메뉴 건너뛰기




Volumn 588, Issue 2, 2014, Pages 206-212

Protein disulfide engineering

Author keywords

Disulfide; Engineering; Kinetics; Protein; Stability; Thermodynamics

Indexed keywords

ALKALINE PHOSPHATASE; AMYLOID BETA PROTEIN; BARNASE; CELLULASE; CYSTEINE; DIHYDROFOLATE REDUCTASE; DISULFIDE; INSULINASE; LIPASE B; LYSOZYME; PHYTASE; PROTEASE PREP; PROTEIN; PROTEINASE; STREPTAVIDIN; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 84892371627     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.11.024     Document Type: Review
Times cited : (214)

References (69)
  • 1
    • 84880633059 scopus 로고    scopus 로고
    • Orchestration of secretory protein folding by ER chaperones
    • T. Gidalevitz, F. Stevens, and Y. Argon Orchestration of secretory protein folding by ER chaperones Biochim. Biophys. Acta 1833 11 2013 2410 2424
    • (2013) Biochim. Biophys. Acta , vol.1833 , Issue.11 , pp. 2410-2424
    • Gidalevitz, T.1    Stevens, F.2    Argon, Y.3
  • 2
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • J.M. Thornton Disulphide bridges in globular proteins J. Mol. Biol. 151 2 1981 261 287
    • (1981) J. Mol. Biol. , vol.151 , Issue.2 , pp. 261-287
    • Thornton, J.M.1
  • 3
    • 0032788590 scopus 로고    scopus 로고
    • Amino acid neighbours and detailed conformational analysis of cysteines in proteins
    • M.T. Petersen, P.H. Jonson, and S.B. Petersen Amino acid neighbours and detailed conformational analysis of cysteines in proteins Protein Eng. 12 7 1999 535 548
    • (1999) Protein Eng. , vol.12 , Issue.7 , pp. 535-548
    • Petersen, M.T.1    Jonson, P.H.2    Petersen, S.B.3
  • 5
    • 0027675668 scopus 로고
    • Energetics of the disulfide bridge: An ab initio study
    • W. Qian, and S. Krimm Energetics of the disulfide bridge: an ab initio study Biopolymers 33 10 1993 1591 1603
    • (1993) Biopolymers , vol.33 , Issue.10 , pp. 1591-1603
    • Qian, W.1    Krimm, S.2
  • 6
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
    • C.N. Pace, G.R. Grimsley, J.A. Thomson, and B.J. Barnett Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds J. Biol. Chem. 263 24 1988 11820 11825
    • (1988) J. Biol. Chem. , vol.263 , Issue.24 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Barnett, B.J.4
  • 7
    • 0027390460 scopus 로고
    • The contribution of cross-links to protein stability: A normal mode analysis of the configurational entropy of the native state
    • B. Tidor, and M. Karplus The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state Proteins 15 1 1993 71 79
    • (1993) Proteins , vol.15 , Issue.1 , pp. 71-79
    • Tidor, B.1    Karplus, M.2
  • 8
    • 0028465478 scopus 로고
    • Entropic effects of disulphide bonds on protein stability
    • T. Zhang, E. Bertelsen, and T. Alber Entropic effects of disulphide bonds on protein stability Nat. Struct. Biol. 1 7 1994 434 438
    • (1994) Nat. Struct. Biol. , vol.1 , Issue.7 , pp. 434-438
    • Zhang, T.1    Bertelsen, E.2    Alber, T.3
  • 9
    • 60249097711 scopus 로고    scopus 로고
    • The effect of additional disulfide bonds on the stability and folding of ribonuclease A
    • P. Pecher, and U. Arnold The effect of additional disulfide bonds on the stability and folding of ribonuclease A Biophys. Chem. 141 1 2009 21 28
    • (2009) Biophys. Chem. , vol.141 , Issue.1 , pp. 21-28
    • Pecher, P.1    Arnold, U.2
