-
1
-
-
0032787876
-
Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
-
Kapust R.B., Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8:1999;1668-1674.
-
(1999)
Protein Sci.
, vol.8
, pp. 1668-1674
-
-
Kapust, R.B.1
Waugh, D.S.2
-
2
-
-
0029828233
-
Stratagies for achieving high-level expression of genes in Escherichia coli
-
Makrides S.C. Stratagies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:1996;512-538.
-
(1996)
Microbiol. Rev.
, vol.60
, pp. 512-538
-
-
Makrides, S.C.1
-
3
-
-
0032789940
-
A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
-
Armstrong N., de Lencastre A., Gouaux E. A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci. 8:1999;1475-1483.
-
(1999)
Protein Sci.
, vol.8
, pp. 1475-1483
-
-
Armstrong, N.1
De Lencastre, A.2
Gouaux, E.3
-
4
-
-
0028103565
-
Improving protein solubility through rationally designed amino acid replacements: Solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase
-
Dale G.E., Broger C., Langen H., D'Arcy A., Stuber D. Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase. Protein Eng. 7:1994;933-939.
-
(1994)
Protein Eng.
, vol.7
, pp. 933-939
-
-
Dale, G.E.1
Broger, C.2
Langen, H.3
D'Arcy, A.4
Stuber, D.5
-
5
-
-
0031779918
-
Design, structure and stability of a hyperthermophilic protein variant
-
Malakauskas S.M., Mayo S.L. Design, structure and stability of a hyperthermophilic protein variant. Nat. Struct. Biol. 5:1998;470-475.
-
(1998)
Nat. Struct. Biol.
, vol.5
, pp. 470-475
-
-
Malakauskas, S.M.1
Mayo, S.L.2
-
6
-
-
0035040915
-
Adaptation of a thermophilic enzyme 3-isopropylmalate dehydrogenase to low temperatures
-
Suzuki T., Yasugi M., Arisaka F., Yamagishi A., Oshima T. Adaptation of a thermophilic enzyme 3-isopropylmalate dehydrogenase to low temperatures. Protein Eng. 14:2001;85-91.
-
(2001)
Protein Eng.
, vol.14
, pp. 85-91
-
-
Suzuki, T.1
Yasugi, M.2
Arisaka, F.3
Yamagishi, A.4
Oshima, T.5
-
7
-
-
0035183586
-
Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution
-
Sun L., Petrounia I.P., Yagasaki M., Bandara G., Arnold F. Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution. Protein Eng. 14:2001;699-704.
-
(2001)
Protein Eng.
, vol.14
, pp. 699-704
-
-
Sun, L.1
Petrounia, I.P.2
Yagasaki, M.3
Bandara, G.4
Arnold, F.5
-
8
-
-
0035712796
-
Directed enzyme evolution
-
A comprehensive review of recent advances in methodologies for engineering enzymes with enhanced functionality and stability, with emphasis on methods for creating and screening functional diversity.
-
Farinas E.T., Butler T., Arnold F. Directed enzyme evolution. Curr. Opin. Biotechnol. 12:2001;545-551 A comprehensive review of recent advances in methodologies for engineering enzymes with enhanced functionality and stability, with emphasis on methods for creating and screening functional diversity.
-
(2001)
Curr. Opin. Biotechnol.
, vol.12
, pp. 545-551
-
-
Farinas, E.T.1
Butler, T.2
Arnold, F.3
-
10
-
-
0028050350
-
Rapid evolution of a protein in vitro by DNA shuffling
-
Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 370:1994;389-391.
-
(1994)
Nature
, vol.370
, pp. 389-391
-
-
Stemmer, W.P.C.1
-
11
-
-
0030754926
-
Optimization of DNA shuffling for high fidelity recombination
-
Zhao H., Arnold F.H. Optimization of DNA shuffling for high fidelity recombination. Nucleic Acids Res. 25:1997;1307-1308.
-
(1997)
Nucleic Acids Res.
, vol.25
, pp. 1307-1308
-
-
Zhao, H.1
Arnold, F.H.2
-
12
-
-
0035421962
-
Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression
-
The first example of a published crystal structure of a recalcitrant protein engineered by a single round of mutagenesis and screening using the GFP fusion folding reporter assay.
-
Kim C.A., Phillips M.L., Kim W., Gingery M., Tran H.H., Robinson M.A., Faham S., Bowie J.U. Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression. EMBO J. 20:2001;4173-4182 The first example of a published crystal structure of a recalcitrant protein engineered by a single round of mutagenesis and screening using the GFP fusion folding reporter assay.
