ST 27:1;O3 (BioDeep_00000636711)

 

Secondary id: BioDeep_00000005822, BioDeep_00000005830, BioDeep_00000005852, BioDeep_00000006122, BioDeep_00000010755, BioDeep_00000010757, BioDeep_00000019589, BioDeep_00000598541, BioDeep_00001868841, BioDeep_00001869081, BioDeep_00001869349, BioDeep_00001869452


代谢物信息卡片


(20R,22R)-20,22-Dihydroxycholesterol;(22R)-20alpha,22-Dihydroxycholesterol

化学式: C27H46O3 (418.3447)
中文名称:
谱图信息: 最多检出来源 Homo sapiens(feces) 18.37%

分子结构信息

SMILES: C1[C@H](O)CC2=CC[C@@]3([H])[C@]4([H])CC[C@]([H])([C@]([H])(C)CCCC(O)(C)C)[C@@]4(C)CC[C@]3([H])[C@@]2(C)[C@H]1O
InChI: InChI=1S/C27H46O3/c1-17(2)7-6-8-18(3)21-9-10-22-20-15-24(29)27(30)16-19(28)11-14-26(27,5)23(20)12-13-25(21,22)4/h17-23,28,30H,6-16H2,1-5H3/t18-,19+,20+,21-,22+,23+,25-,26-,27+/m1/s1

描述信息

7α, 25-dihydroxycholesterol (7α,25-OHC) is a potent and selective agonist and endogenous ligand of the orphan GPCR receptor EBI2 (GPR183). 7α, 25-dihydroxycholesterol is highly potent at activating EBI2 (EC50=140 pM; Kd=450 pM). 7α, 25-dihydroxycholesterol can serve as a chemokine directing migration of B cells, T cells and dendritic cells[1][2].

