A Posteriori Modelling-Discretization Error Estimate for Elliptic Problems with L ∞-Coefficients

We consider elliptic problems with complicated, discontinuous diffusion tensor A0. One of the standard approaches to numerically treat such problems is to simplify the coefficient by some approximation, say Aε, and to use standard finite elements. In [19] a combined modelling-discretization strategy has been proposed which estimates the discretization and modelling errors by a posteriori estimates of functional type. This strategy allows to balance these two errors in a problem adapted way. However, the estimate of the modelling error is derived under the assumption that the difference A0 − Aε is bounded in the L∞-norm, which requires that the approximation of the coefficient matches the discontinuities of the original coefficient. Therefore this theory is not appropriate for applications with discontinuous coefficients along complicated, curved interfaces. Based on bounds for A0 − Aε in an L q -norm with q < ∞ we generalize the combined modelling-discretization strategy to a larger class of coefficients.peerReviewe

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-11

2 peptides as capture antigens at 10 μg/ml (50 μl/well). There are good peptide cross recognitions (n = 4 in each group). PWT = Wild type Aβ1–42, PFM = Aβ1–42 with Flemish mutation, PDM = Aβ1–42 with Dutch mutation, PFDM = Aβ1–42 with Flemish and Dutch mutation, P22W = Aβ1–42 with novel mutation at 22, P24M = Aβ1–42 with novel mutation at 24 amino acid.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-5

E antigens at 20 μg/ml (50 μl/well) and plasma diluted at 1:1024 dilutions. Blue bar represents non-adjuvant vaccine (current study), while purple bar represents results from a previous adjuvant study [10]. PWT = Wild type Aβ1–42, PWT+MPL = Wild type Aβ1–42 mixed with monophosphoryl lipid A (MPL) as an adjuvant.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-8

–42, PDM = Aβ1–42 with Dutch mutation. Striped bars report results from current study; checkered bars report results from a previous study [10].<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Ice-Assisted Transfer of Carbon Nanotube Arrays

Decoupling the growth and the application of nanomaterials by transfer is an important issue in nanotechnology. Here, we developed an efficient transfer technique for carbon nanotube (CNT) arrays by using ice as a binder to temporarily bond the CNT array and the target substrate. Ice makes it an ultraclean transfer because the evaporation of ice ensures that no contaminants are introduced. The transferred superaligned carbon nanotube (SACNT) arrays not only keep their original appearance and initial alignment but also inherit their spinnability, which is the most desirable feature. The transfer-then-spin strategy can be employed to fabricate patterned CNT arrays, which can act as 3-dimensional electrodes in CNT thermoacoustic chips. Besides, the flip-chipped CNTs are promising field electron emitters. Furthermore, the ice-assisted transfer technique provides a cost-effective solution for mass production of SACNTs, giving CNT technologies a competitive edge, and this method may inspire new ways to transfer other nanomaterials

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-3

�g/ml (50 μl/well) and plasma diluted at 1:3200 dilutions. Blue bar shows antibody detection 6 months after third inoculation and just prior to boost, and red bar shows 10 days after boost. PDM = Aβ1–42 with Dutch mutation, P24M = Aβ1–42 with novel mutation at 24 amino acid.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-12

G/ml (50 μl/well), plasma were diluted at 1:2048 dilutions. There is no statistically significant reduction four months after vaccination. PWT = Wild type Aβ1–42, PFM = Aβ1–42 with Flemish mutation, PDM = Aβ1–42 with Dutch mutation, PFDM = Aβ1–42 with Flemish and Dutch mutation, P22W = Aβ1–42 with novel mutation at 22, P24M = Aβ1–42 with novel mutation at 24 amino acid.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-13

G/ml (50 μl/well) and plasma diluted at 1:3200 dilutions. Blue bar shows antibody detection 6 months after third inoculation and just prior to boost, and red bar shows 10 days after boost. PDM = Aβ1–42 with Dutch mutation, P24M = Aβ1–42 with novel mutation at 24 amino acid.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p

Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides-1

42 peptides as capture antigens at 10 μg/ml (50 μl/well). There are good peptide cross recognitions (n = 4 in each group). PWT = Wild type Aβ1–42, PFM = Aβ1–42 with Flemish mutation, PDM = Aβ1–42 with Dutch mutation, PFDM = Aβ1–42 with Flemish and Dutch mutation, P22W = Aβ1–42 with novel mutation at 22, P24M = Aβ1–42 with novel mutation at 24 amino acid.<p><b>Copyright information:</b></p><p>Taken from "Successful adjuvant-free vaccination of BALB/c mice with mutated amyloid β peptides"</p><p>http://www.biomedcentral.com/1471-2202/9/25</p><p>BMC Neuroscience 2008;9():25-25.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2270279.</p><p></p