-
1
-
-
84871365798
-
Expanding the number of “druggable targets”: non-enzymes and protein–protein interactions
-
1 Makley, L.N., Gestwicki, J.E., Expanding the number of “druggable targets”: non-enzymes and protein–protein interactions. Chem Biol Drug Des 81 (2013), 22–32.
-
(2013)
Chem Biol Drug Des
, vol.81
, pp. 22-32
-
-
Makley, L.N.1
Gestwicki, J.E.2
-
2
-
-
84930015010
-
Peptide therapeutics: targeting the undruggable space
-
2 Tsomaia, N., Peptide therapeutics: targeting the undruggable space. Eur J Med Chem 94 (2015), 459–470.
-
(2015)
Eur J Med Chem
, vol.94
, pp. 459-470
-
-
Tsomaia, N.1
-
3
-
-
84979223375
-
Library-based display technologies: where do we stand?
-
3 Galá, A., Comor, L., Horvatić, A., Kuleš, J., Guillemin, N., Mrljak, V., Bhide, M., Library-based display technologies: where do we stand?. Mol BioSyst 12 (2016), 2342–2358.
-
(2016)
Mol BioSyst
, vol.12
, pp. 2342-2358
-
-
Galá, A.1
Comor, L.2
Horvatić, A.3
Kuleš, J.4
Guillemin, N.5
Mrljak, V.6
Bhide, M.7
-
4
-
-
84924705949
-
Encoded libraries of chemically modified peptides
-
4 Heinis, C., Winter, G., Encoded libraries of chemically modified peptides. Curr Opin Chem Biol 26 (2015), 89–98.
-
(2015)
Curr Opin Chem Biol
, vol.26
, pp. 89-98
-
-
Heinis, C.1
Winter, G.2
-
5
-
-
0026419328
-
A new type of synthetic peptide library for identifying ligand-binding activity
-
5 Lam, K.S., Salmon, S.E., Hersh, E.M., Hruby, V.J., Kazmierski, W.M., Knapp, R.J., A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354 (1991), 82–84.
-
(1991)
Nature
, vol.354
, pp. 82-84
-
-
Lam, K.S.1
Salmon, S.E.2
Hersh, E.M.3
Hruby, V.J.4
Kazmierski, W.M.5
Knapp, R.J.6
-
6
-
-
74249109746
-
De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry
-
6 Semmler, A., Weber, R., Przybylski, M., Wittmann, V., De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry. J Am Soc Mass Spectrom 21 (2010), 215–219.
-
(2010)
J Am Soc Mass Spectrom
, vol.21
, pp. 215-219
-
-
Semmler, A.1
Weber, R.2
Przybylski, M.3
Wittmann, V.4
-
7
-
-
84922041528
-
Synthesis and screening of one-bead-one-compound cyclic peptide libraries
-
R. Derda Springer New York
-
7 Qian, Z., Upadhyaya, P., Pei, D., Synthesis and screening of one-bead-one-compound cyclic peptide libraries. Derda, R., (eds.) Peptide Libraries: Methods and Protocols, 2015, Springer, New York, 39–53.
-
(2015)
Peptide Libraries: Methods and Protocols
, pp. 39-53
-
-
Qian, Z.1
Upadhyaya, P.2
Pei, D.3
-
8
-
-
84969506943
-
Recent advances toward the discovery of drug-like peptides de novo
-
8 Goldflam, M., Ullman, C.G., Recent advances toward the discovery of drug-like peptides de novo. Front Chem, 3, 2015, 69.
-
(2015)
Front Chem
, vol.3
, pp. 69
-
-
Goldflam, M.1
Ullman, C.G.2
-
9
-
-
79960610738
-
Evolution of cyclic peptide protease inhibitors
-
9 Young, T.S., Young, D.D., Ahmad, I., Louis, J.M., Benkovic, S.J., Schultz, P.G., Evolution of cyclic peptide protease inhibitors. Proc Natl Acad Sci U S A 108 (2011), 11052–11056.
-
(2011)
Proc Natl Acad Sci U S A
, vol.108
, pp. 11052-11056
-
-
Young, T.S.1
Young, D.D.2
Ahmad, I.3
Louis, J.M.4
Benkovic, S.J.5
Schultz, P.G.6
-
10
-
-
84906060855
-
Peptides come round: using SICLOPPS libraries for early stage drug discovery
-
10 Lennard, K.R., Tavassoli, A., Peptides come round: using SICLOPPS libraries for early stage drug discovery. Chemistry 20 (2014), 10608–10614.
-
(2014)
Chemistry
, vol.20
, pp. 10608-10614
-
-
Lennard, K.R.1
Tavassoli, A.2
-
11
-
-
69249124948
-
Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models
-
11 Kritzer, J.A., Hamamichi, S., McCaffery, J.M., Santagata, S., Naumann, T.A., Caldwell, K.A., Caldwell, G.A., Lindquist, S., Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models. Nat Chem Biol 5 (2009), 655–663.
-
(2009)
Nat Chem Biol
, vol.5
, pp. 655-663
-
-
Kritzer, J.A.1
Hamamichi, S.2
McCaffery, J.M.3
Santagata, S.4
Naumann, T.A.5
Caldwell, K.A.6
Caldwell, G.A.7
Lindquist, S.8
-
12
-
-
0037020080
-
Retrovirally delivered random cyclic peptide libraries yield inhibitors of interleukin-4 signaling in human B cells
-
12 Kinsella, T.M., Ohashi, C.T., Harder, A.G., Yam, G.C., Li, W., Peelle, B., Pali, E.S., Bennett, M.K., Molineaux, S.M., Anderson, D.A., et al. Retrovirally delivered random cyclic peptide libraries yield inhibitors of interleukin-4 signaling in human B cells. J Biol Chem 277 (2002), 37512–37518.
-
(2002)
J Biol Chem
, vol.277
, pp. 37512-37518
-
-
Kinsella, T.M.1
Ohashi, C.T.2
Harder, A.G.3
Yam, G.C.4
Li, W.5
Peelle, B.6
Pali, E.S.7
Bennett, M.K.8
Molineaux, S.M.9
Anderson, D.A.10
-
13
-
-
34447530923
-
Potential of phage-displayed peptide library technology to identify functional targeting peptides
-
13 Krumpe, L., Mori, T., Potential of phage-displayed peptide library technology to identify functional targeting peptides. Expert Opin Drug Discov, 2, 2007, 525.
-
(2007)
Expert Opin Drug Discov
, vol.2
, pp. 525
-
-
Krumpe, L.1
Mori, T.2
-
14
-
-
84922032502
-
Chemical posttranslational modification of phage-displayed peptides
-
R. Derda Springer New York
-
14 Ng, S., Tjhung, K.F., Paschal, B.M., Noren, C.J., Derda, R., Chemical posttranslational modification of phage-displayed peptides. Derda, R., (eds.) Peptide Libraries: Methods and Protocols, 2015, Springer, New York, 155–172.
-
(2015)
Peptide Libraries: Methods and Protocols
, pp. 155-172
-
-
Ng, S.1
Tjhung, K.F.2
Paschal, B.M.3
Noren, C.J.4
Derda, R.5
-
15
-
-
0347359106
-
Phosphotyrosine phosphoepitopes can be rapidly analyzed by coexpression of a tyrosine kinase in bacteria with a T7 bacteriophage display library
-
15 Khati, M., Pillay, T.S., Phosphotyrosine phosphoepitopes can be rapidly analyzed by coexpression of a tyrosine kinase in bacteria with a T7 bacteriophage display library. Anal Biochem 325 (2004), 164–167.