-
(2001)
EMBO J.
, vol.20
, pp. 4173-4182
-
-
Kim, C.A.1
Phillips, M.L.2
Kim, W.3
Gingery, M.4
Tran, H.H.5
Robinson, M.A.6
Faham, S.7
Bowie, J.U.8
-
13
-
-
0036177544
-
Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a β-ketoacyl carrier protein reductase homologue
-
Yang J.K., Park M., Waldo G.S., Suh S. Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a β-ketoacyl carrier protein reductase homologue. Acta Crystallogr. D. 58:2002;303-305.
-
(2002)
Acta Crystallogr. D
, vol.58
, pp. 303-305
-
-
Yang, J.K.1
Park, M.2
Waldo, G.S.3
Suh, S.4
-
14
-
-
0036713170
-
Engineering soluble proteins for structural genomics
-
The first example of a published crystal structure of a recalcitrant protein engineered using multiple rounds of directed evolution driven by the GFP fusion folding reporter assay.
-
Pedelacq J.-D., Piltch E., Liong E.C., Berendzen J., Kim C.-Y., Rho B.-S., Park M.S., Terwilliger T.C., Waldo G.S. Engineering soluble proteins for structural genomics. Nat. Biotechnol. 20:2002;927-932 The first example of a published crystal structure of a recalcitrant protein engineered using multiple rounds of directed evolution driven by the GFP fusion folding reporter assay.
-
(2002)
Nat. Biotechnol.
, vol.20
, pp. 927-932
-
-
Pedelacq, J.-D.1
Piltch, E.2
Liong, E.C.3
Berendzen, J.4
Kim, C.-Y.5
Rho, B.-S.6
Park, M.S.7
Terwilliger, T.C.8
Waldo, G.S.9
-
15
-
-
0036308719
-
Mutations that reduce aggregation of the Alzheimer's A beta 42 peptide: An unbiased search for the sequence determinants of A beta amyloidogenesis
-
Demonstration that the GFP folding reporter can be used to select more soluble variants of a protein normally associated with slow aggregation.
-
Wurth C., Guimard N.K., Hecht M.H. Mutations that reduce aggregation of the Alzheimer's A beta 42 peptide: an unbiased search for the sequence determinants of A beta amyloidogenesis. J. Mol. Biol. 319:2002;1279-1290 Demonstration that the GFP folding reporter can be used to select more soluble variants of a protein normally associated with slow aggregation.
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 1279-1290
-
-
Wurth, C.1
Guimard, N.K.2
Hecht, M.H.3
-
16
-
-
0034816151
-
Random PCR-based screening for soluble domains using green fluorescent protein
-
The authors demonstrate that the GFP folding reporter can be used to find soluble subdomains of a large insoluble protein by screening a random fragment library. The approach is especially promising for NMR and crystallographic studies of otherwise intractable proteins.
-
Kawasaki M., Inagaki F. Random PCR-based screening for soluble domains using green fluorescent protein. Biochem. Biophys. Res. Commun. 280:2001;842-844 The authors demonstrate that the GFP folding reporter can be used to find soluble subdomains of a large insoluble protein by screening a random fragment library. The approach is especially promising for NMR and crystallographic studies of otherwise intractable proteins.
-
(2001)
Biochem. Biophys. Res. Commun.
, vol.280
, pp. 842-844
-
-
Kawasaki, M.1
Inagaki, F.2
-
18
-
-
0035025314
-
Libraries of hybrid proteins from distantly related sequences
-
The authors selected an interspecies hybrid library for protein variants with improved solubility using fusions with chloramphenicol resistance protein, before the application of a lower-throughput functional assay.
-
Sieber V., Martinez C.A., Arnold F.H. Libraries of hybrid proteins from distantly related sequences. Nat. Biotechnol. 19:2001;456-460 The authors selected an interspecies hybrid library for protein variants with improved solubility using fusions with chloramphenicol resistance protein, before the application of a lower-throughput functional assay.
-
(2001)
Nat. Biotechnol.
, vol.19
, pp. 456-460
-
-
Sieber, V.1
Martinez, C.A.2
Arnold, F.H.3
-
19
-
-
0036434301
-
An approach for reducing unwanted oligomerisation of DsRed fusion proteins
-
Gavin P., Devenish R.J., Prescott M. An approach for reducing unwanted oligomerisation of DsRed fusion proteins. Biochem. Biophys. Res. Commun. 298:2002;707-713.
