-
1
-
-
0030220851
-
Engineering new functions and altering existing functions
-
of special interest. A review summarizing recent work on protein re-engineering using rational and random mutagenesis strategies.
-
Shao Z, Arnold FH. Engineering new functions and altering existing functions. of special interest Curr Opin Struct Biol. 6:1996;513-518 A review summarizing recent work on protein re-engineering using rational and random mutagenesis strategies.
-
(1996)
Curr Opin Struct Biol
, vol.6
, pp. 513-518
-
-
Shao, Z.1
Arnold, F.H.2
-
2
-
-
0027499733
-
Soluble proteins: Size, shape and function
-
Goodsell DS, Olson AJ. Soluble proteins: size, shape and function. Trends Biochem Sci. 18:1993;65-68.
-
(1993)
Trends Biochem Sci
, vol.18
, pp. 65-68
-
-
Goodsell, D.S.1
Olson, A.J.2
-
3
-
-
0001265337
-
Genetic selection strategies for generating and characterizing catalysts
-
of special interest. This review highlights the use of genetic selection strategies in vivo to develop novel biocatalysts.
-
Kast P, Hilvert D. Genetic selection strategies for generating and characterizing catalysts. of special interest Pure Appl Chem. 68:1996;2017-2024 This review highlights the use of genetic selection strategies in vivo to develop novel biocatalysts.
-
(1996)
Pure Appl Chem
, vol.68
, pp. 2017-2024
-
-
Kast, P.1
Hilvert, D.2
-
4
-
-
0031029551
-
Protein design: The choice of de novo sequences
-
of special interest. Sequence randomization experiments to define requirements for protein structural features such as turns and packing are reviewed.
-
Beasley JR, Hecht MH. Protein design: the choice of de novo sequences. of special interest J Biol Chem. 272:1997;2031-3034 Sequence randomization experiments to define requirements for protein structural features such as turns and packing are reviewed.
-
(1997)
J Biol Chem
, vol.272
, pp. 2031-3034
-
-
Beasley, J.R.1
Hecht, M.H.2
-
5
-
-
0002983608
-
Protein folding from a combinatorial perspective
-
of outstanding interest. This interesting short review emphasizes the contribution of combinatorial mutagenesis and selection experiments in the elucidation of factors that govern protein structure and folding.
-
Sauer RT. Protein folding from a combinatorial perspective. of outstanding interest Fold Des. 1:1996;R27-R30 This interesting short review emphasizes the contribution of combinatorial mutagenesis and selection experiments in the elucidation of factors that govern protein structure and folding.
-
(1996)
Fold des
, vol.1
-
-
Sauer, R.T.1
-
6
-
-
0023949179
-
Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences
-
Reidhaar-Olson JF, Sauer RT. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. Science. 241:1988;53-57.
-
(1988)
Science
, vol.241
, pp. 53-57
-
-
Reidhaar-Olson, J.F.1
Sauer, R.T.2
-
7
-
-
0025712476
-
Stable, monomeric variants of λ Cro obtained by insertion of a designed β-hairpin sequence
-
Mossing MC, Sauer RT. Stable, monomeric variants of λ Cro obtained by insertion of a designed β-hairpin sequence. Science. 250:1990;1712-1715.
-
(1990)
Science
, vol.250
, pp. 1712-1715
-
-
Mossing, M.C.1
Sauer, R.T.2
-
8
-
-
2142754052
-
In Vitro Mutagenesis Protocols
-
of special interest. M.K. Trower. Humana Press Totowa, NJ, This volume includes a compilation of up-to-date DNA mutagenesis protocols for both site-directed and random approaches. Individual chapters are written by leading scientists in the field.
-
of special interest Trower MK. In Vitro Mutagenesis Protocols. Methods in Molecular Biology. 57:1996;Humana Press, Totowa, NJ, This volume includes a compilation of up-to-date DNA mutagenesis protocols for both site-directed and random approaches. Individual chapters are written by leading scientists in the field.
-
(1996)
Methods in Molecular Biology
, vol.57
-
-
-
9
-
-
0029992806
-
Combinatorial Chemistry
-
of special interest. J.N. Abelson. Academic Press, New York, NY, This volume contains a variety of reports and protocols relevant to the creation of large combinatorial libraries
-
of special interest Abelson JN. Combinatorial Chemistry. Methods in Enzymology. 267:1996;Academic Press, New York, NY, This volume contains a variety of reports and protocols relevant to the creation of large combinatorial libraries.
-
(1996)
Methods in Enzymology
, vol.267
-
-
-
10
-
-
0028110130
-
DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
-
Stemmer WPC. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc Natl Acad Sci USA. 91:1994;10747-10751.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10747-10751
-
-
Stemmer, W.P.C.1
-
11
-
-
0029001752
-
Searching sequence space
-
Stemmer WPC. Searching sequence space. Bio-Technology. 13:1995;549-553.
-
(1995)
Bio-Technology
, vol.13
, pp. 549-553
-
-
Stemmer, W.P.C.1
-
12
-
-
0029785464
-
Potential use of additivity of mutational effects in simplifying protein engineering
-
of special interest. Crystallographic analyses of the proteins encoded by mutant forms of the bacteriophage f1 gene V confirm that the effects of single mutations are structurally (and functionally) additive if the regions affected by the mutations do not substantially overlap.
-
Skinner MM, Terwilliger TC. Potential use of additivity of mutational effects in simplifying protein engineering. of special interest Proc Natl Acad Sci USA. 93:1996;10753-10757 Crystallographic analyses of the proteins encoded by mutant forms of the bacteriophage f1 gene V confirm that the effects of single mutations are structurally (and functionally) additive if the regions affected by the mutations do not substantially overlap.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10753-10757
-
-
Skinner, M.M.1
Terwilliger, T.C.2
-
13
-
-
0029670577
-
Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
-
of special interest. The catalytic activity of an esterase toward an industrial substrate in the presence of an organic solvent was improved by sequential iterations of mutagenesis and screening. It was shown that accumulated mutations were additive.