-
(2004)
Anal Biochem
, vol.325
, pp. 164-167
-
-
Khati, M.1
Pillay, T.S.2
-
16
-
-
0030817279
-
RNA–peptide fusions for the in vitro selection of peptides and proteins
-
16 Roberts, R.W., Szostak, J.W., RNA–peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci U S A 94 (1997), 12297–12302.
-
(1997)
Proc Natl Acad Sci U S A
, vol.94
, pp. 12297-12302
-
-
Roberts, R.W.1
Szostak, J.W.2
-
17
-
-
84940845423
-
Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming
-
17 Rogers, J.M., Suga, H., Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. Org Biomol Chem 13 (2015), 9353–9363.
-
(2015)
Org Biomol Chem
, vol.13
, pp. 9353-9363
-
-
Rogers, J.M.1
Suga, H.2
-
18
-
-
85003550710
-
Improving the binding affinity of in-vitro-evolved cyclic peptides by inserting atoms into the macrocycle backbone
-
18 Wilbs, J., Middendorp, S.J., Heinis, C., Improving the binding affinity of in-vitro-evolved cyclic peptides by inserting atoms into the macrocycle backbone. ChemBioChem 17 (2016), 2299–2303.
-
(2016)
ChemBioChem
, vol.17
, pp. 2299-2303
-
-
Wilbs, J.1
Middendorp, S.J.2
Heinis, C.3
-
19
-
-
84863434152
-
In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors
-
19 Guillen Schlippe, Y.V., Hartman, M.C.T., Josephson, K., Szostak, J.W., In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors. J Am Chem Soc 134 (2012), 10469–10477.
-
(2012)
J Am Chem Soc
, vol.134
, pp. 10469-10477
-
-
Guillen Schlippe, Y.V.1
Hartman, M.C.T.2
Josephson, K.3
Szostak, J.W.4
-
20
-
-
58049219079
-
Ribosomal synthesis of polypeptoids and peptoid–peptide hybrids
-
20 Kawakami, T., Murakami, H., Suga, H., Ribosomal synthesis of polypeptoids and peptoid–peptide hybrids. J Am Chem Soc 130 (2008), 16861–16863.
-
(2008)
J Am Chem Soc
, vol.130
, pp. 16861-16863
-
-
Kawakami, T.1
Murakami, H.2
Suga, H.3
-
21
-
-
84883077144
-
Extensive reprogramming of the genetic code for genetically encoded synthesis of highly N-alkylated polycyclic peptidomimetics
-
21 Kawakami, T., Ishizawa, T., Murakami, H., Extensive reprogramming of the genetic code for genetically encoded synthesis of highly N-alkylated polycyclic peptidomimetics. J Am Chem Soc 135 (2013), 12297–12304.
-
(2013)
J Am Chem Soc
, vol.135
, pp. 12297-12304
-
-
Kawakami, T.1
Ishizawa, T.2
Murakami, H.3
-
22
-
-
0018265171
-
“Chemical aminoacylation” of tRNA's
-
22 Hecht, S.M., Alford, B.L., Kuroda, Y., Kitano, S., “Chemical aminoacylation” of tRNA's. J Biol Chem 253 (1978), 4517–4520.
-
(1978)
J Biol Chem
, vol.253
, pp. 4517-4520
-
-
Hecht, S.M.1
Alford, B.L.2
Kuroda, Y.3
Kitano, S.4
-
23
-
-
77951236321
-
Beyond the canonical 20 amino acids: expanding the genetic lexicon
-
23 Young, T.S., Schultz, P.G., Beyond the canonical 20 amino acids: expanding the genetic lexicon. J Biol Chem 285 (2010), 11039–11044.
-
(2010)
J Biol Chem
, vol.285
, pp. 11039-11044
-
-
Young, T.S.1
Schultz, P.G.2
-
24
-
-
84255189091
-
Flexizymes: their evolutionary history and the origin of catalytic function
-
24 Morimoto, J., Hayashi, Y., Iwasaki, K., Suga, H., Flexizymes: their evolutionary history and the origin of catalytic function. Acc Chem Res 44 (2011), 1359–1368.
