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Volumn 20, Issue 12, 2012, Pages 2161-2173

Crystal structure of the human ecto-5′-nucleotidase (CD73): Insights into the regulation of purinergic signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ECTO 5' NUCLEOTIDASE; FLAVONOID; PURINERGIC RECEPTOR;

EID: 84870480855     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.10.001     Document Type: Article
Times cited : (158)

References (63)
  • 4
    • 0029133140 scopus 로고
    • Distribution of 5′-nucleotidase in the developing mouse retina
    • N. Braun, P. Brendel, and H. Zimmermann Distribution of 5′-nucleotidase in the developing mouse retina Brain Res. Dev. Brain Res. 88 1995 79 86
    • (1995) Brain Res. Dev. Brain Res. , vol.88 , pp. 79-86
    • Braun, N.1    Brendel, P.2    Zimmermann, H.3
  • 5
    • 0001936036 scopus 로고
    • Direct phase determination by entropy maximization and likelihood ranking: Status report and perspectives
    • G. Bricogne Direct phase determination by entropy maximization and likelihood ranking: status report and perspectives Acta Crystallogr. D Biol. Crystallogr. 49 1993 37 60
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 37-60
    • Bricogne, G.1
  • 6
    • 49449100465 scopus 로고    scopus 로고
    • Selective nucleoside triphosphate diphosphohydrolase-2 (NTPDase2) inhibitors: Nucleotide mimetics derived from uridine-5′-carboxamide
    • A. Brunschweiger, J. Iqbal, F. Umbach, A.B. Scheiff, M.N. Munkonda, J. Sévigny, A.F. Knowles, and C.E. Müller Selective nucleoside triphosphate diphosphohydrolase-2 (NTPDase2) inhibitors: nucleotide mimetics derived from uridine-5′-carboxamide J. Med. Chem. 51 2008 4518 4528
    • (2008) J. Med. Chem. , vol.51 , pp. 4518-4528
    • Brunschweiger, A.1    Iqbal, J.2    Umbach, F.3    Scheiff, A.B.4    Munkonda, M.N.5    Sévigny, J.6    Knowles, A.F.7    Müller, C.E.8
  • 11
    • 84864881916 scopus 로고    scopus 로고
    • Selective activation of adenosine A2A receptors on immune cells by a CD73-dependent prodrug suppresses joint inflammation in experimental rheumatoid arthritis
    • 146ra108
    • U. Flögel, S. Burghoff, P.L. van Lent, S. Temme, L. Galbarz, Z. Ding, A. El-Tayeb, S. Huels, F. Bönner, and N. Borg Selective activation of adenosine A2A receptors on immune cells by a CD73-dependent prodrug suppresses joint inflammation in experimental rheumatoid arthritis Sci. Transl. Med. 4 2012 146ra108
    • (2012) Sci. Transl. Med. , vol.4
    • Flögel, U.1    Burghoff, S.2    Van Lent, P.L.3    Temme, S.4    Galbarz, L.5    Ding, Z.6    El-Tayeb, A.7    Huels, S.8    Bönner, F.9    Borg, N.10
  • 12
    • 84055223632 scopus 로고    scopus 로고
    • The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism
    • S. Garavaglia, S. Bruzzone, C. Cassani, L. Canella, G. Allegrone, L. Sturla, E. Mannino, E. Millo, A. De Flora, and M. Rizzi The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism Biochem. J. 441 2012 131 141
    • (2012) Biochem. J. , vol.441 , pp. 131-141
    • Garavaglia, S.1    Bruzzone, S.2    Cassani, C.3    Canella, L.4    Allegrone, G.5    Sturla, L.6    Mannino, E.7    Millo, E.8    De Flora, A.9    Rizzi, M.10
  • 13
    • 0035889558 scopus 로고    scopus 로고
    • Identification of inactive ecto-5′-nucleotidase in normal mouse muscle and its increased activity in dystrophic Lama2(dy) mice
    • M.S. García-Ayllón, F.J. Campoy, C.J. Vidal, and E. Muñoz-Delgado Identification of inactive ecto-5′-nucleotidase in normal mouse muscle and its increased activity in dystrophic Lama2(dy) mice J. Neurosci. Res. 66 2001 656 665
    • (2001) J. Neurosci. Res. , vol.66 , pp. 656-665
    • García-Ayllón, M.S.1    Campoy, F.J.2    Vidal, C.J.3    Muñoz-Delgado, E.4
  • 14
    • 0023389627 scopus 로고
