Lerner, Nature, vol. 299:592-596, Oct. 1982.* |
S. Duke-Cohan et al., “A Novel Form of Dipeptidylpeptidase IV Found in Human Serum,” The Journal of Biological Chemisty 270:14107-14114 (1995). |
S. Duke-Cohan et al., “Serum High Molecular Weight Dipeptidyl Peptidase IV (CD26) Is Similar to a Novel Antigen DPPT-L Released from Activated T Cells,” J. Immunology 156:1714-1721 (1996). |
Bernard et al., “Structure of the Mouse Dipeptidyl Peptidase IV (CD26) Gene,” Biochemistry 33:15204-15214 (1994). |
Buc et al., “Influence of adenosine deaminase inhibition on the phosphoinositide turnover in the initial stages of human T cell activation,” Eur. J. Immunol. 20:611-615 (1990). |
Chikuma et al., “Purification and Properties of Dipeptidyl Peptidase IV for Human Urine,” Biol. Chem. 371:325-330 (1990). |
Chobert et al., “Tissue-specific Expression of Two γ-Glutamyl Transpeptidase mRNAs with Alternative 5′ Ends Encoded by a Single Copy Gene in the Rat,” The Journal of Biological Chemistry 265:2352-2357 (1990). |
Dang et al., “Comitogenic Effect of Solid-Phase Immobilized Anti-1F7 on Human CD4 T Cell Activation Via CD3 and CD2 Pathways,” The Journal of Immunology 144:4092-4100 (1990). |
Darmoul et al., “Isolation of a cDNA probe for the human intestianl dipeptidylpeptidase IV and assignment of the gene locus DPP4 to chromosome 2,” Ann. Hum. Genet. 54:191-197 (1990). |
Fleisher, “CD26: a surface protease involved in T-cell activation,” Immunology Today 15:180-184 (1994). |
Fox et al., “Ta1, A Novel 105 KD Human T Cell Activation Antigen Defined By A Monoclonal Antibody,” The Journal of Immunology 133:1250-1256 (1984). |
Fujita et al., “Serum Glycylproline p-Nitoranilidase Activity in Rheumatoid Arthritis and System Lupus Erythematosus,” Clinica Chimica Acta 88:15-20 (1978). |
Hafler et al., “Antigen Reactive Memory T Cells are Defined by Ta12,” The Journal of Immunology 137:414-418 (1986). |
Hama et al., “Changes in form of dipeptidyl-aminopeptidase IV in urine from patients with ranal disease,” Clinica Chimica Acta 113:217-221 (1981). |
Hegen et al., The T Cell Triggering Molecule Tp103 is Associated with Dipeptidyl Aminopeptidase IV Activity, The Journal of Immunology 144:2908-2914 (1990). |
Heymann and et., “Liver Dipeptidyl Aminopeptidase IV Hydrolyzes Substance P,” FEBS Letters 91:360-364 (1978). |
Hino et al., “X-Prolyl Dipeptidyl-Aminopeptidase Activity, with X-Proline p-Nitroanilides as Substrates, in Normal and Pathological Human Sera,” Clin. Chem. 22:1256-1261 (1976). |
Hirschhorn et al., “Isozymes of Adenosine Deaminase,” Isozymes: Current Topics in Biological and Medical Research 4:131-157 (1980). |
Kameoka et al., “Direct Association of Adenosine Deaminase with T Cell Activation Antigen, CD26,” Science 261:466-469 (1993). |
Kasahara et al., “Glycylprolyl-diaminopeptidase in human leukocytes: selective occurrence in T lymphocytes and influence on the total serum enzyme activity,” Clinica Chimica Acta 139:295-302 (1984). |
Kubota et al., “Dipeptidyl peptidase IV (DP IV) activity in serum and on lymphocytes of MRL/Mp-Ipr/Ipr mice correlates with disease onset,” Clin. Exp. Immunol. 96:292-296 (1994). |
