References
- 전국한의과대학 심계내과학교실, 韓方순환.신경내과학, 서울, 군자출판사, p 190, 2010.
- Brawnwald, E., Kloner, R.A., Myocardial reperfusion. A double edged sword J Chin Invest 76: 1713-1719, 1985. https://doi.org/10.1172/JCI112160
- 전국한의과대학 공동교재편찬위원회, 본초학, 서울, 영림사, p 684, 2004.
- 임종윤 외. 허혈심근 Mitochondria의 Superoxide Anion 생성 및 세포손상기전. 순환기학회지 21(6):1137-1151, 1991.
- 姜秉宗. 芎夏湯이 再灌流將置下의 흰쥐 摘出心藏에 미치는 영향. 서울, 慶熙大學校大學院, 1997.
- 全燦鎔. 虛血性心臟에 대한 勝金湯의 실험적 연구. 서울, 경희대학교대학원, 1994.
- 朴貞美. 苓桂朮甘湯이 虛血性疾患에 미치는 영향. 경희대학교, 74: 414-422, 1991.
- 金仁變. 과루해백반하탕 및 가미과루해백반하탕 허혈성심질환에 미치는 경향. 한방성인병학회지 11: 187-216, 1995.
- 李英彬. 麝香蘇合元이 再灌流將置下의 흰쥐 심장에 미치는 영향. 서울, 경희대학교대학원, 1996.
- 崔赫鎕. 導赤散이 적출 흰쥐 심장의 혈역학적 기능에 미치는 영향. 서울, 慶熙大學校大學院, 1996.
- Pandey, A., Mann, M. Proteomics to study genes and genomes. Nature. Jun 15: 405(6788):837-846, 2000. https://doi.org/10.1038/35015709
- 이진우. 蓮子肉의 항우율 효과 및 프로티움 분석을 통한 기전 연구. 서울, 경희대학교 대학원 학위논문, 2004.
- Pedro Monteiro, Ana I. Duarte, Lino M. Goncalves, Antonio Morenoc, Luıs A. Providencia, Protective effect of trimetazidine on myocardial mitochondrial function in an ex-vivo model of global myocardial ischemia, European Journal of Pharmacology, 503: 123-128, 2004. https://doi.org/10.1016/j.ejphar.2004.09.003
- Dillmann, W.H., Mehta, H.B., Barrieux, A., Guth, B.D., Neeley, W.E., Ross J Jr. Ischemia of the dog heart induces the appearance of a cardiac mRNA coding for a protein with migration characteristics similar to heat-shock/stress protein 71, Circ Res. 59(1):110-114, 1986. https://doi.org/10.1161/01.RES.59.1.110
- Liu, J.H., Ho, S.C., Lai, T.H., Liu, T.H., Chi, P.Y., Wu, R.Y. Protective effects of Chinese herbs on D-galactose-induced oxidative damage, 25(6):447-452, 2003. https://doi.org/10.1358/mf.2003.25.6.769650
- la Cour B., Molgaard P. and Yi Z. Traditional Chinese medicine in treatment of hyperlipidaemia. J Ethnopharmacol. 46(2):125-129, 1995. https://doi.org/10.1016/0378-8741(95)01234-5
- Klose J. Large-gel 2D electrophoresis. Methods Mol Biol 112: 147-172, 2000.
- Pandey, A., Mann, M. Proteomics to study genes and genomes. Nature 405: 837-846, 2000. https://doi.org/10.1038/35015709
- Leimgruber, R.M., Malone, J.P., Radabaugh, M.R., Laporte, M.L., Violand, B.N., Monahan, J.B. Development of improved cell lysis, solubilization and imaging approaches for proteomic analyses. Proteomics 2: 135-144, 2002. https://doi.org/10.1002/1615-9861(200202)2:2<135::AID-PROT135>3.0.CO;2-1
- Hobrook, J.J., Liljas, A., Steindel, S.J. & Rosmann, M.G. in The Enzymes: Oxidation-Reduction, eds. Boyer, P. (Academic, New York), Vol. 11, Part A: 191-192, 1975.
