Academic literature on the topic 'Angiotensin converting enzyme Cancer'

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Journal articles on the topic "Angiotensin converting enzyme Cancer"

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Nielsen, Dorte, Benny Jensen, Jens Eriksen, Torben Skovsgaard, and Henriette Lindberg. "Angiotensin converting enzyme inhibitors for cancer treatment?" Acta Oncologica 43, no. 2 (March 1, 2004): 142–52. http://dx.doi.org/10.1080/02841860310022346.

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Melichar, Bohuslav, Pavel Jandik, Jaroslava Vavrova, Jindřiška Mergancová, Eva Maliřová, and Zbyněk Vobořil. "Serum Neopterin and Angiotensin-converting Enzyme In Cancer Patients." Pteridines 5, no. 4 (November 1994): 133–35. http://dx.doi.org/10.1515/pteridines.1994.5.4.133.

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Summary An elevation of serum angiotensin-converting enzyme (ACE) has been reported in some disorders associated with immune activation, e.g. sarcoidosis, HIV infection or ulcerative colitis. Both endothelial cells and macrophages are thought to be the possible source of increased ACE levels. We have investigated serum ACE and neopterin, an indicator of macrophage activation, in 23 patients with solid tumors as well as in 8 controls. Similar ACE levels have been observed in the cancer patients and the controls (2.6 ± 2.1 vs 3.4 ± 1.1 μkat/1, while neopterin has been significantly higher in the cancer patients (15.4 ± 12.6 vs 7.2 ± 2.2 nmol/I, P<O.02). No correlation has been observed between serum ACE and neopterin. We conclude that an elevation of ACE is not present in cancer patients. Macrophage activation in cancer is not accompanied by increased ACE release.
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Friis, S�ren, Henrik T. S�rensen, Lene Mellemkj�r, Joseph K. McLaughlin, Gunnar L. Nielsen, William J. Blot, and J�rgen H. Olsen. "Angiotensin-converting enzyme inhibitors and the risk of cancer." Cancer 92, no. 9 (2001): 2462–70. http://dx.doi.org/10.1002/1097-0142(20011101)92:9<2462::aid-cncr1596>3.0.co;2-l.

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Batais, Mohammed, Turky Almigbal, Khalid Alotaibi, Abdulaziz Alodhayani, Abdullah Alkhushail, Abdulrahman Altheaby, Mashhor Alhantoushi, Saad Alsaad, Sultan Al Dalbhi, and Yasser Alghamdi. "Angiotensin converting enzyme inhibitors and risk of lung cancer." Medicine 100, no. 17 (April 30, 2021): e25714. http://dx.doi.org/10.1097/md.0000000000025714.

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Stanisz, Beata, Katarzyna Regulska, and Miłosz Regulski. "The angiotensin converting enzyme inhibitors – alternative clinical applications." Journal of Medical Science 83, no. 1 (March 30, 2014): 57–61. http://dx.doi.org/10.20883/medical.e45.

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Angiotensin converting enzyme inhibitors have emerged as a useful strategy in the management of hypertension and other cardiovascular system-related diseases. However, a wide range of their biological effects has turned the scientific interest towards other possible clinical applications of these drugs. The present review demonstrates the available data on the reported angiotensin-converting enzyme inhibitors – based therapies in the treatment of the following human disturbances: cancer, obesity, Barrett syndrome, erythrocytosis, a high-dose-chemotherapy-induced cardiotoxicity, Marfan syndrome, Duchenne muscular dystrophy, migraine, Raynaud’s syndrome and Alzheimer disease.
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Cheng, Zhen, and Zhiwei Liu. "Renin–angiotensin system gene polymorphisms and colorectal cancer risk: a meta-analysis." Journal of the Renin-Angiotensin-Aldosterone System 20, no. 4 (October 2019): 147032031988193. http://dx.doi.org/10.1177/1470320319881932.