-
Moore JC, Arnold FH. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. of special interest Nat Biotechnol. 14:1996;458-467 The catalytic activity of an esterase toward an industrial substrate in the presence of an organic solvent was improved by sequential iterations of mutagenesis and screening. It was shown that accumulated mutations were additive.
-
(1996)
Nat Biotechnol
, vol.14
, pp. 458-467
-
-
Moore, J.C.1
Arnold, F.H.2
-
14
-
-
0029961638
-
Selection of Streptomyces griseus protease B mutants with desired alterations in primary specificity using a library screening strategy
-
Sidhu SS, Borgford TJ. Selection of Streptomyces griseus protease B mutants with desired alterations in primary specificity using a library screening strategy. J Mol Biol. 257:1996;233-245.
-
(1996)
J Mol Biol
, vol.257
, pp. 233-245
-
-
Sidhu, S.S.1
Borgford, T.J.2
-
15
-
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0029868515
-
Selection of RNA-binding peptides in vivo
-
of outstanding interest. A novel strategy is described for the detection of RNA binding in vivo on the basis of antitermination of lacZ transcription. Although this work employs only screening to detect interesting clones, a slightly modified version of this system may allow for genuine selection.
-
Harada K, Martin SS, Frankel AD. Selection of RNA-binding peptides in vivo. of outstanding interest Nature. 380:1996;175-179 A novel strategy is described for the detection of RNA binding in vivo on the basis of antitermination of lacZ transcription. Although this work employs only screening to detect interesting clones, a slightly modified version of this system may allow for genuine selection.
-
(1996)
Nature
, vol.380
, pp. 175-179
-
-
Harada, K.1
Martin, S.S.2
Frankel, A.D.3
-
16
-
-
0030566807
-
Core mutants of the immunoglobulin binding domain of streptococcal protein G: Stability and structural integrity
-
Gronenborn AM, Frank MK, Clore GM. Core mutants of the immunoglobulin binding domain of streptococcal protein G: stability and structural integrity. FEBS Lett. 398:1996;312-316.
-
(1996)
FEBS Lett
, vol.398
, pp. 312-316
-
-
Gronenborn, A.M.1
Frank, M.K.2
Clore, G.M.3
-
17
-
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0030133645
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Glubodies: Randomized libraries of glutathione transferase enzymes
-
of special interest. An alternative to the immunoglobulin framework has been developed for the binding of small organic molecules. A few members of libraries containing randomized loops for ligand binding were screened for interactions with potential inhibitors.
-
Napolitano EW, Villar HO, Kauvar LM, Higgins DL, Roberts D, Mandac J, Lee SK, Engqvist-Goldstein Å, Bukar R, Calio BL, et al. Glubodies: randomized libraries of glutathione transferase enzymes. of special interest Chem Biol. 3:1996;359-367 An alternative to the immunoglobulin framework has been developed for the binding of small organic molecules. A few members of libraries containing randomized loops for ligand binding were screened for interactions with potential inhibitors.
-
(1996)
Chem Biol
, vol.3
, pp. 359-367
-
-
Napolitano, E.W.1
Villar, H.O.2
Kauvar, L.M.3
Higgins, D.L.4
Roberts, D.5
Mandac, J.6
Lee, S.K.7
Engqvist-Goldstein, Å.8
Bukar, R.9
Calio, B.L.10
-
18
-
-
12644264319
-
Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo
-
of special interest. A laborious in vivo screening procedure led to the identification of a potent anticoagulant thrombin variant from a combinatorial library.
-
Tsiang M, Paborsky LR, Li W-X, Jain AK, Mao CT, Dunn KE, Lee DW, Matsumura SY, Matteucci MD, Coutré SE, et al. Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo. of special interest Biochemistry. 35:1996;16449-16457 A laborious in vivo screening procedure led to the identification of a potent anticoagulant thrombin variant from a combinatorial library.
-
(1996)
Biochemistry
, vol.35
, pp. 16449-16457
-
-
Tsiang, M.1
Paborsky, L.R.2
Li, W.-X.3
Jain, A.K.4
Mao, C.T.5
Dunn, K.E.6
Lee, D.W.7
Matsumura, S.Y.8
Matteucci, M.D.9
Coutré, S.E.10
-
19
-
-
0029779670
-
Mutational analysis of a transmembrane segment in a bacterial chemoreceptor
-
Baumgartner JW, Hazelbauer GL. Mutational analysis of a transmembrane segment in a bacterial chemoreceptor. J Bacteriol. 178:1996;4651-4660.
-
(1996)
J Bacteriol
, vol.178
, pp. 4651-4660
-
-
Baumgartner, J.W.1
Hazelbauer, G.L.2
-
20
-
-
0029926618
-
In vitro evolution of thermodynamically stable turns
-
of special interest. Libraries of protein G (B1 domain) variants with a randomized β-turn region were displayed on phage as fusions to the gene III protein and were subsequently screened for their thermodynamic stability by binding to IgG at different temperatures.
-
Zhou HX, Hoess RH, DeGrado WF. In vitro evolution of thermodynamically stable turns. of special interest Nat Struct Biol. 3:1996;446-451 Libraries of protein G (B1 domain) variants with a randomized β-turn region were displayed on phage as fusions to the gene III protein and were subsequently screened for their thermodynamic stability by binding to IgG at different temperatures.
-
(1996)
Nat Struct Biol
, vol.3
, pp. 446-451
-
-
Zhou, H.X.1
Hoess, R.H.2
Degrado, W.F.3
-
21
-
-
0029838225
-
Substitutions of Ser for Asn-163 and Pro for Leu-264 are important for stabilization of lipase from Pseudomonas aeruginosa
-
Shinkai A, Hirano A, Aisaka K. Substitutions of Ser for Asn-163 and Pro for Leu-264 are important for stabilization of lipase from Pseudomonas aeruginosa. J Biochem. 120:1996;915-921.
-
(1996)
J Biochem
, vol.120
, pp. 915-921
-
-
Shinkai, A.1
Hirano, A.2
Aisaka, K.3
-
22
-
-
0029969577
-
Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
-
You L, Arnold FH. Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 9:1996;77-83.
