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Differential Recognition (differential + recognition)

Distribution by Scientific Domains
Medical Sciences50%

Selected Abstracts

Open Metal Sites within Isostructural Metal,Organic Frameworks for Differential Recognition of Acetylene and Extraordinarily High Acetylene Storage Capacity at Room Temperature,

ANGEWANDTE CHEMIE, Issue 27 2010
Shengchang Xiang Dr.
Ungesättigte Metallzentren in isostrukturellen Metall-organischen Gerüsten vom Typ [M2(DHTP)] (M=Co2+, Mn2+, Mg2+ und Zn2+; DHTP=2,5-Dihydroxyterephthalat) zeigen eine abgestufte molekulare Erkennung von Acetylen. Die extrem starke Wechselwirkung von Co2+ mit Acetylen (siehe Struktur) macht [Co2(DHTP)] zum bislang besten Acetylenspeichermaterial mit einer Kapazität von 230,cm3,cm,3 bei 295,K und 1,atm. [source]

Differential recognition of children's cultural practices in middle primary literacy classrooms

LITERACY, Issue 3 2006
Helen Nixon
Abstract This paper argues that teachers' recognition of children's cultural practices is an important positive step in helping socio-economically disadvantaged children engage with school literacies. Based on 21 longitudinal case studies of children's literacy development over a 3-year period, the authors demonstrate that when children's knowledges and practices assembled in home and community spheres are treated as valuable material for school learning, children are more likely to invest in the work of acquiring school literacies. However, they also show that while some children benefit greatly from being allowed to draw on their knowledge of popular culture, sports and the outdoors, other children's interests may be ignored or excluded. Some differences in teachers' valuing of home and community cultures appeared to relate to gender dimensions. [source]

CD8+ T-cell responses to Theileria parva are preferentially directed to a single dominant antigen: Implications for parasite strain-specific immunity

EUROPEAN JOURNAL OF IMMUNOLOGY, Issue 9 2009
Niall D. MacHugh
Abstract Although immunodominance of CD8+ T-cell responses is a well-recognised feature of viral infections, its role in responses to more antigenically complex pathogens is less clear. In previous studies we have observed that CD8+ T-cell responses to Theileria parva exhibit different patterns of parasite strain specificity in cattle of different MHC genotypes. In the current study, we demonstrated that animals homozygous for the A10 and A18 MHC haplotypes have detectable responses to only one of 5 T. parva antigens. Over 60% of the responding T cells from the A18+ and A10+ animals recognised defined epitopes in the Tp1 and Tp2 antigens, respectively. Comparison of T-cell receptor , chain expression profiles of CD8+ T-cell lines and CD8+ T cells harvested ex vivo confirmed that the composition of the T-cell lines was representative of the in vivo memory CD8+ T-cell populations. Analysis of the Tp1 and Tp2 antigens revealed sequence polymorphism, which was reflected by differential recognition by T-cell lines. In conclusion, we have demonstrated a profound immunodominance in the CD8+ T-cell response to T. parva, which we propose is a major determinant of the parasite strain specificity of the response and hence immune protection. [source]

Preferential recognition of the phosphorylated major linear B-cell epitope of La/SSB 349,368aa by anti-La/SSB autoantibodies from patients with systemic autoimmune diseases

CLINICAL & EXPERIMENTAL IMMUNOLOGY, Issue 3 2006
A. G. Terzoglou
Summary Sera from patients with primary Sjögren Syndrome (pSS) or Systemic Lupus Erythematosus (SLE) often contain autoantibodies directed against La/SSB. The sequence 349,368aa represents the major B-cell epitope of La/SSB, also it contains, at position 366, a serine aminoacid residue which constitutes the main phosphorylation site of the protein. In this study we investigated the differential recognition of the 349,368aa epitope and its phosphorylated form by antibodies found in sera from patients with systemic autoimmune diseases. Peptides corresponding to the sequence of the unphosphorylated (pep349,368aa) and the phosphorylated form (pep349,368aaPh) of the La/SSB epitope 349,368aa, as well as to a truncated form spanning the sequence 349,364aa and lacking the phosphorylation site (pep349,364aa), were synthesized. Sera from 53 patients with pSS and SLE with anti-La/SSB specificity, 30 patients with pSS and SLE without anti-La/SSB antibodies, 25 patients with rheumatoid arthritis and 32 healthy individuals were investigated by ELISA experiments. Autoantibodies to pep349,368aaPh were detected in sera of anti-La/SSB positive patients with a higher prevalence compared to the pep349,368aa (66%versus 45%). Pep349,368aaPh inhibited the antibody binding almost completely (92%), while pep349,368aa inhibited the binding only partially (45%). Anti-La/SSB antibodies presented a higher relative avidity for the phosphorylated than the unphosphorylated peptide. Immunoadsorbent experiments using the truncated peptide pep349,364aa indicated that the flowthrough showed a selective specificity for pep349,368aaPh, while the eluted antibodies reacted with both peptide analogues of the La/SSB epitope. These data suggest that sera from pSS and SLE patients with anti-La/SSB reactivity possess autoantibodies that bind more frequently and with a higher avidity to the phosphorylated major B-cell epitope of the molecule. [source]