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Volumn 304, Issue 1, 2003, Pages 73-77

The 3D structure of rat DPPIV/CD26 as obtained by cryo-TEM and single particle analysis

Author keywords

3D reconstruction; CD26; Cryo TEM; Dipeptidyl peptidase IV; Single particle analysis

Indexed keywords

DIMER; DIPEPTIDYL PEPTIDASE IV; PEPTIDASE; SERINE PEPTIDASE; UNCLASSIFIED DRUG;

EID: 0345700783     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00539-4     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36) amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein R., Gallwitz B., Schmidt W.E. Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36) amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214:1993;829-835.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 3
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T-cell immune response
    • Morimoto C., Schlossman S.F. The structure and function of CD26 in the T-cell immune response. Immunol. Rev. 161:1998;55-70.
    • (1998) Immunol. Rev. , vol.161 , pp. 55-70
    • Morimoto, C.1    Schlossman, S.F.2
  • 4
    • 0031932784 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV/CD26 on T cells: Analysis of an alternative T-cell activation pathway
    • von Bonin A., Huhn J., Fleischer B. Dipeptidyl-peptidase IV/CD26 on T cells: analysis of an alternative T-cell activation pathway. Immunol. Rev. 161:1998;43-53.
    • (1998) Immunol. Rev. , vol.161 , pp. 43-53
    • Von Bonin, A.1    Huhn, J.2    Fleischer, B.3
  • 5
    • 0002190040 scopus 로고
    • Functional aspects of the three extracellular domains of dipeptidyl peptidase IV: Characterization of glycosylation events, of the collagen-binding site and endopeptidase activity
    • B. Fleischer. Texas: R.G. Landes Company
    • Reutter W., Baum O., Loester K., Fan H., Bork J.P., Bernt K., Hanski C., Tauber R. Functional aspects of the three extracellular domains of dipeptidyl peptidase IV: characterization of glycosylation events, of the collagen-binding site and endopeptidase activity. Fleischer B. Dipeptidyl Peptidase IV (CD26) in Metabolism and the Immune Response. 1995;55-79 R.G. Landes Company, Texas.
    • (1995) Dipeptidyl Peptidase IV (CD26) in Metabolism and the Immune Response , pp. 55-79
    • Reutter, W.1    Baum, O.2    Loester, K.3    Fan, H.4    Bork, J.P.5    Bernt, K.6    Hanski, C.7    Tauber, R.8
  • 6
    • 0026787020 scopus 로고
    • CDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases
    • Marguet D., Bernard A.M., Vivier I., Darmoul D., Naquet P., Pierres M. cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases. J. Biol. Chem. 267:1992;2200-2208.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2200-2208
    • Marguet, D.1    Bernard, A.M.2    Vivier, I.3    Darmoul, D.4    Naquet, P.5    Pierres, M.6
  • 7
    • 0026665626 scopus 로고
    • Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface
    • Misumi Y., Hayashi Y., Arakawa F., Ikehara Y. Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim. Biophys. Acta. 1131:1992;333-336.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 333-336
    • Misumi, Y.1    Hayashi, Y.2    Arakawa, F.3    Ikehara, Y.4
  • 8
    • 0025194038 scopus 로고
    • Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV
    • Hong W.J., Doyle D. Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV. J. Cell. Biol. 111:1990;323-328.
    • (1990) J. Cell. Biol. , vol.111 , pp. 323-328
    • Hong, W.J.1    Doyle, D.2
  • 9
    • 0030916841 scopus 로고    scopus 로고
    • Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity, and protein folding
    • Fan H., Meng W., Kilian C., Grams S., Reutter W. Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity, and protein folding. Eur. J. Biochem. 246:1997;243-251.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 243-251
    • Fan, H.1    Meng, W.2    Kilian, C.3    Grams, S.4    Reutter, W.5
  • 10
    • 0002139542 scopus 로고    scopus 로고
    • DPPIV/CD26: Structural and biological characteristics of asparagine and cysteine mutants
    • S. Mizutani. Amsterdam: Elsevier science
    • Fan H., Dobers J., Reutter W. DPPIV/CD26: structural and biological characteristics of asparagine and cysteine mutants. Mizutani S. Cell-surface Aminopeptidases: Basic and Clinical Aspects. 2001;303-316 Elsevier science, Amsterdam.
    • (2001) Cell-surface Aminopeptidases: Basic and Clinical Aspects , pp. 303-316
    • Fan, H.1    Dobers, J.2    Reutter, W.3
  • 11
    • 0033895254 scopus 로고    scopus 로고
    • Roles of cysteines in rat dipeptidyl peptidase IV/CD26 in processing and proteolytic activity
