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Volumn 401, Issue 3, 2010, Pages 465-477

Structure-function analysis of the short splicing variant carboxypeptidase encoded by Drosophila melanogaster silver

Author keywords

Activity regulation; Development; Funnelin; Metallocarboxypeptidase; Splicing variant

Indexed keywords

CARBOXYPEPTIDASE; ENZYME VARIANT; HOMODIMER; HYDROLASE; MEMBRANE PROTEIN; METALLOPROTEINASE; MONOMER; PEPTIDASE; PREALBUMIN; CARBOXYPEPTIDASE D; CYSTEINE; ISOPROTEIN; PEPTIDE HYDROLASE;

EID: 77955281659     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.035     Document Type: Article
Times cited : (10)

References (68)
  • 3
    • 0028882212 scopus 로고
    • The silver gene of Drosophila melanogaster encodes multiple carboxypeptidases similar to mammalian prohormone-processing enzymes
    • Settle S.H., Green M.M., Burtis K.C. The silver gene of Drosophila melanogaster encodes multiple carboxypeptidases similar to mammalian prohormone-processing enzymes. Proc. Natl Acad. Sci. USA 1995, 92:9470-9474.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9470-9474
    • Settle, S.H.1    Green, M.M.2    Burtis, K.C.3
  • 5
    • 33744952646 scopus 로고    scopus 로고
    • Characterization of the molecular basis of the Drosophila mutations in carboxypeptidase D. Effect on enzyme activity and expression
    • Sidyelyeva G., Baker N.E., Fricker L.D. Characterization of the molecular basis of the Drosophila mutations in carboxypeptidase D. Effect on enzyme activity and expression. J. Biol. Chem. 2006, 281:13844-13852.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13844-13852
    • Sidyelyeva, G.1    Baker, N.E.2    Fricker, L.D.3
  • 6
    • 0037147319 scopus 로고    scopus 로고
    • Characterization of Drosophila carboxypeptidase D
    • Sidyelyeva G., Fricker L.D. Characterization of Drosophila carboxypeptidase D. J. Biol. Chem. 2002, 277:49613-49620.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49613-49620
    • Sidyelyeva, G.1    Fricker, L.D.2
  • 7
    • 0028790290 scopus 로고
    • Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary
    • Song L., Fricker L.D. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem. 1995, 270:25007-25013.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25007-25013
    • Song, L.1    Fricker, L.D.2
  • 8
    • 0029830745 scopus 로고    scopus 로고
    • Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D
    • Song L., Fricker L.D. Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J. Biol. Chem. 1996, 271:28884-28889.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28884-28889
    • Song, L.1    Fricker, L.D.2
  • 10
    • 77956702352 scopus 로고    scopus 로고
    • Carboxypeptidases D and E
    • Academic Press, Inc., London, UK, R.E. Dalbey, D.S. Sigman (Eds.)
    • Fricker L.D. Carboxypeptidases D and E. The Enzymes. Co- and Posttranslational Proteolysis of Proteins 2002, vol. 23:421-452. Academic Press, Inc., London, UK. R.E. Dalbey, D.S. Sigman (Eds.).
    • (2002) The Enzymes. Co- and Posttranslational Proteolysis of Proteins , vol.23 , pp. 421-452
    • Fricker, L.D.1
  • 11
    • 0031886603 scopus 로고    scopus 로고
    • Cellular carboxypeptidases
    • Skidgel R.A., Erdös E.G. Cellular carboxypeptidases. Immunol. Rev. 1998, 161:129-141.
    • (1998) Immunol. Rev. , vol.161 , pp. 129-141
    • Skidgel, R.A.1    Erdös, E.G.2
  • 12
    • 84944046233 scopus 로고    scopus 로고
    • 251. Metallocarboxypeptidase D
    • Elsevier, London, UK, 2 , A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.)
    • Fricker L.D. 251. Metallocarboxypeptidase D. Handbook of Proteolytic Enzymes 2004, vol. 1:848-851. Elsevier, London, UK, 2 vols. 2nd edit. A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.).
