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Citation: J. Yague et al., Major histocompatibility complex class I molecules bind natural peptide ligands lacking the amino-terminal binding residue in vivo, J BIOL CHEM, 276(47), 2001, pp. 43699-43707
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Citation: S. Ogueta et al., Identification of phosphorylation sites in proteins by nanospray quadrupole ion trap mass spectrometry, J MASS SPEC, 35(4), 2000, pp. 556-565
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Citation: S. Ramon-maiques et al., The 1.5 angstrom resolution crystal structure of the carbamate kinase-likecarbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability incarbamate kinases, J MOL BIOL, 299(2), 2000, pp. 463-476
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Citation: A. Marina et al., High-sensitivity analysis and sequencing of peptides and proteins by quadrupole ion trap mass spectrometry, J MASS SPEC, 34(1), 1999, pp. 17-27
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Citation: F. Gil et al., N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms, ACT CRYST D, 55, 1999, pp. 1350-1352
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Mate, MJ
Ortiz-Lombardia, M
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Citation: Mj. Mate et al., Crystallization and preliminary structural results of catalase from human erythrocytes, ACT CRYST D, 55, 1999, pp. 1066-1068
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Citation: M. Uriarte et al., The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase, J BIOL CHEM, 274(23), 1999, pp. 16295-16303
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Citation: Ma. Garcia et al., Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation, FEBS LETTER, 444(1), 1999, pp. 27-31
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Citation: J. Bueso et al., Photoaffinity labeling with the activator IMP and site-directed mutagenesis of histidine 995 of carbamoyl phosphate synthetase from Escherichia coli demonstrate that the binding site for IMP overlaps with that for the inhibitor UMP, BIOCHEM, 38(13), 1999, pp. 3910-3917
Authors:
Yague, J
Ramos, M
Vazquez, J
Marina, A
Albar, JP
de Castro, JAL
Citation: J. Yague et al., The South Amerindian allotype HLA-B3909 has the largest known similarity in peptide specificity and common natural ligands with HLA-B27, TISSUE ANTI, 53(3), 1999, pp. 227-236