Search Results - (Author, Cooperation:R. Kiley)
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1Latest Papers from Table of Contents or Articles in PressJ. M. Berg ; N. Bhalla ; P. E. Bourne ; M. Chalfie ; D. G. Drubin ; J. S. Fraser ; C. W. Greider ; M. Hendricks ; C. Jones ; R. Kiley ; S. King ; M. W. Kirschner ; H. M. Krumholz ; R. Lehmann ; M. Leptin ; B. Pulverer ; B. Rosenzweig ; J. E. Spiro ; M. Stebbins ; C. Strasser ; S. Swaminathan ; P. Turner ; R. D. Vale ; K. VijayRaghavan ; C. Wolberger
American Association for the Advancement of Science (AAAS)
Published 2016Staff ViewPublication Date: 2016-05-21Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
2Articles: DFG German National LicensesPrilliman, Kiley R. ; Lindsey, Mark ; Jackson, Kenneth W. ; Cole, Jeffrey ; Bonner, Ron ; Hildebrand, W. H.
Springer
Published 1998Staff ViewISSN: 1432-1211Keywords: Key words HLA-Bantigens ; Ligands ; Antigen presentationSource: Springer Online Journal Archives 1860-2000Topics: BiologyMedicineNotes: Abstract Analysis of peptides derived from HLA class I molecules indicates that thousands of unique peptides are bound by a single molecular type, and sequence examination of the pooled constituents yields a motif which collectively defines the peptides bound by a given class I molecule. Motifs resulting from pooled sequencing are then used to infer whether particular viral and tumor protein fragments might serve as class I-presented peptide therapeutics. Still undetermined from a pooled motif is the breadth or range of peptides in the population which are brought together to form the pooled motif, and it is therefore not yet known how representative of the population a pooled motif is. By employing hollow fiber bioreactors for large-scale production of HLA class I molecules, sufficient peptides are produced to investigate individual subsets of peptides comprising a motif. Edman sequencing and mass spectrometric analysis of peptides eluted from HLA-B*1501 reveal that many peptide sequences fail to align with either the N- or C-terminal anchors predicted for the B*1501 peptide motif through whole pool sequencing. These analyses further reveal auxiliary anchors not previously detected and peptides significantly larger and smaller than the predicted nonamer, ranging from 6 to 12 amino acids in length. These results demonstrate that constituents of the B*1501 peptide pool vary markedly in comparison with one another and therefore in comparison with previously established B*1501 motifs, and such complexity indicates that many of the peptide ligands presented to CTL cannot be predicted using class I consensus motifs as search criteria.Type of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesPrilliman, Kiley R. ; Lindsey, Mark ; Wang, Jihua ; Jackson, Kenneth W. ; Hildebrand, W. H.
Springer
Published 1999Staff ViewISSN: 1432-1211Keywords: Key words B*1503 ; HLA class I ; Peptide binding specificity ; Allele-specific motifSource: Springer Online Journal Archives 1860-2000Topics: BiologyMedicineType of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesTozzi, R. ; Hernanz-Schulman, M. ; Kiley, R. ; Genieser, N. ; Ambrosino, M. ; Pinto, R. ; Doyle, E.
Springer
Published 1989Staff ViewISSN: 1432-1998Source: Springer Online Journal Archives 1860-2000Topics: MedicineType of Medium: Electronic ResourceURL: