-
1
-
-
0028592703
-
An in vitro polysome display system for identifying ligands from very large peptide libraries
-
Mattheakis L.C., Bhatt R.R., Dower W.J. 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
-
-
Mattheakis, L.C.1
Bhatt, R.R.2
Dower, W.J.3
-
2
-
-
0031574037
-
Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
-
He M., Taussig M.J. Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. Nucleic Acids Res. 25:1997;5132-5134.
-
(1997)
Nucleic Acids Res
, vol.25
, pp. 5132-5134
-
-
He, M.1
Taussig, M.J.2
-
3
-
-
0030974119
-
In vitro selection and evolution of functional proteins by using ribosome display
-
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.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 4937-4942
-
-
Hanes, J.1
Plückthun, A.2
-
4
-
-
0030817279
-
RNA-peptide fusions for the in vitro selection of peptides and proteins
-
15, and does not require selection conditions that hinge on the preservation of an intact ternary ribosome-mRNA-peptide complex as in ribosome display.
-
15, and does not require selection conditions that hinge on the preservation of an intact ternary ribosome-mRNA-peptide complex as in ribosome display.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 12297-12302
-
-
Roberts, R.W.1
Szostak, J.W.2
-
5
-
-
0031854986
-
Man-made cell-like compartments for molecular evolution
-
The method described here restricts diffusion of a reaction product within aqueous droplets in an oil-water emulsion. This is particularly useful for finding catalytic proteins, because catalyst-modified substrate can be selected by attachment to the enzyme-coding gene.
-
Tawfik D.S., Griffiths A.D. Man-made cell-like compartments for molecular evolution. Nat Biotechnol. 16:1998;652-656. The method described here restricts diffusion of a reaction product within aqueous droplets in an oil-water emulsion. This is particularly useful for finding catalytic proteins, because catalyst-modified substrate can be selected by attachment to the enzyme-coding gene.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 652-656
-
-
Tawfik, D.S.1
Griffiths, A.D.2
-
6
-
-
0031876195
-
Phage display: Applications, innovations, and issues in phage and host biology
-
A broad review of phage display. Topics include history and pioneering work, and an overview of host cell biology and its implications. It also details practical application possibilities and important issues, such as library diversity and bias, alternative display mechanisms and their relative merits, directed evolution of proteins, and emerging areas.
-
Wilson D.R., Finlay B.B. Phage display: applications, innovations, and issues in phage and host biology. Can J Microbiol. 44:1998;313-329. A broad review of phage display. Topics include history and pioneering work, and an overview of host cell biology and its implications. It also details practical application possibilities and important issues, such as library diversity and bias, alternative display mechanisms and their relative merits, directed evolution of proteins, and emerging areas.
-
(1998)
Can J Microbiol
, vol.44
, pp. 313-329
-
-
Wilson, D.R.1
Finlay, B.B.2
-
7
-
-
0031933840
-
Strategies for selection of antibodies by phage display
-
This review gives useful comparisons between various options for displaying antibodies on phage. Includes relative merits of using phage or phagemid vectors, using scFv or Fab antibody fragments, and using natural immune, natural non-immune, or synthetic gene repertoires for primary library construction.
-
Griffiths A.D., Duncan A.R. Strategies for selection of antibodies by phage display. Curr Opin Biotechnol. 9:1998;102-108. This review gives useful comparisons between various options for displaying antibodies on phage. Includes relative merits of using phage or phagemid vectors, using scFv or Fab antibody fragments, and using natural immune, natural non-immune, or synthetic gene repertoires for primary library construction.
-
(1998)
Curr Opin Biotechnol
, vol.9
, pp. 102-108
-
-
Griffiths, A.D.1
Duncan, A.R.2
-
8
-
-
0031812594
-
Antibody phage display technology and its applications
-
Hoogenboom H.R., de Bruine A.P., Hufton S.E., Hoet R.M., Arends J.W., Roovers R.C. Antibody phage display technology and its applications. Immunotechnology. 4:1998;1-20.
-
(1998)
Immunotechnology
, vol.4
, pp. 1-20
-
-
Hoogenboom, H.R.1
De Bruine, A.P.2
Hufton, S.E.3
Hoet, R.M.4
Arends, J.W.5
Roovers, R.C.6
-
9
-
-
0030752337
-
Phage display of combinatorial antibody libraries
-
Rader C., Barbas C.F. Jr. Phage display of combinatorial antibody libraries. Curr Opin Biotechnol. 8:1997;503-508.
-
(1997)
Curr Opin Biotechnol
, vol.8
, pp. 503-508
-
-
Rader, C.1
Barbas C.F., Jr.2
-
10
-
-
2642652226
-
Selection for a periplasmic factor improving phage display and functional periplasmic expression
-
An E. coli periplasmic protein was identified that improved efficiency of displaying scFv fragments on phage. Coexpression of this protein with a phage library could improve screening results by improving functional protein representation of the underlying DNA-encoded library diversity.
-
Bothmann H., Plückthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat Biotechnol. 16:1998;376-380. An E. coli periplasmic protein was identified that improved efficiency of displaying scFv fragments on phage. Coexpression of this protein with a phage library could improve screening results by improving functional protein representation of the underlying DNA-encoded library diversity.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 376-380
-
-
Bothmann, H.1
Plückthun, A.2
-
11
-
-
0032502930
-
Stochastic modeling and optimization of phage display
-
Extensive analysis and simulations of experimental conditions needed for optimal screening of a phage display library. The author considers and makes recommendations on factors including target concentration, phage valency, degree of background (non-specific) binding, washing times, and sample size.
-
Levitan B. Stochastic modeling and optimization of phage display. J Mol Biol. 277:1998;893-916. Extensive analysis and simulations of experimental conditions needed for optimal screening of a phage display library. The author considers and makes recommendations on factors including target concentration, phage valency, degree of background (non-specific) binding, washing times, and sample size.
-
(1998)
J Mol Biol
, vol.277
, pp. 893-916
-
-
Levitan, B.1
-
12
-
-
0030849223
-
Selectively infective phages (SIP)
-
Spada S., Krebber C., Plückthun A. Selectively infective phages (SIP). Biol Chem. 378:1997;445-456.
-
(1997)
Biol Chem
, vol.378
, pp. 445-456
-
-
Spada, S.1
Krebber, C.2
Plückthun, A.3
-
13
-
-
0030869953
-
Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology
-
The quantitative dependence of phage infection efficiency on the affinity of a displayed antibody was examined, and threefold differences were effectively discriminated after three rounds of selection. Folding and stability improvements were also strongly selected.
-
Pedrazzi G., Schwesinger F., Honegger A., Krebber C., Plückthun A. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. FEBS Lett. 415:1997;289-293. The quantitative dependence of phage infection efficiency on the affinity of a displayed antibody was examined, and threefold differences were effectively discriminated after three rounds of selection. Folding and stability improvements were also strongly selected.
-
(1997)
FEBS Lett
, vol.415
, pp. 289-293
-
-
Pedrazzi, G.1
Schwesinger, F.2
Honegger, A.3
Krebber, C.4
Plückthun, A.5
-
14
-
-
0031813249
-
Non-repetitive single-chain Fv linkers selected by selectively infective phage (SIP) technology
-
3 can be troublesome in PCR techniques because of its repetitiveness. Using the SIP technique, the authors found non-repetitive linker sequences that still maintained proper folding, solubility, and ligand binding.
-
3 can be troublesome in PCR techniques because of its repetitiveness. Using the SIP technique, the authors found non-repetitive linker sequences that still maintained proper folding, solubility, and ligand binding.
-
(1998)
Protein Eng
, vol.11
, pp. 405-410
-
-
Hennecke, F.1
Krebber, C.2
Plückthun, A.3
-
15
-
-
0031729179
-
Selecting proteins with improved stability by a phage-based method
-
A variation on the selectively infective phage technique which allows for selecting library members with improved stability by using protease resistance as a proxy for folding stability.