-
(1996)
Protein Eng
, vol.9
, pp. 77-83
-
-
You, L.1
Arnold, F.H.2
-
23
-
-
0029102175
-
Phage display: Protein engineering by directed evolution
-
O'Neil KT, Hoess RH. Phage display: protein engineering by directed evolution. Curr Opin Struct Biol. 5:1995;443-449.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 443-449
-
-
O'Neil, K.T.1
Hoess, R.H.2
-
24
-
-
0030271501
-
Phage display of proteins
-
Dunn IS. Phage display of proteins. Curr Opin Biotechnol. 7:1996;547-553.
-
(1996)
Curr Opin Biotechnol
, vol.7
, pp. 547-553
-
-
Dunn, I.S.1
-
25
-
-
0030561123
-
Selection of biologically active peptides by phage display of random peptide libraries
-
Cortese R, Monaci P, Luzzago A, Santini C, Bartoli F, Cortese I, Fortugno P, Galfrè G, Nicosia A, Felici F. Selection of biologically active peptides by phage display of random peptide libraries. Curr Opin Biotechnol. 7:1996;616-621.
-
(1996)
Curr Opin Biotechnol
, vol.7
, pp. 616-621
-
-
Cortese, R.1
Monaci, P.2
Luzzago, A.3
Santini, C.4
Bartoli, F.5
Cortese, I.6
Fortugno, P.7
Galfrè, G.8
Nicosia, A.9
Felici, F.10
-
26
-
-
0029984192
-
Phage presentation
-
of special interest. This review covers the history, general principles and different variations and applications of phage display, while giving some background about the architecture and life cycle of filamentous phage.
-
Hill HR, Stockley PG. Phage presentation. of special interest Mol Microbiol. 20:1996;685-692 This review covers the history, general principles and different variations and applications of phage display, while giving some background about the architecture and life cycle of filamentous phage.
-
(1996)
Mol Microbiol
, vol.20
, pp. 685-692
-
-
Hill, H.R.1
Stockley, P.G.2
-
27
-
-
0030570513
-
Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage
-
Malik P, Terry TD, Gowda LR, Langara A, Petukhov SA, Symmons MF, Welsh LC, Marvin DA, Perham RN. Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. J Mol Biol. 260:1996;9-21.
-
(1996)
J Mol Biol
, vol.260
, pp. 9-21
-
-
Malik, P.1
Terry, T.D.2
Gowda, L.R.3
Langara, A.4
Petukhov, S.A.5
Symmons, M.F.6
Welsh, L.C.7
Marvin, D.A.8
Perham, R.N.9
-
28
-
-
0029896174
-
Affinity maturation of phage-displayed peptide ligands
-
Yu J, Smith GP. Affinity maturation of phage-displayed peptide ligands. Methods Enzymol. 267:1996;3-27.
-
(1996)
Methods Enzymol
, vol.267
, pp. 3-27
-
-
Yu, J.1
Smith, G.P.2
-
29
-
-
0029927067
-
Phage display of proteases and macromolecular inhibitors
-
Wang C-I, Yang Q, Craik CS. Phage display of proteases and macromolecular inhibitors. Methods Enzymol. 267:1996;52-68.
-
(1996)
Methods Enzymol
, vol.267
, pp. 52-68
-
-
Wang, C.-I.1
Yang, Q.2
Craik, C.S.3
-
32
-
-
0018263844
-
Why genes in pieces?
-
Gilbert W. Why genes in pieces? Nature. 271:1978;501.
-
(1978)
Nature
, vol.271
, pp. 501
-
-
Gilbert, W.1
-
33
-
-
0030048583
-
Construction and evolution of antibody-phage libraries by DNA shuffling
-
7) scFv fragment libraries and proved to be superior to other mutagenesis strategies. The authors point out that in order to select high-affinity binders, it is more effective to start with small but evolving libraries than to simply purify clones from existing larger antibody repertoires. The observation that the evolved scFv fragment lacked affinity for its target when not displayed on phage illustrates a weakness of the technology.
-
7) scFv fragment libraries and proved to be superior to other mutagenesis strategies. The authors point out that in order to select high-affinity binders, it is more effective to start with small but evolving libraries than to simply purify clones from existing larger antibody repertoires. The observation that the evolved scFv fragment lacked affinity for its target when not displayed on phage illustrates a weakness of the technology.
-
(1996)
Nat Med
, vol.2
, pp. 100-102
-
-
Crameri, A.1
Cwirla, S.2
Stemmer, W.P.C.3
-
34
-
-
0028088274
-
The progeny of sexual PCR
-
Smith GP. The progeny of sexual PCR. Nature. 370:1994;324-325.
-
(1994)
Nature
, vol.370
, pp. 324-325
-
-
Smith, G.P.1
-
35
-
-
0029994999
-
Coupling protein design and in vitro selection strategies: Improving specificity and affinity of a designed β-protein IL-6 antagonist
-
Martin F, Toniatti C, Salvati AL, Ciliberto G, Cortese R, Sollazzo M. Coupling protein design and in vitro selection strategies: improving specificity and affinity of a designed β-protein IL-6 antagonist. J Mol Biol. 255:1996;86-97.
-
(1996)
J Mol Biol
, vol.255
, pp. 86-97
-
-
Martin, F.1
Toniatti, C.2
Salvati, A.L.3
Ciliberto, G.4
Cortese, R.5
Sollazzo, M.6
-
36
-
-
0028763728
-
Routes to catalysis: Structure of a catalytic antibody and comparison with its natural counterpart
-
Haynes MR, Stura EA, Hilvert D, Wilson IA. Routes to catalysis: structure of a catalytic antibody and comparison with its natural counterpart. Science. 263:1994;646-652.
-
(1994)
Science
, vol.263
, pp. 646-652
-
-
Haynes, M.R.1
Stura, E.A.2
Hilvert, D.3
Wilson, I.A.4
-
37
-
-
0029955258
-
Selection of linkers for a catalytic single-chain antibody using phage display technology
-
6 different linker variants for the best binders to a transition-state analog. In the second step, 1054 of these clones were screened for high levels of soluble scFv protein. All of the functional linker variants possessed a proline residue at positions 1, 2 or 3 of the 18-residue linker.
