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1
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0345664910
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Peptide mimetic design with the aid of computational chemistry
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K.B. Lipkowitz, Boyd D.B. New York: VCH Publishers Inc
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Damewood JR. Peptide mimetic design with the aid of computational chemistry. Lipkowitz KB, Boyd DB. Reviews in Computational Chemistry. 9:1996;1-80 VCH Publishers Inc, New York.
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(1996)
Reviews in Computational Chemistry
, vol.9
, pp. 1-80
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Damewood, J.R.1
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2
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0027964423
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From peptide to non-peptide. 2. The de novo design of potent, non-peptidal inhibitors of platelet aggregation based on a benzodiazepinedione scaffold
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McDowell RS, Blackburn BK, Gadek TR, McGee LR, Rawson T, Reynolds ME, Robarge KD, Somers TC, Thorsett ED, Tischler M, et al. From peptide to non-peptide. 2. The de novo design of potent, non-peptidal inhibitors of platelet aggregation based on a benzodiazepinedione scaffold. J Am Chem Soc. 116:1994;5077-5083.
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(1994)
J Am Chem Soc
, vol.116
, pp. 5077-5083
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McDowell, R.S.1
Blackburn, B.K.2
Gadek, T.R.3
McGee, L.R.4
Rawson, T.5
Reynolds, M.E.6
Robarge, K.D.7
Somers, T.C.8
Thorsett, E.D.9
Tischler, M.10
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3
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0028512485
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Design of a potent and orally active nonpeptide platelet fibrinogen receptor (GP11b/IIIa) antagonist
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Bondinell WE, Keenan RM, Miller WH, Ali FE, Allen AC, de Brosse CW, Eggleston DS, Erhard KF, Haltiwanger RC, Huffman WF. Design of a potent and orally active nonpeptide platelet fibrinogen receptor (GP11b/IIIa) antagonist. Bioorg Med Chem. 2:1994;897-908.
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(1994)
Bioorg Med Chem
, vol.2
, pp. 897-908
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Bondinell, W.E.1
Keenan, R.M.2
Miller, W.H.3
Ali, F.E.4
Allen, A.C.5
De Brosse, C.W.6
Eggleston, D.S.7
Erhard, K.F.8
Haltiwanger, R.C.9
Huffman, W.F.10
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4
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0030065819
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Design, synthesis and in vitro activities of a series of benzimidazole/benzoxazole glycoprotein IIb/IIIa inhibitors
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of special interest. Modeling studies based on the conformation of a cyclic peptide are used to design a series of benzimidazole/benzoxazole analogs that are highly potent inhibitors of platelet aggregation.
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Chu-Biao X, Rafalski M, Roderick J, Eyermann CG, Mousa S, Olson RE, DeGrado WF. Design, synthesis and in vitro activities of a series of benzimidazole/benzoxazole glycoprotein IIb/IIIa inhibitors. of special interest Bioorg Med Chem. 6:1996;339-344 Modeling studies based on the conformation of a cyclic peptide are used to design a series of benzimidazole/benzoxazole analogs that are highly potent inhibitors of platelet aggregation.
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(1996)
Bioorg Med Chem
, vol.6
, pp. 339-344
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Chu-Biao, X.1
Rafalski, M.2
Roderick, J.3
Eyermann, C.G.4
Mousa, S.5
Olson, R.E.6
Degrado, W.F.7
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5
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0027268487
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Design of peptide enzymes (pepzymes): Surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites and exhibit the activity and specificity of the respective enzyme
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Atassi MZ, Manshouri T. Design of peptide enzymes (pepzymes): surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites and exhibit the activity and specificity of the respective enzyme. Proc Natl Acad Sci USA. 90:1993;8282-8286.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 8282-8286
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Atassi, M.Z.1
Manshouri, T.2
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7
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0028269016
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A reinvestigation of a synthetic peptide (TrPepz) designed to mimic trypsin
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Wells JA, Fairbrother WJ, Otlewski J, Laskowski M Jr, Burnier J. A reinvestigation of a synthetic peptide (TrPepz) designed to mimic trypsin. Proc Natl Acad Sci USA. 91:1994;4110-4114.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 4110-4114
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Wells, J.A.1
Fairbrother, W.J.2
Otlewski, J.3
Laskowski M., Jr.4
Burnier, J.5
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8
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0030593029
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Design of a monomeric 23-residue polypeptide with defined tertiary structure
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of outstanding interest. This paper details the design process and iterative spectroscopic analysis that enables the production of a peptide with a metal-independent zinc-finger-like fold. The NMR structure of the final peptide design is compared with structure of a natural zinc finger peptide.