同义名列表

105 个代谢物同义名

(24S)-Cholest-5-ene-3beta,7alpha,24-triol; 5-Cholesten-3beta,7alpha,24(S)-triol; cholest-5-en-3beta,7alpha,24S-triol; 7alpha,24S-dihydroxycholesterol; ST 27:1;O3; 3beta,7alpha,25-Trihydroxycholest-5-ene; Cholest-5-ene-3beta,7alpha,25-triol; cholest-5-en-3beta,7alpha,25-triol; 5-Cholesten-3beta,7alpha,25-triol; 7alpha,25-dihydroxycholesterol; (25R)-cholest-5-en-3beta,16alpha,27-triol; 16alpha,26-dihydroxycholesterol; 16alpha,27-dihydroxycholesterol; (25R)-cholest-5-en-3beta,7beta,27-triol; 7beta,26-dihydroxycholesterol; 7beta,27-dihydroxycholesterol; (20R)-cholest-5-en-3beta,17alpha,20-triol; (20R)-17alpha,20-dihydroxycholesterol; 17alpha,20alpha-Dihydroxycholesterol; (24R)-cholest-5-ene-3beta,7alpha,24-triol; (24R)-cholest-5-en-3beta,7alpha,24-triol; (24R)-7alpha,24-dihydroxycholesterol; cholest-5-en-3beta,7alpha,24-triol; 7alpha,24-dihydroxycholesterol; 7alpha,24alpha-dihydroxy-5beta-cholestan-3-one; 7alpha,24-dihydroxy-5beta-cholestan-3-one; 5beta-cholestan-7alpha,24-diol-3-one; cholest-5-en-3beta,7alpha,12alpha-triol; 3alpha,7alpha-dihydroxy-5beta-cholestan-26-al; 7alpha,26-dihydroxy-5beta-cholestan-3-one; 5beta-cholestan-7alpha,26-diol-3-one; Cholest-4-ene-3alpha,7alpha,12alpha-triol; 3alpha,12alpha-Dihydroxy-5beta-cholestan-7-one; 7alpha,12alpha-Dihydroxy-5alpha-Cholestan-3-one; 7alpha,12alpha-Dihydroxy-5beta-cholestan-3-one; 7alpha,25-Dihydroxy-5beta-cholestan-3-one; 5alpha-Cholest-25-ene-3alpha,7alpha,12alpha-triol; 5-Cholestene-3beta,7alpha,26-triol; 7alpha,27-dihydroxycholesterol; 3alpha-Hydroxy-5beta-cholestan-26-oic acid; 3beta-Hydroxy-5beta-cholestan-26-oic acid; 5beta-Cholest-25-ene-3alpha,7alpha,12alpha-triol; cholest-5-en-3beta,4beta,27-triol; 4beta,27-dihydroxy-cholesterol; cholest-5-en-3beta,4beta,7alpha-triol; 4beta,7alpha-dihydroxy-cholesterol; 27-hydroxy-5beta,6beta-epoxycholestan-3beta-ol; 5beta,6beta-epoxycholestan-3beta,27-diol; 27-hydroxy-5,6beta-epoxycholesterol; 27-hydroxy-5alpha,6alph-epoxycholestan-3beta-ol; 5alpha,6alpha-epoxycholestan-3beta,27-diol; 