-
Sieber V., Plückthun A., Schmid F. Selecting proteins with improved stability by a phage-based method. Nat Biotechnol. 16:1998;955-960. A variation on the selectively infective phage technique which allows for selecting library members with improved stability by using protease resistance as a proxy for folding stability.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 955-960
-
-
Sieber, V.1
Plückthun, A.2
Schmid, F.3
-
16
-
-
0030704683
-
Making chemistry selectable by linking it to infectivity
-
A catalytic antibody was selected from a library by linking catalytic activity to restoring phage infectivity.
-
Gao C., Lin C.H., Lo C.H.L., Mao S., Wirsching P., Lerner R.A., Janda K.D. Making chemistry selectable by linking it to infectivity. Proc Natl Acad Sci USA. 94:1997;11777-11782. A catalytic antibody was selected from a library by linking catalytic activity to restoring phage infectivity.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 11777-11782
-
-
Gao, C.1
Lin, C.H.2
Lo, C.H.L.3
Mao, S.4
Wirsching, P.5
Lerner, R.A.6
Janda, K.D.7
-
17
-
-
0032168985
-
A method for directed evolution and functional cloning of enzymes
-
Substrate is covalently attached to phage displaying a catalyst protein from a library, with subsequent isolation of product-linked phage via the presence or absence of linkage to a solid support.
-
Pedersen H., Holder S., Sutherlin D.P., Schwitter U., King D.S., Schultz P.G. A method for directed evolution and functional cloning of enzymes. Proc Natl Acad Sci USA. 95:1998;10523-10528. Substrate is covalently attached to phage displaying a catalyst protein from a library, with subsequent isolation of product-linked phage via the presence or absence of linkage to a solid support.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 10523-10528
-
-
Pedersen, H.1
Holder, S.2
Sutherlin, D.P.3
Schwitter, U.4
King, D.S.5
Schultz, P.G.6
-
18
-
-
0031908473
-
Pathfinder selection: In situ isolation of novel antibodies
-
A novel technique to screen phage antibody libraries without cloning or purifying the antigen. Phage binding near cell-surface antigens (for which an antibody or ligand is available) are biotinylated by a proximity reaction. An initial antibody or ligand (the 'pathfinder') against the cell-surface target is conjugated to horse radish peroxidase (HRP), then used to label cells. A phage-displayed antibody library is then added to label the cells as well. Upon addition of biotin tyramine, HRP generates a flux of reactive species that biotinylate those phage particles bound in the immediate vicinity of the 'pathfinder' fusion protein.
-
Osbourn J.K., Derbyshire E.J., Vaughan T.J., Field A.W., Johnson K.S. Pathfinder selection: in situ isolation of novel antibodies. Immunotechnology. 3:1998;293-302. A novel technique to screen phage antibody libraries without cloning or purifying the antigen. Phage binding near cell-surface antigens (for which an antibody or ligand is available) are biotinylated by a proximity reaction. An initial antibody or ligand (the 'pathfinder') against the cell-surface target is conjugated to horse radish peroxidase (HRP), then used to label cells. A phage-displayed antibody library is then added to label the cells as well. Upon addition of biotin tyramine, HRP generates a flux of reactive species that biotinylate those phage particles bound in the immediate vicinity of the 'pathfinder' fusion protein.
-
(1998)
Immunotechnology
, vol.3
, pp. 293-302
-
-
Osbourn, J.K.1
Derbyshire, E.J.2
Vaughan, T.J.3
Field, A.W.4
Johnson, K.S.5
-
19
-
-
0031902108
-
Directed selection of MIP-1 alpha neutralizing CCR5 antibodies from a phage display human antibody library
-
An extension of the pathfinder technique to identify phage antibody library members which inhibit binding of a particular ligand to a cell-surface receptor.
-
Osbourn J.K., Earnshaw J.C., Johnson K.S., Parmentier M., Timmermans V., McCafferty J. Directed selection of MIP-1 alpha neutralizing CCR5 antibodies from a phage display human antibody library. Nat Biotechnol. 16:1998;778-781. An extension of the pathfinder technique to identify phage antibody library members which inhibit binding of a particular ligand to a cell-surface receptor.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 778-781
-
-
Osbourn, J.K.1
Earnshaw, J.C.2
Johnson, K.S.3
Parmentier, M.4
Timmermans, V.5
McCafferty, J.6
-
20
-
-
0031012062
-
Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
-
Georgiou G., Stathopoulos C., Daugherty P.S., Nayak A.R., Iverson B.L., Curtiss R. Jr. Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol. 15:1997;29-34.