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Struthers MD, Cheng RP, Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. of outstanding interest Science. 271:1996;342-345 This paper details the design process and iterative spectroscopic analysis that enables the production of a peptide with a metal-independent zinc-finger-like fold. The NMR structure of the final peptide design is compared with structure of a natural zinc finger peptide.
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(1996)
Science
, vol.271
, pp. 342-345
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Struthers, M.D.1
Cheng, R.P.2
Imperiali, B.3
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9
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0030567375
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Economy in protein design: Evolution of a metal-independent bba motif based on the zinc finger domains
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Struthers MD, Cheng RP, Imperiali B. Economy in protein design: evolution of a metal-independent bba motif based on the zinc finger domains. J Am Chem Soc. 118:1996;3073-3081.
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(1996)
J Am Chem Soc
, vol.118
, pp. 3073-3081
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Struthers, M.D.1
Cheng, R.P.2
Imperiali, B.3
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10
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0021818675
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Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
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Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 228:1985;1315-1317.
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(1985)
Science
, vol.228
, pp. 1315-1317
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Smith, G.P.1
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11
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0025112794
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Searching for peptide ligands with an epitope library
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Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science. 249:1990;386-390.
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(1990)
Science
, vol.249
, pp. 386-390
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Scott, J.K.1
Smith, G.P.2
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13
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0025004285
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Random peptide libraries: A source of specific protein binding molecules
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Devlin JJ, Panganiban LC, Devlin PE. Random peptide libraries: a source of specific protein binding molecules. Science. 249:1990;404-406.
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(1990)
Science
, vol.249
, pp. 404-406
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Devlin, J.J.1
Panganiban, L.C.2
Devlin, P.E.3
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14
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0011958990
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High affinity type I interleukin 1 receptor antagonists discovered by screening recombinant peptide libraries
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of outstanding interest. This paper, along with [15], is the first to successfully mimic the binding of complex protein - protein interfaces with small peptides. In this case, a number of clever strategies are employed to isolate a linear 15-residue peptide that binds and antagonizes the IL-1 receptor.
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Yanofsky SD, Baldwin DN, Butler JH, Holden FR, Jacobs JW, Balasubramanian P, Chinn JP, Cwirla SE, Peters-Bhatt E, Whitehorn EA, et al. High affinity type I interleukin 1 receptor antagonists discovered by screening recombinant peptide libraries. of outstanding interest Proc Natl Acad Sci USA. 93:1996;7381-7386 This paper, along with [15], is the first to successfully mimic the binding of complex protein - protein interfaces with small peptides. In this case, a number of clever strategies are employed to isolate a linear 15-residue peptide that binds and antagonizes the IL-1 receptor.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 7381-7386
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Yanofsky, S.D.1
Baldwin, D.N.2
Butler, J.H.3
Holden, F.R.4
Jacobs, J.W.5
Balasubramanian, P.6
Chinn, J.P.7
Cwirla, S.E.8
Peters-Bhatt, E.9
Whitehorn, E.A.10
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15
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9444236174
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Small peptides as potent mimetics of the protein hormone erythropoietin
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of outstanding interest. This paper describes the isolation of a peptide agonist that binds to the EPO receptor to form an activated peptide - receptor dimeric complex. The structure of this complex is described in a companion paper [19].
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Wrighton NC, Farrell FX, Chang R, Kashyap AK, Barbone FP, Mulcahy LS, Johnson DL, Barrett RW, Jolliffe LK, Dower WJ. Small peptides as potent mimetics of the protein hormone erythropoietin. of outstanding interest Science. 273:1996;458-463 This paper describes the isolation of a peptide agonist that binds to the EPO receptor to form an activated peptide - receptor dimeric complex. The structure of this complex is described in a companion paper [19].