    • (2004) Handbook of Proteolytic Enzymes , vol.1 S , pp. 848-851
    • Fricker, L.D.1
  • 13
    • 77956777446 scopus 로고    scopus 로고
    • Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior
    • In press. doi:10.1007/s00018-010-0369-8
    • Sidyelyeva G., Wegener C., Schoenfeld B.P., Bell A.J., Baker N.E., McBride S.M., Fricker L.D. Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior. Cell. Mol. Life Sci. 2010, In press. doi:10.1007/s00018-010-0369-8.
    • (2010) Cell. Mol. Life Sci.
    • Sidyelyeva, G.1    Wegener, C.2    Schoenfeld, B.P.3    Bell, A.J.4    Baker, N.E.5    McBride, S.M.6    Fricker, L.D.7
  • 14
    • 53249142426 scopus 로고    scopus 로고
    • Prolactin and estrogen up-regulate carboxypeptidase-D to promote nitric oxide production and survival of mcf-7 breast cancer cells
    • Abdelmagid S.A., Too C.K. Prolactin and estrogen up-regulate carboxypeptidase-D to promote nitric oxide production and survival of mcf-7 breast cancer cells. Endocrinology 2008, 149:4821-4828.
    • (2008) Endocrinology , vol.149 , pp. 4821-4828
    • Abdelmagid, S.A.1    Too, C.K.2
  • 15
    • 0035027566 scopus 로고    scopus 로고
    • Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium
    • Hadkar V., Skidgel R.A. Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium. Mol. Pharmacol. 2001, 59:1324-1332.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1324-1332
    • Hadkar, V.1    Skidgel, R.A.2
  • 16
    • 54249136672 scopus 로고    scopus 로고
    • Structure and mechanism of metallocarboxypeptidases
    • Gomis-Rüth F.X. Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 2008, 43:319-345.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 319-345
    • Gomis-Rüth, F.X.1
  • 18
    • 0023690624 scopus 로고
    • Basic carboxypeptidases: regulators of peptide hormone activity
    • Skidgel R.A. Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol. Sci. 1988, 9:299-304.
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 299-304
    • Skidgel, R.A.1
  • 19
    • 0001995439 scopus 로고    scopus 로고
    • Structure and function of mammalian zinc carboxypeptidases
    • Taylor and Francis Ltd., London, UK, N.M. Hooper (Ed.)
    • Skidgel R.A. Structure and function of mammalian zinc carboxypeptidases. Zinc Metalloproteases in Health and Disease 1996, 241-283. Taylor and Francis Ltd., London, UK. N.M. Hooper (Ed.).
    • (1996) Zinc Metalloproteases in Health and Disease , pp. 241-283
    • Skidgel, R.A.1
  • 20
    • 20444426576 scopus 로고    scopus 로고
    • 252. Carboxypeptidase M
    • Elsevier, London, UK, 2 vol, A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.)
    • Skidgel R.A. 252. Carboxypeptidase M. Handbook of Proteolytic Enzymes 2004, vol. 1:851-854. Elsevier, London, UK, 2 vols. 2nd edit. A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.).
    • (2004) Handbook of Proteolytic Enzymes , vol.1 s , pp. 851-854
    • Skidgel, R.A.1
  • 21
    • 0242531024 scopus 로고    scopus 로고
    • Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily
    • Gomis-Rüth F.X., Companys V., Qian Y., Fricker L.D., Vendrell J., Avilés F.X., Coll M. Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily. EMBO J. 1999, 18:5817-5826.
    • (1999) EMBO J. , vol.18 , pp. 5817-5826
    • Gomis-Rüth, F.X.1    Companys, V.2    Qian, Y.3    Fricker, L.D.4    Vendrell, J.5    Avilés, F.X.6    Coll, M.7
  • 22
    • 0035200832 scopus 로고    scopus 로고
    • Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding
    • Reznik S.E., Fricker L.D. Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding. Cell. Mol. Life Sci. 2001, 58:1790-1804.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1790-1804
    • Reznik, S.E.1    Fricker, L.D.2
  • 23
    • 0028295258 scopus 로고
    • A cell surface protein that binds avian hepatitis B virus particles
    • Kuroki K., Cheung R., Marion P.L., Ganem D. A cell surface protein that binds avian hepatitis B virus particles. J. Virol. 1994, 68:2091-2096.
