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  1. Book ; Online: Characterization of aerosol over the Eastern Mediterranean by polarization sensitive Raman lidar measurements during A-LIFE – aerosol type classification and type separation

    Groß, Silke / Freudenthaler, Volker / Haarig, Moritz / Ansmann, Albert / Toledano, Carlos / Mateos, David / Seibert, Petra / Mamouri, Rodanthi-Elisavet / Nisantzi, Argyro / Gasteiger, Josef / Dollner, Maximilian / Tipka, Anne / Schöberl, Manuel / Teri, Marilena / Weinzierl, Bernadett

    eISSN:

    2024  

    Abstract: Aerosols are key players in the Earth’s climate system with mineral dust being one major component of the atmospheric aerosol load. While former campaigns focused on investigating the properties and effects of rather pure mineral dust layers, the A-LIFE ( ...

    Abstract Aerosols are key players in the Earth’s climate system with mineral dust being one major component of the atmospheric aerosol load. While former campaigns focused on investigating the properties and effects of rather pure mineral dust layers, the A-LIFE ( A bsorbing aerosol layers in a changing climate: aging, life time and dynamics) campaign in April 2017 aimed to characterize dust in complex aerosol mixtures. In this study we present ground-based lidar measurements that were performed at Limassol, Cyprus, in April 2017. During our measurement period, the measurement site was affected by complex mixtures of dust from different sources and pollution aerosols from local sources as well as long-range transported. We found mean values of the particle linear depolarization ratio and extinction-to-backscatter ratio (lidar ratio) of 0.27 ± 0.02 and 41 sr ± 5 sr at 355 nm and of 0.30 ± 0.02 and 39 sr ± 5 sr at 532 nm for Arabian dust, and of 0.27 ± 0.02 and 55 sr ± 8 sr at 355 nm and of 0.28 ± 0.02 and 53 sr ± 7 sr at 532 nm for Saharan dust. The values found for pollution aerosols of the particle linear depolarization ratio and the lidar ratio are 0.05 ± 0.02 at 355 nm and 0.04 ± 0.02 at 532 nm, and 65 sr ± 12 sr at 355 nm and 60 sr ± 16 sr at 532 nm, respectively. We use our measurements for aerosol typing and compare that to aerosol typing from sun photometer data, in-situ measurements and trajectory analysis. The different methods agree well for the derived aerosol type, but looking at the derived dust mass concentration from different methods, the trajectory analysis frequently underestimate high dust concentration that were found in major mineral dust events.
    Subject code 333
    Language English
    Publishing date 2024-01-18
    Publishing country de
    Document type Book ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Humanized Monoclonal Antibody Blocking Carbonic Anhydrase 12 Enzymatic Activity Leads to Reduced Tumor Growth

    Uda, Narasimha Rao / Stenner, Frank / Seibert, Volker / Herzig, Petra / Markuly, Norbert / VAN Dijk, Marc / Zippelius, Alfred / Renner, Christoph

    Anticancer research

    2019  Volume 39, Issue 8, Page(s) 4117–4128

    Abstract: Background/aim: Carbonic anhydrase 12 (CA12) is a membrane-associated enzyme that is highly expressed on many human cancers. It is a poor prognostic marker and hence an attractive target for cancer therapy. This study aimed to develop a humanized CA12- ... ...

