Relevant bibliographies by topics / Aminopeptidase inhibition

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  2. Dissertations / Theses
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  5. Conference papers

Academic literature on the topic 'Aminopeptidase inhibition'

Author: Grafiati
Published: 4 June 2025
Last updated: 1 August 2025

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Journal articles on the topic "Aminopeptidase inhibition"

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Baranczyk-Kuzma, Anna, and Kenneth L. Audus. "Characteristics of Aminopeptidase Activity from Bovine Brain Microvessel Endothelium." Journal of Cerebral Blood Flow & Metabolism 7, no. 6 (1987): 801–5. http://dx.doi.org/10.1038/jcbfm.1987.137.

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Blood–brain barrier (BBB) aminopeptidase activity was investigated using an in vitro model consisting of primary cultures of brain microvessel endothelium. Using two different substrates, both membrane-bound and soluble aminopeptidases were found to be associated with brain endothelium. That the enzyme activity was aminopeptidase activity was confirmed with the competitive inhibition of substrate degradation by typical aminopeptidase inhibitors puromycin and bestatin. The aminopeptidase activity was also competitively inhibited by enkephalin, met-enkephalin, and leu-enkephalin. Results from pa
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Sanz, Yolanda, and Fidel Toldrá. "Myoglobin as an Inhibitor of Exopeptidases from Lactobacillus sake." Applied and Environmental Microbiology 64, no. 6 (1998): 2313–14. http://dx.doi.org/10.1128/aem.64.6.2313-2314.1998.

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ABSTRACT The effects of myoglobin on exopeptidases of Lactobacillus sake were determined. Inhibition of the aminopeptidases increased as the myoglobin concentration increased; aminopeptidase 3 was the most affected (90% inhibition). Aminopeptidases 1, 2, and 4 showed similar inhibition levels (around 60%). Myoglobin did not affect tripeptidase activity. Thus, myoglobin could limit amino acid generation in meat systems.
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Cunningham, Eithne, Marcin Drag, Pawel Kafarski та Angus Bell. "Chemical Target Validation Studies of Aminopeptidase in Malaria Parasites Using α-Aminoalkylphosphonate and Phosphonopeptide Inhibitors". Antimicrobial Agents and Chemotherapy 52, № 9 (2008): 3221–28. http://dx.doi.org/10.1128/aac.01327-07.

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ABSTRACT During its intraerythrocytic phase, the most lethal human malarial parasite, Plasmodium falciparum, digests host cell hemoglobin as a source of some of the amino acids required for its own protein synthesis. A number of parasite endopeptidases (including plasmepsins and falcipains) process the globin into small peptides. These peptides appear to be further digested to free amino acids by aminopeptidases, enzymes that catalyze the sequential cleavage of N-terminal amino acids from peptides. Aminopeptidases are classified into different evolutionary families according to their sequence
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Dalal, Seema, and Michael Klemba. "Roles for Two Aminopeptidases in Vacuolar Hemoglobin Catabolism in Plasmodium falciparum." Journal of Biological Chemistry 282, no. 49 (2007): 35978–87. http://dx.doi.org/10.1074/jbc.m703643200.

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During the erythrocytic stage of its life cycle, the human malaria parasite Plasmodium falciparum catabolizes large quantities of host-cell hemoglobin in an acidic organelle, the food vacuole. A current model for the catabolism of globin-derived oligopeptides invokes peptide transport out of the food vacuole followed by hydrolysis to amino acids by cytosolic aminopeptidases. To test this model, we have examined the roles of four parasite aminopeptidases during the erythrocytic cycle. Localization of tagged aminopeptidases, coupled with biochemical analysis of enriched food vacuoles, revealed t
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Salomon, Emmanuel, Marjorie Schmitt, Anil Marapaka, et al. "Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases." Molecules 23, no. 10 (2018): 2607. http://dx.doi.org/10.3390/molecules23102607.

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The synthesis of racemic substituted 7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochlorides was optimized to enhance reproducibility and increase the overall yield. In order to investigate their specificity, series of enzyme inhibition assays were carried out against a diversity of proteases, covering representative members of aspartic, cysteine, metallo and serine endopeptidases and including eight members of the monometallic M1 family of aminopeptidases as well as two members of the bimetallic M17 and M28 aminopeptidase families. This aminobenzosuberone scaffold indeed demonstrated
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Jackson, M. C., Y. Choudry, A. Bourne, J. F. Woodley, and A. J. Kenny. "A fluorimetric assay for aminopeptidase W." Biochemical Journal 253, no. 1 (1988): 299–302. http://dx.doi.org/10.1042/bj2530299.

