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|a 9781461412229
|9 978-1-4614-1222-9
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|a 10.1007/978-1-4614-1222-9
|2 doi
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|a R850.A1-854
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|a Caveolins and Caveolae
|h [electronic resource] :
|b Roles in Signaling and Disease Mechanisms /
|c edited by Jean-François Jasmin, Philippe Frank, Michael P. Lisanti.
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|a 1st ed. 2012.
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|a New York, NY :
|b Springer New York :
|b Imprint: Springer,
|c 2012.
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|a XX, 184 p. 27 illus., 1 illus. in color.
|b online resource.
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
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|a online resource
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|a text file
|b PDF
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|a Advances in Experimental Medicine and Biology,
|x 2214-8019 ;
|v 729
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|a Lipid Rafts, Caveolae and GPI‑Linked Proteins -- Caveolae and the Regulation of Endocytosis -- Caveolin‑1: Role in Cell Signaling -- Regulation of eNOS in Caveolae -- Recent Developments in the Interactions Between Caveolin and Pathogens -- Caveolin‑1 and Breast Cancer: A New Clinical Perspective -- Caveolin‑1 and Prostate Cancer Progression -- Caveolins and Caveolae, Roles in Insulin Signalling and Diabetes -- Atherosclerosis, Caveolae and Caveolin‑1 -- Caveolins and Heart Diseases -- Caveolins and Lung Function.
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|a Caveolae are 50-100 nm flask-shaped invaginations of the plasma membrane that are primarily composed of cholesterol and sphingolipids. Using modern electron microscopy techniques, caveolae can be observed as omega-shaped invaginations of the plasma membrane, fully-invaginated caveolae, grape-like clusters of interconnected caveolae (caveosome), or as transcellular channels as a consequence of the fusion of individual caveolae. The caveolin gene family consists of three distinct members, namely Cav-1, Cav-2 and Cav-3. Cav-1 and Cav-2 proteins are usually co-expressed and particularly abundant in epithelial, endothelial, and smooth muscle cells as well as adipocytes and fibroblasts. On the other hand, the Cav-3 protein appears to be muscle-specific and is therefore only expressed in smooth, skeletal and cardiac muscles. Caveolin proteins form high molecular weight homo- and/or hetero-oligomers and assume an unusual topology with both their N- and C-terminal domains facing the cytoplasm.
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|a Medicine-Research.
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|a Biology-Research.
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|a Biomedical Research.
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|a Jasmin, Jean-François.
|e editor.
|4 edt
|4 http://id.loc.gov/vocabulary/relators/edt
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|a Frank, Philippe.
|e editor.
|4 edt
|4 http://id.loc.gov/vocabulary/relators/edt
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|a Lisanti, Michael P.
|e editor.
|4 edt
|4 http://id.loc.gov/vocabulary/relators/edt
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|a SpringerLink (Online service)
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|t Springer Nature eBook
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|i Printed edition:
|z 9781461412212
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|i Printed edition:
|z 9781461412236
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|a Advances in Experimental Medicine and Biology,
|x 2214-8019 ;
|v 729
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|u https://doi.uam.elogim.com/10.1007/978-1-4614-1222-9
|z Texto Completo
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|a ZDB-2-SBL
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|a ZDB-2-SXB
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|a Biomedical and Life Sciences (SpringerNature-11642)
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|a Biomedical and Life Sciences (R0) (SpringerNature-43708)
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