-
6 different linker variants for the best binders to a transition-state analog. In the second step, 1054 of these clones were screened for high levels of soluble scFv protein. All of the functional linker variants possessed a proline residue at positions 1, 2 or 3 of the 18-residue linker.
-
(1996)
J Biol Chem
, vol.271
, pp. 15682-15686
-
-
Tang, Y.1
Jiang, N.2
Parakh, C.3
Hilvert, D.4
-
39
-
-
0029894775
-
Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin
-
Markland W, Ley AC, Ladner RC. Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin. Biochemistry. 35:1996;8058-8067.
-
(1996)
Biochemistry
, vol.35
, pp. 8058-8067
-
-
Markland, W.1
Ley, A.C.2
Ladner, R.C.3
-
40
-
-
0031053362
-
A general strategy for selecting high-affinity zinc finger proteins for diverse DNA target sites
-
of outstanding interest. This excellent paper describes the sequential evolution of Zif268, a three zinc finger protein, into highly specific TATA box, p53 binding site, or nuclear receptor element binding proteins. The exchange of one finger domain at a time, followed by binding selection using phage display allows context-dependent interactions between individual fingers to be considered. The new proteins bound their DNA targets with subnanomolar dissociation constants and discriminated as effectively as wild-type Zif268 against nonspecific DNA. No simple code for correlating amino acid identities in individual fingers with their recognized DNA sequence could be established.
-
Greisman HA, Pabo CO. A general strategy for selecting high-affinity zinc finger proteins for diverse DNA target sites. of outstanding interest Science. 275:1997;657-661 This excellent paper describes the sequential evolution of Zif268, a three zinc finger protein, into highly specific TATA box, p53 binding site, or nuclear receptor element binding proteins. The exchange of one finger domain at a time, followed by binding selection using phage display allows context-dependent interactions between individual fingers to be considered. The new proteins bound their DNA targets with subnanomolar dissociation constants and discriminated as effectively as wild-type Zif268 against nonspecific DNA. No simple code for correlating amino acid identities in individual fingers with their recognized DNA sequence could be established.
-
(1997)
Science
, vol.275
, pp. 657-661
-
-
Greisman, H.A.1
Pabo, C.O.2
-
42
-
-
0029927342
-
Systematic mutagenesis of the active site omega loop of TEM-1 β-lactamase
-
Petrosino JF, Palzkill T. Systematic mutagenesis of the active site omega loop of TEM-1 β-lactamase. J Bacteriol. 178:1996;1821-1828.
-
(1996)
J Bacteriol
, vol.178
, pp. 1821-1828
-
-
Petrosino, J.F.1
Palzkill, T.2
-
43
-
-
0029829133
-
Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 β-lactamase with altered substrate specificity for aztreonam and ceftazidime
-
Cantu C III, Huang W, Palzkill T. Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 β-lactamase with altered substrate specificity for aztreonam and ceftazidime. J Biol Chem. 271:1996;22538-22545.
-
(1996)
J Biol Chem
, vol.271
, pp. 22538-22545
-
-
Cantu C. III1
Huang, W.2
Palzkill, T.3
-
44
-
-
0029962946
-
Amino acid sequence determinants of β-lactamase structure and activity
-
of special interest. All 263 codons constituting the mature form of TEM-1 β-lactamase were randomized using 88 individual random libraries to probe the importance of each amino acid position. 220 positions were found to tolerate substitutions leaving much sequence space available for the evolution of novel antibiotic specificities. A statistical correlation was established between residue variability and surface exposure. Interestingly, some residues that were determined to be absolutely conserved here can be freely substituted among other members of the β-lactamase protein family.
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Huang W, Petrosino J, Hirsch M, Shenkin PS, Palzkill T. Amino acid sequence determinants of β-lactamase structure and activity. of special interest J Mol Biol. 258:1996;688-703 All 263 codons constituting the mature form of TEM-1 β-lactamase were randomized using 88 individual random libraries to probe the importance of each amino acid position. 220 positions were found to tolerate substitutions leaving much sequence space available for the evolution of novel antibiotic specificities. A statistical correlation was established between residue variability and surface exposure. Interestingly, some residues that were determined to be absolutely conserved here can be freely substituted among other members of the β-lactamase protein family.
-
(1996)
J Mol Biol
, vol.258
, pp. 688-703
-
-
Huang, W.1
Petrosino, J.2
Hirsch, M.3
Shenkin, P.S.4
Palzkill, T.5
-
45
-
-
0029981387
-
Human immunodeficiency virus reverse transcriptase. Functional mutants obtained by random mutagenesis coupled with genetic selection in Escherichia coli
-
of special interest. Randomizing mutagenesis was targeted to the gene segment that encodes a region in HIV reverse transcriptase that may be responsible for interactions with nucleic acid templates. Many clinical isolates from HIV patients treated with nucleoside analogs contain alterations in this region. Genetic selection from the partially randomized library resulted in a variety of active variants which included many previously discovered resistance mutations. Such experiments have a great potential to uncover 'immutable' sites as targets for chemotherapy.
-
Kim B, Hathaway TR, Loeb LA. Human immunodeficiency virus reverse transcriptase. Functional mutants obtained by random mutagenesis coupled with genetic selection in Escherichia coli. of special interest J Biol Chem. 271:1996;4872-4878 Randomizing mutagenesis was targeted to the gene segment that encodes a region in HIV reverse transcriptase that may be responsible for interactions with nucleic acid templates. Many clinical isolates from HIV patients treated with nucleoside analogs contain alterations in this region. Genetic selection from the partially randomized library resulted in a variety of active variants which included many previously discovered resistance mutations. Such experiments have a great potential to uncover 'immutable' sites as targets for chemotherapy.
-
(1996)
J Biol Chem
, vol.271
, pp. 4872-4878
-
-
Kim, B.1
Hathaway, T.R.2
Loeb, L.A.3
-
46
-
-
0029929724
-
Novel human DNA alkyltransferases obtained by random substitution and genetic selection in bacteria
-
of special interest. A stringent in vivo selection system in an E. coli ada ogt mutant strain was developed. The region around the active-site cysteine of the human enzyme was probed for functional information content, and a variant that provided improved alkylation protection in vivo was obtained. In vitro data to support this finding, however, were not provided.