  • 10
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • S.F. Betz Disulfide bonds and the stability of globular proteins Protein Sci. 2 10 1993 1551 1558
    • (1993) Protein Sci. , vol.2 , Issue.10 , pp. 1551-1558
    • Betz, S.F.1
  • 11
    • 0035104132 scopus 로고    scopus 로고
    • Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V
    • M. Zavodszky, C.W. Chen, J.K. Huang, M. Zolkiewski, L. Wen, and R. Krishnamoorthi Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V Protein Sci. 10 1 2001 149 160
    • (2001) Protein Sci. , vol.10 , Issue.1 , pp. 149-160
    • Zavodszky, M.1    Chen, C.W.2    Huang, J.K.3    Zolkiewski, M.4    Wen, L.5    Krishnamoorthi, R.6
  • 12
    • 0023006133 scopus 로고
    • An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of lambda repressor
    • R.T. Sauer, K. Hehir, R.S. Stearman, M.A. Weiss, A. Jeitler-Nilsson, E.G. Suchanek, and C.O. Pabo An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of lambda repressor Biochemistry 25 20 1986 5992 5998
    • (1986) Biochemistry , vol.25 , Issue.20 , pp. 5992-5998
    • Sauer, R.T.1    Hehir, K.2    Stearman, R.S.3    Weiss, M.A.4    Jeitler-Nilsson, A.5    Suchanek, E.G.6    Pabo, C.O.7
  • 13
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide bonds in subtilisin
    • J.A. Wells, and D.B. Powers In vivo formation and stability of engineered disulfide bonds in subtilisin J. Biol. Chem. 261 14 1986 6564 6570
    • (1986) J. Biol. Chem. , vol.261 , Issue.14 , pp. 6564-6570
    • Wells, J.A.1    Powers, D.B.2
  • 15
    • 0021145557 scopus 로고
    • Disulfide bond engineered into T4 lysozyme: Stabilization of the protein toward thermal inactivation
    • L.J. Perry, and R. Wetzel Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation Science 226 4674 1984 555 557
    • (1984) Science , vol.226 , Issue.4674 , pp. 555-557
    • Perry, L.J.1    Wetzel, R.2
  • 16
    • 0027052444 scopus 로고
    • Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme
    • R.H. Jacobson, M. Matsumura, H.R. Faber, and B.W. Matthews Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme Protein Sci. 1 1 1992 46 57
    • (1992) Protein Sci. , vol.1 , Issue.1 , pp. 46-57
    • Jacobson, R.H.1    Matsumura, M.2    Faber, H.R.3    Matthews, B.W.4
  • 19
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulphide bonds
    • M. Matsumura, G. Signor, and B.W. Matthews Substantial increase of protein stability by multiple disulphide bonds Nature 342 6247 1989 291 293
    • (1989) Nature , vol.342 , Issue.6247 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Matthews, B.W.3
  • 20
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • J. Clarke, and A.R. Fersht Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation Biochemistry 32 16 1993 4322 4329
    • (1993) Biochemistry , vol.32 , Issue.16 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 21
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: Simulations and bioninformatics analysis
    • V.I. Abkevich, and E.I. Shakhnovich What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis J. Mol. Biol. 300 4 2000 975 985
    • (2000) J. Mol. Biol. , vol.300 , Issue.4 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 22
    • 0033614848 scopus 로고    scopus 로고
    • Probing the unfolding region in a thermolysin-like protease by site-specific immobilization
    • J. Mansfeld, G. Vriend, B. Van den Burg, V.G. Eijsink, and R. Ulbrich-Hofmann Probing the unfolding region in a thermolysin-like protease by site-specific immobilization Biochemistry 38 26 1999 8240 8245
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8240-8245
    • Mansfeld, J.1    Vriend, G.2    Van Den Burg, B.3    Eijsink, V.G.4    Ulbrich-Hofmann, R.5
  • 23
    • 84856779614 scopus 로고    scopus 로고
    • Geofold: Topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability
    • V. Ramakrishnan, S.P. Srinivasan, S.M. Salem, S.J. Matthews, W. Colon, M. Zaki, and B. Christopher Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability Proteins 80 3 2012 920 934
    • (2012) Proteins , vol.80 , Issue.3 , pp. 920-934
    • Ramakrishnan, V.1    Srinivasan, S.P.2    Salem, S.M.3    Matthews, S.J.4    Colon, W.5    Zaki, M.6    Christopher, B.7
  • 25
    • 0030220763 scopus 로고    scopus 로고
    • Engineering enzymes for stability
    • A. Shaw, and R. Bott Engineering enzymes for stability Curr. Opin. Struct. Biol. 6 4 1996 546 550
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , Issue.4 , pp. 546-550
    • Shaw, A.1    Bott, R.2
  • 26
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • J.M. Sanchez-Ruiz Protein kinetic stability Biophys. Chem. 148 1-3 2010 1 15
    • (2010) Biophys. Chem. , vol.148 , Issue.13 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 28
    • 0037880487 scopus 로고    scopus 로고
    • MODIP revisited: Re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins
    • V.S. Dani, C. Ramakrishnan, and R. Varadarajan MODIP revisited: re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins Protein Eng. 16 3 2003 187 193
    • (2003) Protein Eng. , vol.16 , Issue.3 , pp. 187-193
    • Dani, V.S.1    Ramakrishnan, C.2    Varadarajan, R.3
  • 29
    • 0025319751 scopus 로고
    • Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein
    • P.E. Pjura, M. Matsumura, J.A. Wozniak, and B.W. Matthews Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein Biochemistry 29 10 1990 2592 2598
    • (1990) Biochemistry , vol.29 , Issue.10 , pp. 2592-2598
    • Pjura, P.E.1    Matsumura, M.2    Wozniak, J.A.3    Matthews, B.W.4
  • 30
    • 81455154479 scopus 로고    scopus 로고
    • Study and design of stability in GH5 cellulases
    • S. Badieyan, D.R. Bevan, and C. Zhang Study and design of stability in GH5 cellulases Biotechnol. Bioeng. 109 1 2012 31 44
    • (2012) Biotechnol. Bioeng. , vol.109 , Issue.1 , pp. 31-44
    • Badieyan, S.1    Bevan, D.R.2    Zhang, C.3
  • 32
  • 33
    • 0036227252 scopus 로고    scopus 로고
    • Molecular dynamics simulations as a tool for improving protein stability
    • M.G. Pikkemaat, A.B. Linssen, H.J. Berendsen, and D.B. Janssen Molecular dynamics simulations as a tool for improving protein stability Protein Eng. 15 3 2002 185 192
    • (2002) Protein Eng. , vol.15 , Issue.3 , pp. 185-192
    • Pikkemaat, M.G.1    Linssen, A.B.2    Berendsen, H.J.3    Janssen, D.B.4
  • 34
    • 84895488683 scopus 로고    scopus 로고
    • Engineering proteins for thermostability through Rigidifying Flexible Sites (RFS)
    • 10.1016/j.biotechadv.2013.10.012
    • H. Yu, and H. Huang Engineering proteins for thermostability through Rigidifying Flexible Sites (RFS) Biotechnol. Adv. 2013 10.1016/j.biotechadv. 2013.10.012
    • (2013) Biotechnol. Adv.