    Abstract Background/aim: Carbonic anhydrase 12 (CA12) is a membrane-associated enzyme that is highly expressed on many human cancers. It is a poor prognostic marker and hence an attractive target for cancer therapy. This study aimed to develop a humanized CA12-antibody with anti-cancer activity.
    Materials and methods: Antibody libraries were constructed and screened by the Retrocyte display®. Antibody binding and blocking properties were determined by ELISA, flow cytometry and enzymatic activity assays. Spheroid viability was determined by Cell-Titer-Fluor assay.
    Results: We developed a novel humanized CA12-specific antibody, 4AG4, which recognized CA12 as an antigen and blocked CA12 enzymatic activity. Our humanized CA12-antibody significantly inhibited spheroid growth of lung adenocarcinoma A549-cells in vitro by blocking CA12 enzymatic activity. Similar anti-tumor effects were recapitulated with CA12-gene knockout of A549-cells.
    Conclusion: Our newly identified humanized CA12-antibody with anti-cancer activity, represents a new tool for the treatment of CA12-positive tumors.
    MeSH term(s) A549 Cells ; Adenocarcinoma of Lung/drug therapy ; Adenocarcinoma of Lung/genetics ; Adenocarcinoma of Lung/immunology ; Adenocarcinoma of Lung/pathology ; Antibodies, Monoclonal, Humanized/immunology ; Antibodies, Monoclonal, Humanized/pharmacology ; Carbonic Anhydrases/genetics ; Carbonic Anhydrases/immunology ; Cell Proliferation/drug effects ; Gene Expression Regulation, Neoplastic/drug effects ; Humans ; Spheroids, Cellular/drug effects
    Chemical Substances Antibodies, Monoclonal, Humanized ; Carbonic Anhydrases (EC 4.2.1.1) ; carbonic anhydrase XII (EC 4.2.1.1)
    Language English
    Publishing date 2019-07-31
    Publishing country Greece
    Document type Journal Article
    ZDB-ID 604549-2
    ISSN 1791-7530 ; 0250-7005
    ISSN (online) 1791-7530
    ISSN 0250-7005
    DOI 10.21873/anticanres.13570
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: TCR Fingerprinting and Off-Target Peptide Identification.

    Karapetyan, Armen R / Chaipan, Chawaree / Winkelbach, Katharina / Wimberger, Sandra / Jeong, Jun Seop / Joshi, Bishnu / Stein, Robert B / Underwood, Dennis / Castle, John C / van Dijk, Marc / Seibert, Volker

    Frontiers in immunology

    2019  Volume 10, Page(s) 2501

    Abstract: Adoptive T cell therapy using patient T cells redirected to recognize tumor-specific antigens by expressing genetically engineered high-affinity T-cell receptors (TCRs) has therapeutic potential for melanoma and other solid tumors. Clinical trials ... ...

    Abstract Adoptive T cell therapy using patient T cells redirected to recognize tumor-specific antigens by expressing genetically engineered high-affinity T-cell receptors (TCRs) has therapeutic potential for melanoma and other solid tumors. Clinical trials implementing genetically modified TCRs in melanoma patients have raised concerns regarding off-target toxicities resulting in lethal destruction of healthy tissue, highlighting the urgency of assessing which off-target peptides can be recognized by a TCR. As a model system we used the clinically efficacious NY-ESO-1-specific TCR C
    MeSH term(s) Biological Assay ; Cell Line, Tumor ; Epitopes, T-Lymphocyte/analysis ; Epitopes, T-Lymphocyte/chemistry ; Epitopes, T-Lymphocyte/genetics ; Epitopes, T-Lymphocyte/immunology ; HEK293 Cells ; Humans ; Lymphocyte Activation ; Peptides/analysis ; Peptides/chemistry ; Peptides/genetics ; Peptides/immunology ; Receptors, Antigen/genetics ; Receptors, Antigen/immunology ; T-Lymphocytes/cytology ; T-Lymphocytes/immunology
    Chemical Substances Epitopes, T-Lymphocyte ; Peptides ; Receptors, Antigen
    Language English
    Publishing date 2019-10-22
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2019.02501
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Advances in clinical cancer proteomics: SELDI-ToF-mass spectrometry and biomarker discovery.

    Seibert, Volker / Ebert, Matthias P A / Buschmann, Thomas

    Briefings in functional genomics & proteomics

    2005  Volume 4, Issue 1, Page(s) 16–26

    Abstract: For most cancers, survival rates depend on the early detection of the disease. So far, no biomarkers exist to cope with this difficult task. New proteomic technologies have brought the hope of discovering novel early cancer-specific biomarkers in complex ...

