Results 261 to 270 of about 155,318 (315)

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 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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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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Properties of the Coat Protein of a New Tobacco Mosaic Virus Coat Protein ts-Mutant

Journal of Protein Chemistry, 1997
Amino acid substitutions in a majority of tobacco mosaic virus (TMV) coat protein (CP) ts-mutants have previously been mapped to the same region of the CP molecule tertiary structure, located at a distance of about 70 A from TMV virion axis. In the present work some properties of a new TMV CP ts-mutant ts21-66 (two substitutions I21=>T and D66=>G, both
E N, Dobrov, M M, Abu-Eid, A G, Solovyev, S V, Kust, V K, Novikov   +4 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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Molecular structures of coat and coat-associated proteins: function follows form

Current Opinion in Cell Biology, 2006
Endocytic clathrin-coated vesicles arise through the deformation of a small region of plasma membrane encapsulated by a cytosol-oriented clathrin lattice. The coat assembles from soluble protomers in a rapid and highly cooperative process, and invagination is tightly linked to the selective enrichment of cargo molecules within the nascent bud.
Tom J, Brett, Linton M, Traub
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Coat proteins: shaping membrane transport

Nature Reviews Molecular Cell Biology, 2003
Coat proteins allow the selective transfer of macromolecules from one membrane-enclosed compartment to another by concentrating macromolecules into specialized membrane patches and then deforming these patches into small coated vesicles. Recent findings indicate that coat proteins might also participate in the differentiation of membrane domains within
Juan S, Bonifacino, Jennifer, Lippincott-Schwartz   +1 more
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Formation of protein-coated iron minerals

Dalton Transactions, 2005
The ability of iron to cycle between Fe(2+) and Fe(3+) forms has led to the evolution, in different forms, of several iron-containing protein cofactors that are essential for a wide variety of cellular processes, to the extent that virtually all cells require iron for survival and prosperity.
Allison, Lewin, Geoffrey R, Moore, Nick E, Le Brun   +2 more
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