메뉴 건너뛰기




Volumn 9, Issue 4, 1999, Pages 494-499

Protein redesign

Author keywords

[No Author keywords available]

Indexed keywords

PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RANDOMIZATION; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0033179051     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80070-0     Document Type: Article
Times cited : (30)

References (24)
  • 1
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and protein stability in a four helix bundle protein
    • Nagi AD, Regan L: An inverse correlation between loop length and protein stability in a four helix bundle protein. Fold Des 1997, 2:67-75.
    • (1997) Fold Des , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 2
    • 0033548061 scopus 로고    scopus 로고
    • Using loop length variants to dissect the folding pathway of a four-helix-bundle protein
    • The study of the behavior of loop-length variants aids in the dissection of a folding pathway
    • Nagi AD, Anderson KS, Regan L: Using loop length variants to dissect the folding pathway of a four-helix-bundle protein. J Mol Biol 1999, 286:257-265. The study of the behavior of loop-length variants aids in the dissection of a folding pathway.
    • (1999) J Mol Biol , vol.286 , pp. 257-265
    • Nagi, A.D.1    Anderson, K.S.2    Regan, L.3
  • 3
    • 0031576337 scopus 로고    scopus 로고
    • Glutamine, alanine and glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
    • Ladurner AG, Fersht AR: Glutamine, alanine and glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. J Mol Biol 1997, 273:330-337.
    • (1997) J Mol Biol , vol.273 , pp. 330-337
    • Ladurner, A.G.1    Fersht, A.R.2
  • 4
    • 0029961470 scopus 로고    scopus 로고
    • Equilibrium stability and sub-millisecond folding of a designed single chain Arc repressor
    • Robinson CR, Sauer RT: Equilibrium stability and sub-millisecond folding of a designed single chain Arc repressor. Biochemistry 1996, 35:13878-13884.
    • (1996) Biochemistry , vol.35 , pp. 13878-13884
    • Robinson, C.R.1    Sauer, R.T.2
  • 5
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single-chain proteins by linker length and composition mutagenesis
    • Genetic selection reveals energetically optimal loop sequences and provides guidelines for future redesigns
    • Robinson CR, Sauer RT: Optimizing the stability of single-chain proteins by linker length and composition mutagenesis. Proc Natl Acad Sci USA 1998, 95:5929-5934. Genetic selection reveals energetically optimal loop sequences and provides guidelines for future redesigns.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5929-5934
    • Robinson, C.R.1    Sauer, R.T.2
  • 6
    • 0021659554 scopus 로고
    • Folding pathway of a circular form of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE: Folding pathway of a circular form of bovine pancreatic trypsin inhibitor. J Mol Biol 1984, 179:527-545
    • (1984) J Mol Biol , vol.179 , pp. 527-545
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 7
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
    • Luger K, Hommel U, Hofsteenge J, Kirschner K: Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. Science 1989, 243:206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Hofsteenge, J.3    Kirschner, K.4
  • 8
    • 0026516388 scopus 로고
    • A fully active variant of dihydrofolate reductase with a circularly permuted sequence
    • Buchwalder A, Szadkowski H, Kirschner K: A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry 1992, 31:1621-1630.
    • (1992) Biochemistry , vol.31 , pp. 1621-1630
    • Buchwalder, A.1    Szadkowski, H.2    Kirschner, K.3
  • 11
    • 0032005329 scopus 로고    scopus 로고
    • Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases
    • Ay J, Hahn M, Decanniere K, Piotukh K, Borriss R, Heinemann U: Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases. Proteins 1998, 30:155-167.
    • (1998) Proteins , vol.30 , pp. 155-167
    • Ay, J.1    Hahn, M.2    Decanniere, K.3    Piotukh, K.4    Borriss, R.5    Heinemann, U.6
  • 12
    • 0029751129 scopus 로고    scopus 로고
    • Preclinical development of a recombinant toxin containing circularly permuted interleukin 4 and truncated pseudomonas exotoxin for therapy of malignant astrocytoma
    • Puri RK, Hoon DS, Leland P, Snoy P, Rand RW, Pastan I, Kreitman RJ: Preclinical development of a recombinant toxin containing circularly permuted interleukin 4 and truncated pseudomonas exotoxin for therapy of malignant astrocytoma. Cancer Res 1996, 56:5631-5637.
    • (1996) Cancer Res , vol.56 , pp. 5631-5637
    • Puri, R.K.1    Hoon, D.S.2    Leland, P.3    Snoy, P.4    Rand, R.W.5    Pastan, I.6    Kreitman, R.J.7
  • 13
    • 0028943593 scopus 로고
    • Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Vinais ML, Corbier C, Mulliert G, Branlant C, Branlant G: Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Protein Sci 1995, 4:994-1000.
    • (1995) Protein Sci , vol.4 , pp. 994-1000
    • Vinais, M.L.1    Corbier, C.2    Mulliert, G.3    Branlant, C.4    Branlant, G.5
  • 14
    • 0029786618 scopus 로고    scopus 로고
    • Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional activity by interaction with its ligands
    • Uversky VN, Kutyshenko VP, Protasova N, Rogov VV, Vassilenko KS, Gudkov AT: Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional activity by interaction with its ligands. Protein Sci 1996, 5:1844-1851.