    Abstract For most cancers, survival rates depend on the early detection of the disease. So far, no biomarkers exist to cope with this difficult task. New proteomic technologies have brought the hope of discovering novel early cancer-specific biomarkers in complex biological samples and/or of the setting up of new clinically relevant test systems. Novel mass spectrometry-(MS) based technologies in particular, such as surface-enhanced laser desorption/ionisation time of flight (SELDI-ToF-MS), have shown promising results in the recent literature. Here, proteomic profiles of control and disease states are compared to find biomarkers for diagnosis. This paper aims to address the authors' own work and that of other groups in clinical cancer proteomics based on SELDI-ToF-MS. Shortcomings and hopes for the future are discussed.
    MeSH term(s) Biomarkers, Tumor/chemistry ; Enzyme-Linked Immunosorbent Assay ; Humans ; Neoplasms/diagnosis ; Neoplasms/epidemiology ; Neoplasms/metabolism ; Protein Array Analysis/methods ; Proteomics/methods ; Software ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods
    Chemical Substances Biomarkers, Tumor
    Language English
    Publishing date 2005-06-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2138368-6
    ISSN 1477-4062 ; 1473-9550
    ISSN (online) 1477-4062
    ISSN 1473-9550
    DOI 10.1093/bfgp/4.1.16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Surface-enhanced laser desorption ionization time-of-flight mass spectrometry (SELDI TOF-MS) and ProteinChip technology in proteomics research.

    Seibert, Volker / Wiesner, Andreas / Buschmann, Thomas / Meuer, Jörn

    Pathology, research and practice

    2004  Volume 200, Issue 2, Page(s) 83–94

    Abstract: In this review article, we describe some of the studies that have been performed using the surface-enhanced laser desorption ionization (SELDI) time-of-flight mass spectrometry and ProteinChip technology over the past few years, and highlight both their ... ...

    Abstract In this review article, we describe some of the studies that have been performed using the surface-enhanced laser desorption ionization (SELDI) time-of-flight mass spectrometry and ProteinChip technology over the past few years, and highlight both their findings as well as limitations. Proteomic applications, such as target or marker identification and target validation or toxicology, will be addressed. We will also provide an examination of SELDI technology and go into the question of where possible future research may lead us.
    MeSH term(s) Biomarkers/analysis ; Humans ; Protein Array Analysis/instrumentation ; Protein Array Analysis/methods ; Proteins/analysis ; Proteins/genetics ; Proteomics ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods
    Chemical Substances Biomarkers ; Proteins
    Language English
    Publishing date 2004
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 391889-0
    ISSN 1618-0631 ; 0344-0338
    ISSN (online) 1618-0631
    ISSN 0344-0338
    DOI 10.1016/j.prp.2004.01.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Gute Abschlussnoten zahlen sich aus

    Buch, Tanja / Hell, Stefan / Kotte, Volker / Seibert, Holger / Wydra-Somaggio, Gabriele

    IAB-Kurzbericht : aktuelle Analysen und Kommentare aus dem Institut für Arbeitsmarkt- und Berufsforschung , No. 20 , p. 1-8

    Einstiegsgebühr von Ausbildungsabsolventen

    2010  , Issue 20, Page(s) 1–8

    Author's details von G. Wydra-Somaggio, H. Seibert, T. Buch, St. Hell und V. Kotte
    Keywords Absolventen ; Bildungsabschluss ; Bildungsertrag ; Berufsbildung ; Arbeitsmarktintegration ; Deutschland
    Language German
    Size graph. Darst.
    Publisher IAB
    Publishing place Nürnberg
    Document type Article
    ZDB-ID 1173320-2
    ISSN 0942-167X
    Database ECONomics Information System

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  7. Article ; Online: Esterase activity of carbonic anhydrases serves as surrogate for selecting antibodies blocking hydratase activity.

    Uda, Narasimha Rao / Seibert, Volker / Stenner-Liewen, Frank / Müller, Philipp / Herzig, Petra / Gondi, Gabor / Zeidler, Reinhard / van Dijk, Marc / Zippelius, Alfred / Renner, Christoph

    Journal of enzyme inhibition and medicinal chemistry

    2015  Volume 30, Issue 6, Page(s) 955–960

    Abstract: Carbonic anhydrase 9 (CA9) and carbonic anhydrase 12 (CA12) were proposed as potential targets for cancer therapy more than 20 years ago. However, to date, there are only very few antibodies that have been described to specifically target CA9 and CA12 ... ...