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Objective: The renin–angiotensin system gene has been implicated in the progression of colorectal cancer. Nevertheless, the details of that role remain controversial. We performed a meta-analysis to investigate the correlation between renin–angiotensin system gene polymorphisms and colorectal cancer. Methods: We retrieved relevant studies from PubMed and Embase. Subsequently, fixed or random-effects models were used to calculate pooled odds ratios (ORs) with 95% confidence intervals (CIs). Results: We identified six studies of the angiotensin-converting enzyme insertion/deletion (I/D) polymorphism, and two studies of the angiotensinogen M235T polymorphism. The angiotensin-converting enzyme I/D polymorphism did not significantly correlate with colorectal cancer risk in the total population (DD vs. II: OR 0.77, 95% CI 0.39–1.50; DI vs. II: OR 1.05, 95% CI 0.85–1.30; dominant model: OR 0.94, 95% CI 0.68–1.31; recessive model: OR 1.01, 95% CI 0.80–1.27). Similarly, the angiotensinogen M235T polymorphism was not associated with colorectal cancer risk (TT vs. MM: OR 1.38, 95% CI 0.52–3.67; TM vs. MM: OR 1.19, 95% CI 0.96–1.47; dominant model: OR 1.28, 95% CI 0.77–2.14; recessive model: OR 1.17, 95% CI 0.53–2.59). Conclusion: Our findings suggest that the angiotensin-converting enzyme I/D and angiotensinogen M235T polymorphisms are unlikely to correlate with colorectal cancer.
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Sattar, Naveed, and Donald C. McMillan. "Inhibitors of angiotensin-I-converting enzyme and risk of cancer." Lancet 352, no. 9134 (October 1998): 1151. http://dx.doi.org/10.1016/s0140-6736(05)79800-7.

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Meier, Christoph R., Laura E. Derby, Susan S. Jick, and Hershel Jick. "Angiotensin-Converting Enzyme Inhibitors, Calcium Channel Blockers, and Breast Cancer." Archives of Internal Medicine 160, no. 3 (February 14, 2000): 349. http://dx.doi.org/10.1001/archinte.160.3.349.

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Mao, Yeqing, Xin Xu, Xiao Wang, Xiangyi Zheng, and Liping Xie. "Is angiotensin-converting enzyme inhibitors/angiotensin receptor blockers therapy protective against prostate cancer?" Oncotarget 7, no. 6 (January 7, 2016): 6765–73. http://dx.doi.org/10.18632/oncotarget.6837.

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Helgeson, Scott A., Mark R. Waddle, Rebecca C. Burnside, Yalew T. Debella, Augustine S. Lee, Charles D. Burger, Zhuo Li, Patrick W. Johnson, and Neal M. Patel. "Association between Angiotensin-Converting Enzyme Inhibitors and Angiotensin Receptor Blockers and Lung Cancer." Southern Medical Journal 114, no. 9 (September 2021): 607–13. http://dx.doi.org/10.14423/smj.0000000000001293.

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Dissertations / Theses on the topic "Angiotensin converting enzyme Cancer"

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Christian, Jennifer B. "Beyond the antihypertensive effect: ACE inhibitors and angiotensin receptor blockers." View abstract/electronic edition; access limited to Brown University users, 2008. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3318302.

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HAMAJIMA, NOBUYUKI, HIDEMI GOTO, KAZUO TAJIMA, KENJI WAKAI, KEITARO MATSUO, TAKAFUMI ANDO, YASUYUKI GOTO, and SATOSHI HIBI. "NO ASSOCIATION BETWEEN ANGIOTENSIN I CONVERTING ENZYME (ACE) I/D POLYMORPHISM AND GASTRIC CANCER RISK AMONG JAPANESE." Nagoya University School of Medicine, 2011. http://hdl.handle.net/2237/15359.

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Elliott, Joann Louise. "Homologues of the angiotensin converting enzyme." Thesis, University of Leeds, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424020.

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Prasad, Abhiram. "Angiotensin converting enzyme and endothelial dysfunction." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.248389.

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Clarke, Nicola Elizabeth. "The regulation of angiotensin-converting enzyme 2 (ACE2)." Thesis, University of Leeds, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.582085.