    • (1994) J. Virol. , vol.68 , pp. 2091-2096
    • Kuroki, K.1    Cheung, R.2    Marion, P.L.3    Ganem, D.4
  • 24
    • 0032478636 scopus 로고    scopus 로고
    • Gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity
    • Eng F.J., Novikova E.G., Kuroki K., Ganem D., Fricker L.D. gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity. J. Biol. Chem. 1998, 273:8382-8388.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8382-8388
    • Eng, F.J.1    Novikova, E.G.2    Kuroki, K.3    Ganem, D.4    Fricker, L.D.5
  • 25
    • 67650065404 scopus 로고    scopus 로고
    • Catalytic domain architecture of metzincin metalloproteases
    • Gomis-Rüth F.X. Catalytic domain architecture of metzincin metalloproteases. J. Biol. Chem. 2009, 15353-15357.
    • (2009) J. Biol. Chem. , pp. 15353-15357
    • Gomis-Rüth, F.X.1
  • 26
    • 24944498409 scopus 로고    scopus 로고
    • Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
    • Li F., Li W., Farzan M., Harrison S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 2005, 309:1864-1868.
    • (2005) Science , vol.309 , pp. 1864-1868
    • Li, F.1    Li, W.2    Farzan, M.3    Harrison, S.C.4
  • 27
    • 0023515281 scopus 로고
    • The genetics of biogenic amine metabolism, sclerotization, and melanization in Drosophila melanogaster
    • Wright T.R.F. The genetics of biogenic amine metabolism, sclerotization, and melanization in Drosophila melanogaster. Adv. Genet. 1987, 24:127-222.
    • (1987) Adv. Genet. , vol.24 , pp. 127-222
    • Wright, T.R.F.1
  • 30
    • 70349323001 scopus 로고    scopus 로고
    • Golgi linked protein glycosylation and associated diseases
    • Ungar D. Golgi linked protein glycosylation and associated diseases. Semin. Cell Dev. Biol. 2009, 20:762-769.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 762-769
    • Ungar, D.1
  • 32
    • 0025099627 scopus 로고
    • Comparison of a spectrophotometric, a fluorometric, and a novel radiometric assay for carboxypeptidase E (EC 3.4.17.10) and other carboxypeptidase B-like enzymes
    • Fricker L.D., Devi L. Comparison of a spectrophotometric, a fluorometric, and a novel radiometric assay for carboxypeptidase E (EC 3.4.17.10) and other carboxypeptidase B-like enzymes. Anal. Biochem. 1990, 184:21-27.
    • (1990) Anal. Biochem. , vol.184 , pp. 21-27
    • Fricker, L.D.1    Devi, L.2
  • 35
    • 13544272567 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization
    • Arolas J.L., Lorenzo J., Rovira A., Castella J., Aviles F.X., Sommerhoff C.P. A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 2005, 280:3441-3448.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3441-3448
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3    Castella, J.4    Aviles, F.X.5    Sommerhoff, C.P.6
  • 36
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation
    • Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W., Meijers J.C., Huizinga E.G. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. Blood 2008, 112:2803-2809.
    • (2008) Blood , vol.112 , pp. 2803-2809
    • Marx, P.F.1    Brondijk, T.H.2    Plug, T.3    Romijn, R.A.4    Hemrika, W.5    Meijers, J.C.6    Huizinga, E.G.7
  • 38
    • 0031569199 scopus 로고    scopus 로고
    • The PLEES proteins-a family of structurally related enzymes widely distributed from bacteria to humans
    • Puente X.S., López-Otín C. The PLEES proteins-a family of structurally related enzymes widely distributed from bacteria to humans. Biochem. J. 1997, 332:947-949.
