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A review of the utility of soluble peptide combinatorial libraries
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0038089976
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Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library
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McBride, J.D.1
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0039310043
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Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
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Schatz PJ. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology. 11:1993;1138-1143.
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Schatz, P.J.1
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Gates, C.M.1
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0028947997
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Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein - protein interactions
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Lu Z, Murray KS, Van Cleave V, LaVallie ER, Stahl ML, McCoy JM. Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein - protein interactions. Biotechnol. 13:1995;366-372.
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Lu, Z.1
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0028911488
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Selection of biologically active peptides by phage display of random peptide libraries
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Cortese R, Monaci P, Luzzago A, Santini C, Bartoli F, Cortese I, Fortugno P, Galfré G, Nicosia A, Felici F. Selection of biologically active peptides by phage display of random peptide libraries. Curr Opin Biotechnol. 6:1995;73-80.
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Cortese, R.1
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Substrate phage: Selection of protease substrates by monovalent phage display
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Matthews, D.J.1
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0028556408
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Identifying substrate motifs of protein kinases by a random library approach
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Wu, J.1
Ma, Q.N.2
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9444236174
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Small peptides as potent mimetics of the protein hormone erythropoietin
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Wrighton NC, Farrell FX, Chang R, Kashyap AK, Barbone FP, Mulcahy LS, Johnson DL, Barrett RW, Jolliffe, Dower WJ. Small peptides as potent mimetics of the protein hormone erythropoietin. Science. 273:1996;458-463.
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Wrighton, N.C.1
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0029898609
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Affinity purification of von Willebrand factor using ligands derived from peptide libraries
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Huang PY, Baumbach GA, Dadd CA, Buettner JA, Masecar BL, Hentsch M, Hammond DJ, Carbonell RG. Affinity purification of von Willebrand factor using ligands derived from peptide libraries. Bioorg Med Chem. 4:1996;699-708.
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Huang, P.Y.1
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Masecar, B.L.5
Hentsch, M.6
Hammond, D.J.7
Carbonell, R.G.8
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0028899525
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Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrins
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Koivunen E, Wang B, Rouslahti E. Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Biotechnology. 13:1995;265-270.
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Koivunen, E.1
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0028839787
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Ladner RC. Constrained peptides as binding entities. Trends Biotechnol. 13:1995;426-430.
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Ladner, R.C.1
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0026343486
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Selecting high-affinity binding proteins by monovalent phage display
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Lowman, H.B.1
Bass, S.H.2
Simpson, N.3
Wells, J.A.4
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0028239263
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Production of an atrial natriuretic peptide variant that is specific for type a receptor
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Cunningham BC, Lowe DG, Li B, Bennett BD, Wells JA. Production of an atrial natriuretic peptide variant that is specific for type a receptor. EMBO J. 13:1994;2508-2515.
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Cunningham, B.C.1
Lowe, D.G.2
Li, B.3
Bennett, B.D.4
Wells, J.A.5
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15
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0029989324
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Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection
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Schier R, Bye J, Apell G, McCall A, Adams GP, Malmqvist M, Weiner LM, Marks JD. Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection. J Mol Biol. 255:1996;28-43.
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Schier, R.1
Bye, J.2
Apell, G.3
McCall, A.4
Adams, G.P.5
Malmqvist, M.6
Weiner, L.M.7
Marks, J.D.8
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16
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0029361962
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A combinatorial method for constructing libraries of long peptides displayed by filamentous phage
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Haaparanta T, Huse WD. A combinatorial method for constructing libraries of long peptides displayed by filamentous phage. Mol Diversity. 1:1995;39-52.
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Haaparanta, T.1
Huse, W.D.2
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17
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0030132725
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Construction and screening of M13 phage libraries displaying long random peptides
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McConnell SJ, Uveges AJ, Fowlkes DM, Spinella DG. Construction and screening of M13 phage libraries displaying long random peptides. Mol Diversity. 1:1996;165-176.
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McConnell, S.J.1
Uveges, A.J.2
Fowlkes, D.M.3
Spinella, D.G.4
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18
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0024199422
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Stability of protein structure and hydrophobic interaction
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Privalov PL, Gill SJ. Stability of protein structure and hydrophobic interaction. Adv Protein Chem. 39:1988;191-234.
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Privalov, P.L.1
Gill, S.J.2
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19
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0029821726
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A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage
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11 member) library. The use of the intron facilitates removal of the loxP site from the expression cassette. The authors suggest that sequences other than the five-residue linker can be placed between the exons to yield a wide range of differently structured proteins.
-
11 member) library. The use of the intron facilitates removal of the loxP site from the expression cassette. The authors suggest that sequences other than the five-residue linker can be placed between the exons to yield a wide range of differently structured proteins.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 7761-7766
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Fish, I.1
Kontermann, R.E.2
Finnern, R.3
Hartley, O.4
Soler-Gonzalez, A.S.5
Griffiths, A.6
Winter, G.7
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20
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0031043433
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Mix and match: Building manifold binding sites
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Hoogenboom H. Mix and match: building manifold binding sites. Nat Biotechnol. 15:1997;125-126.
