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Antibody engineering
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Nilsson B. Antibody engineering. Curr Opin Struct Biol. 5:1995;450-456.
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0029102175
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Phage display: Protein engineering by directed evolution
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O'Neil KT, Hoess RH. Phage display: protein engineering by directed evolution. Curr Opin Struct Biol. 5:1995;443-449.
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O'Neil, K.T.1
Hoess, R.H.2
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Protein design: A hierarchic approach
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Bryson JW, Betz SF, Lu HS, Suich DJ, Zhou HX, O'Neil KT, DeGrado WF. Protein design: a hierarchic approach. Science. 270:1995;935-941.
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Bryson, J.W.1
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Zhou, H.X.5
O'Neil, K.T.6
DeGrado, W.F.7
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0029590248
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Engineering nitrile hydratase activity into a cysteine protease by a single mutation
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of outstanding interest. Peptide nitrile hydratase activity was engineered by introducing into papain a single mutation, Gln 19Glu.
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of outstanding interest Dufour E, Storer AC, Ménard R. Engineering nitrile hydratase activity into a cysteine protease by a single mutation. Biochemistry. 34:1995;16382-16388 Peptide nitrile hydratase activity was engineered by introducing into papain a single mutation, Gln 19Glu.
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Biochemistry
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Dufour, E.1
Storer, A.C.2
Ménard, R.3
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0029670330
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Improved green fluorescent protein by molecular evolution using DNA shuffling
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of special interest. `Sexual' PCR and screening improves the yield of soluble, folded green fluorescent protein without altering its excitation and emission maxima.
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of special interest Crameri A, Whitehorn EA, Tate E, Stemmer WPC. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol. 3:1996;315-319 `Sexual' PCR and screening improves the yield of soluble, folded green fluorescent protein without altering its excitation and emission maxima.
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Crameri, A.1
Whitehorn, E.A.2
Tate, E.3
Stemmer, W.P.C.4
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7
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0029670577
-
Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
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of outstanding interest. Multiple generations of random mutagenesis and screening achieve a 60-fold increase in total activity towards an antibiotic synthetic intermediate in aqueous dimethylformamide. The effective amino acid substitutions are distant from the substrate and could not have been predicted.
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of outstanding interest Moore JC, Arnold FH. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nature Biotechnol. 14:1996;458-467 Multiple generations of random mutagenesis and screening achieve a 60-fold increase in total activity towards an antibiotic synthetic intermediate in aqueous dimethylformamide. The effective amino acid substitutions are distant from the substrate and could not have been predicted.
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(1996)
Nature Biotechnol
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, pp. 458-467
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Moore, J.C.1
Arnold, F.H.2
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8
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0029113263
-
Enzyme evolution in Rhodobacter sphaeroides: Selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme
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of special interest. A new enzyme activity is obtained by continuous culture under selective pressure. The previously unknown enzyme is believed to be a result of the activation of a cryptic gene.
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of special interest Schneider KH, Jakel G, Hoffmann R, Giffhorn F. Enzyme evolution in Rhodobacter sphaeroides: selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme. Microbiology. 141:1995;1865-1873 A new enzyme activity is obtained by continuous culture under selective pressure. The previously unknown enzyme is believed to be a result of the activation of a cryptic gene.
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(1995)
Microbiology
, vol.141
, pp. 1865-1873
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Schneider, K.H.1
Jakel, G.2
Hoffmann, R.3
Giffhorn, F.4
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9
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0030032063
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Hybrid restriction enzymes: Zinc finger fusions to Fok I cleavage domain
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Kim Y-G, Cha J, Chandrasegaran S. Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain. Proc Natl Acad Sci USA. 93:1996;1156-1160.
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Proc Natl Acad Sci USA
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Kim Y-G1
Cha, J.2
Chandrasegaran, S.3
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10
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0030049811
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Construction of a multifunctional pneumococcal murein hydrolase by module assembly
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Sanz JM, Garcia P, Garcia JL. Construction of a multifunctional pneumococcal murein hydrolase by module assembly. Eur J Biochem. 235:1996;601-605.
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Sanz, J.M.1
Garcia, P.2
Garcia, J.L.3
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11
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0028857296
-
Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase
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of special interest. Engineered modular polyketide synthases can be used to generate macrolactones with shorter and longer chain lengths.
