Results 251 to 260 of about 80,290 (296)
Clathrin-mediated endocytosis as an axis for the etiopathogenesis of Parkinson's disease. [PDF]
J Cell SciKaci A, Herbst S, Manzoni C, Lewis PA.
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A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis. [PDF]
ElifePetrovic I +5 more
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Correction for Zhang et al., Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera. [PDF]
Proc Natl Acad Sci U S Aeuropepmc +1 more source
Biochimica Et Biophysica Acta - Molecular Cell Research, 1998 Clathrin and adaptors are components of clathrin-coated pits and vesicles. The AP-1 adaptor complex is associated with clathrin-coated vesicles budding from the TGN, while the AP-2 adaptor complex is associated with clathrin-coated vesicles budding from the plasma membrane. The clathrin forms a polyhedral lattice and is believed to be the driving force
Jennifer Hirst, Margaret Robinson
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Life of a clathrin coat: insights from clathrin and AP structures
Nature Reviews Molecular Cell Biology, 2006 Membrane sorting between secretory and endocytic organelles is predominantly controlled by small carrier vesicles or tubules that have specific protein coats on their cytoplasmic surfaces. Clathrin-clathrin-adaptor coats function in many steps of intracellular transport and are the most extensively studied of all transport-vesicle coats.
Corinne Smith
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Annual Review of Biochemistry, 2000
▪ Abstract Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure.
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▪ Abstract Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure.
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Clathrin-Protein Interactions [PDF]
Traffic, 2002 There is a complex network of protein–protein and protein–lipid interactions that underlie clathrin‐mediated vesicular traffic in all compartmentalized cells from yeast to man. Major progress has been made in the determination of the three‐dimensional structures of many of the components.
Eileen Lafer
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Clathrin- and non-clathrin-coated vesicle adaptors
Trends in Biochemical Sciences, 1991Recent advances in our understanding of the protein components of the coat of non-clathrin-coated vesicles has revealed the similarity between one component of the non-clathrin coat and the adaptor proteins of clathrin-coated vesicles. This non-clathrin coat adaptor (β-COP) appears to be directly affected by Brefeldin A, a drug which inhibits secretion,
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Trends in Cell Biology, 1994
Internalization of membrane, fluid and receptor-bound ligands into cells occurs by at least two endocytic mechanisms. One is dependent on clathrin and responsible for concentrative uptake of growth factors and other ligands, whereas the other operates without clathrin.
Sandvig, Kirsten, van Deurs, Bo
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Internalization of membrane, fluid and receptor-bound ligands into cells occurs by at least two endocytic mechanisms. One is dependent on clathrin and responsible for concentrative uptake of growth factors and other ligands, whereas the other operates without clathrin.
Sandvig, Kirsten, van Deurs, Bo
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Stability and structure of clathrin
Biochemistry, 1984The effects of urea on the dissociation and structural transitions of clathrin (8 S) have been evaluated by various techniques. The dissociation of the light chains in 3 M urea has been shown by light scattering, ultracentrifugation, and column chromatography.
H, Edelhoch +3 more
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