987 resultados para his-tagged proteins


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Meyrick, Robert, 'Hugh Blaker: Doing his Bit for the Moderns', Journal of the History of Collections (2004) 16(2):173-189 RAE2008

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Gatherer, D., and McEwan, N.R. (2003). Analysis of sequence periodicity in E. coli proteins: empirical investigation of the 'duplication and divergence' theory of protein evolution. Journal of Molecular Evolution 57, 149-158. RAE2008

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Igor E. Moshkov, Galina V. Novikova, Luis A.J. Mur, Aileen R. Smith, and Michael A. Hall. (2003). Ethylene rapidly up-regulates the activities of both monomeric GTP-binding proteins and protein kinase(s) in epicotyls of pea. Plant Physiology, 131(4), 1718-1726 RAE2008

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Russell M. Morphew, Hazel A. Wright, E. James LaCourse, Debra J. Woods and Peter M. Brophy (2007). Comparative proteomics of excretory-secretory proteins released by the liver fluke Fasciola hepatica in sheep host bile and during in vitro culture ex host. Molecular and Cellular Proteomics, 6 (6), 963-972. Sponsorship: BBSRC / EU RAE2008

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The musicological tradition places Liszt’s Sonata in B minor within the sphere of compositions inspired by the Faustian myth. Its musical material, its structure and its narrative exhibit certain similarities to the ‘Faust’ Symphony. Yet there has appeared a diff erent and, one may say, a rival interpretation of Sonata in B minor. What is more, it is well-documented from both a musical and a historical point of view. It has been presented by Hungarian pianist and musicologist Tibor Szász. He proposes the thesis that the Sonata in B minor has been in fact inspired by Milton’s Paradise Lost, with its three protagonists: Adam, Satan and Christ. He fi nds their illustrations and even some key elements of the plot in the Sonata’s narrative. But yet Milton’s Paradise Lost and Goethe’s Faust are both stories of the Fall and Salvation, of the cosmic struggle between good and evil. The triads of their protagonists – Adam and Eve, Satan, and Christ; Faust, Mephisto and Gretchen – are homological. Thus both interpretations of the Sonata, the Goethean and the Miltonian, or, in other words, the Faustian and the Luciferian, are parallel and complementary rather than rival. It is also highly probable that both have had their impact on the genesis of the Sonata in B minor.

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http://www.archive.org/details/goodbirdindian00goodiala

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http://anglicanhistory.org/bios/pollock/ View document online

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http://www.archive.org/details/arthurdouglasmi00douguoft

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http://www.archive.org/details/johnwesleytheman00pikeuoft

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Rab4 is a member of the Rab superfamily of small GTPases. It is localized to the early sorting endosome and plays a role in regulating the transport from this compartment to the recycling and degradative pathways. In order to further our understanding of the role Rab4 plays in endocytosis, a yeast two-hybrid screen was performed to identify putative Rab4 effectors. A constitutively active mutant of Rab4, Rab4Q67L, when used as bait to screen a HeLa cDNA library, identified a novel 80kDa protein that interacted with Rab4-GTP. This protein was called Rab Coupling Protein (RCP). RCP interacts preferentially with the GTP-bound form of Rab4. Subsequent work demonstrated that RCP also interacts with Rab11, and that this interaction is not nucleotide-depenedent. RCP is predominantly membrane-bound and localised to the perinuclear recycling compartment. Expression of a truncation mutant of RCP, that contains the Rab binding domain, in HeLa cells, results in the formation of an extensive tubular network that can be labelled with transferrin. These tubules are derived from the recycling compartment since they are inaccessible to transferrin when the ligand is internalised at 18oC. The truncation mutant-induced morphology can be rescued by overexpression of active Rab11, but not active Rab4. This suggests that RCP functions between Rab4 and Rab11 in the receptor recycling pathway, and may act as a ‘molecular bridge’ between these two sequentially acting small GTPases. Quantitative assays demonstrated that overexpression of the truncation mutant results in a dramatic inhibition in the rate of receptor recycling. Database analysis revealed that RCP belongs to a family of Rab interacting proteins, each characterised by a carboxy-terminal coiled-coil domain and an amino-terminal phospholipid-binding domain. KIAA0941, an RCP homologue, interacts with Rab11, but not with Rab4. Overexpression of its Rab binding domain also results in a tubular network, however, this tubulation cannot be rescued by active Rab11.