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(1996)
Science
, vol.273
, pp. 458-463
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Wrighton, N.C.1
Farrell, F.X.2
Chang, R.3
Kashyap, A.K.4
Barbone, F.P.5
Mulcahy, L.S.6
Johnson, D.L.7
Barrett, R.W.8
Jolliffe, L.K.9
Dower, W.J.10
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16
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0025910746
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Linkage of recognition and replication functions by assembling combinatorial antibody libraries along phage surfaces
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Kang AS, Barbas CF III, Janda KD, Benkovic SJ, Lerner RA. Linkage of recognition and replication functions by assembling combinatorial antibody libraries along phage surfaces. Proc Natl Acad Sci USA. 88:1991;4363-4366.
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(1991)
Proc Natl Acad Sci USA
, vol.88
, pp. 4363-4366
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Kang, A.S.1
Barbas C.F. III2
Janda, K.D.3
Benkovic, S.J.4
Lerner, R.A.5
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17
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0025678186
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Hormone phage: An enrichment method for variant proteins with altered binding properties
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Bass S, Greene R, Wells JA. Hormone phage: an enrichment method for variant proteins with altered binding properties. Proteins. 8:1990;309-314.
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(1990)
Proteins
, vol.8
, pp. 309-314
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Bass, S.1
Greene, R.2
Wells, J.A.3
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18
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0031000052
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A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist
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of special interest. The structure of the naturally occurring IL-1 receptor antagonist (IL1RA) complexed with the extracellular domain of the IL-1 receptor is elaborated. Five critical IL1RA residues, previously identified in mutagenesis studies, are found to be localized at the center of the binding interface.
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Schreuder H, Tardif C, Trump-Kallmeyer S, Soffientini A, Sarubbi E, Akeson A, Bowlin T, Yanofsky S, Barrett RW. A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. of special interest Nature. 386:1997;194-199 The structure of the naturally occurring IL-1 receptor antagonist (IL1RA) complexed with the extracellular domain of the IL-1 receptor is elaborated. Five critical IL1RA residues, previously identified in mutagenesis studies, are found to be localized at the center of the binding interface.
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(1997)
Nature
, vol.386
, pp. 194-199
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Schreuder, H.1
Tardif, C.2
Trump-Kallmeyer, S.3
Soffientini, A.4
Sarubbi, E.5
Akeson, A.6
Bowlin, T.7
Yanofsky, S.8
Barrett, R.W.9
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19
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0029798402
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Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å
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of outstanding interest. This paper presents the structural detail and mechanism by which a remarkable phage display derived 20-residue peptide is able to promote dimerization of the EPO receptor.
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Livnah O, Stura EA, Johnson DL, Middleton SA, Mulcahy LS, Wrighton NC, Dower WJ, Jolliffe LK, Wilson IA. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å of outstanding interest Science. 273:1996;264-271 This paper presents the structural detail and mechanism by which a remarkable phage display derived 20-residue peptide is able to promote dimerization of the EPO receptor.
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(1996)
Science
, vol.273
, pp. 264-271
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Livnah, O.1
Stura, E.A.2
Johnson, D.L.3
Middleton, S.A.4
Mulcahy, L.S.5
Wrighton, N.C.6
Dower, W.J.7
Jolliffe, L.K.8
Wilson, I.A.9
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20
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0026598960
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Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
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De Vos AM, Ultsch M, Kossiakoff AA. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
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(1992)
Science
, vol.255
, pp. 306-312
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De Vos, A.M.1
Ultsch, M.2
Kossiakoff, A.A.3
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21
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0029619255
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Minimization of a polypeptide hormone
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Li B, Tom JYK, Oare D, Yen R, Fairbrother WJ, Wells JA, Cunningham BC. Minimization of a polypeptide hormone. Science. 270:1994;1657-1660.
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(1994)
Science
, vol.270
, pp. 1657-1660
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Li, B.1
Tom, J.Y.K.2
Oare, D.3
Yen, R.4
Fairbrother, W.J.5
Wells, J.A.6
Cunningham, B.C.7
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22
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0029904435
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Minimizing a binding domain from protein A
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of outstanding interest. Structure-based design and phage display are used to iteratively improve the stability and affinity of a two-helix derivative of the three-helix Z-domain of protein A.
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Braisted AC, Wells JA. Minimizing a binding domain from protein A. of outstanding interest Proc Natl Acad Sci USA. 93:1996;5688-5692 Structure-based design and phage display are used to iteratively improve the stability and affinity of a two-helix derivative of the three-helix Z-domain of protein A.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 5688-5692
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Braisted, A.C.1
Wells, J.A.2
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23
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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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(1994)
EMBO J
, vol.13
, pp. 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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