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Life of a clathrin coat: insights from clathrin and AP structures [PDF]

open access: yesNature 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
exaly   +4 more sources
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Clathrin

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.
openaire   +2 more sources

Clathrin- and non-clathrin-coated vesicle adaptors

Trends in Biochemical Sciences, 1991
Recent 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,
openaire   +2 more sources

Endocytosis without clathrin

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
openaire   +2 more sources

Stability and structure of clathrin

Biochemistry, 1984
The 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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Clathrin, Adaptors, and Sorting

Annual Review of Cell Biology, 1990
CONTENTS INTRODUCTION 15 1 COAT COMPONENTS 153 Clathrin Triskelions and Adaptors ....... 153 Function and Distribution of Adaptors 156 COATED PITS AS MOLECULAR FILTERS ......... ... .. 159 Clathrin-Mediated Endocytosis. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
B M, Pearse, M S, Robinson
openaire   +2 more sources

Clathrin and clathrin-accessory proteins in rat kidney cortex epithelia

Histochemistry and Cell Biology, 2006
Several vectorial transport routes in mammalian cells involve clathrin and associated proteins. In kidney epithelia urine production requires numerous transport processes. However, only little is known about the distribution of clathrin and its associated proteins in this organ in situ. We now report on the presence and distribution of clathrin and its
Sabine, Hasse   +2 more
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Clathrin and Plant Endocytosis

Traffic, 2002
Endocytosis requires the coordinated interaction of a plethora of cytosolic and membrane proteins. In mammalian cells, clathrin plays a crucial role in this process as a scaffolding protein underlying the invaginating plasma membrane and surrounding the primary endocytic vesicle.
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Clathrin

1999
Abstract Clathrin is a triskelion-shaped, self-assembling protein which polymerizes into a polyhedral lattice on the cytoplasmic surface of cellular membranes. Formation of the clathrin lattice constitutes a mechanism for sorting membrane-associated proteins which are incorporated into the lattice via bridging proteins, known as adaptors
openaire   +1 more source

Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling

Nature Reviews Molecular Cell Biology, 2005
The internalization of various cargo proteins and lipids from the mammalian cell surface occurs through the clathrin and lipid-raft endocytic pathways. Protein-lipid and protein-protein interactions control the targeting of signalling molecules and their partners to various specialized membrane compartments in these pathways.
Christine, Le Roy, Jeffrey L, Wrana
openaire   +2 more sources

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