-
(2011)
Acc Chem Res
, vol.44
, pp. 1359-1368
-
-
Morimoto, J.1
Hayashi, Y.2
Iwasaki, K.3
Suga, H.4
-
25
-
-
84961674028
-
Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes
-
Through construction of a PURE-based artificial translation system with all native ARSs omitted the authors demonstrate the potential to significantly expand the genetic code by introduction of all desired pre-amino-acylated tRNAs.
-
25•• Iwane, Y., Hitomi, A., Murakami, H., Katoh, T., Goto, Y., Suga, H., Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes. Nat Chem 8 (2016), 317–325 Through construction of a PURE-based artificial translation system with all native ARSs omitted the authors demonstrate the potential to significantly expand the genetic code by introduction of all desired pre-amino-acylated tRNAs.
-
(2016)
Nat Chem
, vol.8
, pp. 317-325
-
-
Iwane, Y.1
Hitomi, A.2
Murakami, H.3
Katoh, T.4
Goto, Y.5
Suga, H.6
-
26
-
-
84977103522
-
Genetic code expansion by degeneracy reprogramming of arginyl codons
-
The authors artificially divide the arginine codon box by removal of native arginine tRNAs using Colicin D and reintroduction of individually pre-charged arginine tRNAs.
-
26• Lee, K.B., Hou, C.Y., Kim, C.E., Kim, D.M., Suga, H., Kang, T.J., Genetic code expansion by degeneracy reprogramming of arginyl codons. ChemBioChem 17 (2016), 1198–1201 The authors artificially divide the arginine codon box by removal of native arginine tRNAs using Colicin D and reintroduction of individually pre-charged arginine tRNAs.
-
(2016)
ChemBioChem
, vol.17
, pp. 1198-1201
-
-
Lee, K.B.1
Hou, C.Y.2
Kim, C.E.3
Kim, D.M.4
Suga, H.5
Kang, T.J.6
-
27
-
-
84859627442
-
Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems
-
27 Hipolito, C.J., Suga, H., Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems. Curr Opin Chem Biol 16 (2012), 196–203.
-
(2012)
Curr Opin Chem Biol
, vol.16
, pp. 196-203
-
-
Hipolito, C.J.1
Suga, H.2
-
28
-
-
84959019914
-
Ribosomal synthesis of peptides with multiple β-amino acids
-
The authors singly introduce 13 different β-amino acids into a peptide chain, providing the first example of such wildtype ribosomal incorporation.
-
28•• Fujino, T., Goto, Y., Suga, H., Murakami, H., Ribosomal synthesis of peptides with multiple β-amino acids. J Am Chem Soc 138 (2016), 1962–1969 The authors singly introduce 13 different β-amino acids into a peptide chain, providing the first example of such wildtype ribosomal incorporation.
-
(2016)
J Am Chem Soc
, vol.138
, pp. 1962-1969
-
-
Fujino, T.1
Goto, Y.2
Suga, H.3
Murakami, H.4
-
29
-
-
84873389412
-
Reevaluation of the D-amino acid compatibility with the elongation event in translation
-
29 Fujino, T., Goto, Y., Suga, H., Murakami, H., Reevaluation of the D-amino acid compatibility with the elongation event in translation. J Am Chem Soc 135 (2013), 1830–1837.
-
(2013)
J Am Chem Soc
, vol.135
, pp. 1830-1837
-
-
Fujino, T.1
Goto, Y.2
Suga, H.3
Murakami, H.4
-
30
-
-
38349027623
-
Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides
-
30 Goto, Y., Ohta, A., Sako, Y., Yamagishi, Y., Murakami, H., Suga, H., Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides. ACS Chem Biol 3 (2008), 120–129.