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The levels of ACE2 at the cell surface are regulated by cleavage at the plasma membrane Angiotensin-converting-enzyme-2 (ACE2) acts as the protective arm of the renin-angiotensin system (RAS). ACE2 counterbalances the actions of ACE by metabolising the catalytic product of ACE, angiotensin 11 (Ang 11), a vasoconstrictor into Ang-(1-7), a vasodilatory peptide. ACE2 has been found to mediate effects, independently of Ang-(1-7), through non-catalytic actions. The aim of this study was to use cell biology to identify factors regulating ACE2 expression and investigate a potential non-catalytic interaction with integrin β1. Cells endogenously expressing ACE2, Huh7 cells, and HEK cells overexpressing ACE2 or tACE were used to probe for an interaction between the angiotensinases and integrins. Both ACE and ACE2 were found to bind integrin subunits, in an RGD-independent manner and they can act as cell-adhesion substrates. The cellular expression of ACE2 on the cell-surface was found to co-localise with integrin β1 and to enhance cell adhesion. Furthermore, treatment of cells with purified ACE2 but not Ang-(1-7), resulted in suppression of integrin signalling mediated by FAK in Huh7 cells. These results suggest that ACE2 plays a role in cell-cell interactions, possibly acting to fine-tune integrin signalling. Hence the cell surface location of ACE2 may be important for some of its protective effects. ( shedding) and levels of this shed form of ACE2 have been correlated with myocardial dysfunction. Herein it is shown that, Ang 11 acts as an endogenous stimulus of shedding by upregulating the expression of ADAM17 at the cell membrane in Huh7 cells. As such, it is possible that some of the pathological effects of Ang 11 are mediated through disruption of integrin signalling caused by a loss of ACE2 at the cell membrane. Although, understanding the control of ACE2 expression is of therapeutic relevance to diseases including cardiovascular and acute respiratory diseases, few studies have investigated the cellular regulation of ACE2. Several factors regulating ACE2 expression in Huh7 cells were identified in this thesis, including up-regulation by a proinflammatory cytokine and modulation by the action of a microRNA. Furthermore, it was found that the expression of ACE2 transcript was modified by hypoxic conditions and cell energy-stress, suggesting regulation by AMP kinase. Energy-stress-induced increases in ACE2 expression were determined to be under the control of SIRT1.
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Hughes, M. A. "Metal binding by some angiotensin converting enzyme inhibitors." Thesis, Cardiff University, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305894.

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Guy, Jodie Leanne. "Characterisation of an angiotensin-converting enzyme homologue (ACE2)." Thesis, University of Leeds, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400960.

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Ljungberg, Liza. "Angiotensin-converting enzyme in cardiovascular function and dysfunction." Doctoral thesis, Linköpings universitet, Fysiologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-67215.

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Angiotensin-converting enzyme (ACE) is a key enzyme in the renin-angiotensin system, converting angiotensin I to the vasoactive peptide angiotensin II, and degrading bradykinin. Angiotensin II is a multifunctional peptide, acting on a number of different tissues. A common genetic variation in the gene encoding ACE; ACE I/D polymorphism influences the level of ACE in the circulation, and has been linked to increased risk for cardiovascular disease. This thesis aimed to explore the connection between ACE and cardiovascular function and dysfunction. The impact of nicotine and nicotine metabolites on ACE in cultured human endothelial cells was studied. Nicotine as well as nicotine metabolites induced increased ACE activity in cultured human endothelial cells. In elderly men a higher ACE level was seen in smokers compared to non-smokers. Furthermore, diabetes was associated with higher circulating ACE. Increased ACE level may represent a cellular mechanism which contributes to vascular damage. Elderly men carrying the ACE D allele had higher abdominal aortic stiffness compared to men carrying the I/I genotype. Our data suggest that the mechanism by which the ACE D allele modulates aortic wall mechanics is independent of circulating ACE levels. Previous studies have indicated a link between the D allele and abdominal aortic aneurysm. Increased aortic stiffness suggests impaired vessel wall integrity, which combined with local hemodynamic and/or inflammatory factors may have a role in aneurysm formation. Subjects with left ventricular dysfunction had higher levels of circulating ACE compared to those with normal left ventricular function, while there was no association between ACE and central hemodynamics. ACE might play a role in the pathogenesis of left ventricular dysfunction and our findings suggest a direct effect on the heart rather than affecting central blood pressure.
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Day, Stephen Howard. "The influence of circulating angiotensin-converting enzyme activity and angiotensin-converting enzyme genotype on endurance and strength performance in previously sedentary humans." Thesis, Staffordshire University, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.418944.

