자료유형
발행기관
- 대한생리학회-대한약리학회(44)
- 대한생리학회(7)
- 대한수의학회(4)
- 생화학분자생물학회(4)
- 대한약리학회(3)
- 한국동물번식학회(3)
- 한국식물병리학회(2)
- 대한생식의학회(1)
- 대한신경정신의학회(1)
- 대한화학회(1)
- 아세아태평양축산학회(1)
- 이화여자대학교 교과교육연구소(1)
- 한국동물자원과학회(1)
- 한국생물공학회(1)
간행물
- THE KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY(44)
- 대한생리학회지(7)
- 대한약리학잡지(3)
- JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY(2)
- JOURNAL OF VETERINARY SCIENCE(2)
- KOREAN JOURNAL OF VETERINARY RESEARCH(구 대한수의학회지)(2)
- REPRODUCTIVE & DEVELOPMENTAL BIOLOGY(2)
- ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES(1)
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING(1)
- BMB REPORTS(1)
- BULLETIN OF THE KOREAN CHEMICAL SOCIETY(1)
- EXPERIMENTAL & MOLECULAR MEDICINE : EMM(1)
- THE PLANT PATHOLOGY JOURNAL (1)
- 교과교육학연구(1)
- 대한불임학회지(1)
- 식물병연구(1)
- 신경정신의학(1)
- 한국가축번식학회지(1)
- 한국동물자원과학회지(1)
전체 선택해제
총 74건 검색
본문검색 결과만 보기
-
Unchanged Protein Level of Ryanodine Receptor but Reduced [3H] Ryanodine Binding of Cardiac Sarcoplasmic Reticulum from Diabetic Cardiomyopathy Rats
EunHeeLee, YoungJuSeo, Young-HoonKim, HaeWonKim 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 9 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2001, Vol.5 No.5 5 397-405 (9 pages)
ryanodine receptor, and dihydropyridine receptor at the transcriptional and translational levels. Quantitative changes of ryanodine receptors and the dihydropyridine receptors, and the functional consequences of those changes in diabetic heart were investigated. The levels of protein and mRNA of the ryanodine receptor in diabetic rats were comparable to these of the control. However, the binding capacity of ryanodine was significantly decreased in diabetic rat hearts. Furthermore, the reduction... -
Thyroid Hormone-Induced Alterations of Ryanodine and Dihydropyridine Receptor Protein Expression in Rat Heart
HaeWonKim, MiyoungPark, EunHeeLee, HyoungJinCho, HeeRanLee 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 9 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 1999, Vol.3 No.3 11 329-337 (9 pages)
hyperthyroid hearts, [3H]ryanodine binding and ryanodine receptor mRNA levels were increased, but protein levels of ryanodine were not changed significantly. However, the above parameters were markedly decreased in hypothyroid hearts. In case of dihydropyridine receptor, there were a significant increase in the mRNA and protein levels, and [3H]nitrendipine binding, whereas no changes were observed in these parameters of hypothyroid hearts. Our findings indicate that hyperthyroidism is associated... -
Genotyping of the Porcine Ryanodine Receptor 1 (RYR1) and Estrogen Receptor 1 (ESR1) Genes by High Resolution Melting (HRM) Approach
Ma. Jideng, Li. Mingzhou, Wang. Huiyu, Li. Xuewei 한국생물공학회 Biotechnology and bioprocess engineering 4 Pages
한국생물공학회 Biotechnology and bioprocess engineering 2012, Vol.17 No.5 1076-1079 (4 pages)
-
Skeletal Ryanodine Receptor 1-Heterozygous PSE (Pale, Soft and Exudative) Meat Contains a Higher Concentration of Myoglobin than Genetically Normal PSE Meat in Pigs
Obi. T., Matsumoto. M., Miyazaki. K., Kitsutaka. K., Tamaki. M., Takase. K., Miyamoto. A., Oka. T., Kawamoto. Y., Nakada. T. 아세아태평양축산학회 Asian-Australasian journal of animal sciences 6 Pages
아세아태평양축산학회 Asian-Australasian journal of animal sciences 2010, Vol.23 No.9 1244-1249 (6 pages)
-
