Structure and function of the cell surface (tethered) mucins.

By Christine L. Hattrup, S. Gendler. Annual Review of Physiology, 2008

761 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/c83014cc1d59dcc6765e38b8a12508b0bce17bc6

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In Molecular Biology

1. P. Mukherjee
2. R. Fässler
3. S. Nath

Citations in the corpus

• Mucin dynamics and enteric pathogens (2011, background): “Cell surface mucins produced in the gastrointestinal tract include MUC1, MUC3A, MUC3B, MUC4, MUC12, MUC13, MUC15, MUC16 and MUC17 (Ref”
• The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system (2014, neutral): “MUC1 has a longer tail with several tyrosine phosphorylation sites (107).”
• Intestinal Goblet Cells and Mucins in Health and Disease: Recent Insights and Progress (2010, neutral): “Hattrup and Gendler [21], Ho et al.”
• TFOS DEWS II pathophysiology report. (2017, background): “The cytoplasmic tail of MUC1 (MUC1-CT) engages in signaling activities involving phosphorylated serine and tyrosine residues that act as binding sites for molecules such as NF-kB [142].”
• TFOS DEWS II Tear Film Report (2017, background): “These important glycan chains constitute a significant part (50e80%) of the weight of the mucin [354,355].”
• MUC1: a multifaceted oncoprotein with a key role in cancer progression. (2014, background): “The MUC1 gene encodes a single polypeptide chain which, due to conformational stress, is autoproteolytically cleaved immediately after translation at the GSVVV motif, located within the Sea urchin sperm protein enterokinase and agrin (SEA) domain, into two peptide fragments: the longer N-terminal su”
• Integrin-mediated mechanotransduction (2016, background): “, 2016), the glycocalyx can extend >100 nm from the cell surface (Hattrup and Gendler, 2008).”
• Balancing forces: architectural control of mechanotransduction (2011, neutral): “The large, heavily glycosylated transmembrane protein mucin 1 (MUC1) is a major structural component of the tumour cell glycocalyx, being overexpressed in 95% of breast cancers and 70% of solid tumour”