메뉴 건너뛰기




Volumn 93, Issue 9, 2011, Pages 1543-1554

Promiscuity, stability and cold adaptation of a newly isolated acylaminoacyl peptidase

Author keywords

Acylaminoacyl peptidase; Catalytic promiscuity; Cold activity; Enzyme isolation; Flexibility

Indexed keywords

ACYLAMINOACYL PEPTIDASE; ESTER; N ACYLAMINO ACID; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG;

EID: 79960846559     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.05.010     Document Type: Article
Times cited : (21)

References (59)
  • 1
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 2
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • DOI 10.1126/science.1079731
    • L.C. James, P. Roversi, and D.S. Tawfik Antibody multispecificity mediated by conformational diversity Science (New York, N.Y.) 299 2003 1362 1367 (Pubitemid 36254643)
    • (2003) Science , vol.299 , Issue.5611 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 4
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533 (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 5
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J. Mol. Biol. 293 1999 321 331 (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 6
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions
    • DOI 10.1016/S0092-8674(00)80463-8
    • I. Radhakrishnan, G.C. Perez-Alvarado, D. Parker, H.J. Dyson, M.R. Montminy, and P.E. Wright Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions Cell 91 1997 741 752 (Pubitemid 28007731)
    • (1997) Cell , vol.91 , Issue.6 , pp. 741-752
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 8
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • C.J. Oldfield, J. Meng, J.Y. Yang, M.Q. Yang, V.N. Uversky, and A.K. Dunker Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners BMC Genomics 9 Suppl. 1 2008 S1
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1 , pp. 1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 9
    • 34548461275 scopus 로고    scopus 로고
    • Exploiting temperature-dependent substrate promiscuity for nucleoside analogue activation by thymidine kinase from Thermotoga maritima
    • DOI 10.1021/ja0734391
    • S. Lutz, J. Lichter, and L. Liu Exploiting temperature-dependent substrate promiscuity for nucleoside analogue activation by thymidine kinase from Thermotoga maritima J. Am. Chem. Soc. 129 2007 8714 8715 (Pubitemid 47492056)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.28 , pp. 8714-8715
    • Lutz, S.1    Lichter, J.2    Liu, L.3
  • 10
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • DOI 10.1074/jbc.M212508200
    • S. D'Amico, J.C. Marx, C. Gerday, and G. Feller Activity-stability relationships in extremophilic enzymes J. Biol. Chem. 278 2003 7891 7896 (Pubitemid 36800524)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.-C.2    Gerday, C.3    Feller, G.4
  • 13
    • 70450222294 scopus 로고    scopus 로고
    • Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation
    • P. Gatti-Lafranconi, A. Natalello, S. Rehm, S.M. Doglia, J. Pleiss, and M. Lotti Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation J. Mol. Biol. 395 2010 155 166
    • (2010) J. Mol. Biol. , vol.395 , pp. 155-166
    • Gatti-Lafranconi, P.1    Natalello, A.2    Rehm, S.3    Doglia, S.M.4    Pleiss, J.5    Lotti, M.6
  • 16
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • O. Khersonsky, and D.S. Tawfik Enzyme promiscuity: a mechanistic and evolutionary perspective Annu. Rev. Biochem. 79 2010 471 505
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 17
    • 47749127353 scopus 로고    scopus 로고
    • The stereochemical course of 4-hydroxy-2-nonenal metabolism by glutathione S-transferases
    • L.M. Balogh, A.G. Roberts, L.M. Shireman, R.J. Greene, and W.M. Atkins The stereochemical course of 4-hydroxy-2-nonenal metabolism by glutathione S-transferases J. Biol. Chem. 283 2008 16702 16710
    • (2008) J. Biol. Chem. , vol.283 , pp. 16702-16710
    • Balogh, L.M.1    Roberts, A.G.2    Shireman, L.M.3    Greene, R.J.4    Atkins, W.M.5
  • 18