-
(2002)
Biochem. Biophys. Res. Commun.
, vol.298
, pp. 707-713
-
-
Gavin, P.1
Devenish, R.J.2
Prescott, M.3
-
20
-
-
0035130371
-
Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
-
The authors fused lacZα to several test proteins and complementation with the lacZΩ fragment as a solubility reporter assay. Restored enzymatic activity of the lacZ was positively correlated with test protein solubility.
-
Wigley W.C., Stidham R.D., Smith N.M., Hunt J.F., Thomas P.J. Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat. Biotechnol. 19:2001;131-136 The authors fused lacZα to several test proteins and complementation with the lacZΩ fragment as a solubility reporter assay. Restored enzymatic activity of the lacZ was positively correlated with test protein solubility.
-
(2001)
Nat. Biotechnol.
, vol.19
, pp. 131-136
-
-
Wigley, W.C.1
Stidham, R.D.2
Smith, N.M.3
Hunt, J.F.4
Thomas, P.J.5
-
21
-
-
0035424708
-
Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments
-
Michnick S.W. Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments. Curr. Opin. Struct. Biol. 11:2001;472-477.
-
(2001)
Curr. Opin. Struct. Biol.
, vol.11
, pp. 472-477
-
-
Michnick, S.W.1
-
22
-
-
0035941063
-
Antigen-independent selection of stable intracellular single-chain antibodies
-
Fusion of single-chain antibodies to a genetically selectable marker protein allows the identification of soluble single chains expressed in yeast cytoplasm.
-
Auf der Maur A., Escher D., Barberis A. Antigen-independent selection of stable intracellular single-chain antibodies. FEBS Lett. 508:2001;407-412 Fusion of single-chain antibodies to a genetically selectable marker protein allows the identification of soluble single chains expressed in yeast cytoplasm.
-
(2001)
FEBS Lett.
, vol.508
, pp. 407-412
-
-
Auf der Maur, A.1
Escher, D.2
Barberis, A.3
-
23
-
-
0033568093
-
Hypersensitive substrate for ribonucleases
-
Keleman B.R., Klink T.A., Behhlke M.A., Eubanks S.R., Leland P.A., Raines R.T. Hypersensitive substrate for ribonucleases. Nucleic Acids Res. 27:1999;3696-3701.
-
(1999)
Nucleic Acids Res.
, vol.27
, pp. 3696-3701
-
-
Keleman, B.R.1
Klink, T.A.2
Behhlke, M.A.3
Eubanks, S.R.4
Leland, P.A.5
Raines, R.T.6
-
24
-
-
0031729179
-
Selecting proteins with improved stability by a phage-based method
-
Sieber V., Pluckthun A., Schmid F.X. Selecting proteins with improved stability by a phage-based method. Nat. Biotechnol. 16:1998;955-960.
-
(1998)
Nat. Biotechnol.
, vol.16
, pp. 955-960
-
-
Sieber, V.1
Pluckthun, A.2
Schmid, F.X.3
-
25
-
-
0033584889
-
Selection for improved protein stability by phage display
-
Jung S., Honegger A., Pluckthun A. Selection for improved protein stability by phage display. J. Mol. Biol. 294:1999;163-180.
-
(1999)
J. Mol. Biol.
, vol.294
, pp. 163-180
-
-
Jung, S.1
Honegger, A.2
Pluckthun, A.3
-
26
-
-
0035827175
-
In-vitro selection of highly stabilized protein variants with optimized surface
-
Martin A., Sieber V., Schmid F.X. In-vitro selection of highly stabilized protein variants with optimized surface. J. Mol. Biol. 309:2001;717-726.
-
(2001)
J. Mol. Biol.
, vol.309
, pp. 717-726
-
-
Martin, A.1
Sieber, V.2
Schmid, F.X.3
-
27
-
-
0035100492
-
A "loop entropy reduction" phage-display selection for folded amino acid sequences
-
A permissive site for the presentation of peptides on phage-displayed SH2 domain was used as a stratagem to select folded from unfolded sequences, using the function of the SH2 domain for selection. This provides an example of fusion selection in which the test polypeptide is displayed at an internal permissive site, rather than on the ends of the reporter domain.
