Auswahl der wissenschaftlichen Literatur zum Thema „Aminopeptidase N“
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Zeitschriftenartikel zum Thema "Aminopeptidase N":
Jóźwik, Artur, Ewa Polawska, Nina Strzałkowska, Krzysztof Niemczuk, Małgorzata Łysek-Gładysińska, Agnieszka Kamińska und Monika Michalczuk. „Effect of linseed, rapeseed, and vitamin E long term supplementation on the activity of the lysosomal enzymes in ostrich liver“. Bulletin of the Veterinary Institute in Pulawy 57, Nr. 4 (01.12.2013): 573–78. http://dx.doi.org/10.2478/bvip-2013-0098.
Varona, Adolfo, Lorena Blanco, José I. López, Javier Gil, Ekaitz Agirregoitia, Jon Irazusta und Gorka Larrinaga. „Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma“. American Journal of Physiology-Renal Physiology 292, Nr. 2 (Februar 2007): F780—F788. http://dx.doi.org/10.1152/ajprenal.00148.2006.
Veillard, Florian, Barbara Potempa, Marcin Poreba, Marcin Drag und Jan Potempa. „Gingipain aminopeptidase activities in Porphyromonas gingivalis“. Biological Chemistry 393, Nr. 12 (01.12.2012): 1471–76. http://dx.doi.org/10.1515/hsz-2012-0222.
Matsas, R., S. L. Stephenson, J. Hryszko, A. J. Kenny und A. J. Turner. „The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N“. Biochemical Journal 231, Nr. 2 (15.10.1985): 445–49. http://dx.doi.org/10.1042/bj2310445.
Galán-Ocaña, A., M. J. Ramírez-Expósito, J. M. Martínez-Martos, S. Tellado und C. Azorit. „Regulation of aminopeptidases by the renin - angiotensin system: monitoring seasonal variations in red deer and fallow deer from a Mediterranean ecosystem“. Animal Production Science 52, Nr. 8 (2012): 761. http://dx.doi.org/10.1071/an12023.
Jackson, M. C., Y. Choudry, A. Bourne, J. F. Woodley und A. J. Kenny. „A fluorimetric assay for aminopeptidase W“. Biochemical Journal 253, Nr. 1 (01.07.1988): 299–302. http://dx.doi.org/10.1042/bj2530299.
Martínez-Martos, José Manuel, María Correa-Rodríguez, Alma Rus, Francisco Molina, María Jesús Ramírez-Expósito und María Encarnación Aguilar-Ferrandiz. „Altered Serum Oxytocinase and Enkephalin-Degrading Aminopeptidase Activities in Patients With Fibromyalgia“. Biological Research For Nursing 21, Nr. 4 (26.05.2019): 431–39. http://dx.doi.org/10.1177/1099800419854207.
ZHANG, Zhen-Zhong, Satoru NIRASAWA, Yoshiaki NAKAJIMA, Michiteru YOSHIDA und Kiyoshi HAYASHI. „Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus“. Biochemical Journal 350, Nr. 3 (08.09.2000): 671–76. http://dx.doi.org/10.1042/bj3500671.
Cunningham, Eithne, Marcin Drag, Pawel Kafarski und Angus Bell. „Chemical Target Validation Studies of Aminopeptidase in Malaria Parasites Using α-Aminoalkylphosphonate and Phosphonopeptide Inhibitors“. Antimicrobial Agents and Chemotherapy 52, Nr. 9 (05.05.2008): 3221–28. http://dx.doi.org/10.1128/aac.01327-07.
Wanat, Weronika, Michał Talma, Małgorzata Pawełczak und Paweł Kafarski. „Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases: Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds“. Pharmaceuticals 12, Nr. 3 (17.09.2019): 139. http://dx.doi.org/10.3390/ph12030139.
Dissertationen zum Thema "Aminopeptidase N":
Al-Lakkis, Mira. „Application des dérivés d'amino-benzosubérone : inhibition sélective des aminopeptidases mono ou bimétalliques“. Phd thesis, Université de Haute Alsace - Mulhouse, 2012. http://tel.archives-ouvertes.fr/tel-01060176.
Lai, Amy M. „Role of aminopeptidase N in wound healing“. Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/39957.
Sansot, Jean-Luc. „Alanine aminopeptidase approches biochimique et toxicologique /“. Grenoble 2 : ANRT, 1986. http://catalogue.bnf.fr/ark:/12148/cb376010389.
Golich, Frank Carl. „Structural and Functional Characterization of Aminopeptidase N (PEPN) from Escherichia coli“. Miami University / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=miami1143229893.
Fiddler, Christine Alison. „Role of aminopeptidase N/CD13 in neutrophil migration and aggregation“. Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708480.
Gillingham, Helen. „Role and regulation of aminopeptidase N (CD13) in HT1080 fibrosarcoma cells“. Thesis, University of Cambridge, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.610322.
Roux, Lionel. „Conception et synthèse d'inhibiteurs de l'Aminopeptidase membranaire N ([EC. 3.4.11.2], APN ou CD13)“. Thesis, Mulhouse, 2010. http://www.theses.fr/2010MULH4691/document.