    • (1996) Protein Sci , vol.5 , pp. 1844-1851
    • Uversky, V.N.1    Kutyshenko, V.P.2    Protasova, N.3    Rogov, V.V.4    Vassilenko, K.S.5    Gudkov, A.T.6
  • 15
    • 0030663205 scopus 로고    scopus 로고
    • Loop length, intramolecular diffusion and protein folding
    • Viguera AR, Serrano L: Loop length, intramolecular diffusion and protein folding. Nat Struct Biol 1997, 4:939-946.
    • (1997) Nat Struct Biol , vol.4 , pp. 939-946
    • Viguera, A.R.1    Serrano, L.2
  • 16
    • 0039726624 scopus 로고    scopus 로고
    • Thermodynamic analysis of β-spectrin SH3 and two of its circular permutants: Discerning the reasons for rapid folding in proteins
    • A detailed thermodynamic analysis of circular permutants of an SH3 domain
    • Martinez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L: Thermodynamic analysis of β-spectrin SH3 and two of its circular permutants: Discerning the reasons for rapid folding in proteins. Biochemistry 1999, 38:549-559. A detailed thermodynamic analysis of circular permutants of an SH3 domain.
    • (1999) Biochemistry , vol.38 , pp. 549-559
    • Martinez, J.C.1    Viguera, A.R.2    Berisio, R.3    Wilmanns, M.4    Mateo, P.L.5    Filimonov, V.V.6    Serrano, L.7
  • 17
    • 0032474460 scopus 로고    scopus 로고
    • Folding of a circularly permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
    • A completely circular variant, a circular permutant and the wild-type protein were shown to fold by the same pathway and to have closely similar transition states
    • Otzen DE, Fersht AR: Folding of a circularly permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry 1998, 37:8139-8146. A completely circular variant, a circular permutant and the wild-type protein were shown to fold by the same pathway and to have closely similar transition states.
    • (1998) Biochemistry , vol.37 , pp. 8139-8146
    • Otzen, D.E.1    Fersht, A.R.2
  • 18
    • 0032562996 scopus 로고    scopus 로고
    • Eye lens β2-crystallin: Circular permutation does not influence the oligomeric state but enhances the conformational stability
    • Wieligmann K, Norledge B, Jaenicke R, Mayr E-M: Eye lens β2-crystallin: Circular permutation does not influence the oligomeric state but enhances the conformational stability. J Mol Biol 1998, 280:721-729.
    • (1998) J Mol Biol , vol.280 , pp. 721-729
    • Wieligmann, K.1    Norledge, B.2    Jaenicke, R.3    Mayr, E.-M.4
  • 19
    • 0032534916 scopus 로고    scopus 로고
    • Conversion of a catalytic into a structural disulfide bond by circular permutation
    • Hennecke J, Glockshuber R: Conversion of a catalytic into a structural disulfide bond by circular permutation. Biochemistry 1998, 37:17590-17597.
    • (1998) Biochemistry , vol.37 , pp. 17590-17597
    • Hennecke, J.1    Glockshuber, R.2
  • 20
    • 0031956609 scopus 로고    scopus 로고
    • Thermodynamic and structural consequences of flexible loop deletion by circular permutation of the streptavidin-biotin system
    • Chu V, Freitag S, Le Trong I, Stenkamp RE, Stayton PS: Thermodynamic and structural consequences of flexible loop deletion by circular permutation of the streptavidin-biotin system. Protein Sci 1998, 7:848-859.
    • (1998) Protein Sci , vol.7 , pp. 848-859
    • Chu, V.1    Freitag, S.2    Le Trong, I.3    Stenkamp, R.E.4    Stayton, P.S.5
  • 21
    • 0031815941 scopus 로고    scopus 로고
    • Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase
    • Iwakura M, Nakamura T: Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase. Protein Eng 1998, 8:707-713.
    • (1998) Protein Eng , vol.8 , pp. 707-713
    • Iwakura, M.1    Nakamura, T.2
  • 23
    • 0033528731 scopus 로고    scopus 로고
    • Circular permutation of the granulocyte colony-stimulating factor receptor agonist domain of myelopoietin
    • This paper (together with [22••]) describes circular permutants of GCSF, a protein that is currently administered to patients undergoing chemotherapy. Several are successful and, when fused to IL-3, create hybrid molecules with an expanded range of biological activities
    • McWherter CA, Feng Y, ZurfLuh L, Klein BK, Baganoff MP, Polazzi JO, Hood WF, Paik K, Abegg AL, Grabbe ES et al.: Circular permutation of the granulocyte colony-stimulating factor receptor agonist domain of myelopoietin. Biochemistry 1999, 38:4564-4571. This paper (together with [22••]) describes circular permutants of GCSF, a protein that is currently administered to patients undergoing chemotherapy. Several are successful and, when fused to IL-3, create hybrid molecules with an expanded range of biological activities.
    • (1999) Biochemistry , vol.38 , pp. 4564-4571
    • McWherter, C.A.1    Feng, Y.2    Zurfluh, L.3    Klein, B.K.4    Baganoff, M.P.5    Polazzi, J.O.6    Hood, W.F.7    Paik, K.8    Abegg, A.L.9    Grabbe, E.S.10
  • 24
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • An illustration of the power of genetic selection. Enzyme topology was successfully redesigned by identifying the 1 in 2000 loop sequences that could function as desired
    • MacBeath G, Kast P, Hilvert D: Redesigning enzyme topology by directed evolution. Science 1998, 279:1958-1961. An illustration of the power of genetic selection. Enzyme topology was successfully redesigned by identifying the 1 in 2000 loop sequences that could function as desired.
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.