Kyouden et al., “Purification and Characterization of Dipeptidyl Peptidase IV in Rat Liver lysosomal Membranes,” J. Biochem. 111770-777 (1992). |
Matsuda et al., Serum Adenosine Deaminase 2 and Neopterin Levels Are Increased in a Majority of Hemophiliacs Irrespective of Infection with Human Immunodeficiency Virus Type I, CID:260-264 (1993). |
Morimoto et al., “1F7, A Novel Cell Surface Molecule, Involved in Helper Function of CD4 Cells,” The Journal of Immunology 143:3430-3439 (1989). |
Morrison et al., “A Marker for Neoplastic Progression of Human Melanocytes Is a Cell Surface Ectopeptidase,” J. Exp. Med. 177:1135-1143 (1993). |
Niedzwicki et al., “Plasma Adenosine Deaminase2 Is a Marker for Human Immunodeficiency Virus-1 Seroconversion,” American Journal of Hematology 37:152-155 (1991). |
Ollis et al., “The α/β hydrolase fold,” Protein Engineering 5:197-211 (1992). |
Ungerer et al., “Serum Adenosine Deaminase: Isoenzymes and Diagnostic Application,” Clin. Chem. 38:1322-1326 (1992). |
Scanlan et al., “Molecular cloninig of fibroblast acitvation protein α, a member of the serine protease family selectively ezpressed in stromal fibroblasts of epithelial cancers,” proc. Natl. Acad. Sci. USA 91:5657-5661 (1994). |
Schrader et al., “Purification of an Adenosine Deaminase Complexing Protein from Human Plasma,” The Journal of Biological Chemistry 254:11964-11968 (1979). |
Scott et al., “Quantitative and Qualitative Studies of Leukaemic Cell Dipeptidylpeptidase II and IV,” Leukemia Research 12:129-134 (1988). |
Stancikova et al., “Dipeptidyl peptidase IV in patients with systemic lupus erythematosus,” Clin. Exp. Rheumatol. 30:381-385 (1992). |
Stein et al., “Leukocyte Typing IV” (Knapp, W., Oxford University Press, Oxford, Great Britain pp. 411-415 (1989). |
Tanaka et al., “Cloning and Functional Expression of the T Cell Activation Antigen CD26,” The Journal of Immunology 149:481-486 (1992). |
Tanaka et al., “The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase Iv enzymatic activity,” Proc. Natl. Acad. Sci. USA 90:4586-4590 (1993). |
Tanaka et al., “Enhancement of antigen-induced T-cell proliferation by soluble CD26/dipeptidyl peptidase IV,” Proc. Natl. Acad. Sci. USA 91:3082-3086 (1994). |
Torimoto et al., “Biochemical Characterizatio of CD26 (Dipeptidyl Peptidase Iv): Functional Comparison of Distinct Epitopes Recognized by Various Anti-CD26 monoclonal antibodies,” vascular Immunology 29:183-192 (1992). |
Torimoto et al., “Coassociation of CD26 (dipeptidyl Peptidase IV) wtih CD45 on the Surface of Human T Lymphocytes,” The Journal of Immunology 147:2514-2517 (1991). |
Ulmer et al., “CD26 Antigen is a Surface Dipeptidyl Peptidase IV (DPPIV) as Characterized by Monoclonal Antibodies Clone TII-19-4-7 and 4EL1C7,” Scand. J. Immunol. 31:429-435 (1990). |
Vanhoof et al., “Distribution of Proline-Specific Aminopeptidases in Human Tissues and Body Fluids,” Eur. J. Clin. Chem. Clin. Biochem. 30:333-338 (1992). |
Wada et al., “Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family,” Proc. Natl. Acad. Sci. USA 89:197-201 (1992). |
Yaron et al., “Proline-Dependent Structural and Biological Properties of Peptides and Proteins,” Critical Reviews in Biochemistry and Molecular Biology 28:31-81 (1993). |