Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Xin Ting Fu"'
Autor:
Cheryl A. Damico, Xin Ting Fu, Henry F. McFarland, Clara M. Pelfrey, John L. Trotter, Anne H. Cross, Robert W. Karr
Publikováno v:
Journal of Neuroimmunology. 75:95-103
Mutation of the hypoxanthine-guanine phosphoribosyl transferase (HPRT) gene in a T-cell is believed to be an indication that the T-cell has been activated and has proliferated in vivo. HPRT mutant T-cell lines were generated from peripheral blood mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c20f79c17d76d81dddda08633aad416
https://doi.org/10.1016/s0165-5728(97)00007-6
https://doi.org/10.1016/s0165-5728(97)00007-6
Publikováno v:
Human Immunology. 45:111-116
To investigate the functional roles of DR alpha residues in T-cell recognition, 20 mutants of the DR alpha chain were constructed by site-directed mutagenesis. These DR alpha mutants were expressed with WT DR(beta 1*0701) on mouse L cells and used as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::746bf06de0b5bf9deb18e7eec6cf81d2
https://doi.org/10.1016/0198-8859(95)00155-7
https://doi.org/10.1016/0198-8859(95)00155-7
Autor:
Xin-Ting Fu, R W Karr
Publikováno v:
Human Immunology. 39:253-260
The structure-function relationships of the HLA-DR alpha chain have been analyzed by identifying DR alpha residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DR al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22abc864cf9bd2033c296200c77a7df5
https://doi.org/10.1016/0198-8859(94)90268-2
https://doi.org/10.1016/0198-8859(94)90268-2
Publikováno v:
Human immunology. 43(4)
Many residues involved in polymorphic antibody-binding epitopes on class II molecules are located on the alpha-helix of DR beta chains. Although they have received less attention, residues in the peptide-binding groove and second domain of the DR bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f6ed9d31a60684d7c6e445c4dc3a9e4
https://pubmed.ncbi.nlm.nih.gov/7499171
https://pubmed.ncbi.nlm.nih.gov/7499171
Autor:
Craig Swearingen, Francesco Sinigaglia, Robert W. Karr, Alessandro Sette, Neena L. Summers, Xin-Ting Fu, Benjamin D. Schwartz, Susan L. Woulfe, Chris P. Bono
Publikováno v:
The Journal of Experimental Medicine
To investigate the functional roles of individual HLA-DR residues in T cell recognition, transfectants expressing wild-type or mutant DR(alpha,beta 1*0401) molecules with single amino acid substitutions at 14 polymorphic positions of the DR beta 1*04
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59813eef1e4f9f30bcdd0888b7a0757d
https://pubmed.ncbi.nlm.nih.gov/7869051
https://pubmed.ncbi.nlm.nih.gov/7869051
Autor:
Yanourishka Y. R. Jansen, Krista E. van Meijgaarden, Annemieke Geluk, René R. P. de Vries, Xin-Ting Fu, Robert W. Karr, Tom H. M. Ottenhoff
Publikováno v:
European journal of immunology. 24(12)
Previously, we have proposed that the beta 1 residues 9-13, 26, 28 and 86 in HLA-DR17, the most common subtype of DR3, might be critical for the binding of an immunodominant, mycobacterial epitope (peptide 3-13 of the 65-kDa heat shock protein). In o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::275bffffde95b142f5ba65828dd731c3
https://pubmed.ncbi.nlm.nih.gov/7805754
https://pubmed.ncbi.nlm.nih.gov/7805754
Publikováno v:
Human immunology. 40(1)
The specificities for seven mAbs to HLA-DR4 were determined initially using homozygous BCLs and L-cell transfectants expressing wild-type DR molecules. Three antibodies (NFLD.D1, NFLD.M1, and NFLD.D7) bound all DR4 molecules, but only one was specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::890b87d77372038f8e0818dfc9397dda
https://pubmed.ncbi.nlm.nih.gov/7519185
https://pubmed.ncbi.nlm.nih.gov/7519185
Autor:
G. Lombardi, Xin Ting Fu, Enza Piccolella, R W Karr, Loretta Tuosto, Robert I. Lechler, Richard R. Olson, E. Cundari
The contributions of individual amino acids in the polymorphic beta chain and the conserved alpha chain of HLA-DR1 to influenza HA-specific DR1-restricted and anti-DR1 allospecific T-cell recognition were analyzed. The genes encoding HLA-DR1 were sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbf5712a6ff1a2b158124e290ab2a245
http://hdl.handle.net/11573/129962
http://hdl.handle.net/11573/129962
Publikováno v:
Human immunology. 37(1)
The purpose of this study was to identify polymorphic residues in HLA-DR beta chains that are involved in the epitopes recognized by DRw52-like mAbs. Flow cytometric analysis of antibody binding to mouse fibroblast transfectants expressing wild-type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0725b189a14e9372b0b97277e6fe0755
https://pubmed.ncbi.nlm.nih.gov/7690741
https://pubmed.ncbi.nlm.nih.gov/7690741
Autor:
Judith P. Johnson, Rebecca Watts, Cheryl Benson, C. Alber, Robert W. Knowles, Wei-yuan Yu, Xin-ting Fu, R W Karr, Hellmuth Nordwig
Publikováno v:
Human immunology. 33(1)
Based on previous studies it was predicted that amino acids 4 or 25 of the DR4 beta 1 and DR7 beta 1 chains are involved in polymorphic antibody binding epitopes on DR4 or DR7 molecules. These predictions were tested by analyzing monoclonal antibody
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6afe636ac9d744b2947a5cf2bf9f0f65
https://pubmed.ncbi.nlm.nih.gov/1372304
https://pubmed.ncbi.nlm.nih.gov/1372304