-
Christians FC, Loeb LA. Novel human DNA alkyltransferases obtained by random substitution and genetic selection in bacteria. of special interest Proc Natl Acad Sci USA. 93:1996;6124-6128 A stringent in vivo selection system in an E. coli ada ogt mutant strain was developed. The region around the active-site cysteine of the human enzyme was probed for functional information content, and a variant that provided improved alkylation protection in vivo was obtained. In vitro data to support this finding, however, were not provided.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 6124-6128
-
-
Christians, F.C.1
Loeb, L.A.2
-
47
-
-
0029999832
-
Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: The importance of electrostatic catalysis
-
of special interest. A novel complementation system was developed to select for monofunctional chorismate mutase activity in vivo. The mechanistic hypothesis of charge stabilization in the transition state by Arg90 of BsCM was examined by randomization of one or two strategically placed residues. The results show the potential of combinatorial mutagenesis and selection to recover alternative solutions to a given chemical problem. Comparisons with the active-site structure of the unrelated enzyme from E. coli were made.
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Kast P, Asif-Ullah M, Jiang N, Hilvert D. Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis. of special interest Proc Natl Acad Sci USA. 93:1996;5043-5048 A novel complementation system was developed to select for monofunctional chorismate mutase activity in vivo. The mechanistic hypothesis of charge stabilization in the transition state by Arg90 of BsCM was examined by randomization of one or two strategically placed residues. The results show the potential of combinatorial mutagenesis and selection to recover alternative solutions to a given chemical problem. Comparisons with the active-site structure of the unrelated enzyme from E. coli were made.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 5043-5048
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Kast, P.1
Asif-Ullah, M.2
Jiang, N.3
Hilvert, D.4
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48
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0030058137
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Electrostatic catalysis of the Claisen rearrangement: Probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection
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of special interest. Using a similar strategy as described in the previous reference [47], the importance of a negative charge in the active site of BsCM was examined. Combinatorial mutagenesis of codons 75 and 78 (encoding cysteine and glutamate in the wild type, respectively) showed that wild-type-like activity in vivo requires a carboxylic acid at one of the two positions. Some of the selected alternatives resemble the active site of the unrelated E. coli chorismate mutase.
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Kast P, Hartgerink JD, Asif-Ullah M, Hilvert D. Electrostatic catalysis of the Claisen rearrangement: probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection. of special interest J Am Chem Soc. 118:1996;3069-3070 Using a similar strategy as described in the previous reference [47], the importance of a negative charge in the active site of BsCM was examined. Combinatorial mutagenesis of codons 75 and 78 (encoding cysteine and glutamate in the wild type, respectively) showed that wild-type-like activity in vivo requires a carboxylic acid at one of the two positions. Some of the selected alternatives resemble the active site of the unrelated E. coli chorismate mutase.
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(1996)
J Am Chem Soc
, vol.118
, pp. 3069-3070
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Kast, P.1
Hartgerink, J.D.2
Asif-Ullah, M.3
Hilvert, D.4
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50
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0030016226
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A rapid screen of active site mutants in glycinamide ribonucleotide transformylase
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Warren MS, Marolewski AE, Benkovic SJ. A rapid screen of active site mutants in glycinamide ribonucleotide transformylase. Biochemistry. 35:1996;8855-8862.
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(1996)
Biochemistry
, vol.35
, pp. 8855-8862
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Warren, M.S.1
Marolewski, A.E.2
Benkovic, S.J.3
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51
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0029989171
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Exploring the functional robustness of an enzyme by in vitro evolution
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of outstanding interest. This excellent study used RNA hypermutagenesis with HIV reverse transcriptase and unbalanced dNTP ratios to iteratively mutagenize the gene for dihydrofolate reductase from plasmid R67. The gene for the 78-residue enzyme could be extensively mutagenized yielding up to 17 amino acid replacements without loosing its activity or tetramerization and substrate-binding properties. The role of the N-terminal amino acids, which are dispensable for activity but provide tolerance to the remaining 56 residues to substitution, still remains to be elucidated.
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Martinez MA, Pezo V, Marlière P, Wain-Hobson S. Exploring the functional robustness of an enzyme by in vitro evolution. of outstanding interest EMBO J. 15:1996;1203-1210 This excellent study used RNA hypermutagenesis with HIV reverse transcriptase and unbalanced dNTP ratios to iteratively mutagenize the gene for dihydrofolate reductase from plasmid R67. The gene for the 78-residue enzyme could be extensively mutagenized yielding up to 17 amino acid replacements without loosing its activity or tetramerization and substrate-binding properties. The role of the N-terminal amino acids, which are dispensable for activity but provide tolerance to the remaining 56 residues to substitution, still remains to be elucidated.
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(1996)
EMBO J
, vol.15
, pp. 1203-1210
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Martinez, M.A.1
Pezo, V.2
Marlière, P.3
Wain-Hobson, S.4
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52
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0029904146
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Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants
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Jeltsch A, Sobotta T, Pingoud A. Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants. Protein Eng. 9:1996;413-423.
-
(1996)
Protein Eng
, vol.9
, pp. 413-423
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Jeltsch, A.1
Sobotta, T.2
Pingoud, A.3
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53
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0029882043
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Loop replacement and random mutagenesis of Ω-loop D, residues 70-84, in iso-1-cytochrome c
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Mulligan-Pullyblank P, Spitzer JS, Gilden BM, Fetrow JS. Loop replacement and random mutagenesis of Ω-loop D, residues 70-84, in iso-1-cytochrome c. J Biol Chem. 271:1996;8633-8645.