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Martin, Melanie. "Inhibitoren des Angiotensin Converting Enzyme (ACE) in hypoallergenen Säuglingsnahrungen." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2009. http://nbn-resolving.de/urn:nbn:de:bsz:14-ds-1234543148442-91042.

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Als Schlüsselenzym im Renin-Angiotensin System übernimmt das Angiotensin Converting Enzyme (ACE) eine wichtige Rolle bei der Blutdruckregulierung. ACE spaltet das biologisch inaktive Angiotensin I zum vasokonstriktorisch wirksamen Angiotensin II, was zu einem Anstieg des Blutdruckes führt. Tier- und Humanstudien zeigten, dass die Aufnahme bekannter, aus dem Proteinabbau stammender ACE-Inhibitoren eine Absenkung des Blutdruckes bewirkte. In der Lebensmittelindustrie finden Hydrolysate von Milchproteinen, im speziellen von Molkenproteinen, Einsatz in hypoallergenen (HA) Säuglingsnahrungen. Obwohl das Phänomen einer ACE-Inhibierung durch HA-Nahrungen in vitro in der Literatur bereits Erwähnung fand, existieren bislang keine Angaben zu einer potentiellen Wirkung in vivo. In der vorliegenden Arbeit konnte für kommerzielle hypoallergene (HA) Säuglingsnahrung eine sehr starke ACE-Hemmung in vitro zeigen (IC50-Werte zwischen 20 und 104 mg Protein/liter), welche die für fermentierte Sauermilchprodukte dokumentierte Wirkung bei weitem überstieg.] Mittels RP-HPLC und ESI-TOF-MS konnte neben zahlreichen bekannten Peptiden mit ACE-hemmendem Effekt erstmals das aus der Primärsequenz von -Lactalbumin freigesetzte Dipeptid Ile-Trp in den HA-Nahrungen identifiziert und quantifiziert werden. Ile-Trp ist der bislang potenteste in Lebensmitteln nachgewiesene ACE-Inhibitor (IC50 = 0,7µM). HA-Nahrungen zeigten auch ex vivo im Zellsystem (HUVECs) einen stark ACE-hemmenden Effekt. Aus diesem Grunde wurde ein möglicher Einfluss der HA-Nahrungen auf den Blutdruck spontan hypertensiver Ratten untersucht. Hierfür wurden die Tiere im Rahmen einer Fütterungsstudie über 14 Wochen mit standardisiertem Futter, welchem HA-Nahrung (Gruppe 1), konventionelle Säuglingsnahrung (Gruppe 2) bzw. der bekannte ACE-Inhibitor Captopril (Gruppe 3) zugesetzt war, gefüttert. Eine vierte Gruppe mit Standardfutter diente als Kontrolle. Der Blutdruck wurde am wachen Tier nichtinvasiv mittels tail-cuff-Methode gemessen. Der systolische Blutdruck sank bei Verabreichung der HA-Nahrung nach 7 Wochen signifikant um 21 ± 8 mmHg ab im Vergleich zur Kontrollgruppe bzw. den mit konventioneller Säuglingsnahrung gefütterten Tieren. Captopril führte zur einer Blutdrucksenkung um 30 ± 7 mmHg.
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Books on the topic "Angiotensin converting enzyme Cancer"

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A, MacGregor G., and Sever Peter S, eds. Current advances in ACE inhibition 2: Proceedings of an Internationalsymposium, Queen Elizabeth II Conference Centre, London, UK 17-21 February 1991. Edinburgh: Churchill Livingstone, 1991.