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of special interest Kao CM, Luo G, Katz L, Cane DE, Khosla C. Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase. J Am Chem Soc. 117:1995;9105-9106 Engineered modular polyketide synthases can be used to generate macrolactones with shorter and longer chain lengths.
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J Am Chem Soc
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, pp. 9105-9106
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-
Kao, C.M.1
Luo, G.2
Katz, L.3
Cane, D.E.4
Khosla, C.5
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12
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-
0029064652
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Rational redesign of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
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of special interest. The authors describe design rules for manipulation of polyketide biosynthesis by expression of combinations of polyketide synthase subunits.
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of special interest McDaniel R, Ebert-Khosla S, Hopwood DA, Khosla C. Rational redesign of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature. 375:1995;549-554 The authors describe design rules for manipulation of polyketide biosynthesis by expression of combinations of polyketide synthase subunits.
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(1995)
Nature
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, pp. 549-554
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McDaniel, R.1
Ebert-Khosla, S.2
Hopwood, D.A.3
Khosla, C.4
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13
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0029617958
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Pore-forming proteins with built-in triggers and switches
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Bayley H. Pore-forming proteins with built-in triggers and switches. Bioorg Chem. 23:1995;340-354.
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(1995)
Bioorg Chem
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, pp. 340-354
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Bayley, H.1
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15
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0029916620
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Regulation of proteolytic activity by engineered tridentate metal binding loops
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2+ concentrations.
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2+ concentrations.
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(1996)
J Am Chem Soc
, vol.118
, pp. 1227-1228
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Halfon, S.1
Craik, C.S.2
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16
-
-
0028969688
-
Engineered metal regulation of trypsin specificity
-
of special interest. Specificity for histidine-containing substrates is engineered into trypsin by creating binding sites that allow a metal ion to bridge the substrate and enzyme on the leaving group side of the scissile bond.
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of special interest Willett WS, Gillmor SA, Perona JJ, Fletterick RJ, Craik CS. Engineered metal regulation of trypsin specificity. Biochemistry. 34:1995;2172-2180 Specificity for histidine-containing substrates is engineered into trypsin by creating binding sites that allow a metal ion to bridge the substrate and enzyme on the leaving group side of the scissile bond.
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(1995)
Biochemistry
, vol.34
, pp. 2172-2180
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-
Willett, W.S.1
Gillmor, S.A.2
Perona, J.J.3
Fletterick, R.J.4
Craik, C.S.5
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17
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0025102789
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Regulation of serine protease activity by an engineered metal switch
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Higaki JN, Haymore BL, Chen S, Fletterick RJ, Craik CS. Regulation of serine protease activity by an engineered metal switch. Biochemistry. 29:1990;8582-8586.
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Biochemistry
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Higaki, J.N.1
Haymore, B.L.2
Chen, S.3
Fletterick, R.J.4
Craik, C.S.5
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18
-
-
0028800729
-
Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
-
2+ acts like a known non-peptide antagonist towards a receptor with an engineered metal-binding site.
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2+ acts like a known non-peptide antagonist towards a receptor with an engineered metal-binding site.
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(1995)
Nature
, vol.374
, pp. 74-77
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Elling, C.E.1
Nielsen, S.M.2
Schwartz, T.W.3
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19
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0029016430
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Protein design: Novel metal-binding sites
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Regan L. Protein design: novel metal-binding sites. Trends Biochem Sci. 20:1995;280-285.
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(1995)
Trends Biochem Sci
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Regan, L.1
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20
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0029163606
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Interfacial metal-binding site design
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Matthews DJ. Interfacial metal-binding site design. Curr Opin Biotechnol. 6:1995;419-424.
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Curr Opin Biotechnol
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Matthews, D.J.1
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21
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0029556755
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Rational redesign of a metal-dependent nuclease. Engineering the active site of magnesium-dependent ribonuclease H to form an active `metal-independent' enzyme
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2+. The pH activity profile is dramatically altered as a result.
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2+. The pH activity profile is dramatically altered as a result.
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(1995)
J Am Chem Soc
, vol.117
, pp. 11011-11012
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Casareno, R.L.B.1
Li, D.W.2
Cowan, J.A.3
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22
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0029557251
-
A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity
-
of special interest. Six substitutions in the adenosine-binding pocket of E. coli isocitrate dehydrogenase shift the coenzyme preference of the enzyme from NADP towards NAD. Two additional, arbitrary mutations at remote sites further improve coenzyme specificity.
