John W Kehoe

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PufX, the protein encoded by the pufX gene of Rhodobacter capsulatus and Rhodobacter sphaeroides, has been further characterized. The mature forms of these proteins contain 9 and 12 fewer amino acids, respectively, at the C-terminal end of the protein than are encoded by their pufX genes. To identify the portion of PufX responsible for inhibition of LH1(More)
Described are the chemical synthesis, isolation and characterization of each of three polypeptides whose amino acid sequences reproduce portions of the amino acid sequence of the beta-polypeptides of the core light-harvesting complex (LH1) of Rhodobacter sphaeroides or Rhodospirillum rubrum. The native beta-polypeptides of LH1 of these organisms contain 48(More)
Many cellular activities are controlled by post-translational modifications, the study of which is hampered by the lack of specific reagents due in large part to their ubiquitous and non-immunogenic nature. Although antibodies against specifically modified sequences are relatively easy to obtain, it is extremely difficult to derive reagents recognizing(More)
Chemically synthesized polypeptides have been utilized with a reconstitution assay to determine the role of specific amino acid side chains in stabilizing the core light-harvesting complex (LH1) of photosynthetic bacteria and its subunit complex. In the preceding paper [Meadows, K. A., Parkes-Loach, P. S., Kehoe, J. W., and Loach, P. A. (1998) Biochemistry(More)
CCL17 is a homeostatic chemokine associated with several human inflammatory pathologies. This makes CCL17 a potential point of intervention in inflammatory diseases. Using a Fab-pIX phage display system we were able to select antibodies that specifically bind to CCL17 and neutralize CCL17-mediated signaling. Many of the selected antibodies belong to the(More)
Tyrosylprotein sulfotransferases (TPSTs) catalyze the sulfation of tyrosine residues within secreted and membrane-bound proteins. The modification modulates protein-protein interactions in the extracellular environment. Here we use combinatorial target-guided ligand assembly to discover the first known inhibitors of human TPST-2.
Selections from phage-displayed combinatorial peptide libraries are an effective strategy for identifying peptide ligands to target proteins. Existing protocols for constructing phage-displayed libraries utilize either ligation into double-stranded phage DNA or Kunkel mutagenesis with single-stranded phagemid DNA. Although the Kunkel approach rapidly(More)
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