    • Yu, H.1    Huang, H.2
  • 35
    • 84857440017 scopus 로고    scopus 로고
    • Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge
    • Q.A. Le, J.C. Joo, Y.J. Yoo, and Y.H. Kim Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge Biotechnol. Bioeng. 109 4 2012 867 876
    • (2012) Biotechnol. Bioeng. , vol.109 , Issue.4 , pp. 867-876
    • Le, Q.A.1    Joo, J.C.2    Yoo, Y.J.3    Kim, Y.H.4
  • 36
    • 0031439702 scopus 로고    scopus 로고
    • Analysis of temperature factor distribution in high-resolution protein structures
    • S. Parthasarathy, and M.R. Murthy Analysis of temperature factor distribution in high-resolution protein structures Protein Sci. 6 12 1997 2561 2567
    • (1997) Protein Sci. , vol.6 , Issue.12 , pp. 2561-2567
    • Parthasarathy, S.1    Murthy, M.R.2
  • 37
    • 84892368542 scopus 로고    scopus 로고
    • Prediction of temperature factors from protein sequence
    • S. Sonavane, A.A. Jaybhaye, and A.G. Jadhav Prediction of temperature factors from protein sequence Bioinformation 9 3 2013 134 140
    • (2013) Bioinformation , vol.9 , Issue.3 , pp. 134-140
    • Sonavane, S.1    Jaybhaye, A.A.2    Jadhav, A.G.3
  • 38
    • 68049143439 scopus 로고    scopus 로고
    • On the relation between residue flexibility and local solvent accessibility in proteins
    • H. Zhang, T. Zhang, K. Chen, S. Shen, J. Ruan, and L. Kurgan On the relation between residue flexibility and local solvent accessibility in proteins Proteins 76 3 2009 617 636
    • (2009) Proteins , vol.76 , Issue.3 , pp. 617-636
    • Zhang, H.1    Zhang, T.2    Chen, K.3    Shen, S.4    Ruan, J.5    Kurgan, L.6
  • 40
    • 84865331978 scopus 로고    scopus 로고
    • Identifying disordered regions in proteins by limited proteolysis
    • A. Fontana, P.P. de Laureto, B. Spolaore, and E. Frare Identifying disordered regions in proteins by limited proteolysis Methods Mol. Biol. 896 2012 297 318
    • (2012) Methods Mol. Biol. , vol.896 , pp. 297-318
    • Fontana, A.1    De Laureto, P.P.2    Spolaore, B.3    Frare, E.4
  • 42
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • S.J. Hubbard The structural aspects of limited proteolysis of native proteins Biochim. Biophys. Acta 1382 2 1998 191 206
    • (1998) Biochim. Biophys. Acta , vol.1382 , Issue.2 , pp. 191-206
    • Hubbard, S.J.1
  • 43
    • 0023007337 scopus 로고
    • Computer-aided model-building strategies for protein design
    • C.O. Pabo, and E.G. Suchanek Computer-aided model-building strategies for protein design Biochemistry 25 20 1986 5987 5991
    • (1986) Biochemistry , vol.25 , Issue.20 , pp. 5987-5991
    • Pabo, C.O.1    Suchanek, E.G.2
  • 44
    • 0024046835 scopus 로고
    • Model building of disulfide bonds in proteins with known three-dimensional structure
    • B. Hazes, and B.W. Dijkstra Model building of disulfide bonds in proteins with known three-dimensional structure Protein Eng. 2 2 1988 119 125
    • (1988) Protein Eng. , vol.2 , Issue.2 , pp. 119-125
    • Hazes, B.1    Dijkstra, B.W.2
  • 45
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • R. Sowdhamini, N. Srinivasan, B. Shoichet, D.V. Santi, C. Ramakrishnan, and P. Balaram Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis Protein Eng. 3 2 1989 95 103
    • (1989) Protein Eng. , vol.3 , Issue.2 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 46
    • 0141506109 scopus 로고    scopus 로고
    • Disulfide by design: A computational method for the rational design of disulfide bonds in proteins
    • A.A. Dombkowski Disulfide by design: a computational method for the rational design of disulfide bonds in proteins Bioinformatics 19 14 2003 1852 1853
    • (2003) Bioinformatics , vol.19 , Issue.14 , pp. 1852-1853
    • Dombkowski, A.A.1
  • 47
    • 0034529140 scopus 로고    scopus 로고