The fight against the cancer is one of the most important struggles of this century. For the development of the tumors inside the body, they need to receive nutriments by the blood vessels and they use the angiogenic process. During this process, the endothelial cells being shown on the wall of the blood vessel will multiply and design new blood vessel, which will allow the tumor's vascularisation. Today, the angiogenesis is an axis of research for the fight against the cancer. During the tumoral development, the aminopeptidase N (APN) is overexpressed on the wall of endothelial cells. Various studies have shown that the inhibition of this enzyme stops the tumoral progression. My work in the Pr. Céline Tarnus Team consists in the conception and the synthesis of APN's inhibitors. In a first time, a structure activity relationship has been realized. Syntheses of a subnamolar compound have been developed, and then the synthesis of APN's inhibitors with the use of BNCT has been got onto
Al-Masri, Mounir. „Conception, synthèse et évaluation des dérivés d'aminobenzosubérone comme inhibiteurs potentiels des aminopeptidases de la famille M1“. Thesis, Mulhouse, 2017. http://www.theses.fr/2017MULH2862.
Aminopeptidases of the M1 family are proteases that catalyze the hydrolysis of a peptide bond in the N-terminal position. These are metalloproteases with a zinc ion in their active site conserved in all members of this protein family. These enzymes are involved in many normal physiological processes, but also in metabolic disorders, such as tumor progression, autoimmune diseases, as well as in viral, bacterial and parasitic infections. For these reasons, these aminopeptidases are considered potential therapeutic targets for treating or diagnosing various diseases. In 2006, the laboratory discovered the powerful and selectively inhibiting 3-amino-2-benzosuberone molecular chassis and one of the members of this family of aminopeptidases, namely the APN. The design and synthesis of derivatives of this molecular chassis as potential and selective inhibitors for five other members of the M1 family (APN, ERAP1 / 2, IRAP and PfA-M1) is at the heart of this work. Pharmacological, pharmacokinetic and preclinical studies have been conducted and their results will be presented in the case of PfA-M1 inhibition
Geisler, Michael. „Untersuchung der Regulation der Promotoraktivität von Aminopeptidase N (APN) in hämatopoietischen Zellen“. [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975657801.
Frottin, Frédéric. „Analyse intégrative du rôle de l’excision de la méthionine N-terminale dans le cytoplasme des eucaryotes supérieurs“. Thesis, Paris 11, 2011. http://www.theses.fr/2011PA112045/document.
The first amino acid incorporated in nascent polypeptide chain is always methionine so called N-terminale methionine. However, in a given proteome, more than fifty percent of proteins have not this first methionine. Indeed, the early proteolytic event affecting a majority of proteins is N-terminal Methionine Excision (NME) as soon as few residues exit from the ribosome. Enzymes ensuring NME process are conserved along species. This mechanism takes place in all compartments where protein synthesis occurs including cytoplasm, plastids and mitochondria and the enzymes responsible of N-methionine excision are METhionine AminoPeptidases (METAP). Early functional studies of gene deletion has quickly showed that NME is an essential process. Ten years ago, METAPs have been identified as the molecular target of natural compounds with anticancer activities. Now, a growing number of studies suggest that NME is a promising target for treatment of various deseases. Nevertheless, molecular mechanisms making NME an essential process is poorly understood in particular in higher eukaryote cytoplasms.Using a dedicated inducible system in the model organism Arabidopsis thaliana and multiple approaches, including proteomics and metabolomics, I examined the earliest molecular events associated with the inhibition of this process and the contribution of both METAP to NME process. In this context, I demonstrated that cytoplasmic NME in A. thaliana orchestrates a cross-talk between two fundamental signaling pathways frequently deregulated in pathological conditions: thiol status and proteolysis. In these studies, we demonstrated that developmental defects induced by cytoplasmic NME inhibition are associated with an increase of the proteolytic activity due to an increase of the proteins available for rapid degradation. Thus, NME activity that modifies the availability of several proteins for degradation is an integral and fundamental element protein turnover regulation. Finally my preliminary results obtained in Archea, Fungi and human cells seem to suggest the existence of a ubiquitous mechanism associated with NME process
Bücher zum Thema "Aminopeptidase N":
name, No. Ectopeptidases: CD13/aminopeptidase N and CD26/dipeptidylpeptidase IV in medicine and biology. New York, NY: Kluwer Academic/Plenum, 2003.
See, Hilario. Purification of the major stilbene disulfonate- and concanavalin A-binding protein (GP130) of the porcine renal brush border membrane and its identification as aminopeptidase N. Ottawa: National Library of Canada, 1990.
Langner, Jürgen, und Siegfried Ansorge. Ectopeptidases: CD13/Aminopeptidase N and CD26/Dipeptidylpeptidase IV in Medicine and Biology. Springer, 2012.
(Editor), Jürgen Langner, und Siegfried Ansorge (Editor), Hrsg. Ectopeptidases: CD13/Aminopeptidase N and CD26/Dipeptidylpeptidase IV in Medicine and Biology. Springer, 2002.