    • Purification, characterization and cellular localization of 5′-nucleotidase from Torpedo electric organ
    • E.J. Grondal, and H. Zimmermann Purification, characterization and cellular localization of 5′-nucleotidase from Torpedo electric organ Biochem. J. 245 1987 805 810
    • (1987) Biochem. J. , vol.245 , pp. 805-810
    • Grondal, E.J.1    Zimmermann, H.2
  • 15
    • 37049009485 scopus 로고    scopus 로고
    • Capillary electrophoresis-based nanoscale assays for monitoring ecto-5′-nucleotidase activity and inhibition in preparations of recombinant enzyme and melanoma cell membranes
    • J. Iqbal, D. Jirovsky, S.Y. Lee, H. Zimmermann, and C.E. Müller Capillary electrophoresis-based nanoscale assays for monitoring ecto-5′-nucleotidase activity and inhibition in preparations of recombinant enzyme and melanoma cell membranes Anal. Biochem. 373 2008 129 140
    • (2008) Anal. Biochem. , vol.373 , pp. 129-140
    • Iqbal, J.1    Jirovsky, D.2    Lee, S.Y.3    Zimmermann, H.4    Müller, C.E.5
  • 16
    • 77950231071 scopus 로고    scopus 로고
    • CD73 on tumor cells impairs antitumor T-cell responses: A novel mechanism of tumor-induced immune suppression
    • D. Jin, J. Fan, L. Wang, L.F. Thompson, A. Liu, B.J. Daniel, T. Shin, T.J. Curiel, and B. Zhang CD73 on tumor cells impairs antitumor T-cell responses: a novel mechanism of tumor-induced immune suppression Cancer Res. 70 2010 2245 2255
    • (2010) Cancer Res. , vol.70 , pp. 2245-2255
    • Jin, D.1    Fan, J.2    Wang, L.3    Thompson, L.F.4    Liu, A.5    Daniel, B.J.6    Shin, T.7    Curiel, T.J.8    Zhang, B.9
  • 18
    • 0033056159 scopus 로고    scopus 로고
    • In vitro effects of selected flavonoids on the 5′-nucleotidase activity
    • M. Kavutcu, and M.F. Melzig In vitro effects of selected flavonoids on the 5′-nucleotidase activity Pharmazie 54 1999 457 459
    • (1999) Pharmazie , vol.54 , pp. 457-459
    • Kavutcu, M.1    Melzig, M.F.2
  • 19
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • G.J. Kleywegt, and A.T. Brünger Checking your imagination: applications of the free R value Structure 4 1996 897 904
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 20
    • 0032915156 scopus 로고    scopus 로고
    • X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site
    • T. Knöfel, and N. Sträter X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site Nat. Struct. Biol. 6 1999 448 453
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 448-453
    • Knöfel, T.1    Sträter, N.2
  • 21
    • 0035946952 scopus 로고    scopus 로고
    • E. coli 5′-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion
    • T. Knöfel, and N. Sträter E. coli 5′-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion J. Mol. Biol. 309 2001 255 266
    • (2001) J. Mol. Biol. , vol.309 , pp. 255-266
    • Knöfel, T.1    Sträter, N.2
  • 22
    • 0035946945 scopus 로고    scopus 로고
    • Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures
    • T. Knöfel, and N. Sträter Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures J. Mol. Biol. 309 2001 239 254
    • (2001) J. Mol. Biol. , vol.309 , pp. 239-254
    • Knöfel, T.1    Sträter, N.2
  • 23
    • 0028268627 scopus 로고
    • Conserved sequence pattern in a wide variety of phosphoesterases
    • E.V. Koonin Conserved sequence pattern in a wide variety of phosphoesterases Protein Sci. 3 1994 356 358
    • (1994) Protein Sci. , vol.3 , pp. 356-358
    • Koonin, E.V.1
  • 24
    • 79953734276 scopus 로고    scopus 로고
    • Macromolecular complexes in crystals and solutions
    • E. Krissinel Macromolecular complexes in crystals and solutions Acta Crystallogr. D Biol. Crystallogr. 67 2011 376 385
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 376-385
    • Krissinel, E.1
  • 25