27-hydroxy-5,6alpha-epoxycholesterol; 25-hydroxy-5alpha,6alph-epoxycholestan-3beta-ol; 5alpha,6alpha-epoxycholestan-3beta,25-diol; 25-hydroxy-5,6alpha-epoxycholesterol; 25-hydroxy-5beta,6beta-epoxycholestan-3beta-ol; 5beta,6beta-epoxycholestan-3beta,25-diol; 25-hydroxy-5,6beta-epoxycholesterol; (25S)-Cholest-5-en-3beta,7alpha,26-triol; 7alpha,25(S)26-dihydroxycholesterol; (25R)-Cholest-5-en-3beta,7alpha,26-triol; 7alpha,25(R)26-dihydroxycholesterol; 3alpha-hydroxycholest-5-ene-7beta-hydroperoxide; 7alpha-peroxycholest-5-en-3beta-ol; 7alpha-hydroperoxycholesterol; 3beta-hydroxycholest-5-ene-7beta-hydroperoxide; 7beta-peroxycholest-5-en-3beta-ol; 7beta-Hydroperoxycholesterol; Cholest-5-ene-3beta,7beta,25-triol; 7beta,25-dihydroxycholesterol; 3beta,4beta-dihydroxycholest-23-one; 3beta-hydroxy-5beta-cholest-6-ene-5-hydroperoxide; 5beta-hydroperoxy-cholest-6-ene-3beta-ol; Cholesterol-5beta-hydroperoxide; 16beta,20S-dihydroxy-5-alpha-cholestan-3-one; 16beta,20S-dihydroxycholestan-3-one; 16S,20S-diydroxycholestane-3-dione; 3beta-hydroxycholest-4-ene-6beta-hydroperoxide; Cholesterol-6beta-hydroperoxide; 3beta-hydroxycholest-4-ene-6alpha-hydroperoxide; Cholesterol-6alpha-hydroperoxide; 3beta-hydroxy-5alpha-cholest-6-ene-5-hydroperoxide; 5alpha-hydroperoxy-cholest-6-ene-3beta-ol; Cholesterol-5alpha-hydroperoxide; (20R,22R)-20,22-Dihydroxycholesterol;(22R)-20alpha,22-Dihydroxycholesterol; (20R,22R)-20,22-dihydroxycholesterol; 20alpha,22beta-Dihydroxycholesterol; cholest-5-en-3beta,20R,22R-triol; 20R,22R-Dihydroxycholesterol; 20,22-Dihydroxycholesterol; cholest-5-en-3beta,6,24S-triol; 6,24S-dihydroxycholesterol; cholest-5-en-3beta,25,26-triol; 25,27-dihydroxycholesterol; cholest-5-en-3beta,24S,26-triol; 24S,27-dihydroxycholesterol; cholest-5-en-3beta,24S,25-triol; 24S,25-dihydroxycholesterol; cholestan-6-oxo-3beta,5alpha-diol; cholestan-6-oxo-3,5-diol; cholest-5-en-1alpha,3beta,25-triol; 1,25-Dihydroxycholesterol; 7α,25-OHC; 7α,25-Dihydroxycholesterol; 7alpha,27-Dihydroxycholesterol



