CYTOCHALASIN B is a lipid of Polyketides (PK) class. Cytochalasin b is associated with abnormalities such as Renal tubular disorder and Chagas Disease. The involved functions are known as Membrane Protein Traffic, inhibitors, Metabolic Inhibition, Biochemical Pathway and Increased Sensitivy. Cytochalasin b often locates in Cytoplasmic matrix, Plasma membrane, Microtubules, Extracellular and Protoplasm. The associated genes with CYTOCHALASIN B are SLC2A2 gene, PFDN5 gene, SLC2A1 gene, OMG gene and SPEN gene. The related lipids are Steroids, Lipopolysaccharides and Liposomes. The related experimental models are Xenograft Model.
To understand associated biological information of CYTOCHALASIN B, 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.
CYTOCHALASIN B is suspected in Renal tubular disorder, Chagas Disease 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 CYTOCHALASIN B
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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Lipid concept | Cross reference | Weighted score | Related literatures |
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Xenograft Model are used in the study 'Endofacial competitive inhibition of the glucose transporter 1 activity by gossypol.' (Pérez A et al., 2009).
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Authors | Title | Published | Journal | PubMed Link |
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Hensel W | Cytochalasin B affects the structural polarity of statocytes from cress roots (Lepidium sativum L.). | 1985 | Protoplasma | pmid:11540620 |
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Hodick D | Negative gravitropism in Chara protonemata: a model integrating the opposite gravitropic responses of protonemata and rhizoids. | 1994 | Planta | pmid:11541071 |
Sievers A et al. | The polar organization of the growing Chara rhizoid and the transport of statoliths are actin-dependent. | 1991 | Bot. Acta | pmid:11541283 |
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