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • G. Langer, S.X. Cohen, V.S. Lamzin, and A. Perrakis Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3 2008 1171 1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 27
    • 0037263939 scopus 로고    scopus 로고
    • Structural quality assurance
    • R.A. Laskowski Structural quality assurance Methods Biochem. Anal. 44 2003 273 303
    • (2003) Methods Biochem. Anal. , vol.44 , pp. 273-303
    • Laskowski, R.A.1
  • 28
    • 33746336981 scopus 로고    scopus 로고
    • Effect of hypoxia/reoxygenation on CD73 (ecto-5′-nucleotidase) in mouse microvessel endothelial cell lines
    • X. Li, T. Zhou, X. Zhi, F. Zhao, L. Yin, and P. Zhou Effect of hypoxia/reoxygenation on CD73 (ecto-5′-nucleotidase) in mouse microvessel endothelial cell lines Microvasc. Res. 72 2006 48 53
    • (2006) Microvasc. Res. , vol.72 , pp. 48-53
    • Li, X.1    Zhou, T.2    Zhi, X.3    Zhao, F.4    Yin, L.5    Zhou, P.6
  • 31
    • 0031718144 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase from a human colon adenocarcinoma cell line. Correlation between enzyme activity and levels in intact cells
    • J.M. Navarro, N. Olmo, J. Turnay, M.T. López-Conejo, and M.A. Lizarbe Ecto-5′-nucleotidase from a human colon adenocarcinoma cell line. Correlation between enzyme activity and levels in intact cells Mol. Cell. Biochem. 187 1998 121 131
    • (1998) Mol. Cell. Biochem. , vol.187 , pp. 121-131
    • Navarro, J.M.1    Olmo, N.2    Turnay, J.3    López-Conejo, M.T.4    Lizarbe, M.A.5
  • 32
    • 1642444080 scopus 로고    scopus 로고
    • IFN-alpha induced adenosine production on the endothelium: A mechanism mediated by CD73 (ecto-5′-nucleotidase) up-regulation
    • J. Niemelä, T. Henttinen, G.G. Yegutkin, L. Airas, A.M. Kujari, P. Rajala, and S. Jalkanen IFN-alpha induced adenosine production on the endothelium: a mechanism mediated by CD73 (ecto-5′-nucleotidase) up-regulation J. Immunol. 172 2004 1646 1653
    • (2004) J. Immunol. , vol.172 , pp. 1646-1653
    • Niemelä, J.1    Henttinen, T.2    Yegutkin, G.G.3    Airas, L.4    Kujari, A.M.5    Rajala, P.6    Jalkanen, S.7
  • 33
    • 77955508266 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase (CD73) attenuates allograft airway rejection through adenosine 2A receptor stimulation
    • T. Ohtsuka, P.S. Changelian, D. Bouïs, K. Noon, H. Harada, V.N. Lama, and D.J. Pinsky Ecto-5′-nucleotidase (CD73) attenuates allograft airway rejection through adenosine 2A receptor stimulation J. Immunol. 185 2010 1321 1329
    • (2010) J. Immunol. , vol.185 , pp. 1321-1329
    • Ohtsuka, T.1    Changelian, P.S.2    Bouïs, D.3    Noon, K.4    Harada, H.5    Lama, V.N.6    Pinsky, D.J.7
  • 36
    • 33750472374 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase (eN, CD73) is coexpressed with metastasis promoting antigens in human melanoma cells
    • R. Sadej, J. Spychala, and A.C. Skladanowski Ecto-5′-nucleotidase (eN, CD73) is coexpressed with metastasis promoting antigens in human melanoma cells Nucleosides Nucleotides Nucleic Acids 25 2006 1119 1123
    • (2006) Nucleosides Nucleotides Nucleic Acids , vol.25 , pp. 1119-1123
    • Sadej, R.1    Spychala, J.2    Skladanowski, A.C.3
  • 37
    • 84870539986 scopus 로고    scopus 로고
    • Host CD73 impairs anti-tumor immunity
    • M. Salmi, and S. Jalkanen Host CD73 impairs anti-tumor immunity OncoImmunology 1 2012 247 248
    • (2012) OncoImmunology , vol.1 , pp. 247-248
    • Salmi, M.1    Jalkanen, S.2
  • 38
    • 3042670311 scopus 로고    scopus 로고
    • Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges
    • R. Schultz-Heienbrok, T. Maier, and N. Sträter Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges Protein Sci. 13 2004 1811 1822
    • (2004) Protein Sci. , vol.13 , pp. 1811-1822
    • Schultz-Heienbrok, R.1    Maier, T.2    Sträter, N.3
  • 39