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Hoogenboom, H.1
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21
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0027310612
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Naturally occurring antibodies devoid of light chains
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Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R. Naturally occurring antibodies devoid of light chains. Nature. 363:1993;446-448.
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Nature
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Hamers-Casterman, C.1
Atarhouch, T.2
Muyldermans, S.3
Robinson, G.4
Hamers, C.5
Songa, E.B.6
Bendahman, N.7
Hamers, R.8
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23
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0029764444
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H antibody fragment in complex with lysozyme
-
L. This information is of great importance for further engineering studies and library constructions of this class of antibodies.
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L. This information is of great importance for further engineering studies and library constructions of this class of antibodies.
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Nat Struct Biol
, vol.3
, pp. 803-811
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Desmyter, A.1
Transue, T.R.2
Ghahroudi, M.A.3
Dao Thi, M.H.4
Poortmans, F.5
Hamers, R.6
Muyldermans, S.7
Wyns, L.8
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24
-
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0028385766
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The making of the minibody: An engineered β-protein for the display of conformationally constrained peptides
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Tramontano A, Bianchi E, Venturini S, Martin F, Pessi A, Sollazzo M. The making of the minibody: an engineered β-protein for the display of conformationally constrained peptides. J Mol Recognit. 7:1994;9-24.
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J Mol Recognit
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Tramontano, A.1
Bianchi, E.2
Venturini, S.3
Martin, F.4
Pessi, A.5
Sollazzo, M.6
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25
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0028124968
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The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6
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Martin F, Toniatti C, Salvati AL, Venturini S, Ciliberto G, Cortese R, Sollazzo M. The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6. EMBO J. 13:1994;5303-5309.
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EMBO J
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Martin, F.1
Toniatti, C.2
Salvati, A.L.3
Venturini, S.4
Ciliberto, G.5
Cortese, R.6
Sollazzo, M.7
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26
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0029994999
-
Coupling protein design and in vitro selection strategies: Improving specificity and affinity of a designed-protein IL-6 antagonist
-
of special interest. This paper describes an affinity maturation strategy for the minibody involving 'loop swapping' and monovalent display on phage. Using this strategy on a micromolar hIL-6 antagonist minibody, a variant with a threefold higher affinity and improved hIL-6 specificity is isolated.
-
Martin F, Toniatti C, Salvatti AL, Ciliberto G, Cortese R, Sollazzo M. Coupling protein design and in vitro selection strategies: improving specificity and affinity of a designed-protein IL-6 antagonist. of special interest J Mol Biol. 255:1996;86-97 This paper describes an affinity maturation strategy for the minibody involving 'loop swapping' and monovalent display on phage. Using this strategy on a micromolar hIL-6 antagonist minibody, a variant with a threefold higher affinity and improved hIL-6 specificity is isolated.
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J Mol Biol
, vol.255
, pp. 86-97
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Martin, F.1
Toniatti, C.2
Salvatti, A.L.3
Ciliberto, G.4
Cortese, R.5
Sollazzo, M.6
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27
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0029120867
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Tendamistat as a scaffold for conformationally constrained phage peptide libraries
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McConnell S, Hoess RH. Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J Mol Biol. 250:1995;460-470.
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J Mol Biol
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McConnell, S.1
Hoess, R.H.2
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28
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0028982245
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A combinatorial library of an α-helical bacterial receptor domain
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Nord K, Nilsson J, Nilsson B, Uhlén M, Nygren PÅ. A combinatorial library of an α-helical bacterial receptor domain. Protein Eng. 8:1995;601-608.
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Protein Eng
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Nord, K.1
Nilsson, J.2
Nilsson, B.3
Uhlén, M.4
Nygren, P.5
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31
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0029134134
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Designing DNA-binding proteins on the surface of filamentous phage
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Choo Y, Klug A. Designing DNA-binding proteins on the surface of filamentous phage. Curr Opin Biotechnol. 6:1995;431-436.
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Curr Opin Biotechnol
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Choo, Y.1
Klug, A.2
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32
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0028902841
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A conformationally homogeneous combinatorial peptide library
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Bianchi E, Folgori A, Wallace A, Nicotra M, Acali S, Phalipon A, Barbato G, Bazzo R, Corteze R, Felici F, Pessi A. A conformationally homogeneous combinatorial peptide library. J Mol Biol. 247:1995;154-160.
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J Mol Biol
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, pp. 154-160
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Bianchi, E.1
Folgori, A.2
Wallace, A.3
Nicotra, M.4
Acali, S.5
Phalipon, A.6
Barbato, G.7
Bazzo, R.8
Corteze, R.9
Felici, F.10
Pessi, A.11
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33
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0028874645
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A human pancreatic secretory trypsin inhibitor presenting a hypervariable highly constrained epitope via monovalent phagemid display
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Röttgen P, Collins J. A human pancreatic secretory trypsin inhibitor presenting a hypervariable highly constrained epitope via monovalent phagemid display. Gene. 164:1995;243-250.