    • Disulfide recognition in an optimized threading potential
    • A.A. Dombkowski, and G.M. Crippen Disulfide recognition in an optimized threading potential Protein Eng. 13 10 2000 679 689
    • (2000) Protein Eng. , vol.13 , Issue.10 , pp. 679-689
    • Dombkowski, A.A.1    Crippen, G.M.2
  • 48
    • 34249882805 scopus 로고    scopus 로고
    • Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase
    • B. Asgeirsson, B.V. Adalbjornsson, and G.A. Gylfason Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase Biochim. Biophys. Acta 1774 6 2007 679 687
    • (2007) Biochim. Biophys. Acta , vol.1774 , Issue.6 , pp. 679-687
    • Asgeirsson, B.1    Adalbjornsson, B.V.2    Gylfason, G.A.3
  • 49
    • 33646543361 scopus 로고    scopus 로고
    • The closed structure of presequence protease PreP forms a unique 10 000 Angstroms3 chamber for proteolysis
    • K.A. Johnson, S. Bhushan, A. Stahl, B.M. Hallberg, A. Frohn, E. Glaser, and T. Eneqvist The closed structure of presequence protease PreP forms a unique 10 000 Angstroms3 chamber for proteolysis EMBO J. 25 9 2006 1977 1986
    • (2006) EMBO J. , vol.25 , Issue.9 , pp. 1977-1986
    • Johnson, K.A.1    Bhushan, S.2    Stahl, A.3    Hallberg, B.M.4    Frohn, A.5    Glaser, E.6    Eneqvist, T.7
  • 50
    • 53049087303 scopus 로고    scopus 로고
    • Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently
    • Q. Guo, J.E. Jureller, J.T. Warren, E. Solomaha, J. Florian, and W.J. Tang Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently J. Biol. Chem. 283 35 2008 23836 23845
    • (2008) J. Biol. Chem. , vol.283 , Issue.35 , pp. 23836-23845
    • Guo, Q.1    Jureller, J.E.2    Warren, J.T.3    Solomaha, E.4    Florian, J.5    Tang, W.J.6
  • 51
    • 33747730278 scopus 로고    scopus 로고
    • The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity
    • D. Meinhold, M. Beach, Y. Shao, R. Osuna, and W. Colon The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity Biochemistry 45 32 2006 9767 9777
    • (2006) Biochemistry , vol.45 , Issue.32 , pp. 9767-9777
    • Meinhold, D.1    Beach, M.2    Shao, Y.3    Osuna, R.4    Colon, W.5
  • 52
    • 33748282179 scopus 로고    scopus 로고
    • Multi-template approach to modeling engineered disulfide bonds
    • J.L. Pellequer, and S.W. Chen Multi-template approach to modeling engineered disulfide bonds Proteins 65 1 2006 192 202
    • (2006) Proteins , vol.65 , Issue.1 , pp. 192-202
    • Pellequer, J.L.1    Chen, S.W.2
  • 53
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • M. Karplus, and G.A. Petsko Molecular dynamics simulations in biology Nature 347 6294 1990 631 639
    • (1990) Nature , vol.347 , Issue.6294 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 55
    • 33646943202 scopus 로고    scopus 로고
    • Molecular dynamics: Survey of methods for simulating the activity of proteins
    • S.A. Adcock, and J.A. McCammon Molecular dynamics: survey of methods for simulating the activity of proteins Chem. Rev. 106 5 2006 1589 1615
    • (2006) Chem. Rev. , vol.106 , Issue.5 , pp. 1589-1615
    • Adcock, S.A.1    McCammon, J.A.2
  • 56
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • Y. Shen, A. Joachimiak, M.R. Rosner, and W.J. Tang Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism Nature 443 7113 2006 870 874
    • (2006) Nature , vol.443 , Issue.7113 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.J.4
  • 57
    • 84867379923 scopus 로고    scopus 로고
    • Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding
    • A. Hoffmann, A.H. Becker, B. Zachmann-Brand, E. Deuerling, B. Bukau, and G. Kramer Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding Mol. Cell 48 1 2012 63 74
    • (2012) Mol. Cell , vol.48 , Issue.1 , pp. 63-74
    • Hoffmann, A.1    Becker, A.H.2    Zachmann-Brand, B.3    Deuerling, E.4    Bukau, B.5    Kramer, G.6