    • 14044270165 scopus 로고    scopus 로고
    • A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5′-nucleotidase
    • R. Schultz-Heienbrok, T. Maier, and N. Sträter A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5′-nucleotidase Biochemistry 44 2005 2244 2252
    • (2005) Biochemistry , vol.44 , pp. 2244-2252
    • Schultz-Heienbrok, R.1    Maier, T.2    Sträter, N.3
  • 40
    • 77950655571 scopus 로고    scopus 로고
    • Recombinant ecto-5′-nucleotidase (CD73) has long lasting antinociceptive effects that are dependent on adenosine A1 receptor activation
    • N.A. Sowa, M.K. Voss, and M.J. Zylka Recombinant ecto-5′- nucleotidase (CD73) has long lasting antinociceptive effects that are dependent on adenosine A1 receptor activation Mol. Pain 6 2010 20
    • (2010) Mol. Pain , vol.6 , pp. 20
    • Sowa, N.A.1    Voss, M.K.2    Zylka, M.J.3
  • 41
    • 84870490220 scopus 로고    scopus 로고
    • The double-edge sword effect of anti-CD73 cancer therapy
    • J. Stagg The double-edge sword effect of anti-CD73 cancer therapy OncoImmunology 1 2012 217 218
    • (2012) OncoImmunology , vol.1 , pp. 217-218
    • Stagg, J.1
  • 42
    • 77957564570 scopus 로고    scopus 로고
    • Extracellular adenosine triphosphate and adenosine in cancer
    • J. Stagg, and M.J. Smyth Extracellular adenosine triphosphate and adenosine in cancer Oncogene 29 2010 5346 5358
    • (2010) Oncogene , vol.29 , pp. 5346-5358
    • Stagg, J.1    Smyth, M.J.2
  • 44
    • 79954576658 scopus 로고    scopus 로고
    • CD73-deficient mice have increased antitumor immunity and are resistant to experimental metastasis
    • J. Stagg, U. Divisekera, H. Duret, T. Sparwasser, M.W. Teng, P.K. Darcy, and M.J. Smyth CD73-deficient mice have increased antitumor immunity and are resistant to experimental metastasis Cancer Res. 71 2011 2892 2900
    • (2011) Cancer Res. , vol.71 , pp. 2892-2900
    • Stagg, J.1    Divisekera, U.2    Duret, H.3    Sparwasser, T.4    Teng, M.W.5    Darcy, P.K.6    Smyth, M.J.7
  • 46
    • 34047250594 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase: Structure function relationships
    • N. Sträter Ecto-5′-nucleotidase: Structure function relationships Purinergic Signal. 2 2006 343 350
    • (2006) Purinergic Signal. , vol.2 , pp. 343-350
    • Sträter, N.1
  • 49
    • 34547124338 scopus 로고    scopus 로고
    • Crystal structure of human cytosolic 5′-nucleotidase II: Insights into allosteric regulation and substrate recognition
    • K. Walldén, P. Stenmark, T. Nyman, S. Flodin, S. Gräslund, P. Loppnau, V. Bianchi, and P. Nordlund Crystal structure of human cytosolic 5′-nucleotidase II: insights into allosteric regulation and substrate recognition J. Biol. Chem. 282 2007 17828 17836
    • (2007) J. Biol. Chem. , vol.282 , pp. 17828-17836
    • Walldén, K.1    Stenmark, P.2    Nyman, T.3    Flodin, S.4    Gräslund, S.5    Loppnau, P.6    Bianchi, V.7    Nordlund, P.8
  • 50
    • 79957921286 scopus 로고    scopus 로고
    • CD73 has distinct roles in nonhematopoietic and hematopoietic cells to promote tumor growth in mice
    • L. Wang, J. Fan, L.F. Thompson, Y. Zhang, T. Shin, T.J. Curiel, and B. Zhang CD73 has distinct roles in nonhematopoietic and hematopoietic cells to promote tumor growth in mice J. Clin. Invest. 121 2011 2371 2382
    • (2011) J. Clin. Invest. , vol.121 , pp. 2371-2382
    • Wang, L.1    Fan, J.2    Thompson, L.F.3    Zhang, Y.4    Shin, T.5    Curiel, T.J.6    Zhang, B.7
  • 52
    • 41949083203 scopus 로고    scopus 로고
    • Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade
    • G.G. Yegutkin Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade Biochim. Biophys. Acta 1783 2008 673 694
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 673-694
    • Yegutkin, G.G.1
  • 54
    • 35448935001 scopus 로고    scopus 로고