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Townend, Jonathan Nicholas. Studies on angiotensin converting enzyme inhibitors in heart failure. Birmingham: University of Birmingham, 1994.

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H, Opie Lionel. Angiotensin-converting enzyme inhibitors: Scientific basis for clinical use. New York: Wiley-Liss, 1992.

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H, Opie Lionel. Angiotensin-converting enzyme inhibitors: Scientific basis for clinical use. New York: Wiley-Liss, 1992.

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George, Strube, ed. ACE inhibitors in hypertension: A guide for general practitioners. Dordrecht: Kluwer Academic Publishers, 1992.

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O'Donnell, Mark John. The kidney in diabetes mellitus: Urinary transfer in excretion, hypertension, the Renin-Angiotensin-Aldosteronesystem, and the role of angiotensin converting enzyme inhibitors in therapy. Birmingham: University of Birmingham, 1992.

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J, Whalley Lawrence, ed. ACE inhibitors: Central actions. New York: Raven Press, 1994.

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The ACE inhibitor/myocardial infarction trials: From clinical trials to clinical practice. Beckenham: Publishing Initiatives Books, 1995.

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Morlin, A. J. G. The preparation of some chiral 2-hydroxycarboxylic acids and their use in the synthesisof potential angiotensin converting enzyme inhibitors. Norwich: University of East Anglia, 1993.

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Bosch, Sophie J. Effectiveness of Ace inhibitors and ARBs in heart disease treatment. Hauppauge, N.Y: Nova Science Publishers, 2011.

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Book chapters on the topic "Angiotensin converting enzyme Cancer"

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Böning, Dieter, Michael I. Lindinger, Damian M. Bailey, Istvan Berczi, Kameljit Kalsi, José González-Alonso, David J. Dyck, et al. "Angiotensin Converting Enzyme." In Encyclopedia of Exercise Medicine in Health and Disease, 86. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2092.

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Douglas, Ross G., and Edward D. Sturrock. "Angiotensin I-Converting Enzyme." In Encyclopedia of Metalloproteins, 63–68. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_187.

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Skidgel, Randal A., and Ervin G. Erdös. "Angiotensin I Converting Enzyme." In Advances in Experimental Medicine and Biology, 25–28. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-9543-4_4.

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Frishman, William H., Angela Cheng-Lai, and Julie Chen. "Angiotensin-Converting Enzyme Inhibitors." In Current Cardiovascular Drugs, 18–44. London: Current Medicine Group, 2000. http://dx.doi.org/10.1007/978-1-4615-6767-7_4.

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Oparil, Suzanne, Qingcheng Meng, Shuang-dan Sun, Yiu-Fai Chen, and Louis J. Dell’Italia. "Tissue Angiotensin Converting Enzyme." In Vascular Endothelium, 205–39. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0355-8_15.

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Mountokalakis, Theodore D. "Angiotensin Converting Enzyme Inhibitors." In Contemporary Concepts in Cardiology, 228–35. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5007-5_12.

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Özkaya, Esen, and Kurtuluş Didem Yazganoğlu. "Angiotensin-Converting Enzyme Inhibitors." In Adverse Cutaneous Drug Reactions to Cardiovascular Drugs, 67–83. London: Springer London, 2014. http://dx.doi.org/10.1007/978-1-4471-6536-1_2.

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Schomburg, Dietmar, and Ida Schomburg. "angiotensin-converting enzyme 2 3.4.17.23." In Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 29–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_2.

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Barr, M. "Angiotensin-Converting Enzyme Inhibitor Fetopathy." In Drug Toxicity in Embryonic Development II, 265–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60447-8_7.

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Ginat, Daniel Thomas, and Jason M. Johnson. "Angiotensin Converting Enzyme (ACE) Inhibitors." In Neuroimaging Pharmacopoeia, 303–8. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12715-6_43.