Characterization of the Ryanodine Receptor and SERCA in Fetal, Neonatal, and Adult Rat Hearts
Ramesh. Venkat, Kresch. Mitchell J., Park. Woo-Jin, Kim. Do-Han 생화학분자생물학회 Journal of biochemistry and molecular biology 5 Pages
생화학분자생물학회 Journal of biochemistry and molecular biology 2001, Vol.34 No.6 573-577 (5 pages)
-
Effect of IP3 and ryanodine treatments on the development of bovine parthenogenetic and reconstructed embryos
Gook-jun Ahn, Byeong-chun Lee, Woo-suk Hwang 대한수의학회 Journal of Veterinary Science 7 Pages
대한수의학회 Journal of Veterinary Science 2001, 제 2권 제 2호 11 131-137 (7 pages)
morula and blastocyst formation, the IP3 and ryanodine group exhibited significantly higher rates of morula fomation than the IP3 or control groups (40.6% vs 24.2% or 16.7%, respectively). Similarly, the rate of blastocyst formation in the IP3+ryanodine group was significantly higher than the control group (16.3% vs 6.9%) but did not differ significantly from the IP3 group (16.3% vs 9.5%). In nuclear transfer, activation was performed at 30 hpm by microinjection and elecroporation with 25 micro... -
Alteration of Ryanodine-receptors in Cultured Rat Aortic Smooth Muscle Cells
EunJiKim, DongKwanKim, ShinHyeKim, KyungMooLee, HyungSeoPark, SeHoonKim 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 6 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2011, Vol.15 No.6 15 431-436 (6 pages)
release from SR in permeabilized cells. An additional goal was to elucidate alterations of RyRs that occurred during culture. Perfusion of permeabilized, freshly dissociated RASMCs with Ca2＋ stimulated Ca2＋ release from the SR. Caffeine and ryanodine also induced Ca2＋ release from the SR in dissociated RASMCs. In contrast, ryanodine, caffeine and Ca2＋ failed to trigger Ca2＋ release in cultured RASMCs. These results are consistent with results obtained by immunocytochemistry, which showed... -
[3H]Ryanodine Binding Sites of SR Vesicles of the Chicken Pectoral Muscle
Hyo-YungYun, Jong-RyeJeon, Jang-HeeHong, Gang-MinHur, Jae-HeunLee, Jeong-HoSeok* 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 1997, Vol.1 No.4 4 377-384 (8 pages)
chicken pectoral muscle. The chicken SR vesicles have two high molecular weight (HMW) protein bands as in eel SR vesicles on SDS PAGE. The HMW bands on SDS PAGE were found in the [3H] ryanodine peak fraction (Fr3-5) obtained from the purification step of the ryanodine receptor protein. Bmax and KD of the chicken [3H]ryanodine binding sites were 12.52 pmol/mg protein and 14.53 nM, respectively. Specific [3H]ryanodine binding was almost maximal at 50∼100 ՌM Ca2+, but was not increased by 5... -
G Protein-Coupled Receptor Signaling in Gastrointestinal Smooth Muscle
UyDongSohn, DongSeokKim, KarnamSMurthy 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 11 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2001, Vol.5 No.4 1 287-297 (11 pages)
Contraction of smooth muscle is initiated by an increase in cytosolic Ca2 leading to activation of Ca2/ calmodulin-dependnet myosin light chain (MLC) kinase and phosphorylation of MLC. The types of contraction and signaling mechanisms mediating contraction differ depending on the region. The involvement of these different mechanisms varies depending on the source of Ca2 and the kinetic of Ca2 mobilization. Ca2 mobilizing agonists stimulate different...