    • Characterization of Rat NTPDase1, -2, and -3 ectodomains refolded from bacterial inclusion bodies
    • M. Zebisch, and N. Sträter Characterization of Rat NTPDase1, -2, and -3 ectodomains refolded from bacterial inclusion bodies Biochemistry 46 2007 11945 11956
    • (2007) Biochemistry , vol.46 , pp. 11945-11956
    • Zebisch, M.1    Sträter, N.2
  • 55
    • 44349101227 scopus 로고    scopus 로고
    • Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling
    • M. Zebisch, and N. Sträter Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling Proc. Natl. Acad. Sci. USA 105 2008 6882 6887
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6882-6887
    • Zebisch, M.1    Sträter, N.2
  • 56
    • 84855762914 scopus 로고    scopus 로고
    • Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1
    • M. Zebisch, M. Krauss, P. Schäfer, and N. Sträter Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1 J. Mol. Biol. 415 2012 288 306
    • (2012) J. Mol. Biol. , vol.415 , pp. 288-306
    • Zebisch, M.1    Krauss, M.2    Schäfer, P.3    Sträter, N.4
  • 57
    • 77955750932 scopus 로고    scopus 로고
    • CD73: A novel target for cancer immunotherapy
    • B. Zhang CD73: a novel target for cancer immunotherapy Cancer Res. 70 2010 6407 6411
    • (2010) Cancer Res. , vol.70 , pp. 6407-6411
    • Zhang, B.1
  • 58
    • 84869058675 scopus 로고    scopus 로고
    • CD73 promotes tumor growth and metastasis
    • B. Zhang CD73 promotes tumor growth and metastasis OncoImmunology 1 2012 67 70
    • (2012) OncoImmunology , vol.1 , pp. 67-70
    • Zhang, B.1
  • 59
    • 34548435229 scopus 로고    scopus 로고
    • RNA interference of ecto-5′-nucleotidase (CD73) inhibits human breast cancer cell growth and invasion
    • X. Zhi, S. Chen, P. Zhou, Z. Shao, L. Wang, Z. Ou, and L. Yin RNA interference of ecto-5′-nucleotidase (CD73) inhibits human breast cancer cell growth and invasion Clin. Exp. Metastasis 24 2007 439 448
    • (2007) Clin. Exp. Metastasis , vol.24 , pp. 439-448
    • Zhi, X.1    Chen, S.2    Zhou, P.3    Shao, Z.4    Wang, L.5    Ou, Z.6    Yin, L.7
  • 60
    • 78449305587 scopus 로고    scopus 로고
    • RNAi-mediated CD73 suppression induces apoptosis and cell-cycle arrest in human breast cancer cells
    • X. Zhi, Y. Wang, X. Zhou, J. Yu, R. Jian, S. Tang, L. Yin, and P. Zhou RNAi-mediated CD73 suppression induces apoptosis and cell-cycle arrest in human breast cancer cells Cancer Sci. 101 2010 2561 2569
    • (2010) Cancer Sci. , vol.101 , pp. 2561-2569
    • Zhi, X.1    Wang, Y.2    Zhou, X.3    Yu, J.4    Jian, R.5    Tang, S.6    Yin, L.7    Zhou, P.8
  • 61
    • 34548008177 scopus 로고    scopus 로고
    • Effects of ecto-5′-nucleotidase on human breast cancer cell growth in vitro and in vivo
    • X. Zhou, X. Zhi, P. Zhou, S. Chen, F. Zhao, Z. Shao, Z. Ou, and L. Yin Effects of ecto-5′-nucleotidase on human breast cancer cell growth in vitro and in vivo Oncol. Rep. 17 2007 1341 1346
    • (2007) Oncol. Rep. , vol.17 , pp. 1341-1346
    • Zhou, X.1    Zhi, X.2    Zhou, P.3    Chen, S.4    Zhao, F.5    Shao, Z.6    Ou, Z.7    Yin, L.8
  • 62
    • 0026729643 scopus 로고
    • 5′-Nucleotidase: Molecular structure and functional aspects
    • H. Zimmermann 5′-Nucleotidase: molecular structure and functional aspects Biochem. J. 285 1992 345 365
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 63
    • 84861529229 scopus 로고    scopus 로고
    • Cellular function and molecular structure of ecto-nucleotidases
    • H. Zimmermann, M. Zebisch, and N. Sträter Cellular function and molecular structure of ecto-nucleotidases Purinergic Signal. 8 2012 437 502
    • (2012) Purinergic Signal. , vol.8 , pp. 437-502
    • Zimmermann, H.1    Zebisch, M.2    Sträter, N.3


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