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2. A novel human tau knock-in mouse model reveals interaction of Abeta and human tau under progressing cerebral amyloidosis in 5xFAD mice

Author

Barendrecht, Susan, Schreurs, An, Geissler, Stefanie, Sabanov, Victor, Ilse, Victoria, Rieckmann, Vera, Eichentopf, Rico, Künemund, Anja, Hietel, Benjamin, Wussow, Sebastian, Hoffmann, Katrin, Körber-Ferl, Kerstin, Pandey, Ravi, Carter, Gregory W., Demuth, Hans-Ulrich, Holzer, Max, Roßner, Steffen, Schilling, Stephan, Preuss, Christoph, Balschun, Detlef, and Cynis, Holger

Published
2023
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3. Identification of isoaspartate-modified transthyretin as potential target for selective immunotherapy of transthyretin amyloidosis

Author

Köppen, Janett, primary, Kleinschmidt, Martin, additional, Morawski, Markus, additional, Rahfeld, Jens-Ulrich, additional, Wermann, Michael, additional, Cynis, Holger, additional, Hegenbart, Ute, additional, Daniel, Christoph, additional, Roßner, Steffen, additional, Schilling, Stephan, additional, and Schulze, Anja, additional

Published
2024
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4. Focal Cerebral Ischemia Induces Expression of Glutaminyl Cyclase along with Downstream Molecular and Cellular Inflammatory Responses.

Author

Höfling, Corinna, Ulrich, Luise, Burghardt, Sina, Donkersloot, Philippa, Opitz, Michael, Geissler, Stefanie, Schilling, Stephan, Cynis, Holger, Michalski, Dominik, and Roßner, Steffen

Subjects
TRANSIENT ischemic attack, PEPTIDE hormones, CEREBRAL ischemia, NEUROPEPTIDES, CHEMOKINES
Abstract

Glutaminyl cyclase (QC) and its isoenzyme (isoQC) catalyze the formation of N-terminal pyroglutamate (pGlu) from glutamine on a number of neuropeptides, peptide hormones and chemokines. Chemokines of the C-C ligand (CCL) motif family are known to contribute to inflammation in neurodegenerative conditions. Here, we used a model of transient focal cerebral ischemia to explore functional, cellular and molecular responses to ischemia in mice lacking genes for QC, isoQC and their substrate CCL2. Mice of the different genotypes were evaluated for functional consequences of stroke, infarct volume, activation of glia cells, and for QC, isoQC and CCL2 expression. The number of QC-immunoreactive, but not of isoQC-immunoreactive, neurons increased robustly in the infarct area at 24 and 72 h after ischemia. In parallel, immunohistochemical signals for the QC substrate CCL2 increased from 24 to 72 h after ischemia induction without differences between genotypes analyzed. The increase in CCL2 was accompanied by morphological activation of Iba1-immunoreactive microglia and recruitment of MHC-II-positive cells at 72 h after ischemia. Among other chemokines quantified in the brain tissue, CCL17 showed higher concentrations at 72 h compared to 24 h after ischemia. Collectively, these data suggest a critical role for QC in inflammatory processes in the stroke-affected brain. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Consequences of Amyloid‐β Deficiency for the Liver

Author

Buniatian, Gayane Hrachia, primary, Schwinghammer, Ute, additional, Tremmel, Roman, additional, Cynis, Holger, additional, Weiss, Thomas S., additional, Weiskirchen, Ralf, additional, Lauschke, Volker M., additional, Youhanna, Sonia, additional, Ramos, Isbaal, additional, Valcarcel, Maria, additional, Seferyan, Torgom, additional, Rahfeld, Jens‐Ulrich, additional, Rieckmann, Vera, additional, Klein, Kathrin, additional, Buadze, Marine, additional, Weber, Victoria, additional, Kolak, Valentina, additional, Gebhardt, Rolf, additional, Friedman, Scott L., additional, Müller, Ulrike C., additional, Schwab, Matthias, additional, and Danielyan, Lusine, additional

Published
2024
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6. Acute targeting of pre-amyloid seeds in transgenic mice reduces Alzheimer-like pathology later in life

Author

Uhlmann, Ruth E., Rother, Christine, Rasmussen, Jay, Schelle, Juliane, Bergmann, Carina, Ullrich Gavilanes, Emily M., Fritschi, Sarah K., Buehler, Anika, Baumann, Frank, Skodras, Angelos, Al-Shaana, Rawaa, Beschorner, Natalie, Ye, Lan, Kaeser, Stephan A., Obermüller, Ulrike, Christensen, Søren, Kartberg, Fredrik, Stavenhagen, Jeffrey B., Rahfeld, Jens-Ulrich, Cynis, Holger, Qian, Fang, Weinreb, Paul H., Bussiere, Thierry, Walker, Lary C., Staufenbiel, Matthias, and Jucker, Mathias

Published
2020
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9. Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Demuth, Hans-Ulrich, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Published
2020
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13. Immunogenicity of the Envelope Surface Unit of Human Endogenous Retrovirus K18 in Mice

Author

Ilse, Victoria, Scholz, Rebekka, Wermann, Michael, Naumann, Marcel, Staege, Martin S., Roßner, Steffen, Cynis, Holger, Ilse, Victoria, Scholz, Rebekka, Wermann, Michael, Naumann, Marcel, Staege, Martin S., Roßner, Steffen, and Cynis, Holger

Abstract

The triggers for the development of multiple sclerosis (MS) have not been fully understood to date. One hypothesis proposes a viral etiology. Interestingly, viral proteins from human endogenous retroviruses (HERVs) may play a role in the pathogenesis of MS. Allelic variants of the HERV-K18 env gene represent a genetic risk factor for MS, and the envelope protein is considered to be an Epstein–Barr virus-trans-activated superantigen. To further specify a possible role for HERV-K18 in MS, the present study examined the immunogenicity of the purified surface unit (SU). HERV-K18(SU) induced envelope-specific plasma IgG in immunized mice and triggered proliferation of T cells isolated from these mice. It did not trigger phenotypic changes in a mouse model of experimental autoimmune encephalomyelitis. Further studies are needed to investigate the underlying mechanisms of HERV-K18 interaction with immune system regulators in more detail.