-
(1996)
J Biol Chem
, vol.271
, pp. 8633-8645
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Mulligan-Pullyblank, P.1
Spitzer, J.S.2
Gilden, B.M.3
Fetrow, J.S.4
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54
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0029845979
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Random mutagenesis of Thermus aquaticus DNA polymerase I: Concordance of immutable sites in vivo with the crystal structure
-
Suzuki M, Baskin D, Hood L, Loeb LA. Random mutagenesis of Thermus aquaticus DNA polymerase I: concordance of immutable sites in vivo with the crystal structure. Proc Natl Acad Sci USA. 93:1996;9670-9675.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 9670-9675
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Suzuki, M.1
Baskin, D.2
Hood, L.3
Loeb, L.A.4
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55
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0029863983
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In vivo selection of basic region-leucine zipper proteins with altered DNA-binding specificities
-
of special interest. Five amino acids in the basic (α-helical DNA binding) region of a CCAAT/enhancer binding protein were randomized, and the corresponding genes were subjected to selection in vivo using a previously known transcriptional interference assay [79,80]. When the wild-type DNA recognition sequence was used in the selection, the original amino acids re-emerged. Novel binding specificities in vivo could be obtained with specifically altered DNA sites. This work, however, also shows some of the limitations of this selection system regarding the discrimination of signal over noise.
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Sera T, Schultz PG. In vivo selection of basic region-leucine zipper proteins with altered DNA-binding specificities. of special interest Proc Natl Acad Sci USA. 93:1996;2920-2925 Five amino acids in the basic (α-helical DNA binding) region of a CCAAT/enhancer binding protein were randomized, and the corresponding genes were subjected to selection in vivo using a previously known transcriptional interference assay [79,80]. When the wild-type DNA recognition sequence was used in the selection, the original amino acids re-emerged. Novel binding specificities in vivo could be obtained with specifically altered DNA sites. This work, however, also shows some of the limitations of this selection system regarding the discrimination of signal over noise.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2920-2925
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Sera, T.1
Schultz, P.G.2
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56
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0030032124
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Random mutagenesis targeted to the active site of the EcoRV restriction endonuclease
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Vipond IB, Halford SE. Random mutagenesis targeted to the active site of the EcoRV restriction endonuclease. Biochemistry. 35:1996;1701-1711.
-
(1996)
Biochemistry
, vol.35
, pp. 1701-1711
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Vipond, I.B.1
Halford, S.E.2
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57
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0027407935
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A genetic approach to the generation of antibodies with enhanced catalytic activities
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Lesley SA, Patten PA, Schultz PG. A genetic approach to the generation of antibodies with enhanced catalytic activities. Proc Natl Acad Sci USA. 90:1993;1160-1165.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 1160-1165
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Lesley, S.A.1
Patten, P.A.2
Schultz, P.G.3
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58
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0029915311
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Affinity selective isolation of ligands from peptide libraries through display on a lac repressor 'headpiece dimer'
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of special interest. As an alternative to phage display, the strategy of displaying random peptide libraries on DNA-binding proteins such as Lacl was further improved. By using in vitro affinity selection of peptide - Lacl fragment-encoding plasmid complexes starting from a random linker library, a stable covalently linked dimeric variant of the Lacl head piece was obtained. Although this novel and potentially monovalent system proved to be effective in affinity selection of peptide ligands to a monoclonal antibody, the mode of plasmid DNA binding appears (unexpectedly) to be nonspecific and requires further investigation. This work is yet another example for 'you get what you select for' in that the outcome of the selection experiment did not correspond to the design, but still fulfilled the selection criterion.
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Gates CM, Stemmer WPC, Kaptein R, Schatz PJ. Affinity selective isolation of ligands from peptide libraries through display on a lac repressor 'headpiece dimer'. of special interest J Mol Biol. 255:1996;373-386 As an alternative to phage display, the strategy of displaying random peptide libraries on DNA-binding proteins such as Lacl was further improved. By using in vitro affinity selection of peptide - Lacl fragment-encoding plasmid complexes starting from a random linker library, a stable covalently linked dimeric variant of the Lacl head piece was obtained. Although this novel and potentially monovalent system proved to be effective in affinity selection of peptide ligands to a monoclonal antibody, the mode of plasmid DNA binding appears (unexpectedly) to be nonspecific and requires further investigation. This work is yet another example for 'you get what you select for' in that the outcome of the selection experiment did not correspond to the design, but still fulfilled the selection criterion.
-
(1996)
J Mol Biol
, vol.255
, pp. 373-386
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Gates, C.M.1
Stemmer, W.P.C.2
Kaptein, R.3
Schatz, P.J.4
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59
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0031037466
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Chemical selection for catalysis in combinatorial antibody libraries
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of special interest. An enriched antibody library of 100 transition-state analog binders was subjected to a novel catalysis-based in vitro selection strategy. The advantage of the selection is unclear, however, as the catalytic antibody fragment had to be identified after an in vivo screening procedure in E. coli cells.
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Janda KD, Lo L-C, Lo C-HL, Sim M-M, Wang R, Wong C-H, Lerner RA. Chemical selection for catalysis in combinatorial antibody libraries. of special interest Science. 275:1997;945-948 An enriched antibody library of 100 transition-state analog binders was subjected to a novel catalysis-based in vitro selection strategy. The advantage of the selection is unclear, however, as the catalytic antibody fragment had to be identified after an in vivo screening procedure in E. coli cells.
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(1997)
Science
, vol.275
, pp. 945-948
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Janda, K.D.1
Lo, L.-C.2
Lo, C.-H.L.3
Sim, M.-M.4
Wang, R.5
Wong, C.-H.6
Lerner, R.A.7
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60
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0028592703
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An in vitro polysome display system for identifying ligands from very large peptide libraries
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Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA. 91:1994;9022-9026.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 9022-9026
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Mattheakis, L.C.1
Bhatt, R.R.2
Dower, W.J.3
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61
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0029693534
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Cell-free synthesis of peptide libraries displayed on polysomes
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Mattheakis LC, Dias JM, Dower WJ. Cell-free synthesis of peptide libraries displayed on polysomes. Methods Enzymol. 267:1996;195-207.
