Imaging of Mucin Networks with Atomic Force Microscopy
Author:
Publisher
Springer US
Link
https://link.springer.com/content/pdf/10.1007/978-1-0716-3670-1_31
Reference8 articles.
1. Round AN, Berry N, McMaster TJ et al (2004) Glycopolymer charge density determines conformation in human ocular mucin gene products: an atomic force microscope study. J Struct Biol 145(3):246–253. https://doi.org/10.1016/j.jsb.2003.10.029
2. Carpenter J, Kesimer M (2021) Membrane-bound mucins of the airway mucosal surfaces are densely decorated with keratan sulfate: revisiting their role in the Lung’s innate defense. Glycobiology 31(4):436–443. https://doi.org/10.1093/glycob/cwaa089
3. Round AN, Berry N, McMaster TJ et al (2002) Heterogeneity and persistence length in human ocular mucins. Biophys J 83(3):1661–1670. https://doi.org/10.1016/S0006-3495(02)73934-9
4. Round AN, Rigby NM, García-de la Torre A et al (2012) Lamellar structures of MUC2-rich mucin: a potential role in governing the barrier and lubricating functions of intestinal mucus. Biomacromolecules 13(10):3253–3261. https://doi.org/10.1021/bm301024x
5. Carpenter J, Wang Y, Gupta R et al (2021) Assembly and organization of the N-terminal region of mucin MUC5AC: indications for structural and functional distinction from MUC5B. Proc Natl Acad Sci U S A 118(39):e2104490118. https://doi.org/10.1073/pnas.2104490118
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