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • DOI 10.1126/science.1130258
    • D.D. Boehr, D. McElheny, H.J. Dyson, and P.E. Wright The dynamic energy landscape of dihydrofolate reductase catalysis Science (New York, N.Y.) 313 2006 1638 1642 (Pubitemid 44414038)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wrightt, P.E.4
  • 19
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - A 60-year-old hypothesis revisited
    • DOI 10.1016/S0968-0004(03)00135-X
    • L.C. James, and D.S. Tawfik Conformational diversity and protein evolution - a 60-year-old hypothesis revisited Trends Biochem. Sci. 28 2003 361 368 (Pubitemid 36851617)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.7 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 20
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • P.J. O'Brien, and D. Herschlag Catalytic promiscuity and the evolution of new enzymatic activities Chem. Biol. 6 1999 R91 R105
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 22
    • 44749086283 scopus 로고    scopus 로고
    • Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase
    • P. Gatti-Lafranconi, S.M. Caldarazzo, A. Villa, L. Alberghina, and M. Lotti Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase FEBS Lett. 582 2008 2313 2318
    • (2008) FEBS Lett. , vol.582 , pp. 2313-2318
    • Gatti-Lafranconi, P.1    Caldarazzo, S.M.2    Villa, A.3    Alberghina, L.4    Lotti, M.5
  • 23
    • 68049128317 scopus 로고    scopus 로고
    • Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1
    • S. Brocca, M. Samalikova, V.N. Uversky, M. Lotti, M. Vanoni, L. Alberghina, and R. Grandori Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1 Proteins 76 2009 731 746
    • (2009) Proteins , vol.76 , pp. 731-746
    • Brocca, S.1    Samalikova, M.2    Uversky, V.N.3    Lotti, M.4    Vanoni, M.5    Alberghina, L.6    Grandori, R.7
  • 24
    • 79952112988 scopus 로고    scopus 로고
    • How disorder influences order and vice versa: Mutual effects in fusion proteins containing an intrinsically disordered and a globular protein
    • accepted
    • I. Sambi, P. Gatti-Lafranconi, S. Longhi, and M. Lotti How disorder influences order and vice versa: mutual effects in fusion proteins containing an intrinsically disordered and a globular protein FEBS J. 2010 accepted
    • (2010) FEBS J.
    • Sambi, I.1    Gatti-Lafranconi, P.2    Longhi, S.3    Lotti, M.4
  • 26
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • DOI 10.1016/j.febslet.2005.04.085, PII S0014579305006174
    • D. Ami, A. Natalello, P. Gatti-Lafranconi, M. Lotti, and S.M. Doglia Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy FEBS Lett. 579 2005 3433 3436 (Pubitemid 40800294)
    • (2005) FEBS Letters , vol.579 , Issue.16 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 28
    • 0014138449 scopus 로고
    • Taxonomy of psychrophilic strains of Bacillus
    • J.M. Larkin, and J.L. Stokes Taxonomy of psychrophilic strains of Bacillus J. Bacteriol. 94 1967 889 895
    • (1967) J. Bacteriol. , vol.94 , pp. 889-895
    • Larkin, J.M.1    Stokes, J.L.2
  • 29
    • 0034991394 scopus 로고    scopus 로고
    • Sporosarcina aquimarina sp. nov., a bacterium isolated from seawater in Korea, and transfer of Bacillus globisporus (larkin and stokes 1967), Bacillus psychrophilus (Nakamura 1984) and Bacillus pasteurii (Chester 1898) to the genus Sporosarcina as Sporosarcina globispora comb. nov., Sporosarcina psychrophila comb. nov and Sporosarcina pasteurii comb. nov., and emended description of the genus
    • J.H. Yoon, K.C. Lee, N. Weiss, Y.H. Kho, K.H. Kang, and Y.H. Park Sporosarcina aquimarina sp. nov., a bacterium isolated from seawater in Korea, and transfer of Bacillus globisporus (Larkin and Stokes 1967), Bacillus psychrophilus (Nakamura 1984) and Bacillus pasteurii (Chester 1898) to the genus Sporosarcina as Sporosarcina globispora comb. nov., Sporosarcina psychrophila comb. nov. and Sporosarcina pasteurii comb. nov., and emended description of the genus Sporosarcina Int. J. Syst. Evol. Microbiol. 51 2001 1079 1086 (Pubitemid 32505654)
