| 11. |
- Lui, Hoi-Shun, 1980, et al.
(författare)
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A Note on the Mutual-Coupling Problems in Transmitting and Receiving Antenna Arrays
- 2009
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Ingår i: IEEE Antennas and Propagation Magazine. - 1045-9243. ; 51:5, s. 171-176
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Tidskriftsartikel (refereegranskat)abstract
- In antenna arrays, mutual coupling between antenna elements is well known as an undesired effect, which degrades the performance of array signal-processing algorithms. The compensation of such an undesired effect has been a popular research topic throughout the years. Various approaches for mutual-coupling compensation have been developed, and they can easily be found in the open literature. In general, the mutual-coupling problems for a transmitting and receiving array are different, even if the physical geometry of the array remains unchanged. However, it seems that antenna engineers are not well aware of such differences in the analysis of receiving antenna arrays. In this note, the mutual-coupling problems in transmitting and receiving antenna arrays are revisited. The differences between the mutual coupling and mutual impedances for transmitting and receiving antenna arrays are explained. It is concluded that the mutual-coupling problems of transmitting and receiving arrays are in general different, and hence different mutual impedances should be used for mutual-coupling analysis and compensation.
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| 12. |
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| 13. |
- Orrú, Valeria, et al.
(författare)
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A loss-of-function variant of PTPN22 is associated with reduced risk of systemic lupus erythematosus
- 2009
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Ingår i: Human Molecular Genetics. - : Oxford University Press (OUP). - 0964-6906 .- 1460-2083. ; 18:3, s. 569-579
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Tidskriftsartikel (refereegranskat)abstract
- A gain-of-function R620W polymorphism in the PTPN22 gene, encoding the lymphoid tyrosine phosphatase LYP, has recently emerged as an important risk factor for human autoimmunity. Here we report that another missense substitution (R263Q) within the catalytic domain of LYP leads to reduced phosphatase activity. High-resolution structural analysis revealed the molecular basis for this loss of function. Furthermore, the Q263 variant conferred protection against human systemic lupus erythematosus, reinforcing the proposal that inhibition of LYP activity could be beneficial in human autoimmunity.
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| 14. |
- Preston, R J S, et al.
(författare)
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Selective modulation of protein C affinity for EPCR and phospholipids by Gla domain mutation
- 2005
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Ingår i: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 272:1, s. 97-108
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Tidskriftsartikel (refereegranskat)abstract
- Uniquely amongst vitamin K-dependent coagulation proteins, protein C interacts via its Gla domain both with a receptor, the endothelial cell protein C receptor (EPCR), and with phospholipids. We have studied naturally occurring and recombinant protein C Gla domain variants for soluble (s)EPCR binding, cell surface activation to activated protein C (APC) by the thrombin-thrombomodulin complex, and phospholipid dependent factor Va (FVa) inactivation by APC, to establish if these functions are concordant. Wild-type protein C binding to sEPCR was characterized with surface plasmon resonance to have an association rate constant of 5.23x10(5) M-1.s(-1), a dissociation rate constant of 7.61x10(-2) s(-1) and equilibrium binding constant (K-D) of 147 nM. It was activated by thrombin over endothelial cells with a K-m of 213 nM and once activated to APC, rapidly inactivated FVa. Each of these interactions was dramatically reduced for variants causing gross Gla domain misfolding (R-1L, R-1C, E16D and E26K). Recombinant variants Q32A, V34A and D35A had essentially normal functions. However, R9H and H10Q/S11G/S12N/D23S/Q32E/N33D/H44Y (QGNSEDY) variants had slightly reduced (
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