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of special interest Chen R, Greer A, Dean AM. A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proc Natl Acad Sci USA. 92:1995;11666-11670 Six substitutions in the adenosine-binding pocket of E. coli isocitrate dehydrogenase shift the coenzyme preference of the enzyme from NADP towards NAD. Two additional, arbitrary mutations at remote sites further improve coenzyme specificity.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 11666-11670
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Chen, R.1
Greer, A.2
Dean, A.M.3
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23
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0030053257
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An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese
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Vipond IB, Moon BJ, Halford SE. An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese. Biochemistry. 35:1996;1712-1721.
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Biochemistry
, vol.35
, pp. 1712-1721
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Vipond, I.B.1
Moon, B.J.2
Halford, S.E.3
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24
-
-
0028874551
-
Designing subtilisin BPN′ to cleave substrates containing dibasic residues
-
of special interest. Mutants are designed on the basis of the structure of subtilisin and sequences of eukaryotic homologs that are known to cleave dibasic substrates. A library of phage particles containing five contiguous randomized residues is sorted to identify a substrate that is selectively cleaved in the context of a fusion protein.
-
of special interest Ballinger MD, Tom J, Wells JA. Designing subtilisin BPN′ to cleave substrates containing dibasic residues. Biochemistry. 34:1995;13312-13319 Mutants are designed on the basis of the structure of subtilisin and sequences of eukaryotic homologs that are known to cleave dibasic substrates. A library of phage particles containing five contiguous randomized residues is sorted to identify a substrate that is selectively cleaved in the context of a fusion protein.
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(1995)
Biochemistry
, vol.34
, pp. 13312-13319
-
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Ballinger, M.D.1
Tom, J.2
Wells, J.A.3
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25
-
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0029079958
-
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis
-
of special interest. The identity and variation in sequence alignments of related enzymes are used to locate amino acid residues essential for catalysis and substrate specificity.
-
of special interest Onuffer JJ, Kirsch JF. Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci. 4:1995;1750-1757 The identity and variation in sequence alignments of related enzymes are used to locate amino acid residues essential for catalysis and substrate specificity.
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(1995)
Protein Sci
, vol.4
, pp. 1750-1757
-
-
Onuffer, J.J.1
Kirsch, J.F.2
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26
-
-
0028973406
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1 Lys/Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidases
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1 Lys/Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidases. Biochemistry. 34:1995;15689-15699.
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(1995)
Biochemistry
, vol.34
, pp. 15689-15699
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Olesen, K.1
Breddam, K.2
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27
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0028871447
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Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering
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Yuan L, Voelker TA, Hawkins DJ. Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering. Proc Natl Acad Sci USA. 92:1995;10639-10643.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 10639-10643
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Yuan, L.1
Voelker, T.A.2
Hawkins, D.J.3
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28
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0028859754
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Inversion of enantioselectivity in hydrolysis of 1,4-dihydropyridines by point mutation of lipase PS
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Hirose Y, Kariya K, Nakanishi Y, Kurono Y, Achiwa K. Inversion of enantioselectivity in hydrolysis of 1,4-dihydropyridines by point mutation of lipase PS. Tetrahedron Lett. 36:1995;1063-1066.
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Tetrahedron Lett
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, pp. 1063-1066
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Hirose, Y.1
Kariya, K.2
Nakanishi, Y.3
Kurono, Y.4
Achiwa, K.5
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29
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0029144689
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Trypsin specificity increased through substrate-assisted catalysis
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Corey DR, Willett WS, Coombs GS, Craik CS. Trypsin specificity increased through substrate-assisted catalysis. Biochemistry. 34:1995;11521-11527.
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(1995)
Biochemistry
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, pp. 11521-11527
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Corey, D.R.1
Willett, W.S.2
Coombs, G.S.3
Craik, C.S.4
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0023384982
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Engineering enzyme specificity by `substrate-assisted catalysis'
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Carter P, Wells JA. Engineering enzyme specificity by `substrate-assisted catalysis'. Science. 237:1987;394-399.
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Science
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Carter, P.1
Wells, J.A.2
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31
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0028811156
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Conversion of thrombin into an anticoagulant by protein engineering
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Gibbs CS, Coutré SE, Tsiang M, Li WX, Jain AK, Dunn KE, Law VS, Mao CT, Matsumura SY, Mejza SJ, et al. Conversion of thrombin into an anticoagulant by protein engineering. Nature. 378:1995;413-416.