-
(1997)
Nat Biotechnol
, vol.15
, pp. 29-34
-
-
Georgiou, G.1
Stathopoulos, C.2
Daugherty, P.S.3
Nayak, A.R.4
Iverson, B.L.5
Curtiss R., Jr.6
-
21
-
-
0031663081
-
Antibody affinity maturation using bacterial surface display
-
Daugherty P.S., Chen G., Olsen M.J., Iverson B.L., Georgiou G. Antibody affinity maturation using bacterial surface display. Protein Eng. 11:1998;825-832.
-
(1998)
Protein Eng
, vol.11
, pp. 825-832
-
-
Daugherty, P.S.1
Chen, G.2
Olsen, M.J.3
Iverson, B.L.4
Georgiou, G.5
-
22
-
-
0028822096
-
Eukaryotic virus display: Engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface
-
Boublik Y., Di Bonito P., Jones I.M. Eukaryotic virus display: engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface. Biotechnology. 13:1995;1079-1084.
-
(1995)
Biotechnology
, vol.13
, pp. 1079-1084
-
-
Boublik, Y.1
Di Bonito, P.2
Jones, I.M.3
-
23
-
-
0032052263
-
Baculovirus surface display: Construction and screening of a eukaryotic epitope library
-
The first example of library screening using an insect cell-surface display system. Displayed polypeptides were on the surface of the infected cells rather than the virus particle, and screening was performed by flow cytometry.
-
Ernst W., Grabherr R., Wegner D., Borth N., Grassauer A., Katinger H. Baculovirus surface display: construction and screening of a eukaryotic epitope library. Nucleic Acids Res. 26:1998;1718-1723. The first example of library screening using an insect cell-surface display system. Displayed polypeptides were on the surface of the infected cells rather than the virus particle, and screening was performed by flow cytometry.
-
(1998)
Nucleic Acids Res
, vol.26
, pp. 1718-1723
-
-
Ernst, W.1
Grabherr, R.2
Wegner, D.3
Borth, N.4
Grassauer, A.5
Katinger, H.6
-
24
-
-
0031787970
-
In vivo selection of protease cleavage sites from retrovirus display libraries
-
A retroviral library was constructed and screened in cell culture for sequences that allowed intracellular proteolytic removal of a fusion domain that inhibited retroviral infectivity. This proof-of-concept experiment indicates that phage-like libraries might be constructable with this mammalian system.
-
Buchholz C.J., Peng K-W., Morling F.J., Zhang J., Cosset F-L., Russell S.J. In vivo selection of protease cleavage sites from retrovirus display libraries. Nat Biotechnol. 16:1998;951-954. A retroviral library was constructed and screened in cell culture for sequences that allowed intracellular proteolytic removal of a fusion domain that inhibited retroviral infectivity. This proof-of-concept experiment indicates that phage-like libraries might be constructable with this mammalian system.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 951-954
-
-
Buchholz, C.J.1
Peng, K.-W.2
Morling, F.J.3
Zhang, J.4
Cosset, F.-L.5
Russell, S.J.6
-
25
-
-
0029930769
-
Selective isolation of transiently transfected cells from a mammalian cell population with vectors expressing a membrane anchored single-chain antibody
-
Chesnut J.D., Baytan A.R., Russell M., Chang M.P., Bernard A., Maxwell I.H., Hoeffler J.P. Selective isolation of transiently transfected cells from a mammalian cell population with vectors expressing a membrane anchored single-chain antibody. J Immunol Methods. 193:1996;17-27.
-
(1996)
J Immunol Methods
, vol.193
, pp. 17-27
-
-
Chesnut, J.D.1
Baytan, A.R.2
Russell, M.3
Chang, M.P.4
Bernard, A.5
Maxwell, I.H.6
Hoeffler, J.P.7
-
26
-
-
0030690331
-
Tag games in yeast: The two-hybrid system and beyond
-
Brachmann R.K., Boeke J.D. Tag games in yeast: the two-hybrid system and beyond. Curr Opin Biotechnol. 8:1997;561-568.