- RUSSELL J. BUONO and ROBYN K. LANG, Exp. Eye Res. Hypoxic Repression of Lactate Dehydrogenase-B in Retina, 69: 685-693, 1999. https://doi.org/10.1006/exer.1999.0745
- Markert, C.L., shaklee, J.B. & Whitt, G.S. Science 189: 102-114, 1975. https://doi.org/10.1126/science.1138367
- Tsuji, S., Qureshi, M.A., Hou, E.W., Fitch, W.M., Li, S.S. Evolutionary relationships of lactate dehyfrogenases(LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from Xenopus pig and rat,Proc Natl Acad Sci 91: 9392-9396, 1994. https://doi.org/10.1073/pnas.91.20.9392
- W. Qin, Z. Khuchua, J. Cheng, J. Boero, R.M. Payne, A.M. Strauss, Mol. Cell. Biochem 184: 153, 1998. https://doi.org/10.1023/A:1006807515892
- K. Anflous, V. Veksler, P. Mateo, F. Samson, V. Saks, R. Ventura-Clapier, Biochem. J. 322: 73, 1997. https://doi.org/10.1042/bj3220073
- Muller, M., et al. J. Biol. Chem. 260: 3839-3843, 1985.
- Payne, R.M., Haas, R.C. and Strauss, A.W. Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes, Biochim. Biophys. Acta 1089(3): 352-361, 1991. https://doi.org/10.1016/0167-4781(91)90176-M
- O'Gorman, E., Beutner, G., Wallimann, T., and Brdiczka, D. Differential effects of creatine depletion on the regulation of enzyme activities and on creatine-stimulated mitochondrial respiration in skeletal muscle, heart, and brain. Biochim. Biophys. Acta 1276: 161-171, 1996. https://doi.org/10.1016/0005-2728(96)00074-6
- Martin, K.J., Winslow, E.R., O'Keefe, M.O., Khandekar, V.S., Hamlin, A., Lillie, J.W., and Kaddurah-Daouk, R. Specific targeting of tumor cells by the creatine analog cyclocreatine. Int J. Oncol. 9: 993-999, 1996.
- Stadhouders, A.M., Jap, P., Winkler, H.P., Eppenberger, H.M., and Wallimann, T. Mitochondrial creatine kinase: A major constituent of pathological inclusions seen in mitochondrial myopathies. Proc. Natl. Acad. Sci. U.S.A 91: 5089-5094, 1994. https://doi.org/10.1073/pnas.91.11.5089
- Philip Eaton, William Fuller, James R. Bell and Michael J. Shattock, B Crystallin Translocation and Phosphorylation: Signal Transduction Pathways and Preconditioning in the Isolated Rat Heart, J Mol Cell Cardiol 33: 1659-1671, 2001. https://doi.org/10.1006/jmcc.2001.1418
- Ray, P.S., Martin, J.L., Swanson, E.A., Otani, H., Dillman, W.H. Genetically engineered mice overexpressing alpha beta crystallin exhibit protection against myocardial ischemia-reperfusion injury. J Am Coll Cardiol, 35(2):401A. (Abstract), 2000.
- Eaton, P., Awad, W.I., Miller JIA., Hearse, D.J., Shattock, M.J. Ischemic preconditioning: A potential role for constitutive low molecular weight stress protein translocation and phosphorylation. J Mol cell Cardiol 32(6): 961-971, 2000. https://doi.org/10.1006/jmcc.2000.1136
- http://www.neuro.wustl.edu/neuromuscular/mother/myosin. htm
- Veerkamp, J.H. & Maatman, R.G.H.J. Cytoplasmic fatty acid-binding proteins: their structure and genes. Prog. Lipid Res. 34: 17-52, 1995. https://doi.org/10.1016/0163-7827(94)00005-7
- Haunerland, N.H. Fatty acid binding proteins in locust and mammalian muscle. Comparison of structure, function, and regulation. Comp. Biochem. Physiol. 109B: 199-208, 1994.
- Bohmer, F., Kraft, R., Otto, A., Wernstedt, C., Hellman, U., Kurtz, A., Muller, T., Etzold, G., Lehmann, W., Langen, P., Heldin, C. & Grosse, R. Identification of a polypeptide groth inhibitor from bovine mammary gland. J. Biol. Chem. 262: 15136-15143, 1987.