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Nature
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, pp. 413-416
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Gibbs, C.S.1
Coutré, S.E.2
Tsiang, M.3
Li, W.X.4
Jain, A.K.5
Dunn, K.E.6
Law, V.S.7
Mao, C.T.8
Matsumura, S.Y.9
Mejza, S.J.10
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32
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0029091457
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A mutant T7 RNA polymerase as a DNA polymerase
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Sousa R, Padilla R. A mutant T7 RNA polymerase as a DNA polymerase. EMBO J. 14:1995;4609-4621.
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EMBO J
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Sousa, R.1
Padilla, R.2
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33
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0029020345
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Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids
-
of special interest. Incorporation of p-chloro-phenylalanine into luciferase is demonstrated in cells expressing a relaxed substrate specificity mutant of phenylalanyl-tRNA synthetase.
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of special interest Ibba M, Hennecke H. Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids. FEBS Lett. 364:1995;272-275 Incorporation of p-chloro-phenylalanine into luciferase is demonstrated in cells expressing a relaxed substrate specificity mutant of phenylalanyl-tRNA synthetase.
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(1995)
FEBS Lett
, vol.364
, pp. 272-275
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Ibba, M.1
Hennecke, H.2
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34
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0028244324
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Substrate-specificity is determined by amino-acid binding pocket size in Escherichia coli phenylalanyl-transfer-RNA synthetase
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Ibba M, Kast P, Hennecke H. Substrate-specificity is determined by amino-acid binding pocket size in Escherichia coli phenylalanyl-transfer-RNA synthetase. Biochemistry. 33:1994;7107-7112.
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Biochemistry
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Ibba, M.1
Kast, P.2
Hennecke, H.3
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35
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0029159746
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Forced evolution of glutathione-S-transferase to create a more efficient drug detoxication enzyme
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of outstanding interest. Random mutagenesis of the H-site residues and selection are used to identify glutathione S-transferase variants better able to protect a cell against a specific electrophile.
-
of outstanding interest Gulick AM, Fahl WE. Forced evolution of glutathione-S-transferase to create a more efficient drug detoxication enzyme. Proc Natl Acad Sci USA. 92:1995;8140-8144 Random mutagenesis of the H-site residues and selection are used to identify glutathione S-transferase variants better able to protect a cell against a specific electrophile.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 8140-8144
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Gulick, A.M.1
Fahl, W.E.2
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0029008514
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Glutathione transferases with novel active-sites isolated by phage display from a library of random mutants
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Widersten M, Mannervik B. Glutathione transferases with novel active-sites isolated by phage display from a library of random mutants. J Mol Biol. 250:1995;115-122.
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J Mol Biol
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Widersten, M.1
Mannervik, B.2
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37
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0029883624
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Creation of drug specific HSV-1 thymidine kinase mutants for gene therapy
-
of outstanding interest. Randomization of codons for six amino acids adjacent to the putative nucleoside-binding site of thymidine kinase, combined with selection (for bacteria expressing active TK) and screening, yields enzymes capable of phosphorylating nucleoside analogs ganciclovir (GCV) and/or acyclovir (ACV). Mammalian cells expressing one of the mutants are more sensitive to GCV and ACV.
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of outstanding interest Black ME, Newcomb TG, Wilson HMP, Loeb LA. Creation of drug specific HSV-1 thymidine kinase mutants for gene therapy. Proc Natl Acad Sci USA. 93:1996;3525-3529 Randomization of codons for six amino acids adjacent to the putative nucleoside-binding site of thymidine kinase, combined with selection (for bacteria expressing active TK) and screening, yields enzymes capable of phosphorylating nucleoside analogs ganciclovir (GCV) and/or acyclovir (ACV). Mammalian cells expressing one of the mutants are more sensitive to GCV and ACV.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 3525-3529
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Black, M.E.1
Newcomb, T.G.2
Wilson, H.M.P.3
Loeb, L.A.4
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0028985597
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A new TEM β-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions
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Viadiu H, Osuna J, Fink AL, Soberón X. A new TEM β-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions. J Biol Chem. 270:1995;781-787.
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J Biol Chem
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Viadiu, H.1
Osuna, J.2
Fink, A.L.3
Soberón, X.4
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0029091933
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Improvement of the catalytic properties of penicillin G acylase from Escherichia coli ATCC 11105 by selection of a new substrate specificity
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Niersbach H, Kühne A, Tischer W, Weber M, Wedekind F, Plapp R. Improvement of the catalytic properties of penicillin G acylase from Escherichia coli ATCC 11105 by selection of a new substrate specificity. Appl Microbiol Biotechnol. 43:1995;679-684.