    Abstract Carbonic anhydrase 9 (CA9) and carbonic anhydrase 12 (CA12) were proposed as potential targets for cancer therapy more than 20 years ago. However, to date, there are only very few antibodies that have been described to specifically target CA9 and CA12 and also block the enzymatic activity of their targets. One of the early stage bottlenecks in identifying CA9- and CA12-inhibiting antibodies has been the lack of a high-throughput screening system that would allow for rapid assessment of inhibition of the targeted carbon dioxide hydratase activity of carbonic anhydrases. In this study, we show that measuring the esterase activity of carbonic anhydrase offers a robust and inexpensive screening method for identifying antibody candidates that block both hydratase and esterase activities of carbonic anhydrase's. To our knowledge, this is the first implementation of a facile surrogate-screening assay to identify potential therapeutic antibodies that block the clinically relevant hydratase activity of carbonic anhydrases.
    MeSH term(s) Acetazolamide/chemistry ; Acetazolamide/pharmacology ; Aconitate Hydratase/antagonists & inhibitors ; Aconitate Hydratase/metabolism ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/pharmacology ; Antigens, Neoplasm/metabolism ; Carbonic Anhydrase IX ; Carbonic Anhydrases/metabolism ; Dose-Response Relationship, Drug ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Esterases/metabolism ; Humans ; Molecular Structure ; Structure-Activity Relationship
    Chemical Substances Antibodies, Monoclonal ; Antigens, Neoplasm ; Enzyme Inhibitors ; Esterases (EC 3.1.-) ; CA9 protein, human (EC 4.2.1.1) ; Carbonic Anhydrase IX (EC 4.2.1.1) ; Carbonic Anhydrases (EC 4.2.1.1) ; carbonic anhydrase XII (EC 4.2.1.1) ; Aconitate Hydratase (EC 4.2.1.3) ; Acetazolamide (O3FX965V0I)
    Language English
    Publishing date 2015-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2082578-X
    ISSN 1475-6374 ; 1475-6366
    ISSN (online) 1475-6374
    ISSN 1475-6366
    DOI 10.3109/14756366.2014.1001754
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book ; Online: Coexistence, Cooperation and Solidarity (2 vol. set)

    Hestermeyer, Holger P / König, Doris / Matz-Lück, Nele / Röben, Volker / Seibert-Fohr, Anja / Stoll, Peter-Tobias / Vöneky, Silja

    Liber Amicorum R Diger Wolfrum

    2011  

    Abstract: Considering paradigmatic changes and current challenges in international law this collection of essays covers diverse areas such as law of the sea, human rights, international environmental law, international dispute settlement, peace and security, ... ...

    Abstract Considering paradigmatic changes and current challenges in international law this collection of essays covers diverse areas such as law of the sea, human rights, international environmental law, international dispute settlement, peace and security, global governance and its relationship to domestic law
    Language English
    Size Online-Ressource (2258 p.)
    Publisher BRILL
    Publishing place Leiden
    Document type Book ; Online
    Note Description based upon print version of record
    ISBN 9789004188938 ; 9004188932
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  9. Article ; Online: Retrocyte Display® technology: generation and screening of a high diversity cellular antibody library.

    Breous-Nystrom, Ekaterina / Schultze, Kornelia / Meier, Marco / Flueck, Lukas / Holzer, Christina / Boll, Melanie / Seibert, Volker / Schuster, Andrea / Blanusa, Milan / Schaefer, Verena / Grawunder, Ulf / Martin-Parras, Luis / van Dijk, Marc A

    Methods (San Diego, Calif.)

    2014  Volume 65, Issue 1, Page(s) 57–67

    Abstract: Over the last nearly three decades in vitro display technologies have played an important role in the discovery and optimization of antibodies and other proteins for therapeutic applications. Here we describe the use of retroviral expression technology ... ...