    • (2001) International Journal of Systematic and Evolutionary Microbiology , vol.51 , Issue.3 , pp. 1079-1086
    • Yoon, J.-H.1    Lee, K.-C.2    Weiss, N.3    Kho, Y.H.4    Kang, K.H.5    Park, Y.-H.6
  • 30
    • 67349149206 scopus 로고    scopus 로고
    • Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity
    • Z. Snelter, A.L. Kiss, K. Domokos, V. Harmat, G. Náray- Szabó, and L. Polgár Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity Biochim. Biophys. Acta 1794 2009 1204 1210
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1204-1210
    • Snelter, Z.1    Kiss, A.L.2    Domokos, K.3    Harmat, V.4    Náray-Szabó, G.5    Polgár, L.6
  • 31
    • 0036178438 scopus 로고    scopus 로고
    • The prolyl oligopeptidase family
    • DOI 10.1007/s00018-002-8427-5
    • L. Polgár The prolyl oligopeptidase family Cell Mol. Life Sci. 59 2002 349 362 (Pubitemid 34169519)
    • (2002) Cellular and Molecular Life Sciences , vol.59 , Issue.2 , pp. 349-362
    • Polgar, L.1
  • 32
    • 33646869457 scopus 로고    scopus 로고
    • Structure-function properties of prolyl oligopeptidase family enzymes
    • DOI 10.1385/CBB:44:3:349
    • D. Rea, and V. Fülöp Structure-function properties of prolyl oligopeptidase family enzymes Cell Biochem. Biophys. 44 2006 349 365 (Pubitemid 43780391)
    • (2006) Cell Biochemistry and Biophysics , vol.44 , Issue.3 , pp. 349-365
    • Rea, D.1    Fulop, V.2
  • 33
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • DOI 10.1016/S0092-8674(00)81416-6
    • V. Fulop, Z. Bocskei, and L. Polgar Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis Cell 94 1998 161 170 (Pubitemid 28348004)
    • (1998) Cell , vol.94 , Issue.2 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3
  • 34
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • DOI 10.1146/annurev.micro.53.1.315
    • K.E. Jaeger, B.W. Dijkstra, and M.T. Reetz Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases Annu. Rev. Microbiol. 53 1999 315 351 (Pubitemid 29503734)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 315-351
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 35
    • 4143096860 scopus 로고    scopus 로고
    • Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
    • DOI 10.1016/j.str.2004.05.019, PII S0969212604002382
    • M. Bartlam, G. Wang, H. Yang, R. Gao, X. Zhao, G. Xie, S. Cao, Y. Feng, and Z. Rao Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 Structure 12 2004 1481 1488 (Pubitemid 39092092)
    • (2004) Structure , vol.12 , Issue.8 , pp. 1481-1488
    • Bartlam, M.1    Wang, G.2    Yang, H.3    Gao, R.4    Zhao, X.5    Xie, G.6    Cao, S.7    Feng, Y.8    Rao, Z.9
  • 36
    • 33745826249 scopus 로고    scopus 로고
    • Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation
    • DOI 10.1074/jbc.M601015200
    • Q. Wang, G. Yang, Y. Liu, and Y. Feng Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation J. Biol. Chem. 281 2006 18618 18625 (Pubitemid 44035521)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18618-18625
    • Wang, Q.1    Yang, G.2    Liu, Y.3    Feng, Y.4
  • 37
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405 (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 40
    • 33947724046 scopus 로고    scopus 로고
    • The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity
    • DOI 10.1016/j.jmb.2007.02.025, PII S0022283607002069
    • A.L. Kiss, B. Hornung, K. Radi, Z. Gengeliczki, B. Sztaray, T. Juhasz, Z. Szeltner, V. Harmat, and L. Polgar The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity J. Mol. Biol. 368 2007 509 520 (Pubitemid 46505147)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 509-520
    • Kiss, A.L.1    Hornung, B.2    Radi, K.3    Gengeliczki, Z.4    Sztaray, B.5    Juhasz, T.6    Szeltner, Z.7    Harmat, V.8    Polgar, L.9
  • 42
    • 0028362404 scopus 로고
    • Human acylpeptide hydrolase. Studies on its thiol groups and mechanism of action