-
(2008)
ACS Chem Biol
, vol.3
, pp. 120-129
-
-
Goto, Y.1
Ohta, A.2
Sako, Y.3
Yamagishi, Y.4
Murakami, H.5
Suga, H.6
-
31
-
-
58549114677
-
Slow peptide bond formation by proline and other N-alkylamino acids in translation
-
31 Pavlov, M.Y., Watts, R.E., Tan, Z., Cornish, V.W., Ehrenberg, M., Forster, A.C., Slow peptide bond formation by proline and other N-alkylamino acids in translation. Proc Natl Acad Sci U S A 106 (2009), 50–54.
-
(2009)
Proc Natl Acad Sci U S A
, vol.106
, pp. 50-54
-
-
Pavlov, M.Y.1
Watts, R.E.2
Tan, Z.3
Cornish, V.W.4
Ehrenberg, M.5
Forster, A.C.6
-
32
-
-
84929206937
-
The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center
-
32 Englander, M.T., Avins, J.L., Fleisher, R.C., Liu, B., Effraim, P.R., Wang, J., Schulten, K., Leyh, T.S., Gonzalez, R.L. Jr, Cornish, V.W., The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center. Proc Natl Acad Sci U S A 112 (2015), 6038–6043.
-
(2015)
Proc Natl Acad Sci U S A
, vol.112
, pp. 6038-6043
-
-
Englander, M.T.1
Avins, J.L.2
Fleisher, R.C.3
Liu, B.4
Effraim, P.R.5
Wang, J.6
Schulten, K.7
Leyh, T.S.8
Gonzalez, R.L.9
Cornish, V.W.10
-
33
-
-
38349062552
-
Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides
-
33 Kawakami, T., Murakami, H., Suga, H., Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides. Chem Biol 15 (2008), 32–42.
-
(2008)
Chem Biol
, vol.15
, pp. 32-42
-
-
Kawakami, T.1
Murakami, H.2
Suga, H.3
-
34
-
-
45749150319
-
Initiating translation with D-amino acids
-
34 Goto, Y., Murakami, H., Suga, H., Initiating translation with D-amino acids. RNA 14 (2008), 1390–1398.
-
(2008)
RNA
, vol.14
, pp. 1390-1398
-
-
Goto, Y.1
Murakami, H.2
Suga, H.3
-
35
-
-
84942134801
-
Outwitting EF-Tu and the ribosome: translation with D-amino acids
-
35 Achenbach, J., Jahnz, M., Bethge, L., Paal, K., Jung, M., Schuster, M., Albrecht, R., Jarosch, F., Nierhaus, K.H., Klussmann, S., Outwitting EF-Tu and the ribosome: translation with D-amino acids. Nucleic Acids Res 43 (2015), 5687–5698.
-
(2015)
Nucleic Acids Res
, vol.43
, pp. 5687-5698
-
-
Achenbach, J.1
Jahnz, M.2
Bethge, L.3
Paal, K.4
Jung, M.5
Schuster, M.6
Albrecht, R.7
Jarosch, F.8
Nierhaus, K.H.9
Klussmann, S.10
-
36
-
-
85009431697
-
Consecutive elongation of D-amino acids in translation
-
Glu and translation system (increased EF-Tu/Ts, IF2 and decreased EF-G).
-
Glu and translation system (increased EF-Tu/Ts, IF2 and decreased EF-G).
-
(2017)
Cell Chem Biol
, vol.24
, pp. 46-54
-
-
Katoh, T.1
Tajima, K.2
Suga, H.3
-
37
-
-
84943541737
-
Post-translational introduction of D-alanine into ribosomally synthesized peptides by the dehydroalanine reductase NpnJ
-
The authors show the assymetric reduction of dehydroalanine, generated from serine, using NpnJ reductase and NADPH. Their reconstituted in vitro system shows a broad substrate tolerance.