    • Dobers J., Grams S., Reutter W., Fan H. Roles of cysteines in rat dipeptidyl peptidase IV/CD26 in processing and proteolytic activity. Eur. J. Biochem. 267:2000;5093-5100.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5093-5100
    • Dobers, J.1    Grams, S.2    Reutter, W.3    Fan, H.4
  • 12
    • 0026579515 scopus 로고
    • Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis
    • Ogata S., Misumi Y., Tsuji E., Takami N., Oda K., Ikehara Y. Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis. Biochemistry. 31:1992;2582-2587.
    • (1992) Biochemistry , vol.31 , pp. 2582-2587
    • Ogata, S.1    Misumi, Y.2    Tsuji, E.3    Takami, N.4    Oda, K.5    Ikehara, Y.6
  • 13
    • 0027236545 scopus 로고
    • Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases
    • David F., Bernard A.M., Pierres M., Marguet D. Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases. J. Biol. Chem. 268:1993;17247-17252.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17247-17252
    • David, F.1    Bernard, A.M.2    Pierres, M.3    Marguet, D.4
  • 15
    • 0037738967 scopus 로고    scopus 로고
    • Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
    • Böttcher C., Ludwig K., Herrmann A., van Heel M., Stark H. Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy. FEBS Lett. 463:1999;255-259.
    • (1999) FEBS Lett. , vol.463 , pp. 255-259
    • Böttcher, C.1    Ludwig, K.2    Herrmann, A.3    Van Heel, M.4    Stark, H.5
  • 16
    • 0036427905 scopus 로고    scopus 로고
    • Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles
    • De Carlo S., El-Bez C., Alvarez-Rua C., Borge J., Dubochet J. Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. J. Struct. Biol. 138:2002;216-226.
    • (2002) J. Struct. Biol. , vol.138 , pp. 216-226
    • De Carlo, S.1    El-Bez, C.2    Alvarez-Rua, C.3    Borge, J.4    Dubochet, J.5
  • 17
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • Van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy. 21:1987;111-123.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-123
    • Van Heel, M.1
  • 18
    • 0022734418 scopus 로고
    • Resolution criteria for three-dimensional reconstructions
    • Van Heel M., Harauz G. Resolution criteria for three-dimensional reconstructions. Optik. 73:1986;119-122.
    • (1986) Optik , vol.73 , pp. 119-122
    • Van Heel, M.1    Harauz, G.2
  • 19
    • 0035783173 scopus 로고    scopus 로고
    • Using situs for flexible and rigid-body fitting of multiresolution single-molecule data
    • Wriggers W., Birmanns S. Using situs for flexible and rigid-body fitting of multiresolution single-molecule data. J. Struct. Biol. 133:2001;193-202.
    • (2001) J. Struct. Biol. , vol.133 , pp. 193-202
    • Wriggers, W.1    Birmanns, S.2
  • 20
    • 0033852128 scopus 로고    scopus 로고
    • Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides
    • Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I. Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides. Eur. J. Biochem. 267:2000;5608-5613.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5608-5613
    • Durinx, C.1    Lambeir, A.M.2    Bosmans, E.3    Falmagne, J.B.4    Berghmans, R.5    Haemers, A.6    Scharpe, S.7    De Meester, I.8
  • 21
    • 0035839639 scopus 로고    scopus 로고
    • Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family
    • Lambeir A.M., Proost P., Durinx C., Bal G., Senten K., Augustyns K., Scharpe S., Van Damme J., De Meester I. Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J. Biol. Chem. 276:2001;29839-29845.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29839-29845
    • Lambeir, A.M.1    Proost, P.2    Durinx, C.3    Bal, G.4    Senten, K.5    Augustyns, K.6    Scharpe, S.7    Van Damme, J.8    De Meester, I.9
  • 22
    • 0034471660 scopus 로고    scopus 로고
    • Development of a tertiary-structure model of the C-terminal domain of DPP IV
    • Brandt W. Development of a tertiary-structure model of the C-terminal domain of DPP IV. Adv. Exp. Med. Biol. 477:2000;97-101.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 97-101
    • Brandt, W.1
  • 23
    • 0035723325 scopus 로고    scopus 로고
    • CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes
    • Gorrell M.D., Gysbers V., McCaughan G.W. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand. J. Immunol. 54:2001;249-264.
    • (2001) Scand. J. Immunol. , vol.54 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    McCaughan, G.W.3
  • 24
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual beta-propeller domain regulates proteolysis
    • Fulop V., Bocskei Z., Polgar L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell. 94:1998;161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.