Relevant bibliographies by topics / Immunoproteasom

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Academic literature on the topic 'Immunoproteasom'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Immunoproteasom"

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Groll, Michael. "Immunoproteasom: drug development for xenotransplantation." Xenotransplantation 20, no. 1 (2013): 57. http://dx.doi.org/10.1111/xen.12014_14.

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Yasutomo, Koji. "Dysregulation of immunoproteasomes in autoinflammatory syndromes." International Immunology 31, no. 10 (2018): 631–37. http://dx.doi.org/10.1093/intimm/dxy059.

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Abstract Immunoproteasomes degrade ubiquitin-coupled proteins and play a role in creating peptides for presentation by MHC class I proteins. Studies of gene-deficient mice, in which each immunoproteasomal subunit was affected, have demonstrated that dysfunction of immunoproteasomes leads to immunodeficiency, i.e. reduced expression of MHC class I and attenuation of CD8 T-cell responses. Recent studies, however, have uncovered a new type of autoinflammatory syndrome characterized by fever, nodular erythema and progressive partial lipodystrophy that is caused by genetic mutations in immunoprotea
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Dubiella, Christian, Haissi Cui, and Michael Groll. "Regulierbare Sonden mit direktem Fluoreszenzsignal für das konstitutive und das Immunoproteasom." Angewandte Chemie 128, no. 42 (2016): 13524–28. http://dx.doi.org/10.1002/ange.201605753.

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Vagapova, Elmira, Alexander Burov, Daria Spasskaya, et al. "Immunoproteasome Activity and Content Determine Hematopoietic Cell Sensitivity to ONX-0914 and to the Infection of Cells with Lentiviruses." Cells 10, no. 5 (2021): 1185. http://dx.doi.org/10.3390/cells10051185.

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Proteasomes are intracellular structures responsible for protein degradation. The 20S proteasome is a core catalytic element of the proteasome assembly. Variations of catalytic subunits generate different forms of 20S proteasomes including immunoproteasomes (iPs), which are present mostly in the immune cells. Certain cells of the immune system are primary targets of retroviruses. It has been shown that several viral proteins directly affect proteasome functionality, while inhibition of proteasome activity with broad specificity proteasome inhibitors stimulates viral transduction. Here we speci
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Downey-Kopyscinski, Sondra, Ellen W. Daily, Marc Gautier та ін. "An inhibitor of proteasome β2 sites sensitizes myeloma cells to immunoproteasome inhibitors". Blood Advances 2, № 19 (2018): 2443–51. http://dx.doi.org/10.1182/bloodadvances.2018016360.

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Abstract Proteasome inhibitors bortezomib, carfilzomib and ixazomib (approved by the US Food and Drug Administration [FDA]) induce remissions in patients with multiple myeloma (MM), but most patients eventually become resistant. MM and other hematologic malignancies express ubiquitous constitutive proteasomes and lymphoid tissue–specific immunoproteasomes; immunoproteasome expression is increased in resistant patients. Immunoproteasomes contain 3 distinct pairs of active sites, β5i, β1i, and β2i, which are different from their constitutive β5c, β1c, and β2c counterparts. Bortezomib and carfilz
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Kammerl, Ilona E., and Silke Meiners. "Proteasome function shapes innate and adaptive immune responses." American Journal of Physiology-Lung Cellular and Molecular Physiology 311, no. 2 (2016): L328—L336. http://dx.doi.org/10.1152/ajplung.00156.2016.

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The proteasome system degrades more than 80% of intracellular proteins into small peptides. Accordingly, the proteasome is involved in many essential cellular functions, such as protein quality control, transcription, immune responses, cell signaling, and apoptosis. Moreover, degradation products are loaded onto major histocompatibility class I molecules to communicate the intracellular protein composition to the immune system. The standard 20S proteasome core complex contains three distinct catalytic active sites that are exchanged upon stimulation with inflammatory cytokines to form the so-c
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Khan, Selina, Albert Zimmermann, Michael Basler, Marcus Groettrup, and Hartmut Hengel. "A Cytomegalovirus Inhibitor of Gamma Interferon Signaling Controls Immunoproteasome Induction." Journal of Virology 78, no. 4 (2004): 1831–42. http://dx.doi.org/10.1128/jvi.78.4.1831-1842.2004.

