NS Harhaj, DA Antonetti - The international journal of biochemistry & cell …, 2004 - Elsevier
The mechanism by which epithelial and endothelial cells interact to form polarized tissue is of fundamental importance to multicellular organisms. Dysregulation of these barriers occurs …
B Grant, D Hirsh - Molecular biology of the cell, 1999 - Am Soc Cell Biol
The Caenorhabditis elegans oocyte is a highly amenable system for forward and reverse genetic analysis of receptor-mediated endocytosis. We describe the use of transgenic …
The low-density lipoprotein (LDL) receptor-related protein 2 (LRP2 or megalin) is representative of the phylogenetically conserved subfamily of giant LDL receptor-related …
TL Le, AS Yap, JL Stow - The Journal of cell biology, 1999 - rupress.org
E-Cadherin plays critical roles in many aspects of cell adhesion, epithelial development, and the establishment and maintenance of epithelial polarity. The fate of E-cadherin once it is …
M Ren, G Xu, J Zeng… - Proceedings of the …, 1998 - National Acad Sciences
Rab11 is a small GTP-binding protein that in cultured mammalian cells has been shown to be concentrated in the pericentriolar endosomal recycling compartment and to play a key …
N Bayer, D Schober, E Prchla, RF Murphy… - Journal of …, 1998 - Am Soc Microbiol
ABSTRACT Bafilomycin A1 (baf), a specific inhibitor of vacuolar proton ATPases, is commonly employed to demonstrate the requirement of low endosomal pH for viral …
ML Eshbach, OA Weisz - Annual review of physiology, 2017 - annualreviews.org
Cells lining the proximal tubule (PT) of the kidney are highly specialized for apical endocytosis of filtered proteins and small bioactive molecules from the glomerular …
M Gekle - Annu. Rev. Physiol., 2005 - annualreviews.org
▪ Abstract Albumin is the most abundant protein in serum and contributes to the maintenance of oncotic pressure as well as to transport of hydrophobic molecules. Although albumin is a …
I Martinez, S Chakrabarti, T Hellevik… - The Journal of cell …, 2000 - rupress.org
Synaptotagmins (Syts) are transmembrane proteins with two Ca2+-binding C2 domains in their cytosolic region. Syt I, the most widely studied isoform, has been proposed to function …