![]() 2,5-二叔丁基对苯二酚结构式
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常用名 | 2,5-二叔丁基对苯二酚 | 英文名 | 2,5-Di-tert-butylhydroquinone |
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CAS号 | 88-58-4 | 分子量 | 222.323 | |
密度 | 1.0±0.1 g/cm3 | 沸点 | 334.4±37.0 °C at 760 mmHg | |
分子式 | C14H22O2 | 熔点 | 216-218 °C(lit.) | |
MSDS | 中文版 美版 | 闪点 | 151.5±21.1 °C | |
符号 |
![]() GHS07 |
信号词 | Warning |
Discovery of novel SERCA inhibitors by virtual screening of a large compound library.
Eur. J. Med. Chem. 46 , 1512-23, (2011) Two screening protocols based on recursive partitioning and computational ligand docking methodologies, respectively, were employed for virtual screens of a compound library with 345,000 entries for novel inhibitors of the enzyme sarco/endoplasmic reticulum c... |
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Effect of methoxychlor on Ca(2+) movement and viability in MDCK renal tubular cells.
Basic Clin Pharmacol Toxicol. 111(4) , 224-31, (2012) The effect of the insecticide methoxychlor on the physiology of renal tubular cells is unknown. This study aimed to explore the effect of methoxychlor on cytosolic Ca(2+) concentrations ([Ca(2+) ](i) ) in MDCK renal tubular cells using the Ca(2+) -sensitive f... |
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Two distinct calcium pools in the endoplasmic reticulum of HEK-293T cells.
Biochem. J. 435(1) , 227-35, (2011) Agonist-sensitive intracellular Ca2+ stores may be heterogeneous and exhibit distinct functional features. We have studied the properties of intracellular Ca2+ stores using targeted aequorins for selective measurements in different subcellular compartments. B... |
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Effects of high-affinity inhibitors on partial reactions, charge movements, and conformational States of the Ca2+ transport ATPase (sarco-endoplasmic reticulum Ca2+ ATPase).
Mol. Pharmacol. 73(4) , 1134-40, (2008) The inhibitory effects of thapsigargin, cyclopiazonic acid, and 2,5-di(tert-butyl)hydroquinone, and 1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene on the Ca(2+) ATPase were characterized by comparative measurements of sequential reactions of the catalytic... |
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Functional relevance of the de novo coupling between hTRPC1 and type II IP3 receptor in store-operated Ca2+ entry in human platelets.
Cell. Signal. 20(4) , 737-47, (2008) Store-operated Ca2+ entry (SOCE), a major mechanism for Ca2+ entry in non-excitable cells, is regulated by the filling state of the intracellular Ca2+ stores. We have previously reported that a de novo conformational coupling between the type II IP3 receptor ... |
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Synthesis and SERCA activities of structurally simplified cyclopiazonic acid analogues.
Bioorg. Med. Chem. 19 , 4669-78, (2011) The indole alkaloid cyclopiazonic acid (CPA) is one of the few known nanomolar inhibitors of sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA) besides the anticancer drug thapsigargin and the antiplasmoidal terpenoid artemisinin. Due to its less complex struct... |
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Effects of peanut-skin procyanidin A1 on degranulation of RBL-2H3 cells.
Biosci. Biotechnol. Biochem. 75(9) , 1644-8, (2011) Peanut skin contains large amounts of polyphenols having antiallergic effects. We found that a peanut-skin extract (PSE) inhibits the degranulation induced by antigen stimulation of rat basophilic leukemia (RBL-2H3) cells. A low-molecular-weight fraction from... |
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Effects of elevated physiological temperatures on sarcoplasmic reticulum function in mechanically skinned muscle fibers of the rat.
Am. J. Physiol. Cell Physiol. 293(1) , C133-41, (2007) Properties of the sarcoplasmic reticulum (SR) with respect to Ca(2+) loading and release were measured in mechanically skinned fiber preparations from isolated extensor digitorum longus (EDL) muscles of the rat that were either kept at room temperature (23 de... |
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Structure-based virtual screening for novel inhibitors of the sarco/endoplasmic reticulum calcium ATPase and their experimental evaluation.
Bioorg. Med. Chem. 17 , 1353-60, (2009) A public compound library with 260,000 compounds was screened virtually by computational docking for novel inhibitors of the transmembrane enzyme sarco/endoplasmic reticulum calcium ATPase (SERCA). Docking was performed with the program GOLD in conjunction wi... |
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Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum.
Biochem. J. 396(1) , 173-82, (2006) Considering the physiological Ca2+ dynamics within the ER (endoplasmic reticulum), it remains unclear how efficient protein folding is maintained in living cells. Thus, utilizing the strictly folding-dependent activity and secretion of LPL (lipoprotein lipase... |