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0033548061
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Using loop length variants to dissect the folding pathway of a four-helix-bundle protein
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The study of the behavior of loop-length variants aids in the dissection of a folding pathway
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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.
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0031576337
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Glutamine, alanine and glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
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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.
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Genetic selection reveals energetically optimal loop sequences and provides guidelines for future redesigns
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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.
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A fully active variant of dihydrofolate reductase with a circularly permuted sequence
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Permutins of interleukin 1 beta-a simplified approach for the construction of permuted proteins having new termini
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Horlick RA, George HJ, Cooke GM, Tritch RJ, Newton RC, Dwivedi A, Lischwe M, Salemme FR, Weber PC, Horuk R: Permutins of interleukin 1 beta-a simplified approach for the construction of permuted proteins having new termini. Protein Eng 1992, 5:427-431.
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Zhange T, Bertelsen E, Benvegnu D, Alber T: Circular permutation of T4 lysozyme. Biochemistry 1993, 32:12311-12318.
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Zhange, T.1
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0032005329
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Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases
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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.
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0029751129
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Preclinical development of a recombinant toxin containing circularly permuted interleukin 4 and truncated pseudomonas exotoxin for therapy of malignant astrocytoma
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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.
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0028943593
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Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
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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.
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0029786618
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Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional activity by interaction with its ligands
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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.
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Rogov, V.V.4
Vassilenko, K.S.5
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Loop length, intramolecular diffusion and protein folding
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Viguera AR, Serrano L: Loop length, intramolecular diffusion and protein folding. Nat Struct Biol 1997, 4:939-946.
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Serrano, L.2
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Thermodynamic analysis of β-spectrin SH3 and two of its circular permutants: Discerning the reasons for rapid folding in proteins
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A detailed thermodynamic analysis of circular permutants of an SH3 domain
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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.
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Martinez, J.C.1
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Mateo, P.L.5
Filimonov, V.V.6
Serrano, L.7
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17
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0032474460
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Folding of a circularly permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
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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
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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.
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Biochemistry
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Otzen, D.E.1
Fersht, A.R.2
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18
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0032562996
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Eye lens β2-crystallin: Circular permutation does not influence the oligomeric state but enhances the conformational stability
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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.
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Wieligmann, K.1
Norledge, B.2
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19
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0032534916
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Conversion of a catalytic into a structural disulfide bond by circular permutation
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Hennecke J, Glockshuber R: Conversion of a catalytic into a structural disulfide bond by circular permutation. Biochemistry 1998, 37:17590-17597.
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Hennecke, J.1
Glockshuber, R.2
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20
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0031956609
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Thermodynamic and structural consequences of flexible loop deletion by circular permutation of the streptavidin-biotin system
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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.
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Chu, V.1
Freitag, S.2
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Stenkamp, R.E.4
Stayton, P.S.5
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21
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0031815941
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Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase
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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.
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Protein Eng
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Iwakura, M.1
Nakamura, T.2
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22
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0033528665
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Circular permutation of granulocyte colony-stimulating factor
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See annotation to [23••]
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Feng Y, Minnerly JC, Zurfluh LL, Joy WD, Hood WF, Abegg AL, Grabbe ES, Shieh J-J, Thurman TL, McKearn JP, McWherter CA: Circular permutation of granulocyte colony-stimulating factor. Biochemistry 1999, 38:4553-4563. See annotation to [23••].
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Biochemistry
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Feng, Y.1
Minnerly, J.C.2
Zurfluh, L.L.3
Joy, W.D.4
Hood, W.F.5
Abegg, A.L.6
Grabbe, E.S.7
Shieh, J.-J.8
Thurman, T.L.9
McKearn, J.P.10
McWherter, C.A.11
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23
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0033528731
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Circular permutation of the granulocyte colony-stimulating factor receptor agonist domain of myelopoietin
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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
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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.
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Biochemistry
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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
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24
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0032549781
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Redesigning enzyme topology by directed evolution
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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
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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.
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Science
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MacBeath, G.1
Kast, P.2
Hilvert, D.3
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