| 1. |
- Chen, S, et al.
(författare)
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Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells
- 2003
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Ingår i: International Immunology. - : Oxford University Press (OUP). - 1460-2377. ; 15:3, s. 403-409
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Tidskriftsartikel (refereegranskat)abstract
- TCR signaling is mediated by intracellular signaling molecules and nuclear transcription factors, which are tightly regulated by interaction with regulatory proteins such as Grb2 and SLAP. We reported recently that TCR stimulation induces the expression of cytokine-induced SH2 protein (CIS). The expression of CIS promotes TCR-mediated activation. We have now found specific interactions between CIS and activated protein kinase C (PKC) alpha, beta and theta in TCR-stimulated T cells. CIS was shown by in vitro kinase assay to associate with activated PKC. In CIS-expressing T cells isolated from CIS-transgenic mice, the amount of activated PKC associated with CIS was found to increase following TCR stimulation. By immunohistochemical analysis, CIS was also found to co-localize with PKCtheta at the plasma membrane of activated T cells. In addition to the interaction and intracellular co-localization of the CIS and PKC, an increase in the activation of AP-1 and NF-kappaB was noted in CIS-expressing T cells, after stimulation by either anti-CD3/CD28 or phorbol myristate acetate + ionomycin. These results suggest that CIS regulates PKC activation, and that this may be important for the activation of both the AP-1 and NF-kappaB pathways in TCR signaling.
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| 2. |
- Ding, HT, et al.
(författare)
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Parallel cloning, expression, purification and crystallization of human proteins for structural genomics
- 2002
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Ingår i: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; 58, s. 2102-2108
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Tidskriftsartikel (refereegranskat)abstract
- 54 human genes were selected as test targets for parallel cloning, expression, purification and crystallization. Proteins from these genes were selected to have a molecular weight of between 14 and 50 kDa, not to have a high percentage of hydrophobic residues (i.e. more likely to be soluble) and to have no known crystal structures and were not known to be subunits of heterocomplexes. Four proteins containing transmembrane regions were selected for comparative tests. To date, 44 expression clones have been constructed with the Gateway(TM) cloning system (Invitrogen, The Netherlands). Of these, 35 clones were expressed as recombinant proteins in Escherichia coli strain BL21 (DE3)-pLysS, of which 12 were soluble and four have been purified to homogeneity. Crystallization conditions were screened for the purified proteins in 96-well plates under oil. After further refinement with the same device or by the hanging-drop method, crystals were grown, with needle, plate and prism shapes. A 2.12 Angstrom data set was collected for protein NCC27. The results provide insights into the high-throughput target selection, cloning, expression and crystallization of human genomic proteins.
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| 3. |
- Chen, W, et al.
(författare)
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Full-color emission from In2S3 and ln(2)S(3): Eu3+ nanoparticles
- 2004
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Ingår i: The Journal of Physical Chemistry Part B. - : American Chemical Society (ACS). - 1520-5207 .- 1520-6106. ; 108:32, s. 11927-11934
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Tidskriftsartikel (refereegranskat)abstract
- New observations on the luminescence Of In2S3 and europium-doped In2S3 nanoparticles show a green (5 10 nm) emission from In2S3 and In1.8Eu0.2S3 nanoparticles while a blue (425 nm) emission is observed from ln(1.6)Eu(0.4)S(3) nanoparticles. Both the blue and green emissions have large Stokes shifts of 62 and 110 nm, respectively. Excitation with longer-wavelength photons causes the blue emission to shift to a longer wavelength while the green emission wavelength remains unchanged. The lifetimes of both the green and blue emissions are similar to reported values for excitonic recombination. When doped with Eu3+, in addition to the broad blue and green emissions, a red emission near 615 nm attributed to Eu3+ is observed. Temperature dependences on nanoparticle thin films indicate that with increasing temperature, the green emission wavelength remains constant, however, the blue emission shifts toward longer wavelengths. Based on these observations, the blue emission is attributed to exciton recombination and the green emission to Indium interstitial defects. These nanoparticles show full-color emission with high efficiency, fast lifetime decays, and good stability; they are also relatively simple to prepare, thus making them a new type of phosphor with potential applications in lighting, flat-panel displays, and communications.
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| 4. |
- Chen, W, et al.
(författare)
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Temperature and pressure dependences of the Mn2+ and donor-acceptor emissions in ZnS : Mn2+ nanoparticles
- 2002
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Ingår i: Applied Physics Reviews. - : AIP Publishing. - 1931-9401. ; 92:4, s. 1950-1955
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Tidskriftsartikel (refereegranskat)abstract
- Temperature and pressure dependent measurements have been performed on 3.5 nm ZnS:Mn2+ nanoparticles. As temperature increases, the donor-acceptor (DA) emission of ZnS:Mn2+ nanoparticles at 440 nm shifts to longer wavelengths while the Mn2+ emission (T-4(1)-(6)A(1)) shifts to shorter wavelengths. Both the DA and Mn2+ emission intensities decrease with temperature with the intensity decrease of the DA emission being much more pronounced. The intensity decreases are fit well with the theory of thermal quenching. As pressure increases, the Mn2+ emission shifts to longer wavelengths while the DA emission wavelength remains almost constant. The pressure coefficient of the DA emission in ZnS:Mn2+ nanoparticles is approximately -3.2 meV/GPa, which is significantly smaller than that measured for bulk materials. The relatively weak pressure dependence of the DA emission is attributed to the increase of the binding energies and the localization of the defect wave functions in nanoparticles. The pressure coefficient of Mn2+ emission in ZnS:Mn2+ nanoparticles is roughly -34.3 meV/GPa, consistent with crystal field theory. The results indicate that the energy transfer from the ZnS host to Mn2+ ions is mainly from the recombination of carriers localized at Mn2+ ions. (C) 2002 American Institute of Physics.
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| 5. |
- Paulsson, Kajsa M, et al.
(författare)
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Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum
- 2002
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 277:21, s. 18266-18271
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Tidskriftsartikel (refereegranskat)abstract
- Tapasin is a subunit of the transporter associated with antigen processing (TAP). It associates with the major histocompatibility complex (MHC) class I. We show that tapasin interacts with beta- and gamma-subunits of COPI coatomer. COPI retrieves membrane proteins from the Golgi network back to the endoplasmic reticulum (ER). The COPI subunit-associated tapasin also interacts with MHC class I molecules suggesting that tapasin acts as the cargo receptor for packing MHC class I molecules as cargo proteins into COPI-coated vesicles. In tapasin mutant cells, neither TAP nor MHC class I are detected in association with the COPI coatomer. Interestingly, tapasin-associated MHC class I molecules are antigenic peptide-receptive and detected in both the ER and the Golgi. Our data suggest that tapasin is required for the COPI vesicle-mediated retrograde transport of immature MHC class I molecules from the Golgi network to the ER.
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