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ABSTRACT Both human and mouse cytomegaloviruses (HCMV and MCMV) avoid peptide presentation through the major histocompatibility complex (MHC) class I pathway to CD8+ T cells. Within the MHC class I pathway, the vast majority of antigenic peptides are generated by the proteasome system, a multicatalytic protease complex consisting of constitutive subunits, three of which can be replaced by enzymatically active gamma interferon (IFN-γ)-inducible subunits, i.e., LMP2, LMP7, and MECL1, to form the so-called immunoproteasomes. Here, we show that steady-state levels of immunoproteasomes are readily
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Huber, Eva Maria, and Michael Groll. "Inhibitoren für das konstitutive Proteasom und das Immunoproteasom: aktuelle und zukünftige Tendenzen in der Medikamentenentwicklung." Angewandte Chemie 124, no. 35 (2012): 8838–50. http://dx.doi.org/10.1002/ange.201201616.

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Grimm, Stefanie, Christiane Ott, Melanie Hörlacher, Daniela Weber, Annika Höhn, and Tilman Grune. "Advanced-glycation-end-product-induced formation of immunoproteasomes: involvement of RAGE and Jak2/STAT1." Biochemical Journal 448, no. 1 (2012): 127–39. http://dx.doi.org/10.1042/bj20120298.

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AGEs (advanced glycation-end products) accumulate during aging and several pathologies such as Alzheimer's disease and diabetes. These protein products are known to inhibit proteolytic pathways. Moreover, AGEs are known to be involved in the activation of immune responses. In the present study we demonstrate that AGEs induce the expression of immunoproteasomal subunits. To elucidate a molecular basis underlying the observed effects we were able to demonstrate an activation of the Jak2 (Janus kinase 2)/STAT1 (signal transducer and activator of transcription 1) pathway. Inhibition of Jak2 by AG-
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Kuhn, Deborah J., Sally A. Hunsucker, Qing Chen, Peter M. Voorhees, Marian Orlowski, and Robert Z. Orlowski. "Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors." Blood 113, no. 19 (2009): 4667–76. http://dx.doi.org/10.1182/blood-2008-07-171637.

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Abstract Proteasome inhibition is a validated strategy for therapy of multiple myeloma, but this disease remains challenging as relapses are common, and often associated with increasing chemoresistance. Moreover, nonspecific proteasome inhibitors such as bortezomib can induce peripheral neuropathy and other toxicities that may compromise the ability to deliver therapy at full doses, thereby decreasing efficacy. One novel approach may be to target the immunoproteasome, a proteasomal variant found predominantly in cells of hematopoietic origin that differs from the constitutive proteasome found
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Dissertations / Theses on the topic "Immunoproteasom"

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Steiner, Melanie [Verfasser]. "Immunoproteasom und Proteasomaktivator 28 als Marker in der Diagnostik von Autoimmun- und Tumorerkrankungen / Melanie Steiner." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2017. http://d-nb.info/1148425691/34.

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von, Lachner Carolin [Verfasser]. "Die Pathogenese der Escherichia coli-induzierten Sepsis in einem Immunoproteasom defizienten Mausmodell / Carolin von Lachner." Berlin : Freie Universität Berlin, 2019. http://d-nb.info/1201346924/34.

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Stohwasser, Ralf. "Untersuchungen zur strukturellen und funktionellen Plastizität des 20S-Proteasoms der Maus und seiner Modulierung durch den Proteasomaktivator PA28." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2000. http://dx.doi.org/10.18452/13718.

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Die Studie beinhaltet eine biochemisch-molekularbiologische Analyse des 20S-Proteasoms und seiner Aktivierung durch Proteine der PA28-Familie. Das 20S-Proteasom ist die zentrale Epitop-prozessierende cytosolisch-nukleäre Protease des MHC-Klasse-I-Antigenpräsentationsweges. In Mikroglia, wie auch in anderen Zellen, unterliegt das Proteasom einer Interferon-g-(IFN-g)-vermittelten strukturellen Plastizität, d.h. einer Substitution der Untereinheiten der Aktiven Zentren. Durch diesen Austauschmechanismus werden proteolytische Schnittpräferenzen modifiziert, was für die Hierarchie von cytotoxische
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Brzezinski, Laura [Verfasser]. "Vergleich des Proteasom-Inhibitors Bortezomib und des Immunoproteasom-Inhibitors ONX-0914 in ihrer Wirkung auf kortikale Primärkulturen der Ratte / Laura Brzezinski." Magdeburg : Universitätsbibliothek, 2018. http://d-nb.info/1177881470/34.