Published
2022

14. Pyroglutamate-3 Amyloid-β Deposition in the Brains of Humans, Non-Human Primates, Canines, and Alzheimer Disease–Like Transgenic Mouse Models

Author

Frost, Jeffrey L., Le, Kevin X., Cynis, Holger, Ekpo, Elizabeth, Kleinschmidt, Martin, Palmour, Roberta M., Ervin, Frank R., Snigdha, Shikha, Cotman, Carl W., Saido, Takaomi C., Vassar, Robert J., George-Hyslop, Peter St., Ikezu, Tsuneya, Schilling, Stephan, Demuth, Hans-Ulrich, and Lemere, Cynthia A.

Published
2013
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19. IsoQC (QPCTL) knock-out mice suggest differential substrate conversion by glutaminyl cyclase isoenzymes

Author

Becker, Andreas, Eichentopf, Rico, Sedlmeier, Reinhard, Waniek, Alexander, Cynis, Holger, Koch, Birgit, Stephan, Anett, Bäuscher, Christoph, Kohlmann, Stephanie, Hoffmann, Torsten, Kehlen, Astrid, Berg, Sabine, Freyse, Ernst-Joachim, Osmand, Alexander, Plank, Anne-Christine, Roner, Steffen, von Hörsten, Stephan, Graubner, Sigrid, Demuth, Hans-Ulrich, and Schilling, Stephan

Published
2016
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20. Identification of Differentially Expressed Human Endogenous Retrovirus Families in Human Leukemia and Lymphoma Cell Lines and Stem Cells

Author

Engel, Kristina, Wieland, Lisa, Krüger, Anna, Volkmer, Ines, Cynis, Holger, Emmer, Alexander, Staege, Martin Sebastian, and Publica

Subjects
hematopoietic stem cells (HSCs), Embryonic stem cells (ESC), viruses, leukemia, RNA sequencing, lymphoma, Leukämie, human endogenous retroviruses (HERVs), differential RNA sequencing, Hematopoietic stem celld (HSC), Oncology, Human endogenous retroviruses (HERV), embryonic stem cells (ESCs), embryonic structures, gene expression, LL-100 panel, Original Research
Abstract

Endogenous retroviruses (ERVs) are becoming more and more relevant in cancer research and might be potential targets. The oncogenic potential of human ERVs (HERVs) has been recognized and includes immunosuppression, cell fusion, antigenicity of viral proteins, and regulation of neighboring genes. To decipher the role of HERVs in human cancers, we used a bioinformatics approach and analyzed RNA sequencing data from the LL-100 panel, covering 22 entities of hematopoietic neoplasias including T cell, B cell and myeloid malignancies. We compared HERV expression in this panel with hematopoietic stem cells (HSCs), embryonic stem cells (ESCs) and normal blood cells. RNA sequencing data were mapped against a comprehensive synthetic viral metagenome with 116 HERV sequences from 14 different HERV families. Of these, 13 HERV families and elements were differently expressed in malignant hematopoietic cells and stem cells. We found transcriptional upregulation of HERVE family in acute megakaryocytic and erythroid leukemia and of HERVFc family in multiple myeloma/plasma cell leukemia (PCL). The HERVFc member HERVFc-1 was found transcriptionally active in the multiple myeloma cell line OPM-2 and also in the Hodgkin lymphoma cell line L-428. The expression of HERVFc-1 in L-428 cells was validated by qRT-PCR. We also confirm transcriptional downregulation of ERV3 in acute megakaryocytic and erythroid leukemia, and HERVK in acute monocytic and myelocytic leukemia and a depression of HERVF in all malignant entities. Most of the higher expressed HERV families could be detected in stem cells including HERVK (HML-2), HERV-like, HERVV, HERVT, ERV9, HERVW, HERVF, HERVMER, ERV3, HERVH and HERVPABLB.

Published
2021

21. Endogenous Retroviral–K Envelope Is a Novel Tumor Antigen and Prognostic Indicator of Renal Cell Carcinoma

Author

Weyerer, Veronika, primary, Strissel, Pamela L., additional, Stöhr, Christine, additional, Eckstein, Markus, additional, Wach, Sven, additional, Taubert, Helge, additional, Brandl, Lisa, additional, Geppert, Carol I., additional, Wullich, Bernd, additional, Cynis, Holger, additional, Beckmann, Matthias W., additional, Seliger, Barbara, additional, Hartmann, Arndt, additional, and Strick, Reiner, additional

Published
2021
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22. Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β

Author

Nussbaum, Justin M., Schilling, Stephan, Cynis, Holger, Silva, Antonia, Swanson, Eric, Wangsanut, Tanaporn, Tayler, Kaycie, Wiltgen, Brian, Hatami, Asa, Ronicke, Raik, Reymann, Klaus, Hutter-Paier, Birgit, Alexandru, Anca, Jagla, Wolfgang, Graubner, Sigrid, Glabe, Charles G., Demuth, Hans-Ulrich, and Bloom, George S.

Subjects
Medical research, Medicine, Experimental, Prions -- Physiological aspects, Amyloid beta-protein -- Physiological aspects, Alzheimer's disease -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Extracellular plaques of amyloid-β and intraneuronal neurofibrillary tangles made from tau are the histopathological signatures of Alzheimer's disease. Plaques comprise amyloid-β fibrils that assemble from monomeric and oligomeric intermediates, and [...]