数据库引用编号

145 个数据库交叉引用编号

分类词条

3 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表
Cytoplasm 8 AIMP2, BECN1, CASP3, CASP9, MAP1A, PIK3R6, PTGS2, SREBF1
Golgi apparatus, trans-Golgi network membrane 1 BECN1
Peripheral membrane protein 4 BECN1, CYP11A1, PIK3R6, PTGS2
Endosome membrane 1 BECN1
Endoplasmic reticulum membrane 6 BECN1, CD4, CH25H, CYP7B1, PTGS2, SREBF1
Mitochondrion membrane 2 BECN1, CYP11A1
Cytoplasmic vesicle, autophagosome 1 BECN1
Nucleus 5 AIMP2, BECN1, CASP3, CASP9, SREBF1
autophagosome 2 BECN1, MAP1LC3A
cytosol 10 AIMP2, BECN1, CASP3, CASP9, CH25H, IL1B, MAP1A, MAP1LC3A, PIK3R6, SREBF1
dendrite 2 BECN1, MAP1A
mitochondrial membrane 1 BECN1
nuclear body 1 BECN1
phagocytic vesicle 1 BECN1
phosphatidylinositol 3-kinase complex, class III 1 BECN1
trans-Golgi network 1 BECN1
nucleoplasm 2 CASP3, SREBF1
Cell membrane 4 CD4, GPR183, GPRC5A, PIK3R6
Lipid-anchor 1 MAP1LC3A
Multi-pass membrane protein 5 CH25H, CYP7B1, GPR183, GPRC5A, SREBF1
Golgi apparatus membrane 1 SREBF1
Synapse 2 ACAN, MAP1A
dendritic shaft 1 MAP1A
glutamatergic synapse 3 ACAN, CASP3, MAP1LC3A
Golgi membrane 1 SREBF1
mitochondrial inner membrane 1 CYP11A1
neuronal cell body 2 CASP3, MAP1A
Cytoplasm, cytosol 2 AIMP2, IL1B
Lysosome 1 IL1B
endosome 1 BECN1
plasma membrane 4 CD4, GPR183, GPRC5A, PIK3R6
Membrane 4 AIMP2, CYP11A1, CYP7B1, PIK3R6
axon 1 MAP1A
caveola 1 PTGS2
extracellular exosome 1 GPRC5A
endoplasmic reticulum 3 BECN1, PTGS2, SREBF1
extracellular space 4 ACAN, IL10, IL17A, IL1B
lysosomal lumen 1 ACAN
mitochondrion 3 CASP9, CYP11A1, FDX1
protein-containing complex 3 CASP9, PTGS2, SREBF1
intracellular membrane-bounded organelle 2 GPRC5A, MAP1LC3A
Microsome membrane 2 CYP7B1, PTGS2
postsynaptic density 1 CASP3
Single-pass type I membrane protein 1 CD4
Secreted 3 IL10, IL17A, IL1B
extracellular region 4 ACAN, IL10, IL17A, IL1B
Mitochondrion matrix 1 FDX1
mitochondrial matrix 2 CYP11A1, FDX1
external side of plasma membrane 2 CD4, IL17A
Secreted, extracellular space, extracellular matrix 1 ACAN
nucleolus 1 GPRC5A
axon cytoplasm 1 MAP1A
Early endosome 1 CD4
vesicle 1 GPRC5A
Mitochondrion inner membrane 1 CYP11A1
Membrane raft 1 CD4
Cytoplasm, cytoskeleton 2 MAP1A, MAP1LC3A
microtubule 2 MAP1A, MAP1LC3A
GABA-ergic synapse 1 ACAN
basement membrane 1 ACAN
collagen-containing extracellular matrix 1 ACAN
secretory granule 1 IL1B
Nucleus inner membrane 1 PTGS2
Nucleus outer membrane 1 PTGS2
nuclear inner membrane 1 PTGS2
nuclear outer membrane 1 PTGS2
Late endosome 1 MAP1LC3A
receptor complex 1 GPRC5A
neuron projection 2 MAP1A, PTGS2
chromatin 1 SREBF1
microtubule associated complex 1 MAP1A
Cytoplasmic vesicle, autophagosome membrane 1 MAP1LC3A
autophagosome membrane 1 MAP1LC3A
organelle membrane 1 MAP1LC3A
nuclear envelope 1 SREBF1
Endomembrane system 1 MAP1LC3A
phagophore assembly site 1 BECN1
phosphatidylinositol 3-kinase complex, class III, type I 1 BECN1
phosphatidylinositol 3-kinase complex, class III, type II 1 BECN1
Cytoplasmic vesicle membrane 2 GPRC5A, SREBF1
axon initial segment 1 MAP1A
Golgi lumen 1 ACAN
endoplasmic reticulum lumen 2 CD4, PTGS2
phosphatidylinositol 3-kinase complex 1 PIK3R6
phosphatidylinositol 3-kinase complex, class IA 1 PIK3R6
Secreted, extracellular exosome 1 IL1B
perineuronal net 1 ACAN
ER to Golgi transport vesicle membrane 1 SREBF1
apoptosome 1 CASP9
clathrin-coated endocytic vesicle membrane 1 CD4
death-inducing signaling complex 1 CASP3
aminoacyl-tRNA synthetase multienzyme complex 1 AIMP2
Cytoplasmic vesicle, COPII-coated vesicle membrane 1 SREBF1
dendritic microtubule 1 MAP1A
T cell receptor complex 1 CD4
Autolysosome 1 MAP1LC3A
dendritic branch 1 MAP1A
primary dendrite 1 MAP1A
perisynaptic extracellular matrix 1 ACAN
cytoplasmic side of mitochondrial outer membrane 1 BECN1
[Sterol regulatory element-binding protein 1]: Endoplasmic reticulum membrane 1 SREBF1
[Processed sterol regulatory element-binding protein 1]: Nucleus 1 SREBF1
[Isoform SREBP-1aDelta]: Nucleus 1 SREBF1
[Isoform SREBP-1cDelta]: Nucleus 1 SREBF1
phosphatidylinositol 3-kinase complex, class IB 1 PIK3R6
caspase complex 1 CASP9
[Beclin-1-C 35 kDa]: Mitochondrion 1 BECN1
[Beclin-1-C 37 kDa]: Mitochondrion 1 BECN1


