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Establishment of the stroke-prone spontaneously hypertensive rat (SHR). <i>Cire. Res.<\/i>, <b>34\/35<\/b> (Suppl. I), 143\u2013153 (1974\u20131975)."},{"key":"2","doi-asserted-by":"crossref","unstructured":"2) Yamori Y, Nagaoka A, Okamoto K. Importance of genetic factors in stroke: an evidence obtained by selective breeding of stroke-prone and -resistant SHR. <i>Jpn. Circ. J.<\/i>, <b>38<\/b>, 1095\u20131100 (1974).","DOI":"10.1253\/jcj.38.1095"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3) Yamori Y, Horie R. Developmental course of hypertension and regional cerebral blood flow in stroke-prone spontaneously hypertensive rats. <i>Stroke<\/i>, <b>8<\/b>, 456\u2013461 (1977).","DOI":"10.1161\/01.STR.8.4.456"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Morikawa T, Kajimura M, Nakamura T, Hishiki T, Nakanishi T, Yukutake Y, Nagahata Y, Ishikawa M, Hattori K, Takenouchi T, Takahashi T, Ishii I, Matsubara K, Kabe Y, Uchiyama S, Nagata E, Gadalla MM, Snyder SH, Suematsu M. Hypoxic regulation of the cerebral microcirculation is mediated by a carbon monoxide-sensitive hydrogen sulfide pathway. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>109<\/b>, 1293\u20131298 (2012).","DOI":"10.1073\/pnas.1119658109"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5) Zhao W, Zhang J, Lu Y, Wang R. The vasorelaxant effect of H(2)S as a novel endogenous gaseous K(ATP) channel opener. <i>EMBO J.<\/i>, <b>20<\/b>, 6008\u20136016 (2001).","DOI":"10.1093\/emboj\/20.21.6008"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6) Zhao W, Wang R. H<sub>2<\/sub>S-induced vasorelaxation and underlying cellular and molecular mechanisms. <i>Am. J. Physiol. Heart Circ. Physiol.<\/i>, <b>283<\/b>, H474\u2013H480 (2002).","DOI":"10.1152\/ajpheart.00013.2002"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Huang P, Shen Z, Liu J, Huang Y, Chen S, Yu W, Wang S, Ren Y, Li X, Tang C, Du J, Jin H. Hydrogen sulfide inhibits high-salt diet-induced renal oxidative stress and kidney injury in Dahl rats. <i>Oxid. Med. Cell. Longev.<\/i>, <b>2016<\/b>, 2807490 (2016).","DOI":"10.1155\/2016\/2807490"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Hadadha M, Vakili A, Bandegi AR. Effect of the inhibition of hydrogen sulfide synthesis on ischemic injury and oxidative stress biomarkers in a transient model of focal cerebral ischemia in rats. <i>J. Stroke Cerebrovasc. Dis.<\/i>, <b>24<\/b>, 2676\u20132684 (2015).","DOI":"10.1016\/j.jstrokecerebrovasdis.2015.07.020"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Enokido Y, Suzuki E, Iwasawa K, Namekata K, Okazawa H, Kimura H. Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia\/astrocyte lineage of developing mouse CNS. <i>FASEB J.<\/i>, <b>19<\/b>, 1854\u20131856 (2005).","DOI":"10.1096\/fj.05-3724fje"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Mustafa AK, Gadalla MM, Sen N, Kim S, Mu W, Gazi SK, Barrow RK, Yang G, Wang R, Snyder SH. H<sub>2<\/sub>S signals through protein <i>S<\/i>-sulfhydration. <i>Sci. 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Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue. <i>J. Cell Biol.<\/i>, <b>85<\/b>, 890\u2013902 (1980).","DOI":"10.1083\/jcb.85.3.890"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15) Yamagata K, Kitazawa T, Shinoda M, Tagawa C, Chino M, Matsufuji H. Stroke status evoked adhesion molecule genetic alterations in astrocytes isolated from stroke-prone spontaneously hypertensive rats and the apigenin inhibition of their expression. <i>Stroke Res. Treat.<\/i>, <b>2010<\/b>, 386389 (2010).","DOI":"10.4061\/2010\/386389"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Lin VS, Lippert AR, Chang CJ. Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H<sub>2<\/sub>O<sub>2<\/sub>-dependent H<sub>2<\/sub>S production. <i>Proc. Natl. Acad. Sci. 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