1,721,020 research outputs found
The Interaction of N-Ethyl Retinamide with Plasma Retinol-Binding Protein (RBP) and the Crystal Structure of the Retinoid-RBP Complex at 1.9 Å Resolution"
The three-dimensional structure of bovine plasma retinol-binding protein (RBP) complexed with N-ethyl retinamide has been determined at 1.9-angstrom resolution. The crystals of the complex (space group P2(1)2(1)2(1), a = 46.27, b = 49.11, c = 76.41 angstrom) are isomorphous with those of bovine holo and apoRBP. The final crystallographic R factor is 0.172 for 11,261 observed reflections. The model of the retinoid-RBP complex is nearly identical to that of bovine retinol-RBP complex; the root mean square deviations between the alpha-carbons in the two proteins is 0.15 angstrom. The N-ethyl retinamide molecule fits in the beta-barrel in the same position previously occupied by the vitamin. The ethyl group of the retinoid replaces the retinol hydroxyl group and a water molecule hydrogen bonded to it. This substitution has no consequence on the overall conformation of the protein. The modification of the functional end group of retinol does not lead to an apparent loss of affinity of the retinol analog for apoRBP, as established by means of fluorometric titrations with N-ethyl retinamide. However, the binding of the retinoid to RBP abolishes or greatly reduces the affinity of RBP for transthyretin. This behavior further supports the hypothesis that the area of the entrance of the beta-barrel, which includes the ethyl group of the retinoid bound to RBP, is involved in the interaction with transthyretin. Moreover, it indicates a high degree of complementarity of interacting surfaces between RBP and transthyretin. In fact, the replacement of the retinol hydroxyl group and quite small structural changes in the above region of the RBP molecule drastically affect the protein-protein recognition
Retinoid binding to retinol-binding protein and the interference with the interaction with transthyretin
The Interaction of N-Ethyl Retinamide with Plasma Retinol-Binding Protein (RBP) and the Crystal Structure of the Retinoid-RBP Complex at 1.9 Å Resolution.
Structure of pig plasma retinol-binding protein at 1.65 Å resolution
The crystal structure of pig plasma retinol-binding protein (REP) has been determined at 1.65 Angstrom resolution. The space group is P2(1)2(1)2(1), with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) Angstrom and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R factor of 0.1844 and an R-free of 0.237 for 18 874 and 1001 independent reflections, respectively. The relatively high resolution structure of pig holoRBP has revealed some new structural details. Moreover, it has provided a description of the binding site for Cd2+, a metal ion which is required for protein crystallization. The hepta-coordination of the REP-bound cadmium ion involves different residues of two symmetry-related REP molecules, consistent with the participation of the cation in intermolecular interactions that in turn promote protein crystallization
Retinoids: in vitro interaction with retinol-binding protein and influence on plasma retinol
FASEB J
Il laboratorio: tra curricolo formativo e profilo professionale nella LMCU in Scienze della Formazione Primaria. Un’indagine esplorativa sul contributo pedagogico-didattico della sede di Reggio Emilia al rapporto tra didattica, ricerca e terza missione.
Going Beyond Counting First Authors in Author Co-citation Analysis
The present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
Variations on the Author
“Variations on the Author” discusses two of Eduardo Coutinho’s recent films (Um Dia na Vida, from 2010, and Últimas Conversas, posthumously released in 2015) and their contribution to the general question of documentary authorship. The director’s filmography is characterized by a consistent yet self-effacing form of authorial self-inscription: Coutinho often features as an interviewer that rather than express opinions propels discourses; an interviewer that is good at listening. This mode of self-inscription characterizes him as an author who is not expressive but who is nonetheless markedly present on the screen. In Um Dia na Vida, however, Coutinho is completely absent form the image, while Últimas Conversas, on the contrary, includes a confessional prologue that moves the director from the margins to the center of his films. This article examines the ways in which these works stand out in the filmography of a director who offers new insights into the notion of cinematic authorship
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