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Heink, Sylvia. "Die proteasomale Homöostase." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2005. http://dx.doi.org/10.18452/15308.

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Das Proteasom spielt eine zentrale Rolle beim Proteinabbau und der Antigen-Generierung für die adaptive Immunantwort. Vertebraten exprimieren zwei Typen des proteolytischen 20S-Kernkomplexes: das konstitutive c20S (mit den aktiven Untereinheiten beta 1, 2, 5) und das Immunoproteasom i20S (mit den Immunountereinheiten LMP2, MECL-1, LMP7). Die i20S-Expression wird durch Interferon_gamma (IFNg) induziert, was die Antigen-Präsentation auf MHC Klasse I und die Immunantwort gegen infizierte bzw. maligne entartete Zellen durch cytotoxische T-Zellen steigert. Proteasomen werden über komplexe, bisher
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Schmidt, Christian [Verfasser]. "Immunoproteasome Function in Lymphocyte Activation / Christian Schmidt." Konstanz : Bibliothek der Universität Konstanz, 2019. http://d-nb.info/117832544X/34.

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Opitz, Elisa. "The impact of immunoproteasomes in murine CVB3-associated myocarditis." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2013. http://dx.doi.org/10.18452/16734.

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Das Proteasom ist ein multikatalytischer, ATP-abhängiger Enzymkomplex, der kurzlebige und regulatorische Proteine in der Zelle abbaut. Im Rahmen der Proteinqualitätskontrolle werden durch das Proteasom auch fehlerhaft synthetisierte bzw. falsch gefaltete oder chemisch geschädigte Proteine degradiert. Zellen hämatopoetischen Ursprungs exprimieren sogenannte Immunoproteasomen, die durch drei alternative katalytische Untereinheiten (LMP2, MECL-1 und LMP7) charakterisiert sind. Unter dem Einfluss von Interferonen kommt es auch in nicht-hämatopoetischen Zellen zur de novo Assemblierung von IP. Sie
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Mundt, Sarah [Verfasser]. "Targeting the Immunoproteasome in Health and Disease / Sarah Mundt." Konstanz : Bibliothek der Universität Konstanz, 2016. http://d-nb.info/1155722892/34.

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Rieger, Melanie. "Strukturelle und funktionelle Anpassung des Ubiquitin-Proteasomsystems an IFN-gamma." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2009. http://dx.doi.org/10.18452/15888.

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Das Ubiquitin-Proteasom-System ist an der Degradation cytosolischer Proteine und der Generierung von Antigenen beteiligt, die über MHC Klasse I Moleküle CD8+ T Zellen präsentiert werden. Die Antigenprozessierung wird durch Typ I und II Interferone beeinflusst, welche die Formierung des Immunoproteasoms und des Proteasomen-Aktivators PA28 induzieren und so die katalytische Aktivität des Ubiquitin-Proteasom-Systems qualitativ verändern. In der vorliegenden Arbeit wurde im Zellkulturmodell unter dem Einfluss von IFN gamma die zunehmende Inkorporation der Immunountereinheiten in de novo assemblie
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Brooks, Paul. "Subcellular localization, induction by #gamma#-interferon and purification of the proteasome activator PA28." Thesis, University of Bristol, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324332.

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Books on the topic "Immunoproteasom"

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Huber, Eva Maria. Structural and Functional Characterization of the Immunoproteasome. Springer International Publishing, 2013. http://dx.doi.org/10.1007/978-3-319-01556-9.

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Huber, Eva Maria. Structural and Functional Characterization of the Immunoproteasome. Springer, 2013.

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Book chapters on the topic "Immunoproteasom"

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Basler, Michael, and Marcus Groettrup. "Immunoproteasome-Specific Inhibitors and Their Application." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2_27.

