Results 181 to 190 of about 10,834,965 (260)

Brain Coated Vesicle Destabilization and Phosphorylation of Coat Proteins

Journal of Neurochemistry, 1988
Abstract: Two basic polypeptides, bee venom melittin and poly‐L‐lysine, induced concentration‐dependent destabilization of bovine brain coated vesicles. Ultrastructurally the changes observed were aggregation of clathrin coats and segregation of the vesicle membrane, concomitant with the appearance of elongated cisternae of various sizes.
V, Georgieva-Hanson, W J, Schook, S, Puszkin   +2 more
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Molecular properties of the reassembled coat protein of coated vesicles

Biochemistry, 1980
Clathrin has been prepared from human and bovine brains by a rapid technique which does not require sucrose gradient centrifugation. The promoter molecule which is obtained has the ability to polymerize and form protein coats, i.e., so-called cages or baskets, which resemble the structures observed in coated vesicles.
P K, Nandi, H T, Pretorius, R E, Lippoldt, M L, Johnson, H, Edelhoch   +4 more
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Clathrin: anatomy of a coat protein

Trends in Cell Biology, 1999
Clathrin is a vesicle coat protein involved in the assembly of membrane and cargo into transport vesicles at the plasma membrane and on certain intracellular organelles. Recently, crystal structures of two separate parts of the clathrin heavy chain, a fragment of the proximal leg and the N-terminal domain, have been analysed, providing the first high ...
C J, Smith, B M, Pearse
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Bacteriophage Coat Protein as Repressor

Nature, 1968
It seems that viral coat protein acts as a repressor of protein synthesis at the level of transcription rather than translation.
H, Robertson, R E, Webster, N D, Zinder
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Coat protein of potyviruses

Archives of Virology, 1987
K H Gough, C W Ward, D D Shukla
exaly   +2 more sources

Coat Proteins and Vesicle Budding

Science, 1996
The trafficking of proteins within eukaryotic cells is achieved by the capture of cargo and targeting molecules into vesicles that bud from a donor membrane and deliver their contents to a receiving compartment. This process is bidirectional and may involve multiple organelles within a cell.
R, Schekman, L, Orci
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Insoluble coat protein mutants of TMV: Their origin, and characterization of the defective coat proteins

Virology, 1973
A method is described for the purification of the defective protein of TMV mutants, from a class of mutants which engender an insoluble coat protein in their host. These proteins are unable to aggregate with TMV-RNA to form a functional virion. Amino acid compositions of one isolate each of mutant PM1 and PM2I and two of mutant PM4 showed a small ...
V, Hariharasubramanian, R C, Smith, M, Zaitlin   +2 more
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Recruitment of Coat Proteins to Peptidoliposomes

2008
Intracellular transport between compartments within the cell is generally mediated by membrane vesicles. Their formation is initiated by activation of small GTPases that then recruit cytosolic proteins to the membrane surface to form a coat, interact with cargo proteins, and deform the lipid bilayer.
Suri, Gregor, Spiess, Martin, Crottet, Pascal   +2 more
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Membrane deformation by protein coats

Current Opinion in Cell Biology, 2006
Protein coats deform lipid membranes into spherical buds, which undergo fission at the neck to become vesicles. To induce membrane curvature, protein coats use basic tools including amphipathic helices and concave protein surfaces, and take advantage of the bulk properties of cellular membranes, such as loose lipid packing in the endoplasmic reticulum ...
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The role of coat proteins in the biosynthesis of secretory proteins

Current Opinion in Cell Biology, 1995
The biosynthesis of secretory proteins requires vesicle-mediated transport between the organelles of the secretory pathway. Biochemical and genetic analysis of the secretory pathway has identified two non-clathrin coats--COPI and COPII--that drive the formation of vesicles that mediate transport between the endoplasmic reticulum and the Golgi apparatus,
N R, Salama, R W, Schekman
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