Published
2012
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26. Glutaminyl cyclase inhibition attenuates pyroglutamate A[beta] and Alzheimer's disease--like pathology

Author

Schilling, Stephan, Zeitschel, Ulrike, Hoffmann, Torsten, Heiser, Ulrich, Francke, Mike, Kehlen, Astrid, Holzer, Max, Hutter-Paier, Birgit, Prokesch, Manuela, Windisch, Manfred, Jagla, Wolfgang, Schlenzig, Dagmar, Lindner, Christiane, Rudolph, Thomas, Reuters, Gunter, Cynis, Holger, Montag, Dirk, Demuth, Hans-Ulrich, and Rossner, Steffen

Subjects
Alzheimer's disease -- Genetic aspects, Alzheimer's disease -- Care and treatment, Alzheimer's disease -- Research, Amyloid beta-protein -- Health aspects, Amyloid beta-protein -- Genetic aspects, Amyloid beta-protein -- Research, Glutamine synthetase -- Health aspects, Glutamine synthetase -- Control, Glutamine synthetase -- Research, Proteolysis -- Health aspects, Proteolysis -- Research
Abstract

Because of their abundance, resistance to proteolysis, rapid aggregation and neurotoxicity, N-terminally truncated and, in particular, pyroglutamate (pE)-modified A[beta] peptides have been suggested as being important in the initiation of pathological cascades resulting in the development of Alzheimer's disease (1-6). We found that the N-terminal pE-formation is catalyzed by glutaminyl cyclase in vivo. Glutaminyl cyclase expression was upregulated in the cortices of individuals with Alzheimer's disease and correlated with the appearance of pE-modified A[beta]. Oral application of a glutaminyl cyclase inhibitor resulted in reduced A[[beta].sub.3(pE)-42] burden in two different transgenic mouse models of Alzheimer's disease and in a new Drosophila model. Treatment of mice was accompanied by reductions in A[[beta].sub.3(pE)-40/42], diminished plaque formation and gliosis and improved performance in context memory and spatial learning tests. These observations are consistent with the hypothesis that A[[beta].sub.3(pE)-42] acts as a seed for A[beta] aggregation by self-aggregation and co-aggregation with A[[beta].sub.1-40/42]. Therefore, A[[beta].sub.3(pE)-40/42] peptides seem to represent A/3 forms with exceptional potency for disturbing neuronal function. The reduction of brain pE-A[beta] by inhibition of glutaminyl cyclase offers a new therapeutic option for the treatment of Alzheimer's disease and provides implications for other amyloidoses, such as familial Danish dementia., The brains of individuals with Alzheimer's disease are characterized by the presence of neurofibrillary tangles and by deposits of A[beta] in neocortical brain structures (1). Sequential [beta]- and [gamma]-secretase cleavage [...]

Published
2008

27. Additional file 1 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 1. Summary of isoD7-Aβ specific antibodies obtained from murine hybridoma cells. Binding affinities of isoD7-Aβ (1–18) as well as Aβ (1–18) peptides to immobilized antibodies were determined by using Biacore 3000 at a temperature of 25 °C. Goat anti mouse IgG was immobilized to a CM5 sensor chip, followed by binding of mouse antibodies. Kinetic constants were determined by applying Aβ peptides at different concentrations and calculated from the combined set of data by using BIAevaluation software (Biacore AB).

Published
2020
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28. Additional file 8 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 8. Elevated Plus Maze (EPM) test of mice treated weekly for 38 weeks with 12 mg/kg K11_IgG2a, 3D6_IgG2a and isotype control. Antibody-treated 5xFAD groups were compared with wildtype animals treated with 12 mg/kg isotype control. Test animals were placed with their head to the end of a defined closed arm of an elevated, plus-shaped (+) maze with two open and two enclosed arms. During the next 10 min, every movement of test animals has been recorded by a video tracking system. Arm entries are defined as presence of the complete animal (except tail) in the open arm. For statistical analysis Bonferroni’s Multiple Comparison Test was used. Sample size was at least 9 animals per group. * means p ≤ 0.05; ** means p ≤ 0.01. The error bars represent SEM.

Published
2020
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29. Additional file 5 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 5. Determination of isoD7-Aβ percentage in Aβ fibrils of different ages. Aβ (1–40) and Aβ (1–42) fibrils were incubated for 1 year at 37 °C. Samples were taken at different time points, monomerized by formic acid treatment and subsequently analyzed by isoD7-Aβ and total Aβ ELISA. A – Formation of isoD7-Aβ (1–40); B – Formation of isoD7-Aβ (1–42) within fibrillary structures.

Published
2020
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30. Additional file 2 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 2. Immunohistochemical analysis of Aβ deposits in human brain samples by using different anti-isoD7-Aβ antibodies. Brain slices of gray and white matter from an AD patient were incubated with the antibodies A – from the first immunization experiment: K11, K16, K23 and K29 and B – from the second immunization experiment: K119, K129 and K211, followed by application of biotinylated anti-mouse IgG.

Published
2020
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31. Additional file 4 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 4. Transmission electron microscope image of Aβ1–40 and Aβ1–42 fibrils. In each case, 10 μl of the 10 μM Aβ1–40 and Aβ1–42 fibril solutions were applied to a carbon-coated copper grid and treated with 2% (v/v) phosphotungstic acid for contrasting. Images were obtained by high-angle annular dark field scanning transmission electron microscopy using 200 kV acceleration voltage. A: Aβ (1–40)-fibrils, B: Aβ (1–42)-fibrils.

Published
2020
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32. Additional file 6 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Subjects
animal structures, viruses, fungi, embryonic structures
Abstract

Additional file 6. isoD7-Aβ formation in APP_D678N transfected HEK293 cells. HEK293 cells were transfected with wild type APP (APP_WT) and the Tottori variant APP_D678N. Samples were taken 4 and 5 days after transfection and analyzed by isoD7-Aβ and total Aβ ELISA. The error bars represent SEM. A – % isoD7-Aβ 4 days after transfection B – % isoD7-Aβ 5 days after transfection.