文献列表

  • Yoshiro Saito, Noriko Noguchi, Etsuo Niki. Cholesterol is more readily oxidized than phospholipid linoleates in cell membranes to produce cholesterol hydroperoxides. Free radical biology & medicine. 2024 Feb; 211(?):89-95. doi: 10.1016/j.freeradbiomed.2023.12.011. [PMID: 38101585]
  • Pawel Pabisz, Jerzy Bazak, Michal Sabat, Albert W Girotti, Witold Korytowski. Cholesterol Hydroperoxide Co-trafficking in Testosterone-generating Leydig Cells: GPx4 Inhibition of Cytotoxic and Anti-steroidogenic Effects. Cell biochemistry and biophysics. 2023 Nov; ?(?):. doi: 10.1007/s12013-023-01194-5. [PMID: 37995086]
  • Pawel Pabisz, Jerzy Bazak, Albert W Girotti, Witold Korytowski. Anti-steroidogenic effects of cholesterol hydroperoxide trafficking in MA-10 Leydig cells: Role of mitochondrial lipid peroxidation and inhibition thereof by selenoperoxidase GPx4. Biochemical and biophysical research communications. 2022 02; 591(?):82-87. doi: 10.1016/j.bbrc.2021.12.117. [PMID: 34999258]
  • Albert W Girotti, Witold Korytowski. Pathophysiological potential of lipid hydroperoxide intermembrane translocation: Cholesterol hydroperoxide translocation as a special case. Redox biology. 2021 10; 46(?):102096. doi: 10.1016/j.redox.2021.102096. [PMID: 34418596]
  • Sayuri Miyamoto, Rodrigo S Lima, Alex Inague, Lucas G Viviani. Electrophilic oxysterols: generation, measurement and protein modification. Free radical research. 2021 Apr; 55(4):416-440. doi: 10.1080/10715762.2021.1879387. [PMID: 33494620]
  • Jin Huang, Seung-Jin Lee, Saeromi Kang, Man Ho Choi, Dong-Soon Im. 7α,25-Dihydroxycholesterol Suppresses Hepatocellular Steatosis through GPR183/EBI2 in Mouse and Human Hepatocytes. The Journal of pharmacology and experimental therapeutics. 2020 07; 374(1):142-150. doi: 10.1124/jpet.120.264960. [PMID: 32341017]
  • Albert W Girotti, Witold Korytowski. Cholesterol Hydroperoxide Generation, Translocation, and Reductive Turnover in Biological Systems. Cell biochemistry and biophysics. 2017 Dec; 75(3-4):413-419. doi: 10.1007/s12013-017-0799-0. [PMID: 28434137]
  • Feng Wang, Frank Stappenbeck, William Matsui, Farhad Parhami. Inhibition of Pancreatic Cancer Cell-Induced Paracrine Hedgehog Signaling by Liver X Receptor Agonists and Oxy16, a Naturally Occurring Oxysterol. Journal of cellular biochemistry. 2017 03; 118(3):499-509. doi: 10.1002/jcb.25668. [PMID: 27490478]
  • Zosia A M Zielinski, Derek A Pratt. Cholesterol Autoxidation Revisited: Debunking the Dogma Associated with the Most Vilified of Lipids. Journal of the American Chemical Society. 2016 06; 138(22):6932-5. doi: 10.1021/jacs.6b03344. [PMID: 27210001]
  • Witold Korytowski, Katarzyna Wawak, Pawel Pabisz, Jared C Schmitt, Alexandra C Chadwick, Daisy Sahoo, Albert W Girotti. Impairment of Macrophage Cholesterol Efflux by Cholesterol Hydroperoxide Trafficking: Implications for Atherogenesis Under Oxidative Stress. Arteriosclerosis, thrombosis, and vascular biology. 2015 Oct; 35(10):2104-13. doi: 10.1161/atvbaha.115.306210. [PMID: 26315403]
  • Thiago C Genaro-Mattos, Raphael F Queiroz, Daniela Cunha, Patricia P Appolinario, Paolo Di Mascio, Iseli L Nantes, Ohara Augusto, Sayuri Miyamoto. Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals. Biochemistry. 2015 May; 54(18):2841-50. doi: 10.1021/bi501409d. [PMID: 25865416]
  • S L Pierens, D R Fraser. The origin and metabolism of vitamin D in rainbow trout. The Journal of steroid biochemistry and molecular biology. 2015 Jan; 145(?):58-64. doi: 10.1016/j.jsbmb.2014.10.005. [PMID: 25305412]