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Gene
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Röttgen, P.1
Collins, J.2
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34
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0029020237
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Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin
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Wang CI, Yang Q, Craik CS. Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin. J Biol Chem. 270:1995;12250-12256.
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J Biol Chem
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Wang, C.I.1
Yang, Q.2
Craik, C.S.3
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35
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0029953760
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Iterative optimization of high-affinity protease inhibitors using phage display. 1. Plasmin
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Markland W, Ley AC, Ladner RC. Iterative optimization of high-affinity protease inhibitors using phage display. 1. Plasmin. Biochemistry. 35:1996;8045-8057.
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Biochemistry
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Markland, W.1
Ley, A.C.2
Ladner, R.C.3
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36
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0029894775
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Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin
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of special interest. This paper describes the selection of high-affinity plasma kallikrein inhibitors using an iterative approach starting from a first library of a Kunitz domain of human LACI-D1, which was previously used to find inhibitors to human plasmin. Interestingly, while selecting for inhibitors for human thrombin, binders to a different site than the catalytic site are found.
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Markland W, Ley AC, Ladner RC. Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin. of special interest Biochemistry. 35:1996;8058-8067 This paper describes the selection of high-affinity plasma kallikrein inhibitors using an iterative approach starting from a first library of a Kunitz domain of human LACI-D1, which was previously used to find inhibitors to human plasmin. Interestingly, while selecting for inhibitors for human thrombin, binders to a different site than the catalytic site are found.
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(1996)
Biochemistry
, vol.35
, pp. 8058-8067
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Markland, W.1
Ley, A.C.2
Ladner, R.C.3
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0029033034
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Alternate protein frameworks for molecular recognition
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Ku J, Schultz PG. Alternate protein frameworks for molecular recognition. Proc Natl Acad Sci USA. 92:1995;6552-6556.
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Proc Natl Acad Sci USA
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Ku, J.1
Schultz, P.G.2
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38
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0027265713
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The role of turns in the structure of an α-helical protein
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Brunet AP, Huang ES, Huffine ME, Joeb JE, Weltman RJ, Hecht MH. The role of turns in the structure of an α-helical protein. Nature. 364:1993;355-358.
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Nature
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Brunet, A.P.1
Huang, E.S.2
Huffine, M.E.3
Joeb, J.E.4
Weltman, R.J.5
Hecht, M.H.6
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39
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0030595361
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Use of a conformationally restricted secondary structural element to display peptide libraries: A two stranded alpha-helical coiled-coil stabilized by lactam bridges
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of special interest. The grafting of a discontinuous five-residue IgA epitope into a synthetic α-helical lactam-bridged coiled-coil scaffold yields IgA-binding molecules. The potential of the scaffold for use in the construction of random libraries is demonstrated by the successful introduction of five glycine residues - one of the most helix-destabilizing substitutions likely to occur in a random library of the five sites suggested for randomization.
-
Houston ME Jr, Wallace A, Bianchi E, Pessi A, Hodges RS. Use of a conformationally restricted secondary structural element to display peptide libraries: a two stranded alpha-helical coiled-coil stabilized by lactam bridges. of special interest J Mol Biol. 262:1996;270-282 The grafting of a discontinuous five-residue IgA epitope into a synthetic α-helical lactam-bridged coiled-coil scaffold yields IgA-binding molecules. The potential of the scaffold for use in the construction of random libraries is demonstrated by the successful introduction of five glycine residues - one of the most helix-destabilizing substitutions likely to occur in a random library of the five sites suggested for randomization.
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(1996)
J Mol Biol
, vol.262
, pp. 270-282
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Houston M.E., Jr.1
Wallace, A.2
Bianchi, E.3
Pessi, A.4
Hodges, R.S.5
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40
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0029977511
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The coiled coil stem loop miniprotein as a presentation scaffold
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Miceli R, Myszka D, Mao J, Sathe G, Chaiken I. The coiled coil stem loop miniprotein as a presentation scaffold. Drug Des Discov. 13:1996;95-105.
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Drug des Discov
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, pp. 95-105
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Miceli, R.1
Myszka, D.2
Mao, J.3
Sathe, G.4
Chaiken, I.5
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41
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0030047220
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Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries
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of special interest. This paper describes attempts to construct synthetic combinatorial libraries employing an 18-residue amphipatic α-helical scaffold sequence. This is an important step towards conformationally defined libraries. In addition, the results yield important information on the helix propensity for the L-amino acids.
-
Pérez-Payá E, Houghten RA, Blondelle SE. Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries. of special interest J Biol Chem. 271:1996;4120-4126 This paper describes attempts to construct synthetic combinatorial libraries employing an 18-residue amphipatic α-helical scaffold sequence. This is an important step towards conformationally defined libraries. In addition, the results yield important information on the helix propensity for the L-amino acids.
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(1996)
J Biol Chem
, vol.271
, pp. 4120-4126
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Pérez-Payá, E.1
Houghten, R.A.2
Blondelle, S.E.3
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