    • A. Scaloni, D. Barra, W. Jonen, and J. Manning Human acylpeptide hydrolase. Studies on its thiol groups and mechanism of action J. Biol. Chem. 269 1994 15076 15084
    • (1994) J. Biol. Chem. , vol.269 , pp. 15076-15084
    • Scaloni, A.1    Barra, D.2    Jonen, W.3    Manning, J.4
  • 44
    • 0023664803 scopus 로고
    • Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction
    • K. Kobayashi, and J. Smith Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction J. Biol. Chem. 262 1987 11435 11445
    • (1987) J. Biol. Chem. , vol.262 , pp. 11435-11445
    • Kobayashi, K.1    Smith, J.2
  • 46
    • 64549144156 scopus 로고    scopus 로고
    • Deactivation and unfolding are uncoupled in a bacterial lipase exposed to heat, low pH and organic solvents
    • G. Invernizzi, L. Casiraghi, R. Grandori, and M. Lotti Deactivation and unfolding are uncoupled in a bacterial lipase exposed to heat, low pH and organic solvents J. Biotechnol. 141 2009 42 46
    • (2009) J. Biotechnol. , vol.141 , pp. 42-46
    • Invernizzi, G.1    Casiraghi, L.2    Grandori, R.3    Lotti, M.4
  • 48
    • 4043175563 scopus 로고    scopus 로고
    • Different roles of electrostatics in heat and in cold: Adaptation by citrate synthase
    • DOI 10.1002/cbic.200300627
    • S. Kumar, and R. Nussinov Different roles of electrostatics in heat and in cold: adaptation by citrate synthase Chembiochem. 5 2004 280 290 (Pubitemid 39257121)
    • (2004) ChemBioChem , vol.5 , Issue.3 , pp. 280-290
    • Kumar, S.1    Nussinov, R.2
  • 49
    • 34247131307 scopus 로고    scopus 로고
    • Enzyme promiscuity: Mechanism and applications
    • DOI 10.1016/j.tibtech.2007.03.002, PII S016777990700073X
    • K. Hult, and P. Berglund Enzyme promiscuity: mechanism and applications Trends Biotechnol. 25 2007 231 238 (Pubitemid 46589665)
    • (2007) Trends in Biotechnology , vol.25 , Issue.5 , pp. 231-238
    • Hult, K.1    Berglund, P.2
  • 50
    • 59849106371 scopus 로고    scopus 로고
    • Protein promiscuity and its implications for biotechnology
    • I. Nobeli, A.D. Favia, and J.M. Thornton Protein promiscuity and its implications for biotechnology Nat. Biotechnol. 27 2009 157 167
    • (2009) Nat. Biotechnol. , vol.27 , pp. 157-167
    • Nobeli, I.1    Favia, A.D.2    Thornton, J.M.3
  • 51
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • G. Feller, and C. Gerday Psychrophilic enzymes: hot topics in cold adaptation Nat. Rev. Microbiol. 1 2003 200 208
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 52
    • 0032499603 scopus 로고    scopus 로고
    • Characterization of trypsin-modified bovine lens acylpeptide hydrolase
    • DOI 10.1006/bbrc.1998.8747
    • K. Chongcharoen, and K.K. Sharma Characterization of trypsin-modified bovine lens acylpeptide hydrolase Biochem. Biophys. Res. Commun. 247 1998 136 141 (Pubitemid 28412539)
    • (1998) Biochemical and Biophysical Research Communications , vol.247 , Issue.1 , pp. 136-141
    • Chongcharoen, K.1    Sharma, K.K.2
  • 53
    • 0027265970 scopus 로고
    • Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation
    • K. Sharma, and B. Ortwerth Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation Eur. J. Biochem. 216 1993 631 637 (Pubitemid 23276312)
    • (1993) European Journal of Biochemistry , vol.216 , Issue.2 , pp. 631-637
    • Sharma, K.K.1    Rotwerth, B.J.2
  • 55
    • 52649134528 scopus 로고    scopus 로고
    • Effect of chaotropic agents on the structure-function of recombinant acylpeptide hydrolase
    • DOI 10.1023/A:1019938217294
    • R. Senthilkumar, and K. Sharma Effect of chaotropic agents on the structure-function of recombinant acylpeptide hydrolase J. Protein Chem. 21 2002 323 332 (Pubitemid 34913067)
    • (2002) Journal of Protein Chemistry , vol.21 , Issue.5 , pp. 323-332
    • Senthilkumar, R.1    Sharma, K.K.2
  • 56
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • T.F. Smith, and M.S. Waterman Identification of common molecular subsequences J. Mol. Biol. 147 1981 195 197
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 59
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.