  • Albert W Girotti, Tamas Kriska. Binding and cytotoxic trafficking of cholesterol hydroperoxides by sterol carrier protein-2. Methods in molecular biology (Clifton, N.J.). 2015; 1208(?):421-35. doi: 10.1007/978-1-4939-1441-8_30. [PMID: 25323524]
  • Soliman Khatib, Jacob Vaya. Oxysterols and symptomatic versus asymptomatic human atherosclerotic plaque. Biochemical and biophysical research communications. 2014 Apr; 446(3):709-13. doi: 10.1016/j.bbrc.2013.12.116. [PMID: 24393847]
  • Witold Korytowski, Katarzyna Wawak, Pawel Pabisz, Jared C Schmitt, Albert W Girotti. Macrophage mitochondrial damage from StAR transport of 7-hydroperoxycholesterol: implications for oxidative stress-impaired reverse cholesterol transport. FEBS letters. 2014 Jan; 588(1):65-70. doi: 10.1016/j.febslet.2013.10.051. [PMID: 24269887]
  • Junji Terao. Cholesterol hydroperoxides and their degradation mechanism. Sub-cellular biochemistry. 2014; 77(?):83-91. doi: 10.1007/978-94-007-7920-4_7. [PMID: 24374920]
  • Toshiyuki Nakamura, Ayako Noma, Sachiko Shimada, Nanase Ishii, Noriko Bando, Yoshichika Kawai, Junji Terao. Non-selective distribution of isomeric cholesterol hydroperoxides to microdomains in cell membranes and activation of matrix metalloproteinase activity in a model of dermal cells. Chemistry and physics of lipids. 2013 Sep; 174(?):17-23. doi: 10.1016/j.chemphyslip.2013.05.004. [PMID: 23751409]
  • Soo-Ho Choi, Huiyong Yin, Amir Ravandi, Aaron Armando, Darren Dumlao, Jungsu Kim, Felicidad Almazan, Angela M Taylor, Coleen A McNamara, Sotirios Tsimikas, Edward A Dennis, Joseph L Witztum, Yury I Miller. Polyoxygenated cholesterol ester hydroperoxide activates TLR4 and SYK dependent signaling in macrophages. PloS one. 2013; 8(12):e83145. doi: 10.1371/journal.pone.0083145. [PMID: 24376657]
  • Tau Benned-Jensen, Christoffer Norn, Stephane Laurent, Christian M Madsen, Hjalte M Larsen, Kristine N Arfelt, Romain M Wolf, Thomas Frimurer, Andreas W Sailer, Mette M Rosenkilde. Molecular characterization of oxysterol binding to the Epstein-Barr virus-induced gene 2 (GPR183). The Journal of biological chemistry. 2012 Oct; 287(42):35470-35483. doi: 10.1074/jbc.m112.387894. [PMID: 22875855]
  • Lisa M Kelly, João P Pereira, Tangsheng Yi, Ying Xu, Jason G Cyster. EBI2 guides serial movements of activated B cells and ligand activity is detectable in lymphoid and nonlymphoid tissues. Journal of immunology (Baltimore, Md. : 1950). 2011 Sep; 187(6):3026-32. doi: 10.4049/jimmunol.1101262. [PMID: 21844396]
  • Sébastien Hannedouche, Juan Zhang, Tangsheng Yi, Weijun Shen, Deborah Nguyen, João P Pereira, Danilo Guerini, Birgit U Baumgarten, Silvio Roggo, Ben Wen, Richard Knochenmuss, Sophie Noël, Francois Gessier, Lisa M Kelly, Mirka Vanek, Stephane Laurent, Inga Preuss, Charlotte Miault, Isabelle Christen, Ratna Karuna, Wei Li, Dong-In Koo, Thomas Suply, Christian Schmedt, Eric C Peters, Rocco Falchetto, Andreas Katopodis, Carsten Spanka, Marie-Odile Roy, Michel Detheux, Yu Alice Chen, Peter G Schultz, Charles Y Cho, Klaus Seuwen, Jason G Cyster, Andreas W Sailer. Oxysterols direct immune cell migration via EBI2. Nature. 2011 Jul; 475(7357):524-7. doi: 10.1038/nature10280. [PMID: 21796212]
  • Miriam Uemi, Graziella E Ronsein, Fernanda M Prado, Flávia D Motta, Sayuri Miyamoto, Marisa H G Medeiros, Paolo Di Mascio. Cholesterol hydroperoxides generate singlet molecular oxygen [O(2) ((1)Δ(g))]: near-IR emission, (18)O-labeled hydroperoxides, and mass spectrometry. Chemical research in toxicology. 2011 Jun; 24(6):887-95. doi: 10.1021/tx200079d. [PMID: 21510702]