-
(1996)
Methods Enzymol
, vol.267
, pp. 195-207
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Mattheakis, L.C.1
Dias, J.M.2
Dower, W.J.3
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62
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0030974119
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In vitro selection and evolution of functional proteins by using ribosome display
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Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA. 94:1997;4937-4942.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 4937-4942
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Hanes, J.1
Plückthun, A.2
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64
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0031029554
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Discrimination of a single base change in a ribozyme using the gene for dihydrofolate reductase as a selective marker in Escherichia coli
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of special interest. An in vivo selection system for ribozyme activity is proposed that is based on the acquired trimethoprim resistance of E. coli cells which occurs if an active ribozyme cleaves the primary transcript of an engineered dihydrofolate reductase gene to make the initiation region accessible for translation. Unfortunately, the signal-to-background ratio in the current configuration is too low to make this system useful for genuine evolutionary experiments.
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Fujita S, Koguma T, Ohkawa J, Mori K, Kohda T, Kise H, Nishikawa S, Iwakura M, Taira K. Discrimination of a single base change in a ribozyme using the gene for dihydrofolate reductase as a selective marker in Escherichia coli. of special interest Proc Natl Acad Sci USA. 94:1997;391-396 An in vivo selection system for ribozyme activity is proposed that is based on the acquired trimethoprim resistance of E. coli cells which occurs if an active ribozyme cleaves the primary transcript of an engineered dihydrofolate reductase gene to make the initiation region accessible for translation. Unfortunately, the signal-to-background ratio in the current configuration is too low to make this system useful for genuine evolutionary experiments.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 391-396
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-
Fujita, S.1
Koguma, T.2
Ohkawa, J.3
Mori, K.4
Kohda, T.5
Kise, H.6
Nishikawa, S.7
Iwakura, M.8
Taira, K.9
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65
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0024406857
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A novel genetic system to detect protein - protein interactions
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Fields S, Song O. A novel genetic system to detect protein - protein interactions. Nature. 340:1989;245-246.
-
(1989)
Nature
, vol.340
, pp. 245-246
-
-
Fields, S.1
Song, O.2
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66
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0028985657
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The yeast two-hybrid system for studying protein - protein interactions
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Luban J, Goff SP. The yeast two-hybrid system for studying protein - protein interactions. Curr Opin Biotechnol. 6:1995;59-64.
-
(1995)
Curr Opin Biotechnol
, vol.6
, pp. 59-64
-
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Luban, J.1
Goff, S.P.2
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67
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0029842096
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Gene identification using the yeast two-hybrid system
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Bai C, Elledge SJ. Gene identification using the yeast two-hybrid system. Methods Enzymol. 273:1996;331-347.
-
(1996)
Methods Enzymol
, vol.273
, pp. 331-347
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Bai, C.1
Elledge, S.J.2
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68
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0030272124
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Genetic and biochemical probes for protein - protein interactions
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of special interest. Recent developments in the application of the two-hybrid system and its derivatives are discussed in this useful short review, and a comprehensive list of relevant references is provided.
-
McNabb DS, Guarente L. Genetic and biochemical probes for protein - protein interactions. of special interest Curr Opin Biotechnol. 7:1996;554-559 Recent developments in the application of the two-hybrid system and its derivatives are discussed in this useful short review, and a comprehensive list of relevant references is provided.
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(1996)
Curr Opin Biotechnol
, vol.7
, pp. 554-559
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McNabb, D.S.1
Guarente, L.2
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69
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0030066615
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Determinants of helix-loop-helix dimerization affinity. Random mutational analysis of SCL/tal
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of special interest. The basic helix-loop-helix domain of the hematopoietic transcription factor SCL/tal was examined for its dimerization specificity with another transcription factor, E2-2, using the yeast two-hybrid system. Randomizing mutagenesis using error-prone PCR, coupled with selection for transcriptional activation of LEU2 (restoring leucine prototrophy), resulted in the identification of variants with higher affinity for E2-2. The structural consequences of one of the mutations were analyzed by computational modeling using the crystallographic coordinates of a related protein.
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Goldfarb AN, Lewandowska K, Shoham M. Determinants of helix-loop-helix dimerization affinity. Random mutational analysis of SCL/tal. of special interest J Biol Chem. 271:1996;2683-2688 The basic helix-loop-helix domain of the hematopoietic transcription factor SCL/tal was examined for its dimerization specificity with another transcription factor, E2-2, using the yeast two-hybrid system. Randomizing mutagenesis using error-prone PCR, coupled with selection for transcriptional activation of LEU2 (restoring leucine prototrophy), resulted in the identification of variants with higher affinity for E2-2. The structural consequences of one of the mutations were analyzed by computational modeling using the crystallographic coordinates of a related protein.
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(1996)
J Biol Chem
, vol.271
, pp. 2683-2688
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Goldfarb, A.N.1
Lewandowska, K.2
Shoham, M.3
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70
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0029876415
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Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
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of outstanding interest. A combinatorial library of 20-residue peptides displayed in the active-site loop of E. coli thioredoxin was subjected to selection in vivo using the yeast two-hybrid system. Individual recombinant proteins containing the constrained peptides were shown to bind (and inhibit) the target protein, human cyclin-dependent kinase 2. Specific in vivo selected protein aptamers that have inhibitory function inside cells could be used to dissect complex networks of protein interactions. To test whether individual free (unconstrained) peptides have inhibitory activity would be interesting.
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Colas P, Cohen B, Jessen T, Grishina I, McCoy J, Brent R. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. of outstanding interest Nature. 380:1996;548-550 A combinatorial library of 20-residue peptides displayed in the active-site loop of E. coli thioredoxin was subjected to selection in vivo using the yeast two-hybrid system. Individual recombinant proteins containing the constrained peptides were shown to bind (and inhibit) the target protein, human cyclin-dependent kinase 2. Specific in vivo selected protein aptamers that have inhibitory function inside cells could be used to dissect complex networks of protein interactions. To test whether individual free (unconstrained) peptides have inhibitory activity would be interesting.