Published
2020
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33. Additional file 7 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 7. Quantification of total Aβ and isoD7-Aβ peptides in T-Per fractions of 5xFAD mice brain treated with K11_IgG2a and isotype control. Three months old 5xFAD mice were treated intraperitoneally once a week with 500 μg, 150 μg K11_IgG2a or 500 μg isotype control. After 12-weeks treatment, mice were sacrificed and the left hemisphere was homogenized in T-Per buffer, followed by centrifugation. In the resulting supernatants (T-Per fractions), the amount of total Aβ (A) and isoD7-Aβ (B) was analyzed by ELISA. The error bars represent SEM.

Published
2020
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34. Additional file 9 of Targeting isoaspartate-modified Aβ rescues behavioral deficits in transgenic mice with Alzheimer’s disease-like pathology

Author

Gnoth, Kathrin, Piechotta, Anke, Kleinschmidt, Martin, Konrath, Sandra, Schenk, Mathias, Taudte, Nadine, Ramsbeck, Daniel, Rieckmann, Vera, Geissler, Stefanie, Eichentopf, Rico, Barendrecht, Susan, Hartlage-Rübsamen, Maike, Hans-Ulrich Demuth, Roßner, Steffen, Cynis, Holger, Rahfeld, Jens-Ulrich, and Schilling, Stephan

Abstract

Additional file 9. Fear conditioning test of mice treated weekly with 12 mg/kg K11_IgG2a, 3D6_IgG2a and isotype control. Antibody-treated 5xFAD groups were compared with wild type animals treated with 12 mg/kg isotype control. Test animals were placed in an automated Fear Conditioning System and submitted to the following procedure: pause (180 s), sound (28 s), electrical stimulus (0.7 mA for 2 s). A – Contextual Memory: After 24 h, test animals were again placed in the Fear Conditioning System, left there for 210 s and removed. B – Memory of Cue: One hour later, animals were placed back in the system, which was now covered with black walls and a black floor, in order to expose them to 180 s pause, followed by 180 s of sound (neutral stimulus). State of fear is expressed by freezing. For statistical analysis Tukey’s Multiple Comparison Test was used. Sample size was at least 8 animals per group. * means p ≤ 0.05. The error bars represent SEM.

Published
2020
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35. Formation of HERV-K and HERV-Fc1 Envelope Family Members is Suppressed on Transcriptional and Translational Level

Author

Gröger, Victoria, Wieland, Lisa, Naumann, Marcel, Meinecke, Ann-Christin, Meinhardt, Beate, Rossner, Steffen, Ihling, Christian, Emmer, Alexander, Staege, Martin S., Cynis, Holger, Gröger, Victoria, Wieland, Lisa, Naumann, Marcel, Meinecke, Ann-Christin, Meinhardt, Beate, Rossner, Steffen, Ihling, Christian, Emmer, Alexander, Staege, Martin S., and Cynis, Holger

Abstract

The human genome comprises 8% sequences of retroviral origin, so-called human endogenous retroviruses (HERVs). Most of these proviral sequences are defective, but some possess open reading frames. They can lead to the formation of viral transcripts, when activated by intrinsic and extrinsic factors. HERVs are thought to play a pathological role in inflammatory diseases and cancer. Since the consequences of activated proviral sequences in the human body are largely unexplored, selected envelope proteins of human endogenous retroviruses associated with inflammatory diseases, namely HERV-K18, HERV-K113, and HERV-Fc1, were investigated in the present study. A formation of glycosylated envelope proteins was demonstrated in different mammalian cell lines. Nevertheless, protein maturation seemed to be incomplete as no transport to the plasma membrane was observed. Instead, the proteins remained in the ER where they induced the expression of genes involved in unfolded protein response, such as HSPA5 and sXBP1. Furthermore, low expression levels of native envelope proteins were increased by codon optimization. Cell-free expression systems showed that both the transcriptional and translational level is affected. By generating different codon-optimized variants of HERV-K113 envelope, the influence of single rare t-RNA pools in certain cell lines was demonstrated. The mRNA secondary structure also appears to play an important role in the translation of the tested viral envelope proteins. In summary, the formation of certain HERV proteins is basically possible. However, their complete maturation and thus full biologic activity seems to depend on additional factors that might be disease-specific and await elucidation in the future.