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A novel two-step enzyme-linked assay for aminopeptidase W is described and validated by comparison with other assays. L-alpha-Glutamyl-L-tryptophan (Glu-Trp) is a favoured substrate for this enzyme. With the use of glutamate dehydrogenase (EC 1.4.1.2) in a second step, the assay measured the release of free glutamate from L-alpha-glutamyl-L-tryptophan by the increase in NADH fluorescence. In the presence of 5 mM-1,10-phenanthroline and 50 microM-cilastatin the contribution of other membrane peptidases, in particular aminopeptidases N and A and microsomal dipeptidase in kidney, was very small.
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Farsa, Oldřich, Veronika Ballayová, Radka Žáčková, Peter Kollar, Tereza Kauerová, and Peter Zubáč. "Aminopeptidase N Inhibitors as Pointers for Overcoming Antitumor Treatment Resistance." International Journal of Molecular Sciences 23, no. 17 (2022): 9813. http://dx.doi.org/10.3390/ijms23179813.

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Aminopeptidase N (APN), also known as CD13 antigen or membrane alanyl aminopeptidase, belongs to the M1 family of the MA clan of zinc metallopeptidases. In cancer cells, the inhibition of aminopeptidases including APN causes the phenomenon termed the amino acid deprivation response (AADR), a stress response characterized by the upregulation of amino acid transporters and synthetic enzymes and activation of stress-related pathways such as nuclear factor kB (NFkB) and other pro-apoptotic regulators, which leads to cancer cell death by apoptosis. Recently, APN inhibition has been shown to augment
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Hooper, N. M., R. J. Hesp, and S. Tieku. "Metabolism of aspartame by human and pig intestinal microvillar peptidases." Biochemical Journal 298, no. 3 (1994): 635–39. http://dx.doi.org/10.1042/bj2980635.

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The artificial sweetener aspartame (N-L-alpha-aspartyl-L-phenyl-alanine-1-methyl ester; Nutrasweet), its decomposition product alpha Asp-Phe and the related peptide alpha Asp-PheNH2 were rapidly hydrolysed by microvillar membranes prepared from human duodenum, jejunum and ileum, and from pig duodenum and kidney. The metabolism of aspartame by the human and pig intestinal microvillar membrane preparations was inhibited significantly (> 78%) by amastatin or 1,10-phenanthroline, and partially (> 38%) by actinonin or bestatin, and was activated 2.9-4.5-fold by CaCl2. The inhibition by amasta
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Herranz, Rosario, Julia Castro-Pichel, M. Teresa García-López, Isabel Gómez-Monterrey, Concepción Pérez, and Soledad Vinuesa. "Ketomethylenebestatin: Synthesis and Aminopeptidase Inhibition." Archiv der Pharmazie 326, no. 7 (1993): 395–98. http://dx.doi.org/10.1002/ardp.19933260705.

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Albiston, Anthony L., Mauricio Cacador, Puspha Sinnayah, Peta Burns, and Siew Yeen Chai. "Insulin-regulated aminopeptidase inhibitors do not alter glucose handling in normal and diabetic rats." Journal of Molecular Endocrinology 58, no. 4 (2017): 193–98. http://dx.doi.org/10.1530/jme-17-0033.

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Insulin-regulated aminopeptidase (IRAP) co-localizes with the glucose transporter 4 (GLUT4) in GLUT4 storage vesicles (GSV) in insulin-responsive cells. In response to insulin, IRAP is the only transmembrane enzyme known to translocate together with GLUT4 to the plasma membrane in adipocytes and muscle cells. Although the intracellular region of IRAP is associated with GLUT4 vesicle trafficking, the role of the aminopeptidase activity in insulin-responsive cells has not been elucidated. The aim of this study was to investigate whether the inhibition of the aminopeptidase activity of IRAP facil
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Dissertations / Theses on the topic "Aminopeptidase inhibition"

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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.

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Les aminopeptidases sont des cibles thérapeutiques importantes pour plusieurs maladies, car elles sont impliquées dans divers processus physiologiques et pathologiques comme la progression tumorale, l'angiogenèse, et certaines infections (virales, bactériennes, et parasitaires). Il en existe deux classes : les aminopeptidases avec un ion métallique (Aminopeptidase N [APN ou CD13] et leukotrien A4 hydrolase [LTA4H]) et les aminopeptidases avec deux ions métalliques (Aminopeptidase de l'Aeromonas proteolytica [APaero], Leucine Aminopeptidase cytosolique [LAPc] et Méthionine aminopeptidase 1 ou 2
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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.