    • (1997) Biochem. J. , vol.332 , pp. 947-949
    • Puente, X.S.1    López-Otín, C.2
  • 39
    • 34250185374 scopus 로고    scopus 로고
    • Caught after the act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide
    • Bayés A., Fernández D., Solà M., Marrero A., García-Piqué S., Avilés F.X., et al. Caught after the act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide. Biochemistry 2007, 46:6921-6930.
    • (2007) Biochemistry , vol.46 , pp. 6921-6930
    • Bayés, A.1    Fernández, D.2    Solà, M.3    Marrero, A.4    García-Piqué, S.5    Avilés, F.X.6
  • 40
    • 1842557330 scopus 로고    scopus 로고
    • Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity
    • Reverter D., Maskos K., Tan F., Skidgel R.A., Bode W. Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity. J. Mol. Biol. 2004, 338:257-269.
    • (2004) J. Mol. Biol. , vol.338 , pp. 257-269
    • Reverter, D.1    Maskos, K.2    Tan, F.3    Skidgel, R.A.4    Bode, W.5
  • 41
    • 33846448485 scopus 로고    scopus 로고
    • Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain
    • Keil C., Maskos K., Than M., Hoopes J.T., Huber R., Tan F., et al. Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. J. Mol. Biol. 2007, 366:504-516.
    • (2007) J. Mol. Biol. , vol.366 , pp. 504-516
    • Keil, C.1    Maskos, K.2    Than, M.3    Hoopes, J.T.4    Huber, R.5    Tan, F.6
  • 42
    • 70349260510 scopus 로고    scopus 로고
    • Evolutionary changes to transthyretin: structure-function relationships
    • Prapunpoj P., Leelawatwattana L. Evolutionary changes to transthyretin: structure-function relationships. FEBS J. 2009, 276:5330-5341.
    • (2009) FEBS J. , vol.276 , pp. 5330-5341
    • Prapunpoj, P.1    Leelawatwattana, L.2
  • 43
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren I.M.A., Thornton J.M. Structural characterisation and functional significance of transient protein-protein interactions. J. Mol. Biol. 2003, 325:991-1018.
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 44
    • 36249014859 scopus 로고    scopus 로고
    • Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator
    • Skidgel R.A., Erdös E.G. Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator. Int. Immunopharmacol. 2007, 7:1888-1899.
    • (2007) Int. Immunopharmacol. , vol.7 , pp. 1888-1899
    • Skidgel, R.A.1    Erdös, E.G.2
  • 45
    • 0034055985 scopus 로고    scopus 로고
    • Function and mechanism of zinc metalloenzymes
    • McCall K.A., Huang C., Fierke C.A. Function and mechanism of zinc metalloenzymes. J. Nutr. 2000, 130:1437S-1446S.
    • (2000) J. Nutr. , vol.130
    • McCall, K.A.1    Huang, C.2    Fierke, C.A.3
  • 46
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld D.S. Zinc coordination sphere in biochemical zinc sites. BioMetals 2001, 14:271-313.
    • (2001) BioMetals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 48
    • 0035844274 scopus 로고    scopus 로고
    • The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases
    • Aloy P., Companys V., Vendrell J., Avilés F.X., Fricker L.D., Coll M., Gomis-Rüth F.X. The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases. J. Biol. Chem. 2001, 276:16177-16184.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16177-16184
    • Aloy, P.1    Companys, V.2    Vendrell, J.3    Avilés, F.X.4    Fricker, L.D.5    Coll, M.6    Gomis-Rüth, F.X.7
  • 49
    • 0027516469 scopus 로고
    • Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process
    • Avilés F.X., Vendrell J., Guasch A., Coll M., Huber R. Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process. Eur. J. Biochem. 1993, 211:381-389.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 381-389
    • Avilés, F.X.1    Vendrell, J.2    Guasch, A.3    Coll, M.4    Huber, R.5
  • 50
    • 0038660604 scopus 로고    scopus 로고
    • Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking
    • Kalinina E.V., Fricker L.D. Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking. J. Biol. Chem. 2003, 278:9244-9249.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9244-9249
    • Kalinina, E.V.1    Fricker, L.D.2
  • 51
    • 0029921147 scopus 로고    scopus 로고
    • Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody
    • Zappacosta F., Pessi A., Bianchi E., Venturini S., Sollazzo M., Tramontano A., et al. Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody. Protein Sci. 1996, 5:802-813.