Published
2020

37. Contributors

Author

Aalen, Reidunn B., primary, Abdel-Wahab, Yasser H.A., additional, Adams, Michael E., additional, Adan, Roger A.H., additional, Ahima, Rexford S., additional, Ahmed, Naima, additional, Al-Massadi, Omar, additional, Altstein, Miriam, additional, Anouar, Youssef, additional, Anselmi, Laura, additional, Ansorge, Siegfried, additional, Antcheva, Nikolinka, additional, Antonova-Koch, Yevgeniya, additional, Appel, Jon R., additional, Arik, Anam J., additional, Arter, Alison L., additional, Arvan, Peter, additional, Ashkenazi, Avraham, additional, Baas, P.W., additional, Bado, André, additional, Baird, Andrew, additional, Baiula, Monica, additional, Bakaletz, Lauren O., additional, Bakken, Earl E., additional, Balaskó, Márta, additional, Baldwin, Graham S., additional, Banks, William A., additional, Barra, Donatella, additional, Barson, Jessica R., additional, Basille, Magali, additional, Bauer, Natalie N., additional, Bedini, Andrea, additional, Beeton, Christine, additional, Begley, David J., additional, Beinfeld, Margery C., additional, Bendena, William G., additional, Benoit, Stephen C., additional, Bentov, Itay, additional, Bern, Howard, additional, Bierbaum, Gabriele, additional, Billington, Charles J., additional, Blasiak, Anna, additional, Block, Norman L., additional, Bloom, Stephen. R., additional, Bonney, Iwona, additional, Bowie, John H., additional, Boyd, Sunny K., additional, Brain, Susan D., additional, Brede, Dag A., additional, Broeck, Jozef Vanden, additional, Brown, Kelly L., additional, Brown, Mark R., additional, Bugni, James M., additional, Bundgaard, Jens R., additional, Burel, Delphine, additional, Butenko, Melinka A., additional, Call, Melissa J., additional, Calò, Girolamo, additional, Campbell, Duncan John, additional, Carlsson, Anna, additional, Carr, Daniel B., additional, Carraway, Robert E., additional, Carreira, Marcos C., additional, Casanueva, Felipe F., additional, Cassella, Sarah N., additional, Casson, Stuart A., additional, Castaño, Justo P., additional, Cebrat, Marek, additional, Chappe, Valerie, additional, Chatenet, David, additional, Chen, Keqiang, additional, Chen, Chen, additional, Chen, Longchuan, additional, Chen, Duan, additional, Cheng, Carrie Y.Y., additional, Cho, Sung Ki, additional, Chow, Billy K.C., additional, Christopoulos, Arthur, additional, Chu, Shijian, additional, Clarke, Iain J., additional, Coast, Geoffrey M., additional, Compere, Vincent, additional, Concepcion, Gisela P., additional, Cone, Roger D., additional, Conlon, J. Michael, additional, Cornélissen, Germaine, additional, Courel, Maité, additional, Couture, Réjean, additional, Cramer, W.A., additional, Croft, Nathan P., additional, Crujeiras, Ana B., additional, Cuttitta, Frank, additional, Cynis, Holger, additional, D’Acquisto, F., additional, Davis, Jon F., additional, Davis, Thomas P., additional, de La Serre, Claire Barbier, additional, de Lartigue, Guillaume, additional, de Lecea, Luis, additional, de Oliveira Santos, Marcelo, additional, De Waard, Michel, additional, Bolette Hartmann, Carolyn F. Deacon, additional, Delestre, Charlène, additional, Delgado, Mario, additional, Demuth, Hans-Ulrich, additional, Deng, Xiaoming, additional, Dharmawardhana, Palitha, additional, Di Cosmo, Anna, additional, Dias, Simoni Campos, additional, Dickerson, Jonathan W., additional, Diep, Dzung B., additional, Dircksen, H., additional, Dischinger, Jasmin, additional, do Rego, Jean-Claude, additional, Dobner, Paul R., additional, Dockray, Graham J., additional, Dores, Robert M., additional, Ducroc, Robert, additional, Dudek, Nadine L., additional, Dumont, Yvan, additional, Duraffourd, Celine, additional, Duterte-Boucher, Dominique, additional, Eberlé, Alex N., additional, Egleton, Richard D., additional, Eipper, Betty A., additional, Engel, Jorg B., additional, Englander, Ella W., additional, Epelbaum, Jacques, additional, Erlanson-Albertsson, Charlotte, additional, Evangelista, S., additional, Fagan, Karen A., additional, Farber, Joshua M., additional, Farkasfalvi, Klára, additional, Fekete, Csaba, additional, Flatt, Peter R., additional, Flower, R.J., additional, Forssmann, Wolf-Georg, additional, Fournier, Alain, additional, Foy, Kevin Chu, additional, Franco, Octávio Luiz, additional, Frenkel, Dan, additional, Fricker, Lloyd D., additional, de la Fuente-Núñez, César, additional, Fukuda, Hiroo, additional, Gäde, Gerd, additional, Galas, Ludovic, additional, Gallagher, Patricia E., additional, Gandolfo, Pierrick, additional, Garcia-Espinosa, Maria A., additional, García-Sanmartín, Josune, additional, Geary, Nori, additional, Geng, Hua, additional, Germano, Patrizia M., additional, Goetze, Jens P., additional, Gonzalez, Alexis A., additional, Gonzalez, Ana, additional, Gosnell, Blake A., additional, Goto, Katsutoshi, additional, Gourcerol, Guillaume, additional, Gozes, I., additional, Gracia-Navarro, Francisco, additional, Grayson, Bernadette E., additional, Greeley, George H., additional, Greenwald-Yarnell, Megan, additional, Gressens, Pierre, additional, Grider, John R., additional, Grünewald, Jan, additional, Guerreiro, Juliano R., additional, Guerrini, Remo, additional, Guida, Filomena, additional, Guilhaudis, Laure, additional, Guilmeau, Sandra, additional, Gundlach, Andrew L., additional, Gutkowska, Jolanta, additional, Hackbarth, Clifton, additional, Haim Ohana, Y., additional, Halberg, Franz, additional, Hallberg, Mathias, additional, Hamidi, Sayyed A., additional, Han, Song, additional, Han, Ji-Sheng, additional, Hancock, Robert E.W., additional, Haque, Samer-ul, additional, Hara-Nishimura, Ikuko, additional, Hariton, Aliza, additional, Hartsock, Wendy J., additional, Harvey, Alan L., additional, Hasunuma, Itaru, additional, Henning, Robert J., additional, Heppner, Kristy M., additional, Hertweck, Kate