957 resultados para class 1 integron
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"July 1977."
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"July 1977."
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"July 1977."
AA 157: Ann Arbor Engine 1520 ex 50 2-8-0 Alco (Brooks) 1920 22 1/2x28-51 BP210 TF 49612 class U C-2
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For a polish space M and a Banach space E let B1 (M, E) be the space of first Baire class functions from M to E, endowed with the pointwise weak topology. We study the compact subsets of B1 (M, E) and show that the fundamental results proved by Rosenthal, Bourgain, Fremlin, Talagrand and Godefroy, in case E = R, also hold true in the general case. For instance: a subset of B1 (M, E) is compact iff it is sequentially (resp. countably) compact, the convex hull of a compact bounded subset of B1 (M, E) is relatively compact, etc. We also show that our class includes Gulko compact. In the second part of the paper we examine under which conditions a bounded linear operator T : X ∗ → Y so that T |BX ∗ : (BX ∗ , w∗ ) → Y is a Baire-1 function, is a pointwise limit of a sequence (Tn ) of operators with T |BX ∗ : (BX ∗ , w∗ ) → (Y, · ) continuous for all n ∈ N. Our results in this case are connected with classical results of Choquet, Odell and Rosenthal.
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The glucagon-like peptide 1 (GLP-1) receptor is a class B G protein-coupled receptor (GPCR) that is a key target for treatments for type II diabetes and obesity. This receptor, like other class B GPCRs, displays biased agonism, though the physiologic significance of this is yet to be elucidated. Previous work has implicated R2.60190 , N3.43240 , Q7.49394 , and H6.52363 as key residues involved in peptide-mediated biased agonism, with R2.60190 , N3.43240 , and Q7.49394 predicted to form a polar interaction network. In this study, we used novel insight gained from recent crystal structures of the transmembrane domains of the glucagon and corticotropin releasing factor 1 (CRF1) receptors to develop improved models of the GLP-1 receptor that predict additional key molecular interactions with these amino acids. We have introduced E6.53364 A, N3.43240 Q, Q7.49493N, and N3.43240 Q/Q7.49 Q/Q7.49493N mutations to probe the role of predicted H-bonding and charge-charge interactions in driving cAMP, calcium, or extracellular signal-regulated kinase (ERK) signaling. A polar interaction between E6.53364 and R2.60190 was predicted to be important for GLP-1- and exendin-4-, but not oxyntomodulin-mediated cAMP formation and also ERK1/2 phosphorylation. In contrast, Q7.49394 , but not R2.60190 /E6.53364 was critical for calcium mobilization for all three peptides. Mutation of N3.43240 and Q7.49394 had differential effects on individual peptides, providing evidence for molecular differences in activation transition. Collectively, this work expands our understanding of peptide-mediated signaling from the GLP-1 receptor and the key role that the central polar network plays in these events.
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Issued June 2002 F-123-R-8; NOTE: Two different reports numbered 02/06 were issued from the CAE.
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F-123-R; issued June 1, 1997; two different reports were issued from the Center for Aquatic Ecology with report number 1997 (9)
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issued June 2001