    • (1996) Protein Sci. , vol.5 , pp. 802-813
    • Zappacosta, F.1    Pessi, A.2    Bianchi, E.3    Venturini, S.4    Sollazzo, M.5    Tramontano, A.6
  • 52
    • 0037189532 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression
    • Llano E., Adam G., Pendas A.M., Quesada V., Sánchez L.M., Santamaria I., et al. Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression. J. Biol. Chem. 2002, 277:23321-23329.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23321-23329
    • Llano, E.1    Adam, G.2    Pendas, A.M.3    Quesada, V.4    Sánchez, L.M.5    Santamaria, I.6
  • 53
    • 43749123507 scopus 로고    scopus 로고
    • Characterization of carboxypeptidase A6, an extracellular matrix peptidase
    • Lyons P.J., Callaway M.B., Fricker L.D. Characterization of carboxypeptidase A6, an extracellular matrix peptidase. J. Biol. Chem. 2008, 283:7054-7063.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7054-7063
    • Lyons, P.J.1    Callaway, M.B.2    Fricker, L.D.3
  • 54
    • 0030461020 scopus 로고    scopus 로고
    • Expression and functional analysis of Euglena gracilis chloroplast initiation factor 3
    • Lin Q., Yu N.J., Spremulli L.L. Expression and functional analysis of Euglena gracilis chloroplast initiation factor 3. Plant Mol. Biol. 1996, 32:937-945.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 937-945
    • Lin, Q.1    Yu, N.J.2    Spremulli, L.L.3
  • 55
    • 0036384505 scopus 로고    scopus 로고
    • Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)
    • Barbosa Pereira P.J., Segura-Martin S., Oliva B., Ferrer-Orta C., Avilés F.X., Coll M., et al. Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI). J. Mol. Biol. 2002, 321:537-547.
    • (2002) J. Mol. Biol. , vol.321 , pp. 537-547
    • Barbosa Pereira, P.J.1    Segura-Martin, S.2    Oliva, B.3    Ferrer-Orta, C.4    Avilés, F.X.5    Coll, M.6
  • 56
    • 0020513608 scopus 로고
    • Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase
    • Fricker L.D., Snyder S.H. Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase. J. Biol. Chem. 1983, 258:10950-10955.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10950-10955
    • Fricker, L.D.1    Snyder, S.H.2
  • 59
    • 0038786304 scopus 로고    scopus 로고
    • Chapter 25.2.9: XDS
    • Kluwer Academic Publishers (for The International Union of Crystallography), Dordrecht, The Netherlands, M.G. Rossmann, E. Arnold (Eds.)
    • Kabsch W. Chapter 25.2.9: XDS. International Tables for Crystallography. Volume F: Crystallography of Biological Macromolecules 2001, 730-734. Kluwer Academic Publishers (for The International Union of Crystallography), Dordrecht, The Netherlands. 1st edit. M.G. Rossmann, E. Arnold (Eds.).
    • (2001) International Tables for Crystallography. Volume F: Crystallography of Biological Macromolecules , pp. 730-734
    • Kabsch, W.1
  • 62
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • (Web Server issue)
    • Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 2007, 35:W375-W383. (Web Server issue).
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 66
    • 0027609916 scopus 로고
    • SETOR: hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S.V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 1993, 11:134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 67
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modelling and drug design program
    • Vriend G. WHAT IF: a molecular modelling and drug design program. J. Mol. Graphics 1990, 8:52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 68
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.