Výsledky vyhledávání - "Aideen C. M. Young"

The Identification of Hereditary and Environmental Determinants of Frailty in a Cohort of UK Twins

Autor: Karen Glaser, Tim D. Spector, Aideen C. M. Young, Claire J. Steves

Publikováno v: Twin Research and Human Genetics. 19:600-609

Our study examines the contribution of genetic and environmental factors (both shared and unique) to frailty, measured using the Rockwood Frailty Index (FI) in a sample of twins from the St Thomas’ UK Adult Twin Registry. The FI was based on 39 ite

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bf61112adf63530e723234c6d54c787
https://doi.org/10.1017/thg.2016.72

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Binding of Longer Peptides to the H-2Kb Heterodimer Is Restricted to Peptides Extended at Their C Terminus: Refinement of the Inherent MHC Class I Peptide Binding Criteria

Autor: Heidi Hörig, Aideen C. M. Young, Nicholas J. Papadopoulos, Teresa P. DiLorenzo, Stanley G. Nathenson

Publikováno v: The Journal of Immunology. 163:4434-4441

MHC class I molecules usually bind short peptides of 8–10 amino acids, and binding is dependent on allele-specific anchor residues. However, in a number of cellular systems, class I molecules have been found containing peptides longer than the cano

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::14fa13a7192ca73743514fdb577b2f4c
https://doi.org/10.4049/jimmunol.163.8.4434

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Point mutations in the β chain CDR3 can alter the T cell receptor recognition pattern on an MHC class I\peptide complex over a broad interface area

Autor: Nicolas J. Papadopoulos, Heidi Hörig, Cole T. Thomson, Earl C. Goyarts, Alexis M. Kalergis, Hsiu-Ching Chang, Sebastian Joyce, Aideen C. M. Young, Zsuzsa Vegh, Stanley G. Nathenson

Publikováno v: Molecular Immunology. 35:593-607

To study how the T cell receptor interacts with its cognate ligand, the MHC/peptide complex, we used site directed mutagenesis to generate single point mutants that alter amino acids in the CDR3beta loop of a H-2Kb restricted TCR (N30.7) specific for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c1232be53f056d4baeba6908c5b08d1
https://doi.org/10.1016/s0161-5890(98)00056-x

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The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neoformans and its complex with a peptide from a phage display library: implications for the identification of peptide mimotopes

Autor: Philippe Valadon, Aideen C. M. Young, Matthew D. Scharff, Arturo Casadevall, James C. Sacchettini

Publikováno v: Journal of Molecular Biology. 274:622-634

The three-dimensional structure of 2H1, a protective monoclonal antibody to Cryptococcus neoformans, has been solved at 2.4 A resolution, in both its unbound form and in complex with the 12 amino acid residue peptide PA1 (GLQYTPSWMLVG). PA1 was previ

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https://doi.org/10.1006/jmbi.1997.1407

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Molecular mapping of the 8.12 sle-associated idiotype specificity at the single amino acid level

Autor: Aideen C. M. Young, Macarena Irigoyen, James C. Sacchettini, Czeslawa Kowal, Betty Diamond

Publikováno v: Molecular Immunology. 33:1255-1265

The 8.12 idiotype is expressed in elevated titer in the serum of patients with systemic lupus erythematosus and is a marker for a subpopulation of anti-DNA antibodies that possess a V(lambda)II encoded light chain. This study utilized a eukaryotic ex

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https://doi.org/10.1016/s0161-5890(96)00093-4

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Presentation by a major histocompatibility complex class I molecule of nucleoprotein peptide expressed in two different genes of an influenza virus transfectant

Autor: Peter Palese, Thomas M. Moran, Aideen C. M. Young, H Isobe, Constantin A. Bona, S. Nathenson, Shengqiang Li

Publikováno v: The Journal of Experimental Medicine

Major histocompatibility (MHC) class I glycoproteins are specialized to present to CD8+ T cells, peptides that originate from proteins synthesized within the cytoplasm. Conventional killed vaccines are unable to get into the cell cytoplasm and theref

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https://doi.org/10.1084/jem.181.1.203

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The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection

Autor: Aideen C. M. Young, Weiguo Zhang, James C. Sacchettini, Stanley G. Nathenson

Publikováno v: Cell. 76:39-50

Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interacti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8770dce626212b41caf492a2f26bc50d
https://doi.org/10.1016/0092-8674(94)90171-6

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Comparison of radiation-induced decay and structure refinement from X-ray data collected from lysozyme crystals at low and ambient temperatures

Autor: R. F. Tilton, Colin Nave, J. C. Dewan, Aideen C. M. Young

Publikováno v: Journal of Applied Crystallography. 26:309-319

Two crystals of monoclinic hen egg-white lysozyme were irradiated in a monochromatic synchrotron X-ray beam (λ = 1.488 A), the first as a rapidly frozen crystal mounted at the end of a glass fiber at low temperature (120 K) and the second mounted in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::48032a4e902b3c86a7a4cc1ce211a55c
https://doi.org/10.1107/s0021889892010070

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High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid: protein interactions

Autor: Jacques H. Veerkamp, Arno Kromminga, Aideen C. M. Young, James C. Sacchettini, Giovanna Scapin, Jeffrey I. Gordon

Publikováno v: Molecular and Cellular Biochemistry. 123:3-13

The structure of E. coli-derived rat intestinal fatty acid-binding protein has recently been refined to 1.2 A without bound fatty acid and to 2.0 A and 1.75 A with bound hexadecanoate (palmitate) and 9Z-octadecenoate (oleate), respectively. The struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62726f9913c4718f45b4f8199d6efa48
https://doi.org/10.1007/bf01076469

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Structure of an adenine tetrafluoroborate salt

Autor: A. J. Edwards, Aideen C. M. Young, J. C. Dewan

Publikováno v: Acta Crystallographica Section C Crystal Structure Communications. 47:580-584

C 5 H 5 N 5 •C 5 H 6 N 5 + •BF 4 − •2H 2 O cristallise dans P2 1 /m avec a=5,358, b=19,468, c=7,905 A, β=104,75°, Z=2; affinement jusqu'a R=0,062. Les molecules d'adenine et adeninium sont desordonnees sur un site cristallographique et dans

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https://doi.org/10.1107/s0108270190005418

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