-
37• Yang, X., Van Der Donk, W.A., Post-translational introduction of D-alanine into ribosomally synthesized peptides by the dehydroalanine reductase NpnJ. J Am Chem Soc 137 (2015), 12426–12429 The authors show the assymetric reduction of dehydroalanine, generated from serine, using NpnJ reductase and NADPH. Their reconstituted in vitro system shows a broad substrate tolerance.
-
(2015)
J Am Chem Soc
, vol.137
, pp. 12426-12429
-
-
Yang, X.1
Van Der Donk, W.A.2
-
38
-
-
85016293162
-
Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium
-
Polytheonamide is a ribosomal peptide, with up to 50 site specific post-translational modifications including epimerization and methylation. Here, the authors show that only seven enzymes are sufficient for generating the final peptide.
-
38• Freeman, M.F., Helf, M.J., Bhushan, A., Morinaka, B.I., Piel, J., Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium. Nat Chem, 2016, 10.1038/NCHEM.2666 Polytheonamide is a ribosomal peptide, with up to 50 site specific post-translational modifications including epimerization and methylation. Here, the authors show that only seven enzymes are sufficient for generating the final peptide.
-
(2016)
Nat Chem
-
-
Freeman, M.F.1
Helf, M.J.2
Bhushan, A.3
Morinaka, B.I.4
Piel, J.5
-
39
-
-
84903151161
-
One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase
-
The authors have established a one-pot procedure for generating azoline containing peptidesin vitro by combining the FIT system with the posttranslational cyclodehydratase PatD.
-
39• Goto, Y., Ito, Y., Kato, Y., Tsunoda, S., Suga, H., One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase. Chem Biol 21 (2014), 766–774 The authors have established a one-pot procedure for generating azoline containing peptidesin vitro by combining the FIT system with the posttranslational cyclodehydratase PatD.
-
(2014)
Chem Biol
, vol.21
, pp. 766-774
-
-
Goto, Y.1
Ito, Y.2
Kato, Y.3
Tsunoda, S.4
Suga, H.5
-
40
-
-
84994026531
-
A post-translational cyclodehydratase, PatD, tolerates sequence variation in the C-terminal region of substrate peptides
-
40 Goto, Y., Suga, H., A post-translational cyclodehydratase, PatD, tolerates sequence variation in the C-terminal region of substrate peptides. Chem Lett 45 (2016), 1247–1249.
-
(2016)
Chem Lett
, vol.45
, pp. 1247-1249
-
-
Goto, Y.1
Suga, H.2
-
41
-
-
84902244730
-
Rapid, hydrolytically stable modification of aldehyde-terminated proteins and phage libraries
-
41 Kitov, P.I., Vinals, D.F., Ng, S., Tjhung, K.F., Derda, R., Rapid, hydrolytically stable modification of aldehyde-terminated proteins and phage libraries. J Am Chem Soc 136 (2014), 8149–8152.
-
(2014)
J Am Chem Soc
, vol.136
, pp. 8149-8152
-
-
Kitov, P.I.1
Vinals, D.F.2
Ng, S.3
Tjhung, K.F.4
Derda, R.5
-
42
-
-
84954443573
-
Silent encoding of chemical post-translational modifications in phage-displayed libraries
-
42 Tjhung, K.F., Kitov, P.I., Ng, S., Kitova, E.N., Deng, L., Klassen, J.S., Derda, R., Silent encoding of chemical post-translational modifications in phage-displayed libraries. J Am Chem Soc 138 (2016), 32–35.
-
(2016)
J Am Chem Soc
, vol.138
, pp. 32-35
-
-
Tjhung, K.F.1
Kitov, P.I.2
Ng, S.3
Kitova, E.N.4
Deng, L.5
Klassen, J.S.6
Derda, R.7
-
43
-
-
84881369201
-
A monosaccharide-modified peptide phage library for screening of ligands to carbohydrate-binding proteins
-
43 Arai, K., Tsutsumi, H., Mihara, H., A monosaccharide-modified peptide phage library for screening of ligands to carbohydrate-binding proteins. Bioorg Med Chem Lett 23 (2013), 4940–4943.
