Results 341 to 350 of about 6,491,357 (404)

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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Coat proteins in intracellular membrane transport

Current Opinion in Cell Biology, 1994
Transport of newly synthesized material from the endoplasmic reticulum (ER) towards the Golgi complex, through the Golgi cisternae, and out of the trans-Golgi network (TGN) is thought to be mediated by vesicular carriers. Different types of vesicle are involved in this biosynthetic membrane traffic.
T E, Kreis, R, Pepperkok
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Protein-containing hydrophobic coatings and films

Biomaterials, 2002
The incorporation of enzymes and other proteins into hydrophobic polymeric coatings and films has been investigated in this study with the goal of generating biologically active materials for biocatalysis, antifouling surfaces, and biorecognition. The protein-polymer composites are created using standard solution coating techniques with poly(methyl ...
Scott J, Novick, Jonathan S, Dordick
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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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Bacterial Adhesion to Protein-Coated Hydrogels

Journal of Biomaterials Applications, 1993
Extended wear soft contact lenses have been implicated in the increased occurrence of corneal bacterial infections. This research investigated the effects of polymer chemistry, water content, and pre-sorbed proteins upon the adherence of Pseudomonas aeruginosa to model hydrogels with chemistries similar to those of extended wear soft contact lenses ...
A D, Cook, R D, Sagers, W G, Pitt
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History of Coat Protein-Mediated Protection

1998
A decade of research has proven that plants can be genetically engineered to resist virus infection through expression of viral CP genes, as well as other viral genes and sequences. Additional opportunities for development of resistant plants will require research focused on mechanisms of protection, improvements in expression vector design, and ...
E D, Miller, C, Hemenway
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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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Complementation of coat protein-defective TMV mutants in transgenic tobacco plants expressing TMV coat protein

Virology, 1990
Transgenic tobacco plants (Nicotiana tabacum cv. Xanthi) which express tobacco mosaic virus (TMV) U1 strain coat protein (CP) can complement both the assembly and the long-distance spread of CP-defective (DT1) or coat proteinless (DT1G) mutants of TMV.
J K, Osbourn, S, Sarkar, T M, Wilson
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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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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
openaire   +2 more sources