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Conference papers on the topic "Angiotensin converting enzyme Cancer"

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Chae, Y., M. Valsecchi, A. Lucca, J. Kim, and A. Desai. "Angiotensin Converting Enzyme Inhibitors and Angiotensin Receptor Blockers May Reduce Breast Cancer Recurrence." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-3121.

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Arnaout, Karim, Shatha Farhan, Jatin Rana, Michelle Jankowski, and Ding Wang. "Abstract B93: Angiotensin‐converting enzyme inhibitors and angiotensin receptor blockers may decrease cancer‐related mortality in patients with small‐cell lung cancer." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Dec 6–9, 2009; Houston, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-09-b93.

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Menon, Shyam, and Ray Mathew. "P203 Angiotensin converting enzyme inhibitors and the risk of hepatocellular cancer: a nested cohort analysis." In Abstracts of the BSG Campus, 21–29 January 2021. BMJ Publishing Group Ltd and British Society of Gastroenterology, 2021. http://dx.doi.org/10.1136/gutjnl-2020-bsgcampus.278.

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Alekperov, RT, ML Stanislav, MA Myagkova, TV Abramenko, OA Kost, and Nikolskaya. "FRI0184 Angiotensin-converting enzyme and anti-angiotensin-converting enzyme antibodies in systemic sclerosis." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.265.

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Munster, P., J. Krischer, R. Tamura, A. Fink, L. Bello-Matricaria, and M. Guilin. "Abstract GS5-01: A randomized community-based trial of an angiotensin converting enzyme inhibitor, lisinopril or a beta blocker, carvedilol for the prevention of cardiotoxicity in patients with early stage HER2-positive breast cancer receiving adjuvant trastuzumab." In Abstracts: 2018 San Antonio Breast Cancer Symposium; December 4-8, 2018; San Antonio, Texas. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-gs5-01.

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Inoue, Yoshikazu, Masaki Hirose, Toru Arai, Chikatoshi Sugimoto, Akiko Matsumuro, Tomomi Homma, Yoshinobu Matsuda, et al. "Serum angiotensin-converting enzyme activity in lymphangioleiomyomatosis." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa3814.

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Ghann, William E., Young-Seung Kim, Su Xu, Xin Lu, Mark F. Smith, Rao Gullapalli, Thorsten Fleiter, Martin W. Brechbiel, and Marie-Christine Daniel. "Bifunctional gold nanoparticles for targeted dual imaging of angiotensin converting enzyme." In SPIE Defense, Security, and Sensing, edited by Brian M. Cullum and Eric S. McLamore. SPIE, 2013. http://dx.doi.org/10.1117/12.2016219.

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Junaid, Imran, Guy W. Soo Hoo, and William B. Klaustermeyer. "Severe Angiotensin Converting Enzyme-Inhibitor (ACEI) Associated Angioedema Admitted To An ICU." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1643.

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Johnson, Meshell, Mandi Wong, and Susanne Mathew. "Angiotensin Converting Enzyme 2 Modulates ENaC Expression In Alveolar Type I Cells." 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.a3538.

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Jin-Chao, Wu, Huang Guang-Rong, Yu Miao, and Tan Yong-Hua. "Preparation of angiotensin converting enzyme (ACE) inhibitory peptides from silver carp (Hypophthalmichthys molitrix)." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6028957.

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Reports on the topic "Angiotensin converting enzyme Cancer"

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Pencheva, Mina, Yvetta Koeva, Ilian Dimitrov, and Nina Atanassova. Angiotensin Converting Enzyme (ACE) in Seminal Plasma and Sperm Membrane as a Marker for Male Infertility. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, May 2020. http://dx.doi.org/10.7546/crabs.2020.05.05.

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Yao, Jia, Xiayu Gong, Xiaoyan Shi, Simin Fan, Junmin Chen, and Qiu Chen. The efficacy of angiotensin converting enzyme inhibitors versus angiotensin II receptor blockers on insulin resistance in hypertensive patients:A protocol for a systematic review and Meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, May 2020. http://dx.doi.org/10.37766/inplasy2020.5.0032.

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