-
(1997)
Curr Opin Biotechnol
, vol.8
, pp. 561-568
-
-
Brachmann, R.K.1
Boeke, J.D.2
-
27
-
-
0028926048
-
Protein-protein interactions: Methods for detection and analysis
-
Phizicky E.M., Fields S. Protein-protein interactions: methods for detection and analysis. Microbiol Rev. 59:1995;94-123.
-
(1995)
Microbiol Rev
, vol.59
, pp. 94-123
-
-
Phizicky, E.M.1
Fields, S.2
-
28
-
-
0032584227
-
Parallel analysis of genetic selections using whole genome oligonucleotide arrays
-
Rather than sequencing hundreds of DNA plasmids identified in yeast two-hybrid assays, a DNA hybridization technique to an ordered oligonucleotide array is used to directly identify isolated genes. Such a strategy successfully identified genes involved in mRNA splicing and microtubule assembly.
-
Cho R.J., Fromont-Racine M., Wodicka L., Feierbach B., Stearns T., Legrain P., Lockhart D.J., Davis R.W. Parallel analysis of genetic selections using whole genome oligonucleotide arrays. Proc Natl Acad Sci USA. 95:1998;3752-3757. Rather than sequencing hundreds of DNA plasmids identified in yeast two-hybrid assays, a DNA hybridization technique to an ordered oligonucleotide array is used to directly identify isolated genes. Such a strategy successfully identified genes involved in mRNA splicing and microtubule assembly.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 3752-3757
-
-
Cho, R.J.1
Fromont-Racine, M.2
Wodicka, L.3
Feierbach, B.4
Stearns, T.5
Legrain, P.6
Lockhart, D.J.7
Davis, R.W.8
-
29
-
-
0029554485
-
Investigation of ligand binding to members of the cytokine receptor family within a microbial system
-
Young K.H., Ozenberger B.A. Investigation of ligand binding to members of the cytokine receptor family within a microbial system. Ann NY Acad Sci. 766:1995;279-281.
-
(1995)
Ann NY Acad Sci
, vol.766
, pp. 279-281
-
-
Young, K.H.1
Ozenberger, B.A.2
-
30
-
-
0030923133
-
Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions
-
Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol Cell Biol. 17:1997;3094-3102.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 3094-3102
-
-
Aronheim, A.1
Zandi, E.2
Hennemann, H.3
Elledge, S.J.4
Karin, M.5
-
31
-
-
0032497564
-
The ras recruitment system, a novel approach to the study of protein-protein interactions
-
The Sos recruitment system uses a temperature sensitive yeast mutant in the ras pathway whose growth can be rescued by the Sos protein. Thus, a fusion protein with Sos in combination with a myristolated protein can artificially recruit Sos to the membrane where it rescues the genetic defect. This variation of the two hybrid system does not require nuclear localization, and could have applications with membrane protein interactions.
-
Broder Y.C., Katz S., Aronheim A. The ras recruitment system, a novel approach to the study of protein-protein interactions. Curr Biol. 8:1998;1121-1124. The Sos recruitment system uses a temperature sensitive yeast mutant in the ras pathway whose growth can be rescued by the Sos protein. Thus, a fusion protein with Sos in combination with a myristolated protein can artificially recruit Sos to the membrane where it rescues the genetic defect. This variation of the two hybrid system does not require nuclear localization, and could have applications with membrane protein interactions.
-
(1998)
Curr Biol
, vol.8
, pp. 1121-1124
-
-
Broder, Y.C.1
Katz, S.2
Aronheim, A.3
-
32
-
-
0032566753
-
The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression
-
Yu X., Wu L.C., Bowcock A.M., Aronheim A., Baer R. The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression. J Biol Chem. 273:1998;25388-25392.
-
(1998)
J Biol Chem
, vol.273
, pp. 25388-25392
-
-
Yu, X.1
Wu, L.C.2
Bowcock, A.M.3
Aronheim, A.4
Baer, R.5
-
33
-
-
0029876415
-
Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
-
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. Nature. 380:1996;548-550.