  • 59
    • 84861876642 scopus 로고    scopus 로고
    • Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine
    • S.E. Glynn, A.R. Nager, T.A. Baker, and R.T. Sauer Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine Nat. Struct. Mol. Biol. 19 6 2012 616 622
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , Issue.6 , pp. 616-622
    • Glynn, S.E.1    Nager, A.R.2    Baker, T.A.3    Sauer, R.T.4
  • 61
    • 80053595082 scopus 로고    scopus 로고
    • Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies
    • T. Hard Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies FEBS J. 278 20 2011 3884 3892
    • (2011) FEBS J. , vol.278 , Issue.20 , pp. 3884-3892
    • Hard, T.1
  • 63
    • 77955680341 scopus 로고    scopus 로고
    • A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation
    • T. Yamaguchi, H. Yagi, Y. Goto, K. Matsuzaki, and M. Hoshino A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation Biochemistry 49 33 2010 7100 7107
    • (2010) Biochemistry , vol.49 , Issue.33 , pp. 7100-7107
    • Yamaguchi, T.1    Yagi, H.2    Goto, Y.3    Matsuzaki, K.4    Hoshino, M.5
  • 65
    • 77954995716 scopus 로고    scopus 로고
    • Design and introduction of a disulfide bridge in firefly luciferase: Increase of thermostability and decrease of pH sensitivity
    • M. Imani, S. Hosseinkhani, S. Ahmadian, and M. Nazari Design and introduction of a disulfide bridge in firefly luciferase: increase of thermostability and decrease of pH sensitivity Photochem. Photobiol. Sci. 9 8 2010 1167 1177
    • (2010) Photochem. Photobiol. Sci. , vol.9 , Issue.8 , pp. 1167-1177
    • Imani, M.1    Hosseinkhani, S.2    Ahmadian, S.3    Nazari, M.4
  • 66
    • 79959841388 scopus 로고    scopus 로고
    • Design of disulfide bridge as an alternative mechanism for color shift in firefly luciferase and development of secreted luciferase
    • M. Nazari, and S. Hosseinkhani Design of disulfide bridge as an alternative mechanism for color shift in firefly luciferase and development of secreted luciferase Photochem. Photobiol. Sci. 10 7 2011 1203 1215
    • (2011) Photochem. Photobiol. Sci. , vol.10 , Issue.7 , pp. 1203-1215
    • Nazari, M.1    Hosseinkhani, S.2
  • 67
    • 84873327580 scopus 로고    scopus 로고
    • Step-wise addition of disulfide bridge in firefly luciferase controls color shift through a flexible loop: A thermodynamic perspective
    • M. Nazari, S. Hosseinkhani, and L. Hassani Step-wise addition of disulfide bridge in firefly luciferase controls color shift through a flexible loop: a thermodynamic perspective Photochem. Photobiol. Sci. 12 2 2013 298 308
    • (2013) Photochem. Photobiol. Sci. , vol.12 , Issue.2 , pp. 298-308
    • Nazari, M.1    Hosseinkhani, S.2    Hassani, L.3
  • 68
    • 70349464722 scopus 로고    scopus 로고
    • Engineering monomeric streptavidin and its ligands with infinite affinity in binding but reversibility in interaction
    • S.C. Wu, K.K. Ng, and S.L. Wong Engineering monomeric streptavidin and its ligands with infinite affinity in binding but reversibility in interaction Proteins 77 2 2009 404 412
    • (2009) Proteins , vol.77 , Issue.2 , pp. 404-412
    • Wu, S.C.1    Ng, K.K.2    Wong, S.L.3
  • 69
    • 84888312300 scopus 로고    scopus 로고
    • Disulfide by design 2.0: A web-based tool for disulfide engineering in proteins
    • [Epub ahead of print] PubMed PMID: 24289175
    • Craig, D.B., and Dombkowski, A.A. (2013) Disulfide by design 2.0: a web-based tool for disulfide engineering in proteins. Bioinformatics. 14 (1), 346. [Epub ahead of print] PubMed PMID: 24289175. http://dx.doi.org/10.1186/ 1471-2105-14-346.
    • (2013) Bioinformatics , vol.14 , Issue.1 , pp. 346
    • Craig, D.B.1    Dombkowski, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.