Rottlerin is a lipid of Polyketides (PK) class. Rottlerin is associated with abnormalities such as PARAGANGLIOMAS 2, Hyperostosis, Diffuse Idiopathic Skeletal, Virus Diseases, Perisylvian syndrome and Autoimmune disease (systemic) NOS. The involved functions are known as Apoptosis, Regulation, Signal Transduction, inhibitors and Proteasome Inhibitors [MoA]. Rottlerin often locates in Clone, Membrane, Body tissue, Plasma membrane and soluble. The associated genes with Rottlerin are XIAP gene, GAPDH gene, ICAM1 gene, P4HTM gene and TNFSF10 gene. The related lipids are Promega, Fatty Acids, Sphingolipids, Lipopolysaccharides and Saponin. The related experimental models are Mouse Model, Xenograft Model and Cancer Model.
To understand associated biological information of rottlerin, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
rottlerin is suspected in Infection, Morphologically altered structure, Ischemia, Pulmonary Edema, Asthma, Cardiovascular Diseases and other diseases in descending order of the highest number of associated sentences.
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We collected disease MeSH terms mapped to the references associated with rottlerin
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
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Cancer Model are used in the study 'Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family.' (Ohno I et al., 2010) and Cancer Model are used in the study 'Rottlerin induces Wnt co-receptor LRP6 degradation and suppresses both Wnt/β-catenin and mTORC1 signaling in prostate and breast cancer cells.' (Lu W et al., 2014).
Mouse Model are used in the study 'Neuroprotective effect of protein kinase C delta inhibitor rottlerin in cell culture and animal models of Parkinson's disease.' (Zhang D et al., 2007).
Xenograft Model are used in the study 'Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family.' (Ohno I et al., 2010).
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Authors | Title | Published | Journal | PubMed Link |
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Frank DE and Carter WG | Laminin 5 deposition regulates keratinocyte polarization and persistent migration. | 2004 | J. Cell. Sci. | pmid:14996912 |
Shimamura K et al. | Expression of adhesion molecules by sphingosine 1-phosphate and histamine in endothelial cells. | 2004 | Eur. J. Pharmacol. | pmid:14975703 |
Rao VU et al. | PKC-epsilon regulation of extracellular signal-regulated kinase: a potential role in phenylephrine-induced cardiocyte growth. | 2004 | Am. J. Physiol. Heart Circ. Physiol. | pmid:14975926 |
Cummings R et al. | Protein kinase Cdelta mediates lysophosphatidic acid-induced NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells. | 2004 | J. Biol. Chem. | pmid:15280372 |
Anantharam V et al. | Blockade of PKCdelta proteolytic activation by loss of function mutants rescues mesencephalic dopaminergic neurons from methylcyclopentadienyl manganese tricarbonyl (MMT)-induced apoptotic cell death. | 2004 | Ann. N. Y. Acad. Sci. | pmid:15681813 |
Huda R et al. | Selective activation of protein kinase C delta in human neutrophils following ischemia reperfusion of skeletal muscle. | 2004 | Shock | pmid:15167677 |
Kajimoto T et al. | Ceramide-induced apoptosis by translocation, phosphorylation, and activation of protein kinase Cdelta in the Golgi complex. | 2004 | J. Biol. Chem. | pmid:14715667 |
Woo CH et al. | Lipopolysaccharide induces matrix metalloproteinase-9 expression via a mitochondrial reactive oxygen species-p38 kinase-activator protein-1 pathway in Raw 264.7 cells. | 2004 | J. Immunol. | pmid:15557194 |
Kang HS et al. | Receptor activator of nuclear factor-kappaB is induced by a rottlerin-sensitive and p38 MAP kinase-dependent pathway during monocyte differentiation. | 2004 | Mol. Cells | pmid:15232218 |
Cho CH et al. | Localization of VEGFR-2 and PLD2 in endothelial caveolae is involved in VEGF-induced phosphorylation of MEK and ERK. | 2004 | Am. J. Physiol. Heart Circ. Physiol. | pmid:14704231 |