L., additional, Herzog, Herbert, additional, Higashiyama, Tetsuya, additional, Hinuma, Shuji, additional, Hippenstiel, Stefan, additional, Hirakawa, Yuki, additional, Hirose, Shuichi, additional, Hirsch, Jochen R., additional, Hocke, Andreas C., additional, Hodges, Robert S., additional, Hoffmann, Werner, additional, Hökfelt, Tomas, additional, Holst, Jens Juul, additional, Holzer, Peter, additional, Horodyski, Frank M., additional, Hosoda, Hiroshi, additional, Hou, Xiaowen, additional, Huffaker, Alisa, additional, Iijima, Norio, additional, Ikeuchi, Momoko, additional, Imperial, Julita S., additional, Improta, Giovanna, additional, Inui, Akio, additional, Irwin, Nigel, additional, Ishii, Munehiro, additional, Iturrioz, Xavier, additional, Ivanisevic, Ljubica, additional, Iwao, Hiroshi, additional, Iwata, Takeo, additional, Izumi, Yasukatsu, additional, Izumiyama, Hajime, additional, Jankowski, Marek, additional, Janssen, Tom, additional, Jégou, Sylvie, additional, Jensen, Robert T., additional, Jethwa, Preeti H., additional, Johannessen, Helene, additional, Johanson, Conrad, additional, Judkowski, Valeria, additional, Kaczmarek, Przemyslaw, additional, Kageyama, Haruaki, additional, Kakimoto, Tatsuo, additional, Kang, Ki Sung, additional, Kangawa, Kenji, additional, Kastin, Abba J., additional, Kato, Johji, additional, Kaumaya, Pravin T.P., additional, Keep, Richard F., additional, Kem, William R., additional, Khomenko, Tetyana, additional, Kikuyama, Sakae, additional, Kim, Young-Joon, additional, Kimura, Sadao, additional, King, Ross, additional, Kiptoo, Paul, additional, Kishimoto, Ichiro, additional, Kitamura, Kazuo, additional, Kluczyk, Alicja, additional, Kobori, Hiroyuki, additional, Kodama, Yosuke, additional, Kojima, Masayasu, additional, Kondo, Yuki, additional, Körner, Meike, additional, Kosson, Piotr, additional, Kotz, Catherine M., additional, Krishnan, Bhavani, additional, Kulseng, Bård, additional, Kumpf, Robert, additional, Laburthe, Marc, additional, Lacaille, Hélène, additional, Ladenheim, Ellen E., additional, Ladram, Ali, additional, Laksitorini, Marlyn D., additional, Lambert, David G., additional, Lange, Angela B., additional, Langhans, Wolfgang, additional, Larauche, Muriel, additional, Larhammar, Dan, additional, Larráyoz, Ignacio M., additional, Lattanzi, Roberta, additional, Lechan, Ronald M., additional, Lefranc, Benjamin, additional, Leibowitz, Sarah F., additional, Lelièvre, Vincent, additional, Leprince, Jérôme, additional, Levine, Allen S., additional, Li, Qun, additional, Lifshitz, Veronica, additional, Lihrmann, Isabelle, additional, Chi-Jen Lin, James, additional, Lindberg, Iris, additional, Lindsey, Keith, additional, Lipkowski, Andrzej W., additional, Liron, T., additional, Liu, Junli, additional, Liu, Ying, additional, Liu, Min, additional, Llorens-Cortes, Catherine, additional, Loizidou, Marilena, additional, Lopez, C., additional, Lovejoy, David A., additional, Luca, Vincenzo, additional, Lutz, Thomas A., additional, Ma, Sherie, additional, Mains, Richard E., additional, Malagon, Maria M., additional, Malendowicz, Ludwik K., additional, Wan, Jennifer Man-Fan, additional, Mangoni, Maria Luisa, additional, Manigrasso, Michaele B, additional, Marahiel, Mohamed A., additional, Marco, Heather G., additional, Maric-Bilkan, Christine, additional, Marks, Nikki J., additional, Martin, Roland, additional, Martinez, Vicente, additional, Martínez, Alfredo, additional, Martinez-Fuentes, Antonio J., additional, Masler, Edward P., additional, Matsubayashi, Yoshikatsu, additional, Mattu, Harman S., additional, Maule, Aaron G., additional, McLaughlin, Patricia J., additional, McMurtry, Ivan F., additional, Meelkop, Ellen, additional, Mehdi, Saher, additional, Melchiorri, Pietro, additional, Millar, R.P., additional, Miller, Laurence J., additional, Miller, Miles, additional, Million, Mulugeta, additional, Minamino, Naoto, additional, Mittelman, M., additional, Miyauchi, Takashi, additional, Miyazato, Mikiya, additional, Mizoguchi, Hirokazu, additional, Mohme, Malte, additional, Montero-Hadjadje, Maité, additional, Moody, Terry W., additional, Mookherjee, Neeloffer, additional, Moran, Timothy H., additional, Morganstern, Irene, additional, Mori, Masatomo, additional, Morin, Fabrice, additional, Morris, John F., additional, Moura, Daniel S., additional, Mudge, Anna J., additional, Mul, Joram D., additional, Murthy, Karnam S., additional, Myers, Martin G., additional, Nachman, Ronald J., additional, Nahon, Jean-Louis, additional, Naithani, Sushma, additional, Nakada, Tomoaki, additional, Nakamachi, Tomoya, additional, Nakamura, Yuki, additional, Nalivaeva, Natalia N., additional, Nasrallah, June B., additional, Nässel, Dick R., additional, Navar, L. Gabriel, additional, Neelakantan, Pratap, additional, Negri, Lucia, additional, Nes, Ingolf F., additional, Neumann, D., additional, Neveu, Cindy, additional, Ng, Tzi Bun, additional, Ng, Stephanie Y.L., additional, Nicholson, Graham M., additional, Nicolas, Pierre, additional, Nishikimi, Toshio, additional, Nishiyama, Mariko, additional, Nogueiras, Rubén, additional, Norton, Raymond S., additional, Novotny, Laura A., additional, Nowak, Krzysztof W., additional, Nyberg, Fred, additional, Ochoa-Callejero, Laura, additional, Ove Ögren, Sven, additional, Ohgusu, Hideko, additional, Oh-I, Shinsuke, additional, Ojo, Opeolu O., additional, Olivera, Baldomero M., additional, Olucha-Bordonau, Francisco E., additional, Oppenheim, Joost J., additional, Orchard, Ian, additional, Ouellette, André J., additional, Pacheco-López, Gustavo, additional, Page, Nigel M., additional, Palma, Mario Sergio, additional, Pan, Weihong, additional, Park, Yoonseong, additional, Parmentier, Marc, additional, Passemard, Sandrine, additional, Patterson, Michael, additional, Paunovic, Brankica, additional, Pearce, Gregory, additional, Pedersen, Jens, additional, Peeters, Theo