Buchteile zum Thema "Aminopeptidase N":
Sjöström, Hans, Ove Norén und Jørgen Olsen. „Structure and Function of Aminopeptidase N“. In Cellular Peptidases in Immune Functions and Diseases 2, 25–34. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46826-3_2.
Olsen, Jørgen, Klaus Kokholm, Ove Norén und Hans Sjöström. „Structure and Expression of Aminopeptidase N“. In Advances in Experimental Medicine and Biology, 47–57. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_7.
Petrovic, Nenad, Wolfgang Schacke und Linda H. Shapiro. „CD13/Aminopeptidase N in Tumor Growth and Angiogenesis“. In Aminopeptidases in Biology and Disease, 179–200. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-8869-0_9.
Fournié-Zaluski, Marie-Claude, und Bernard P. Roques. „New Selective Aminopeptidase N Inhibitors as Potential Therapeutics“. In Ectopeptidases, 51–94. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0619-5_3.
Delmas, Bernard, Jacqueline Gelfi, Hans Sjöström, Ove Noren und Hubert Laude. „Further Characterization of Aminopeptidase-N as a Receptor for Coronaviruses“. In Coronaviruses, 293–98. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2996-5_45.
Sato, Ryoichi. „Aminopeptidase N as a Receptor for Bacillus Thuringiensis Cry Toxins“. In Advances in Microbial Control of Insect Pests, 1–13. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-4437-8_1.
Kolb, Andreas F., Annette Hegyi, Julia Maile, Angelien Heister, Margitta Hagemann und Stuart G. Siddell. „Molecular Analysis of the Coronavirus-Receptor Function of Aminopeptidase N“. In Advances in Experimental Medicine and Biology, 61–67. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_8.
Tresnan, Dina B., und Kathryn V. Holmes. „Feline Aminopeptidase N is a Receptor for All Group I Coronaviruses“. In Advances in Experimental Medicine and Biology, 69–75. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_9.
Löhn, M., C. Mueller, K. Thiele, T. Kähne, D. Riemann und J. Langner. „Aminopeptidase N-Mediated Signal Transduction and Inhibition of Proliferation of Human Myeloid Cells“. In Advances in Experimental Medicine and Biology, 85–91. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_12.
Thiele, Katja, Dagmar Riemann, Astrid Kehlen, Matthias Löhn, Lotte K. Vogel und Jürgen Langner. „Two Transfected Endothelial Cell Lines Expressing High Levels of Membrane Bound or Soluble Aminopeptidase N“. In Advances in Experimental Medicine and Biology, 81–84. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_11.
Konferenzberichte zum Thema "Aminopeptidase N":
James, J., M. Valuparampil Varghese, O. Rafikova und R. Rafikov. „Aminopeptidase-N Triggers Uncontrolled Proliferation of Pulmonary Artery Smooth Muscle Cells“. 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.a3644.
Katsumata, M., und S. Wilkinson. „Diurnal variations of activities of disaccharidases and aminopeptidase N in growing barrows“. In 6th EAAP International Symposium on Energy and Protein Metabolism and Nutrition. The Netherlands: Wageningen Academic Publishers, 2019. http://dx.doi.org/10.3920/978-90-8686-891-9_90.
Wickström, Malin, Kristina Viktorsson, Lovisa Lundholm, Reidun Aesoy, Helen Nygren, Linda Sooman, Mårten Fryknäs, Rolf Lewensohn, Rolf Larsson und Joachim Gullbo. „Abstract B187: Role of aminopeptidase N in the activation of the alkylating prodrug J1“. In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b187.
Huang, Qing, Yong Wang, Wenjie Zhu, Shibin Ai, Elfed Lewis und Minghong Yang. „Aminopeptidase N (CD13) Modified Gold Films for the Affinity Quantitative Detection of CNGRC-coupled Derivative“. In 2019 18th International Conference on Optical Communications and Networks (ICOCN). IEEE, 2019. http://dx.doi.org/10.1109/icocn.2019.8934768.
Laitinen, Sara, Malin Wickstrom, Peder Fredlund Fuchs, Par Gerwins, Rolf Larsson und Joachim Gullbo. „Abstract B6: Aminopeptidase N-activated prodrug melphalan-flufenamide (J1) inhibits angiogenesis in vitro and in vivo.“ In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-b6.
Kadefors, Måns, Sara Rolandsson Enes, Maria Weitoft, Stefan Scheding und Gunilla Westergren-Thorsson. „Late Breaking Abstract - Aminopeptidase N/CD13 distinguishes two populations of colony-forming mesenchymal stromal cells in human lung tissue“. In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.4467.
Berichte der Organisationen zum Thema "Aminopeptidase N":
Yeager, Curtis. Identification of Aminopeptidase N as a Cellular Receptor for Human Coronavirus-229E. Fort Belvoir, VA: Defense Technical Information Center, April 1992. http://dx.doi.org/10.21236/ad1011150.
Wong, Eric A., und Zehava Uni. Nutrition of the Developing Chick Embryo: Nutrient Uptake Systems of the Yolk Sac Membrane and Embryonic Intestine. United States Department of Agriculture, Juni 2012. http://dx.doi.org/10.32747/2012.7697119.bard.