-
(1996)
Nature
, vol.380
, pp. 548-550
-
-
Colas, P.1
Cohen, B.2
Jessen, T.3
Grishina, I.4
McCoy, J.5
Brent, R.6
-
35
-
-
0028080090
-
Split ubiquitin as a sensor of protein interactions in vivo
-
Johnsson N., Varshavsky A. Split ubiquitin as a sensor of protein interactions in vivo. Proc Natl Acad Sci USA. 91:1994;10340-10344.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10340-10344
-
-
Johnsson, N.1
Varshavsky, A.2
-
36
-
-
0032574840
-
A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
-
Stagljar I., Korostensky C., Johnsson N., te Heesen S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc Natl Acad Sci USA. 95:1998;5187-5192.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 5187-5192
-
-
Stagljar, I.1
Korostensky, C.2
Johnsson, N.3
Te Heesen, S.4
-
37
-
-
0030994634
-
Yeast surface display for screening combinatorial polypeptide libraries
-
Boder E.T., Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol. 15:1997;553-557.
-
(1997)
Nat Biotechnol
, vol.15
, pp. 553-557
-
-
Boder, E.T.1
Wittrup, K.D.2
-
38
-
-
0031424522
-
Isolation of anti-T cell receptor scFv mutants by yeast surface display
-
Kieke M.C., Cho B.K., Boder E.T., Kranz D.M., Wittrup K.D. Isolation of anti-T cell receptor scFv mutants by yeast surface display. Protein Eng. 10:1997;1303-1310.
-
(1997)
Protein Eng
, vol.10
, pp. 1303-1310
-
-
Kieke, M.C.1
Cho, B.K.2
Boder, E.T.3
Kranz, D.M.4
Wittrup, K.D.5
-
39
-
-
0031791599
-
A yeast surface display system for the discovery of ligands that trigger cell activation
-
Cho B.K., Kieke M.C., Boder E.T., Wittrup K.D., Kranz D.M. A yeast surface display system for the discovery of ligands that trigger cell activation. J Immunol Methods. 220:1998;179-188.
-
(1998)
J Immunol Methods
, vol.220
, pp. 179-188
-
-
Cho, B.K.1
Kieke, M.C.2
Boder, E.T.3
Wittrup, K.D.4
Kranz, D.M.5
-
40
-
-
0025082684
-
Additivity of mutational effects in proteins
-
Wells J.A. Additivity of mutational effects in proteins. Biochemistry. 29:1990;8509-8517.
-
(1990)
Biochemistry
, vol.29
, pp. 8509-8517
-
-
Wells, J.A.1
-
41
-
-
0030722164
-
Applications of DNA shuffling to pharmaceuticals and vaccines
-
Patten P.A., Howard R.J., Stemmer W.P. Applications of DNA shuffling to pharmaceuticals and vaccines. Curr Opin Biotechnol. 8:1997;724-733.
-
(1997)
Curr Opin Biotechnol
, vol.8
, pp. 724-733
-
-
Patten, P.A.1
Howard, R.J.2
Stemmer, W.P.3
-
42
-
-
0032479179
-
Anatomy of hot spots in protein interfaces
-
Bogan A.A., Thorn K.S. Anatomy of hot spots in protein interfaces. J Mol Biol. 280:1998;1-9.
-
(1998)
J Mol Biol
, vol.280
, pp. 1-9
-
-
Bogan, A.A.1
Thorn, K.S.2
-
43
-
-
0032540358
-
Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
-
Clackson T., Ultsch M.H., Wells J.A., de Vos A.M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J Mol Biol. 277:1998;1111-1128.
-
(1998)
J Mol Biol
, vol.277
, pp. 1111-1128
-
-
Clackson, T.1
Ultsch, M.H.2
Wells, J.A.3
De Vos, A.M.4
-
44
-
-
2642711705
-
Optimal screening of surface-displayed polypeptide libraries
-
Boder E.T., Wittrup K.D. Optimal screening of surface-displayed polypeptide libraries. Biotechnol Prog. 14:1998;55-62.
-
(1998)
Biotechnol Prog
, vol.14
, pp. 55-62
-
-
Boder, E.T.1
Wittrup, K.D.2
|