L., additional, Eugene Pekary, A., additional, Pelletier, Georges, additional, Perboni, Simona, additional, Pérez-Tilve, Diego, additional, Perjés, Ábel, additional, Perretti, M., additional, Pétervári, Erika, additional, Pinilla, Clemencia, additional, Pinskim, Jacek, additional, Pisegna, Joseph R., additional, Plankensteiner, Kristof, additional, Podvin, Sonia, additional, Poitras, Pierre, additional, Polese, Gianluca, additional, Pollock, David M., additional, Porto, William Farias, additional, Possani, Lourival D., additional, Pothoulakis, Charalabos, additional, Presse, Françoise, additional, Prieto, Minolfa C., additional, Prutchi-Sagiv, S., additional, Purcell, Anthony W., additional, Purtell, Louise, additional, Quirion, Rémi, additional, Rabat, Catalina Abad, additional, Rademaker, Miriam, additional, Rajpal, Gautam, additional, Randeva, Harpal S., additional, Rebuffat, Sylvie, additional, Reeve, Joseph R., additional, Rehfeld, Jens F., additional, Reinhold, Dirk, additional, Reinscheid, Rainer K., additional, Reubi, Jean Claude, additional, Rezvani, Katayoun, additional, Ribeiro, Suzana Meira, additional, Richard, D., additional, Richards, Mark, additional, Riehle, Michael A., additional, Rinaldi, Andrea C., additional, Rode, Bernd M., additional, de la Vega, Ricardo C. Rodríguez, additional, Rotzinger, Susan, additional, Rucinski, Marcin, additional, Ruskoaho, Heikki, additional, Ryan, Philip J., additional, Sabatier, Jean-Marc, additional, Sahl, Hans-Georg, additional, Said, Sami I., additional, Sakurada, Tsukasa, additional, Sakurada, Shinobu, additional, Salomon, David S., additional, Samson, Willis K., additional, Sandor, Zsuzsanna, additional, Saragovi, H. Uri, additional, Sasaki, Kazuki, additional, Sato, Takahiro, additional, Satou, Ryousuke, additional, Sawa, Shinichiro, additional, Sayegh, Ayman I., additional, Schally, Andrew V., additional, Schilling, Stephan, additional, Schoofs, Liliane, additional, Schooley, David A., additional, Schubert, Mitchell L., additional, Segalas-Milazzo, Isabelle, additional, Seidah, Nabil G., additional, Selsted, Michael E., additional, Seroogy, Kim B., additional, Severini, Cinzia, additional, Sexton, Patrick M., additional, Shai, Yechiel, additional, Sharma, O., additional, Shichiri, Masayoshi, additional, Shimada, Tomoo, additional, Shimizu, Hiroyuki, additional, Shioda, Seiji, additional, Shulkes, Arthur, additional, Siahaan, Teruna J., additional, Siemion, Ignacy Z., additional, Silva, Osmar Nascimento, additional, Silva-Filho, Marcio C., additional, Skwarczynski, Mariusz, additional, Small, Caroline. J., additional, Smith, Craig M., additional, Smith, David E., additional, Smith, A. Ian, additional, Solomon, Beka, additional, Solomon, Travis E., additional, Sospedra, Mireia, additional, Souroujon, M.C., additional, Spampinato, Santi, additional, Spindel, Eliot R., additional, Steiger, A., additional, Stengel, Andreas, additional, Sternini, Catia, additional, Steyn, Frederik J., additional, Stopa, Edward, additional, Strowski, Mathias Z., additional, Sugano, Shigeo S., additional, Sundström, Görel, additional, Sutcliffe, J. Gregor, additional, Suttorp, Norbert, additional, Sweedler, Jonathan V., additional, Szabo, Sandor, additional, Székely, Miklós, additional, Szokodi, István, additional, Taché, Yvette, additional, Takahashi, Kazuhiro, additional, Takei, Yoshio, additional, Takenoya, Fumiko, additional, Talbot, Sébastien, additional, Tallant, E. Ann, additional, Tan, Tricia M., additional, Temmerman, Liesbet, additional, Temmesfeld-Wollbrück, Bettina, additional, Tena-Sempere, Manuel, additional, Thorsell, Annika, additional, Tilakaratne, Nanda, additional, Tobe, Stephen S., additional, Tokudome, Takeshi, additional, Tolstanova, Ganna, additional, Tonon, Marie-Christine, additional, Topping, Jennifer F., additional, Tossi, Alessandro, additional, Tostivint, Hervé, additional, Toth, Istvan, additional, Totsune, Kazuhito, additional, Toyoda, Fumiyo, additional, Troke, Rachel, additional, Tschöp, Matthias H., additional, Tso, Patrick, additional, Tsukaya, Hirokazu, additional, Tsutsui, Kazuyoshi, additional, Tu, Hong, additional, Turner, Anthony J., additional, Ubuka, Takayoshi, additional, Valdivia, Elene R., additional, Vandersmissen, Hans Peter, additional, Vaudry, David, additional, Vaudry, Hubert, additional, Vazquez-Martinez, Rafael, additional, Verbalis, Joseph G., additional, Vicari, Daniele, additional, Vidal, Nicolas, additional, Vignoni, Marzia, additional, Viollet, Cécile, additional, Vishwanatha, K.S., additional, Vivoli, Mirella, additional, Voisin, Thierry, additional, Vu, John P., additional, Walker, John C., additional, Wallace, B.A., additional, Wang, Ji Ming, additional, Wang, Lixin, additional, Wardman, Jonathan H., additional, Watanabe, Takuya, additional, Welch, Hazel, additional, Werner, Haim, additional, Whitmore, L., additional, Wiedemann, Imke, additional, Winsky-Sommerer, Raphaelle, additional, Witt, Ken A., additional, Wojciechowicz, Tatiana, additional, Wong, Jack Ho, additional, Woods, Stephen C., additional, Wootten, Denise, additional, Wu, Vincent, additional, Wurtz, Olivier, additional, Xiong, Ximing, additional, David Xu, Zhi-Qing, additional, Yamaguchi, Yube, additional, Yamaguchi, Takahiro, additional, Yamamoto, Kazutoshi, additional, Yamashita, E., additional, Yamazaki, Hiroyuki, additional, Yang, De, additional, Yoshikawa, Masaaki, additional, Yuan, Pu-Qing, additional, Yung, Sunny C., additional, Zagon, Ian S., additional, Zakharov, S.D., additional, Zaman, Mehfuz, additional, Zhalnina, M.V., additional, Zhang, Ning, additional, Zhang-Auberson, Lixin, additional, Zhao, Chun-Mei, additional, Ziolkowska, Agnieszka, additional, and Zitnan, Dusan, additional