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Les aminopeptidases de la famille M1 sont des protéases qui catalysent l’hydrolyse d’une liaison peptidique en position N-terminale. Ce sont des métalloprotéases avec un ion zinc dans leur site actif conservé dans tous les membres de cette famille de protéine. Ces enzymes sont impliqués dans de nombreux processus physiologiques normaux, mais également dans des désordres métaboliques, tels que la progression tumorale, des maladies auto-immunes, ainsi que dans des infections virales, bactériennes et parasitaires. Pour ces raisons, ces aminopeptidases sont considérées comme des cibles thérapeutiq
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Maben, Zachary. "The Relationship Between Inhibition, Conformation, and Catalysis of the Aminopeptidase ERAP1." eScholarship@UMMS, 2018. https://escholarship.umassmed.edu/gsbs_diss/1003.

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ERAP1 is an aminopeptidase that is a component of antigen processing. To distinguish the role of ERAP1 from homologs ERAP2 and IRAP, I identified three specific ERAP1 inhibitors via a high-throughput screen. These compounds inhibit hydrolysis of a decamer peptide, and some inhibit ERAP1 in a cellular assay. These inhibitors enable dissection of ERAP1 mechanism. ERAP1 has been crystallized in two conformations: open and closed. I collected SAXS data on ERAP1 in the presence of various inhibitors. ERAP1 adopts an open conformation in solution, but some inhibitors stabilize the closed form. Compo
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Andersson, Hanna. "Design and Synthesis of Angiotensin IV Peptidomimetics Targeting the Insulin-Regulated Aminopeptidase (IRAP)." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-122218.

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Nakamura, Kimihiko. "An aminopeptidase inhibitor,bestatin, enhances gonadotropin-stimulated ovulation in mice." Kyoto University, 1997. http://hdl.handle.net/2433/202239.

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Camberlein, Virgyl. "Target-guided synthesis of metalloenzymes ligands with therapeutic applications." Thesis, Université de Lille (2022-....), 2022. http://www.theses.fr/2022ULILS004.

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La synthèse guidée par la cible de ligands protéiques est une stratégie innovante pour découvrir des composés bioactifs. En particulier, la Kinetic Target-Guided Synthesis (KTGS) and the Dynamic Combinatorial Chemistry (DCC) ont permis, ces dernières années, de découvrir des ligands originaux pour des cibles thérapeutiques mal explorées, ce qui a permis de lancer des projets de découverte de médicaments. Ce projet de thèse vise à utiliser la KTGS pour découvrir, puis optimiser des ligands de deux classes de métalloenzymes que sont les aminopeptidases du réticulum endoplasmiques (ERAP) et l’éla
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Harbeson, Scott L. "Inhibition of aminopeptidases by peptides incorporating amide bond replacements." 1986. http://catalog.hathitrust.org/api/volumes/oclc/14171031.html.

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Thesis (Ph. D.)--University of Wisconsin--Madison, 1986.<br>Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 250-262).
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Wang, Li-Wen, and 王麗雯. "To study the effect of aminopeptidase A inhibitor on breast cancer." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/25604887795017951472.

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碩士<br>國立陽明大學<br>醫學生物技術暨檢驗學系<br>103<br>Breast cancer is one of the most common cancers in female. According to 2013 statistics from Cancer Journal for Clinicians, the incidence of female breast cancer accounted for the first and the mortality rate was the second among all cancers. The treatments for breast cancer include surgery, radiotherapy, chemotherapy, hormone therapy and target therapy. Previous studies showed that miR-125b is a tumor suppressor miRNA in many tumor types and ENPEP gene is one of miR-125b target genes. Besides, they found that ENPEP gene was overexpressed in 56% breast can
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Cheng, Pei-Chen, and 鄭佩甄. "To study the potential inhibitory mechanism of aminopeptidase A inhibitor in colorectal cancer stem cells." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/gg7j6r.

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碩士<br>國立陽明大學<br>醫學生物技術暨檢驗學系<br>105<br>Colorectal cancer (CRC) is the third most common cancer in the world and ranked third in cancer relating deaths in 2015. Approximately sixty percent of CRC patients can be treated by surgery, chemotherapy, radiation therapy and targeted therapy. However, CRC is seldom cured due to recurrence. Previous studies indicates that cancer stem cells (CSCs) are responsible for self-renewal and resistance to cytotoxic agents. Traditional cancer therapies usually kill differentiated cancer cells but not CSCs, and often lead to relapse. Meanwhile, CSC-targeted therapi
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Su, Pin-Chen, and 蘇品甄. "To study the effect of aminopeptidase A inhibitor on head and neck squamous cell carcinoma." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/98vn6f.

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Books on the topic "Aminopeptidase inhibition"

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The effect of bestatin, an aminopeptidase inhibitor, in reducing ethanol consumption in the rat: Mechanism of action and clinical significance. National Library of Canada, 1994.