-
Minard P., Scalley-Kim M., Watters A., Baker D. A "loop entropy reduction" phage-display selection for folded amino acid sequences. Protein Sci. 10:2001;129-134 A permissive site for the presentation of peptides on phage-displayed SH2 domain was used as a stratagem to select folded from unfolded sequences, using the function of the SH2 domain for selection. This provides an example of fusion selection in which the test polypeptide is displayed at an internal permissive site, rather than on the ends of the reporter domain.
-
(2001)
Protein Sci.
, vol.10
, pp. 129-134
-
-
Minard, P.1
Scalley-Kim, M.2
Watters, A.3
Baker, D.4
-
28
-
-
0001141671
-
Green fluorescent protein as a noninvasive stress probe in resting Escherichia coli cells
-
Cha H.J., Srivastava R., Vakharia V.N., Rao G., Bentley W.E. Green fluorescent protein as a noninvasive stress probe in resting Escherichia coli cells. Appl. Environ. Microbiol. 65:1999;409-414.
-
(1999)
Appl. Environ. Microbiol.
, vol.65
, pp. 409-414
-
-
Cha, H.J.1
Srivastava, R.2
Vakharia, V.N.3
Rao, G.4
Bentley, W.E.5
-
29
-
-
0033672578
-
A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli
-
Gill R.T., Valdes J.J., Bentley W.E. A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli. Metab. Eng. 2:2000;178-189.
-
(2000)
Metab. Eng.
, vol.2
, pp. 178-189
-
-
Gill, R.T.1
Valdes, J.J.2
Bentley, W.E.3
-
30
-
-
0036295371
-
Silent mutations affect in vivo protein folding in Escherichia coli
-
Cortazzo P., Cerveñansky C., Marín M., Reiss C., Ehrlich R., Deana A. Silent mutations affect in vivo protein folding in Escherichia coli. Biochem. Biophys. Res. Comm. 293:2002;547-551.
-
(2002)
Biochem. Biophys. Res. Comm.
, vol.293
, pp. 547-551
-
-
Cortazzo, P.1
Cerveñansky, C.2
Marín, M.3
Reiss, C.4
Ehrlich, R.5
Deana, A.6
-
31
-
-
0036213467
-
Gene expression response to misfolded protein as a screen for soluble recombinant protein
-
The heat shock promoter IbpA is used to drive the expression of the lacZ reporter gene, whose expression is up-regulated during expression of misfolded recombinant polypeptides. The authors use the stress reporter and an antipolyhistidine antibody blot assay to distinguish soluble, partially soluble, and insoluble protein expression, and to identify a small soluble domain from a library of fragments of a larger insoluble protein.
-
Lesley S.A., Graziano J., Cho C.Y., Knuth M.W., Klock H.E. Gene expression response to misfolded protein as a screen for soluble recombinant protein. Protein Eng. 15:2002;153-160 The heat shock promoter IbpA is used to drive the expression of the lacZ reporter gene, whose expression is up-regulated during expression of misfolded recombinant polypeptides. The authors use the stress reporter and an antipolyhistidine antibody blot assay to distinguish soluble, partially soluble, and insoluble protein expression, and to identify a small soluble domain from a library of fragments of a larger insoluble protein.
-
(2002)
Protein Eng.
, vol.15
, pp. 153-160
-
-
Lesley, S.A.1
Graziano, J.2
Cho, C.Y.3
Knuth, M.W.4
Klock, H.E.5
-
32
-
-
0035477627
-
Screening for soluble expression of recombinant proteins in a 96-well format
-
Knaust R.K.C., Nordlund P. Screening for soluble expression of recombinant proteins in a 96-well format. Anal. Biochem. 297:2001;79-85.
-
(2001)
Anal. Biochem.
, vol.297
, pp. 79-85
-
-
Knaust, R.K.C.1
Nordlund, P.2
-
33
-
-
0035891782
-
Isolation of viral coat protein mutants with altered assembly and aggregation properties
-
Colonies expressing recombinant proteins are lysed in an agarose overlay and the liberated proteins diffuse at rates dependent on their molecular sizes. The proteins are transferred to a membrane and visualized by antibody probe.
-
Peabody D.S., Al-Bitar L. Isolation of viral coat protein mutants with altered assembly and aggregation properties. Nucleic Acids Res. 29:2001;E113 Colonies expressing recombinant proteins are lysed in an agarose overlay and the liberated proteins diffuse at rates dependent on their molecular sizes. The proteins are transferred to a membrane and visualized by antibody probe.
-
(2001)
Nucleic Acids Res.
, vol.29
, pp. 113
-
-
Peabody, D.S.1
Al-Bitar, L.2
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