-
(1996)
Nature
, vol.380
, pp. 548-550
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Colas, P.1
Cohen, B.2
Jessen, T.3
Grishina, I.4
McCoy, J.5
Brent, R.6
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71
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0029824170
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A three-hybrid system for detecting small ligand-protein receptor interactions
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Licitra EJ, Liu JO. A three-hybrid system for detecting small ligand-protein receptor interactions. Proc Natl Acad Sci USA. 93:1996;12817-12821.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 12817-12821
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Licitra, E.J.1
Liu, J.O.2
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72
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0029776689
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A three-hybrid system to detect RNA - protein interactions in vivo
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SenGupta DJ, Zhang B, Kraemer B, Pochart P, Fields S, Wickens M. A three-hybrid system to detect RNA - protein interactions in vivo. Proc Natl Acad Sci USA. 93:1996;8496-8501.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 8496-8501
-
-
Sengupta, D.J.1
Zhang, B.2
Kraemer, B.3
Pochart, P.4
Fields, S.5
Wickens, M.6
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73
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0029843413
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A tri-hybrid system for the analysis and detection of RNa-protein interactions
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Putz U, Skehel P, Kuhl D. A tri-hybrid system for the analysis and detection of RNa-protein interactions. Nucleic Acids Res. 24:1996;4838-4840.
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(1996)
Nucleic Acids Res
, vol.24
, pp. 4838-4840
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Putz, U.1
Skehel, P.2
Kuhl, D.3
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74
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0029809862
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Reverse two-hybrid and one-hybrid systems to detect dissociation of protein - protein and DNA - protein interactions
-
of outstanding interest. A novel method termed 'reverse two (one)-hybrid system' is introduced which allows the direct selection of proteins or peptides that have impaired protein - protein interactions. The system is based on the yeast URA3 gene, whose expression by a transcriptional activator (which binds to its promoter-proximal DNA sequence) leads to cytotoxicity in the presence of 5-fluoroorotic acid. Disruption of DNA-binding and transcriptional activation in the context of a two (one)-hybrid system allows cell survival under those conditions. This novel technology could be used to directly select for peptides and proteins that induce specific protein - protein dissociation. Such tools may be useful as therapeutic agents to reverse aberrant protein interactions associated with disease.
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Vidal M, Brachmann RK, Fattaey A, Harlow E, Boeke JD. Reverse two-hybrid and one-hybrid systems to detect dissociation of protein - protein and DNA - protein interactions. of outstanding interest Proc Natl Acad Sci USA. 93:1996;10315-10320 A novel method termed 'reverse two (one)-hybrid system' is introduced which allows the direct selection of proteins or peptides that have impaired protein - protein interactions. The system is based on the yeast URA3 gene, whose expression by a transcriptional activator (which binds to its promoter-proximal DNA sequence) leads to cytotoxicity in the presence of 5-fluoroorotic acid. Disruption of DNA-binding and transcriptional activation in the context of a two (one)-hybrid system allows cell survival under those conditions. This novel technology could be used to directly select for peptides and proteins that induce specific protein - protein dissociation. Such tools may be useful as therapeutic agents to reverse aberrant protein interactions associated with disease.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10315-10320
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Vidal, M.1
Brachmann, R.K.2
Fattaey, A.3
Harlow, E.4
Boeke, J.D.5
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75
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0029840668
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Genetic characterization of a mammalian protein - protein interaction domain by using a yeast reverse two-hybrid system
-
of special interest. The feasibility of the 'reverse two-hybrid system' is demonstrated by selecting variants from a partially mutagenized gene library encoding the C-terminal domain of transcription factor E2F1 that are unable to interact with protein DP1 (selection step 1) but are still of full length (selection step 2). Before selecting for full-length clones from those that did not bind DP1, however, plasmid curing and yeast mating was necessary.
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Vidal M, Braun P, Chen E, Boeke JD, Harlow E. Genetic characterization of a mammalian protein - protein interaction domain by using a yeast reverse two-hybrid system. of special interest Proc Natl Acad Sci USA. 93:1996;10321-10326 The feasibility of the 'reverse two-hybrid system' is demonstrated by selecting variants from a partially mutagenized gene library encoding the C-terminal domain of transcription factor E2F1 that are unable to interact with protein DP1 (selection step 1) but are still of full length (selection step 2). Before selecting for full-length clones from those that did not bind DP1, however, plasmid curing and yeast mating was necessary.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10321-10326
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Vidal, M.1
Braun, P.2
Chen, E.3
Boeke, J.D.4
Harlow, E.5
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76
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0029790263
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The yeast two-hybrid system: Forward and reverse
-
of special interest. This commentary on the reports by Vidal and coworkers [74,75] suggests a modification of the 'reverse two-hybrid system' to allow the simultaneous selection of binders to one protein and nonbinders to another. The modification would exploit genetic selection for two different auxotrophic markers, his and ura, and circumvent an involved screening option in the original system.
-
White MA. The yeast two-hybrid system: forward and reverse. of special interest Proc Natl Acad Sci USA. 93:1996;10001-10003 This commentary on the reports by Vidal and coworkers [74,75] suggests a modification of the 'reverse two-hybrid system' to allow the simultaneous selection of binders to one protein and nonbinders to another. The modification would exploit genetic selection for two different auxotrophic markers, his and ura, and circumvent an involved screening option in the original system.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10001-10003
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White, M.A.1
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77
-
-
0027274818
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Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog
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Chook YM, Ke H, Lipscomb WN. Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog. Proc Natl Acad Sci USA. 90:1993;8600-8603.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 8600-8603
-
-
Chook, Y.M.1
Ke, H.2
Lipscomb, W.N.3
-
78
-
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0027992458
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The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction
-
Chook YM, Gray JV, Ke H, Lipscomb WN. The monofunctional chorismate mutase from Bacillus subtilis: structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction. J Mol Biol. 240:1994;476-500.
-
(1994)
J Mol Biol
, vol.240
, pp. 476-500
-
-
Chook, Y.M.1
Gray, J.V.2
Ke, H.3
Lipscomb, W.N.4
-
79
-
-
0024616602
-
Position and density effects on repression by stationary and mobile DNA-binding proteins
-
Elledge SJ, Davis RW. Position and density effects on repression by stationary and mobile DNA-binding proteins. Genes Dev. 3:1989;185-197.
-
(1989)
Genes Dev
, vol.3
, pp. 185-197
-
-
Elledge, S.J.1
Davis, R.W.2
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