an emerging paradigm in proteomics. Depending on the nature of the small molecule used as a bait, entire protein families can be monitored in biological samples, or new functions can be attributed to previously uncharacterized proteins. With pharmaceutical compounds as baits, drug targets and toxicity-relevant off-targets can be discovered in an unbiased proteomic screen. At the heart of this strategy are synthetic bi- or trifunctional small molecule probes. These probes carry the small molecules of interest as baits (selectivity function), as well as a sorting function for the isolation of small molecule-protein complexes or conjugates from complex protein mixtures. In some designs, a covalent linkage of the bound protein to the probe is established through a separate reactivity function or a combined selectivity/reactivity function. The covalent linkage allows for isolation or detection of probe-protein conjugates also under harsh or denaturing conditions. Ultimately, specifically isolated proteins are commonly identified by mass spectrometry. This review summarizes probe designs, workflows, and published applications of the three dominant approaches in the field, namely affinity pulldown, activity-based protein profiling, and Capture Compound Mass Spectrometry.
MeSH term(s)	Animals ; Gene Expression Profiling/methods ; Humans ; Mass Spectrometry/methods ; Proteins/analysis ; Proteins/chemistry ; Proteins/metabolism ; Proteomics/methods ; Small Molecule Libraries/analysis ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/metabolism
Chemical Substances	Proteins ; Small Molecule Libraries
Language	English
Publishing date	2011-12-10
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2011.07.017
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