  • Agnieszka Broniec, Radoslaw Klosinski, Anna Pawlak, Marta Wrona-Krol, David Thompson, Tadeusz Sarna. Interactions of plasmalogens and their diacyl analogs with singlet oxygen in selected model systems. Free radical biology & medicine. 2011 Apr; 50(7):892-8. doi: 10.1016/j.freeradbiomed.2011.01.002. [PMID: 21236336]
  • Graziella E Ronsein, Mauricio Cesar Bof de Oliveira, Marisa H G Medeiros, Sayuri Miyamoto, Paolo Di Mascio. DNA strand breaks and base modifications induced by cholesterol hydroperoxides. Free radical research. 2011 Mar; 45(3):266-75. doi: 10.3109/10715762.2010.524215. [PMID: 20942561]
  • Tamas Kriska, Anna Pilat, Jared C Schmitt, Albert W Girotti. Sterol carrier protein-2 (SCP-2) involvement in cholesterol hydroperoxide cytotoxicity as revealed by SCP-2 inhibitor effects. Journal of lipid research. 2010 Nov; 51(11):3174-84. doi: 10.1194/jlr.m008342. [PMID: 20656919]
  • Witold Korytowski, Daniel Rodriguez-Agudo, Anna Pilat, Albert W Girotti. StarD4-mediated translocation of 7-hydroperoxycholesterol to isolated mitochondria: deleterious effects and implications for steroidogenesis under oxidative stress conditions. Biochemical and biophysical research communications. 2010 Jan; 392(1):58-62. doi: 10.1016/j.bbrc.2009.12.165. [PMID: 20059974]
  • Yuko Minami, Kyuichi Kawabata, Yoshiaki Kubo, Seiji Arase, Katsuya Hirasaka, Takeshi Nikawa, Noriko Bando, Yoshichika Kawai, Junji Terao. Peroxidized cholesterol-induced matrix metalloproteinase-9 activation and its suppression by dietary beta-carotene in photoaging of hairless mouse skin. The Journal of nutritional biochemistry. 2009 May; 20(5):389-98. doi: 10.1016/j.jnutbio.2008.04.010. [PMID: 18656335]
  • Migiwa Asano, Hideyuki Nushida, Junko Adachi, Yasushi Nagasaki, Kanako Nakagawa, Azumi Kuse, Yasuhiro Ueno. Lipid hydroperoxides in human plasma after ethanol consumption. Legal medicine (Tokyo, Japan). 2009 Apr; 11 Suppl 1(?):S223-5. doi: 10.1016/j.legalmed.2009.01.054. [PMID: 19261511]
  • Yuko Minami, Sayuri Yokoi, Mari Setoyama, Noriko Bando, Sayaka Takeda, Yoshichika Kawai, Junji Terao. Combination of TLC blotting and gas chromatography-mass spectrometry for analysis of peroxidized cholesterol. Lipids. 2007 Nov; 42(11):1055-63. doi: 10.1007/s11745-007-3099-4. [PMID: 17701239]
  • Junko Adachi, Emiko Kurisaki, Risa Kudo, Kanako Nakagawa, Katsuhiko Hatake, Kouichi Hiraiwa, Yasuhiro Ueno. Enhanced lipid peroxidation in tourniquet-release mice. Clinica chimica acta; international journal of clinical chemistry. 2006 Sep; 371(1-2):79-84. doi: 10.1016/j.cca.2006.02.024. [PMID: 16624265]
  • Tamas Kriska, Vladislav V Levchenko, Witold Korytowski, Barbara P Atshaves, Friedhelm Schroeder, Albert W Girotti. Intracellular dissemination of peroxidative stress. Internalization, transport, and lethal targeting of a cholesterol hydroperoxide species by sterol carrier protein-2-overexpressing hepatoma cells. The Journal of biological chemistry. 2006 Aug; 281(33):23643-51. doi: 10.1074/jbc.m600744200. [PMID: 16772292]
  • Kanako Nakagawa, Junko Adachi, Max C Y Wong, Yasuhiro Ueno. Protective effect of daidzein against acute ethanol-induced lipid peroxidation in rat jejunum. The Kobe journal of medical sciences. 2006; 52(5):141-9. doi: ". [PMID: 17006054]
  • Tamas Kriska, Albert W Girotti. A thin layer chromatographic method for determining the enzymatic activity of peroxidases catalyzing the two-electron reduction of lipid hydroperoxides. Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. 2005 Nov; 827(1):58-64. doi: 10.1016/j.jchromb.2005.03.045. [PMID: 15899595]
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