    Abstract Over the last nearly three decades in vitro display technologies have played an important role in the discovery and optimization of antibodies and other proteins for therapeutic applications. Here we describe the use of retroviral expression technology for the display of full-length IgG on B lineage cells in vitro with a hallmark of a tight and stable genotype to phenotype coupling. We describe the creation of a high-diversity (>1.0E09 different heavy- and light-chain combinations) cell displayed fully human antibody library from healthy donor-derived heavy- and light-chain gene libraries, and demonstrate the recovery of high affinity target-specific antibodies from this library by staining of cells with a labeled target antigen and their magnetic- and flow cytometry-based cell sorting. The present technology represents a further evolution in the discovery of full-length, fully human antibodies using mammalian display, and is termed Retrocyte Display® (Retroviral B lymphocyte Display).
    MeSH term(s) Animals ; Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/genetics ; B-Lymphocytes/metabolism ; Cryopreservation ; Drug Evaluation, Preclinical ; Flow Cytometry ; Genetic Variation ; Genetic Vectors ; HEK293 Cells ; Humans ; Immunoglobulin Heavy Chains/biosynthesis ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Light Chains/biosynthesis ; Immunoglobulin Light Chains/genetics ; Immunomagnetic Separation ; Peptide Library ; Protein Binding ; Retroviridae/genetics
    Chemical Substances Antibodies, Monoclonal ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Peptide Library
    Language English
    Publishing date 2014-01-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1066584-5
    ISSN 1095-9130 ; 1046-2023
    ISSN (online) 1095-9130
    ISSN 1046-2023
    DOI 10.1016/j.ymeth.2013.09.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Characterization of a gene cluster encoding the maleylacetate reductase from Ralstonia eutropha 335T, an enzyme recruited for growth with 4-fluorobenzoate.

    Seibert, Volker / Thiel, Monika / Hinner, Isabelle-S / Schlömann, Michael

    Microbiology (Reading, England)

    2003  Volume 150, Issue Pt 2, Page(s) 463–472

    Abstract: A gene cluster containing a gene for maleylacetate reductase (EC 1.3.1.32) was cloned from Ralstonia eutropha 335(T) (DSM 531(T)), which is able to utilize 4-fluorobenzoate as sole carbon source. Sequencing of this gene cluster showed that the R. ... ...

    Abstract A gene cluster containing a gene for maleylacetate reductase (EC 1.3.1.32) was cloned from Ralstonia eutropha 335(T) (DSM 531(T)), which is able to utilize 4-fluorobenzoate as sole carbon source. Sequencing of this gene cluster showed that the R. eutropha 335(T) maleylacetate reductase gene, macA, is part of a novel gene cluster, which is not related to the known maleylacetate-reductase-encoding gene clusters. It otherwise comprises a gene for a hypothetical membrane transport protein, macB, possibly co-transcribed with macA, and a presumed regulatory gene, macR, which is divergently transcribed from macBA. MacA was found to be most closely related to TftE, the maleylacetate reductase from Burkholderia cepacia AC1100 (62 % identical positions) and to a presumed maleylacetate reductase from a dinitrotoluene catabolic gene cluster from B. cepacia R34 (61 % identical positions). By expressing macA in Escherichia coli, it was confirmed that macA encodes a functional maleylacetate reductase. Purification of maleylacetate reductase from 4-fluorobenzoate-grown R. eutropha 335(T) cells allowed determination of the N-terminal sequence of the purified protein, which was shown to be identical to that predicted from the cloned macA gene, thus proving that the gene is, in fact, recruited for growth of R. eutropha 335(T) with this substrate.
    MeSH term(s) Amino Acid Sequence ; Base Sequence ; Benzoates/pharmacokinetics ; Cloning, Molecular ; Conserved Sequence ; Cupriavidus necator/classification ; Cupriavidus necator/enzymology ; Cupriavidus necator/genetics ; Cupriavidus necator/growth & development ; DNA, Bacterial/chemistry ; DNA, Bacterial/genetics ; Molecular Sequence Data ; Multigene Family ; Oxidoreductases Acting on CH-CH Group Donors/chemistry ; Oxidoreductases Acting on CH-CH Group Donors/genetics ; Phylogeny ; Plasmids ; Restriction Mapping ; Sequence Alignment ; Sequence Homology, Amino Acid
    Chemical Substances Benzoates ; DNA, Bacterial ; Oxidoreductases Acting on CH-CH Group Donors (EC 1.3.-) ; maleylacetate reductase (EC 1.3.1.32) ; 4-fluorobenzoic acid (V5ROO2HOU4)
    Language English
    Publishing date 2003-10-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 1180712-x
    ISSN 1465-2080 ; 1350-0872
    ISSN (online) 1465-2080
    ISSN 1350-0872
    DOI 10.1099/mic.0.26602-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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