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Appl Microbiol Biotechnol
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, pp. 679-684
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Niersbach, H.1
Kühne, A.2
Tischer, W.3
Weber, M.4
Wedekind, F.5
Plapp, R.6
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40
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0028954931
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Improved specificity toward substrates with positively charged side chains by site-directed mutagenesis of the L-lactate dehydrogenase of Bacillus stearothermophilus
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Hogan JK, Pittol CA, Jones JB, Gold M. Improved specificity toward substrates with positively charged side chains by site-directed mutagenesis of the L-lactate dehydrogenase of Bacillus stearothermophilus. Biochemistry. 34:1995;4225-4230.
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Biochemistry
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, pp. 4225-4230
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Hogan, J.K.1
Pittol, C.A.2
Jones, J.B.3
Gold, M.4
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0029137716
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Partial reversal of the substrate stereospecificity of an L-lactate dehydrogenase by site-directed mutagenesis
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Sakowicz R, Gold M, Jones JB. Partial reversal of the substrate stereospecificity of an L-lactate dehydrogenase by site-directed mutagenesis. J Am Chem Soc. 117:1995;2387-2394.
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J Am Chem Soc
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Sakowicz, R.1
Gold, M.2
Jones, J.B.3
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Proteins that glow in green and blue
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Coxon A, Bestor TH. Proteins that glow in green and blue. Chem Biol. 2:1995;119-121.
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Chem Biol
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Coxon, A.1
Bestor, T.H.2
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0028832822
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Understanding, improving and using green fluorescent proteins
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Cubitt AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien TY. Understanding, improving and using green fluorescent proteins. Trends Biochem Sci. 20:1995;448-455.
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Trends Biochem Sci
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Cubitt, A.B.1
Heim, R.2
Adams, S.R.3
Boyd, A.E.4
Gross, L.A.5
Tsien, T.Y.6
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44
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0028894696
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Red-shifted excitation mutants of the green fluorescent protein
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of special interest. Combinatorial mutagenesis applied to a six-codon sequence spanning the tyrosine chromophore region and spectroscopic screening yields red-shifted GFP mutants.
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of special interest Delagrave S, Hawtin RE, Silva CM, Yang MM, Youvan DC. Red-shifted excitation mutants of the green fluorescent protein. Bio/Technology. 13:1995;151-154 Combinatorial mutagenesis applied to a six-codon sequence spanning the tyrosine chromophore region and spectroscopic screening yields red-shifted GFP mutants.
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Bio/Technology
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, pp. 151-154
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Delagrave, S.1
Hawtin, R.E.2
Silva, C.M.3
Yang, M.M.4
Youvan, D.C.5
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45
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0030087710
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Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
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of special interest. Sequential random mutagenesis and screening improve the brightness of blue-shifted GFP mutants and further shift the excitation and emission peaks of a red-shifted mutant. A fusion of linked blue- and green-fluorescent proteins exhibits fluorescence resonance energy transfer.
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of special interest Heim R, Tsien RY. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Biol. 6:1996;178-182 Sequential random mutagenesis and screening improve the brightness of blue-shifted GFP mutants and further shift the excitation and emission peaks of a red-shifted mutant. A fusion of linked blue- and green-fluorescent proteins exhibits fluorescence resonance energy transfer.
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(1996)
Curr Biol
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, pp. 178-182
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Heim, R.1
Tsien, R.Y.2
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46
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0029061274
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Green-fluorescent protein mutants with altered fluorescence excitation spectra
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Ehrig T, O'Kane DJ, Prendergast FG. Green-fluorescent protein mutants with altered fluorescence excitation spectra. FEBS Lett. 367:1995;163-166.
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FEBS Lett
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Ehrig, T.1
O'Kane, D.J.2
Prendergast, F.G.3
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47
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0028580734
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Wavelength mutations and posttranslational autoxidation of green fluorescent protein
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Kinetic and structural characterization of mutations of glycine-216 in α-lytic protease: A new target for engineering substrate specificity
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Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
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Directed evolution: Creating biocatalysts for the future
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of special interest Arnold FH. Directed evolution: creating biocatalysts for the future. Chem Eng Sci. 1996; This review describes practical strategies for directed enzyme evolution when variants must be screened rather than selected.
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