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Book chapters on the topic "Aminopeptidase inhibition"

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Löhn, M., C. Mueller, K. Thiele, T. Kähne, D. Riemann, and J. Langner. "Aminopeptidase N-Mediated Signal Transduction and Inhibition of Proliferation of Human Myeloid Cells." In Advances in Experimental Medicine and Biology. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_12.

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Wex, T., U. Lendeckel, D. Reinhold, et al. "Antisense-Mediated Inhibition of Aminopeptidase N (CD13) Markedly Decreases Growth Rates of Hematopoietic Tumour Cells." In Advances in Experimental Medicine and Biology. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_9.

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Andrew Pospisilik, J., Jan A. Ehses, Timothy Doty, Christopher H. S. McIntosh, Hans-Ulrich Demuth, and Raymond A. Pedersohn. "Dipeptidyl Peptidase IV Inhibition in Animal Models of Diabetes." In Dipeptidyl Aminopeptidases in Health and Disease. Springer US, 2004. http://dx.doi.org/10.1007/0-306-47920-6_34.

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Scornik, Oscar A., and Violeta Botbol. "Effects on Mammals of the Aminopeptidase Inhibitor Bestatin." In Aminopeptidases in Biology and Disease. Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-8869-0_13.

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Singh, Sundaram, and Savita Kumari. "Use of Barbituric Acid as a Precursor for the Synthesis of Bioactive Compound." In Advances in Organic Synthesis. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815040791123180005.

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Barbituric acid is an organic compound containing a pyrimidine heterocyclic skeleton. It is a water-soluble and odorless compound. Barbituric acid served as a starting material for many barbiturate drugs. The variable properties of the products achieved from barbituric acid motivate organic chemists to investigate its chemistry and current developments have suggested it by multicomponent reactions (MCR). Barbituric acid and its derivatives, commonly known as barbiturates, are important in pharmaceutical chemistry because they are fascinating building blocks for synthesizing biologically active
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Conference papers on the topic "Aminopeptidase inhibition"

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Wells, James M., Patricia L. Jackson, Philip J. O'Reilly, and J. E. Blalock. "Selective Inhibition Of Leukotriene A4 Hydrolase Aminopeptidase Activity Occurs In COPD And Reflects Clinical Outcomes." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1422.

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Cornelius, Peter, Benjamin Mayes, Sara Little, et al. "Abstract P3-11-13: Synergistic inhibition of MCF-7 mammary gland tumor growth with Piqray® (alpelisib) plus SDX-7320, a novel polymer-conjugated methionine aminopeptidase 2 (MetAP2) inhibitor." In Abstracts: 2019 San Antonio Breast Cancer Symposium; December 10-14, 2019; San Antonio, Texas. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.sabcs19-p3-11-13.

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WANG, YONGTAO, Mozhdeh Sojoodi, Guoliang Qiao, et al. "Abstract 108: Inhibiting methionine aminopeptidase 2 prevents liver fibrosis and hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-108.

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Stratikos, Efstratios, Ioannis Temponeras, Lykourgos Chiniadis, and Athanasios Papakyriakou. "Discovery of selective inhibitor leads by targeting an allosteric site in insulin-regulated aminopeptidase." In 6th International Electronic Conference on Medicinal Chemistry. MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07443.

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Friese-Hamim, Manja, Olga Bogatyrova, Maria J. Ortiz, et al. "Abstract 3075: Antitumor activity of M8891, a potent and reversible inhibitor of methionine aminopeptidase 2." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3075.

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Friese-Hamim, Manja, Olga Bogatyrova, Maria J. Ortiz, et al. "Abstract 3075: Antitumor activity of M8891, a potent and reversible inhibitor of methionine aminopeptidase 2." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3075.

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Cornelius, Peter, Benjamin Mayes, Pierre Dufour, et al. "Abstract 1068: SDX-7320, a novel inhibitor of methionine aminopeptidase 2 (MetAP2), inhibits MCF-7 tumor growth in combination with palbociclib (Ibrance®)." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1068.

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Cornelius, Peter, Benjamin Mayes, Sara Little, et al. "Abstract 1226: A novel polymer-conjugated methionine aminopeptidase 2 (MetAP2) inhibitor SDX-7320 inhibits the growth of EO771 mammary gland tumors and ameliorates the immunosuppressive tumor immune micro-environment (TIME)." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1226.

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Cornelius, Peter, Benjamin Mayes, Sara Little, et al. "Abstract 1226: A novel polymer-conjugated methionine aminopeptidase 2 (MetAP2) inhibitor SDX-7320 inhibits the growth of EO771 mammary gland tumors and ameliorates the immunosuppressive tumor immune micro-environment (TIME)." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1226.

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