Journal Article10.1016/0960-9822(93)90257-O
Barriers to diffusion
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About: This article is published in Current Biology. The article was published on 01 Mar 1993. The article focuses on the topics: Diffusion (business).
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Citations
Polarized distribution of Listeria monocytogenes surface protein ActA at the site of directional actin assembly.
TL;DR: This work has used immunocytochemistry to show that the actA gene product, ActA, is distributed asymmetrically on the bacterial surface: it is not expressed at one pole and is increasingly concentrated towards the other.
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References
Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture
Carlos G. Dotti,Kai Simons +1 more
TL;DR: It is proposed that the molecular mechanisms of surface protein sorting share common features in the two cell types, and the same viral glycoproteins are sorted in a polarized fashion in both neuronal and epithelial cells.
451
Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells
TL;DR: The asymmetric surface localization of viral glycoproteins suggests that these proteins share with intrinsic surface proteins of epithelial cells common biogenetic mechanisms and informational features or "sorting out" signals that determine their compartmentalization in the plasma membrane.
282
Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers.
TL;DR: Major histocompatibility complex (MHC) class 1 molecules that were either transmembrane- or glycosylphosphatidylinositol-anchored (Qa2) were labeled with antibody-coated gold particles and moved across the cell surface with a laser optical tweezers until they encountered a barrier, the barrier-free path length (BFP).
273
Micrometer-scale domains in fibroblast plasma membranes.
Elishalom Yechiel,Michael Edidin +1 more
TL;DR: The data strongly indicate that fibroblast surface membranes consist of protein-rich domains approximately 1 micron in diameter, embedded in a relatively protein-poor lipid continuum.
ACh receptor-rich membrane domains organized in fibroblasts by recombinant 43-kildalton protein.
William D. Phillips,Carrie Kopta,Paul Blount,Paul D. Gardner,Joe Henry Steinbach,John P. Merlie +5 more
TL;DR: The mechanism of clustering was analyzed with fibroblast cell lines that were stably transfected with mouse muscle nicotinic acetylcholine receptors and it was suggested that 43-kilodalton protein can induce A ChR clustering and that cluster induction involves direct contact between AChR and 43- KilodAlton protein.
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