Published
2013
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41. The isoenzyme of glutaminyl cyclase is an important regulator of monocyte infiltration under inflammatory conditions

Author

Cynis, Holger, Hoffmann, Torsten, Friedrich, Daniel, Kehlen, Astrid, Gans, Kathrin, Kleinschmidt, Martin, Rahfeld, Jens-Ulrich, Wolf, Raik, Wermann, Michael, Stephan, Anett, Haegele, Monique, Sedlmeier, Reinhard, Graubner, Sigrid, Jagla, Wolfgang, Müller, Anke, Eichentopf, Rico, Heiser, Ulrich, Seifert, Franziska, Quax, Paul H. A., de Vries, Margreet R., Hesse, Isabel, Trautwein, Daniela, Wollert, Ulrich, Berg, Sabine, Freyse, Ernst-Joachim, Schilling, Stephan, and Demuth, Hans-Ulrich

Published
2011
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42. Antifibrotic Effects of Amyloid-Beta and Its Loss in Cirrhotic Liver

Author

Buniatian, Gayane Hrachia, primary, Weiskirchen, Ralf, additional, Weiss, Thomas S., additional, Schwinghammer, Ute, additional, Fritz, Martin, additional, Seferyan, Torgom, additional, Proksch, Barbara, additional, Glaser, Michael, additional, Lourhmati, Ali, additional, Buadze, Marine, additional, Borkham-Kamphorst, Erawan, additional, Gaunitz, Frank, additional, Gleiter, Christoph H., additional, Lang, Thomas, additional, Schaeffeler, Elke, additional, Tremmel, Roman, additional, Cynis, Holger, additional, Frey, William H., additional, Gebhardt, Rolf, additional, Friedman, Scott L., additional, Mikulits, Wolfgang, additional, Schwab, Matthias, additional, and Danielyan, Lusine, additional

Published
2020
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45. Structure-guided design, synthesis, and characterization of next-generation meprin v inhibitors

Author

Ramsbeck, Daniel, Hamann, Antje, Richter, Georg, Schlenzig, Dagmar, Geißler, Stefanie, Nykiel, Vera, Cynis, Holger, Schilling, Stephan, Buchholz, Mirko, and Publica

Abstract

The metalloproteinase meprin v emerged as a current drug target for the treatment of a number of disorders, among those fibrosis, inflammatory bowel disease and Morbus Alzheimer. A major obstacle in the development of metalloprotease inhibitors is target selectivity to avoid side effects by blocking related enzymes with physiological functions. Here, we describe the structure-guided design of a novel series of compounds, based on previously reported highly active meprin v inhibitors. The bioisosteric replacement of the sulfonamide scaffold gave rise to a next generation of meprin inhibitors. Selected compounds based on this novel amine scaffold exhibit high activity against meprin v and also remarkable selectivity over related metalloproteases, i.e., matrix metalloproteases and A disintegrin and metalloproteinases.

Published
2018

46. P4‐689: INACTIVATION OF PATHOGENIC Aβ SEEDS AT PRE‐AMYLOID DISEASE STAGES

Author

Uhlmann, Ruth E., primary, Rasmussen, Jay, additional, Rother, Christine, additional, Schelle, Juliane, additional, Fritschi, Sarah K., additional, Buehler, Anika, additional, Baumann, Frank, additional, Kaeser, Stephan A., additional, Ullrich-Gavilanes, Emily M., additional, Obermüller, Ulrike, additional, Christensen, Søren, additional, Kartberg, Fredrik, additional, Stavenhagen, Jeffrey B., additional, Cynis, Holger, additional, Walker, Lary C., additional, Staufenbiel, Matthias, additional, and Jucker, Mathias, additional

Published
2019
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48. Dipeptidyl-Peptidase Activity of Meprin β Links N-truncation of Aβ with Glutaminyl Cyclase-Catalyzed pGlu-Aβ Formation

Author

Schlenzig, Dagmar, primary, Cynis, Holger, additional, Hartlage-Rübsamen, Maike, additional, Zeitschel, Ulrike, additional, Menge, Katja, additional, Fothe, Anja, additional, Ramsbeck, Daniel, additional, Spahn, Claudia, additional, Wermann, Michael, additional, Roßner, Steffen, additional, Buchholz, Mirko, additional, Schilling, Stephan, additional, and Demuth, Hans-Ulrich, additional

Published
2018
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