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Rinaudo, M. T., and M. Piccinini. "Immunoproteasome Activity in the Nervous System." In Handbook of Neurochemistry and Molecular Neurobiology. Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-30398-7_9.

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Pickering, Andrew M., and Richard A. Miller. "Immunoproteasome System in Aging, Lifespan, and Age-Associated Disease." In Handbook of Immunosenescence. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-64597-1_111-1.

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Pickering, Andrew M., and Richard A. Miller. "Immunoproteasome System in Aging, Lifespan, and Age-Associated Disease." In Handbook of Immunosenescence. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-99375-1_111.

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Visekruna, A., H. J. Buhr, J. P. Ritz, et al. "Enhanced activity of immunoproteasomes in patiens with Crohn’s disease." In Deutsche Gesellschaft für Chirurgie. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00625-8_86.

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"Immunoproteasome." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_101204.

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"Immunoproteasomes." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_8349.

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Ferrington, Deborah A., and Dale S. Gregerson. "Immunoproteasomes." In Progress in Molecular Biology and Translational Science. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-397863-9.00003-1.

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Conference papers on the topic "Immunoproteasom"

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Nowak, Johannes, Gabriel Stoleriu, Christina Lukas, et al. "Role of immunoproteasomes in fibrotic remodeling." In Abstracts from the 17th ERS Lung Science Conference: ‘Mechanisms of Acute Exacerbation of Respiratory Disease’. European Respiratory Society, 2019. http://dx.doi.org/10.1183/23120541.lungscienceconference-2019.pp124.

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Jenkins, Tyler W., Sondra Downey-Kopyscinski, William C. Colley, Jennifer L. Fields, Steven N. Fiering, and Alexei F. Kisselev. "Abstract 1936: Immunoproteasome inhibitors for the treatment of ALL." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1936.

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Chen, Jie, Judith Brands, Marta Bueno, et al. "Effect of cigarette smoke on immunoproteasome function during virus infection." In Abstracts from the 17th ERS Lung Science Conference: ‘Mechanisms of Acute Exacerbation of Respiratory Disease’. European Respiratory Society, 2019. http://dx.doi.org/10.1183/23120541.lungscienceconference-2019.pp119.

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Wang, Xinyuan, Ilona Kammerl, Oliver Eickelberg, Andrea Schamberger, and Silke Meiners. "Role of the immunoproteasome during of bronchial epithelial cell differentiation." In Abstracts from the 17th ERS Lung Science Conference: ‘Mechanisms of Acute Exacerbation of Respiratory Disease’. European Respiratory Society, 2019. http://dx.doi.org/10.1183/23120541.lungscienceconference-2019.pp220.

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Kammerl, Ilona, Shanze Chen, Martin Irmler, et al. "Deficiency of immunoproteasome subunit LMP2 increases alternative polarization of alveolar macrophages." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa1817.

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Negasi, Z. H., J. J. Rojas-Quintero, D. Tassew, and Y. Tesfaigzi. "Noxa Increases Assembly of Immunoproteasome to Block the Development of COPD." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4272.

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Chen, Jie, Judith Brands, Marta Bueno, et al. "LSC - 2019 - Effect of cigarette smoke on immunoproteasome function during virus infection." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa2405.

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Lee, Na-Ra, Kimberly C. Carmony, Ying Wu, Zachary Miller, and Kyung-Bo Kim. "Abstract 4744: Development of an immunoproteasome fluorescent substrate: A functional proteomics tool." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4744.

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Meul, T., X. Wang, I. Angelidis, et al. "Mitochondrial dysfunction induce immunoproteasome and MHC class I responses in lung aging." In ERS Lung Science Conference 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/23120541.lsc-2020.89.

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OR-GUIL, MICHAL, FABIO LUCIANI, and JORGE CARNEIRO. "CLONAL EXPANSION OF CYTOTOXIC T CELL CLONES: THE ROLE OF THE IMMUNOPROTEASOME." In Proceedings of the International Symposium on Mathematical and Computational Biology. WORLD SCIENTIFIC, 2006. http://dx.doi.org/10.1142/9789812773685_0012.

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