-
(2013)
Bioorg Med Chem Lett
, vol.23
, pp. 4940-4943
-
-
Arai, K.1
Tsutsumi, H.2
Mihara, H.3
-
44
-
-
0037348840
-
A novel strategy for in vitro selection of peptide–drug conjugates
-
44 Li, S., Roberts, R.W., A novel strategy for in vitro selection of peptide–drug conjugates. Chem Biol 10 (2003), 233–239.
-
(2003)
Chem Biol
, vol.10
, pp. 233-239
-
-
Li, S.1
Roberts, R.W.2
-
45
-
-
84896691426
-
Discovery of light-responsive ligands through screening of a light-responsive genetically encoded library
-
45 Jafari, M.R., Deng, L., Kitov, P.I., Ng, S., Matochko, W.L., Tjhung, K.F., Zeberoff, A., Elias, A., Klassen, J.S., Derda, R., Discovery of light-responsive ligands through screening of a light-responsive genetically encoded library. ACS Chem Biol 9 (2014), 443–450.
-
(2014)
ACS Chem Biol
, vol.9
, pp. 443-450
-
-
Jafari, M.R.1
Deng, L.2
Kitov, P.I.3
Ng, S.4
Matochko, W.L.5
Tjhung, K.F.6
Zeberoff, A.7
Elias, A.8
Klassen, J.S.9
Derda, R.10
-
46
-
-
67650305952
-
Phage-encoded combinatorial chemical libraries based on bicyclic peptides
-
46 Heinis, C., Rutherford, T., Freund, S., Winter, G., Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat Chem Biol 5 (2009), 502–507.
-
(2009)
Nat Chem Biol
, vol.5
, pp. 502-507
-
-
Heinis, C.1
Rutherford, T.2
Freund, S.3
Winter, G.4
-
47
-
-
21044441799
-
Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces
-
47 Timmerman, P., Beld, J., Puijk, W.C., Meloen, R.H., Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces. ChemBioChem 6 (2005), 821–824.
-
(2005)
ChemBioChem
, vol.6
, pp. 821-824
-
-
Timmerman, P.1
Beld, J.2
Puijk, W.C.3
Meloen, R.H.4
-
48
-
-
84964400045
-
Phage selection of chemically stabilized α-helical peptide ligands
-
48 Diderich, P., Bertoldo, D., Dessen, P., Khan, M.M., Pizzitola, I., Held, W., Huelsken, J., Heinis, C., Phage selection of chemically stabilized α-helical peptide ligands. ACS Chem Biol 11 (2016), 1422–1427.
-
(2016)
ACS Chem Biol
, vol.11
, pp. 1422-1427
-
-
Diderich, P.1
Bertoldo, D.2
Dessen, P.3
Khan, M.M.4
Pizzitola, I.5
Held, W.6
Huelsken, J.7
Heinis, C.8
-
49
-
-
84935007768
-
Synthesis of fused tricyclic peptides using a reprogrammed translation system and chemical modification
-
49 Bashiruddin, N.K., Nagano, M., Suga, H., Synthesis of fused tricyclic peptides using a reprogrammed translation system and chemical modification. Bioorg Chem 61 (2015), 45–50.
-
(2015)
Bioorg Chem
, vol.61
, pp. 45-50
-
-
Bashiruddin, N.K.1
Nagano, M.2
Suga, H.3
-
50
-
-
82955227984
-
Bacterial display and screening of posttranslationally thioether-stabilized peptides
-
50 Bosma, T., Kuipers, A., Bulten, E., de Vries, L., Rink, R., Moll, G.N., Bacterial display and screening of posttranslationally thioether-stabilized peptides. Appl Environ Microbiol 77 (2011), 6794–6801.
-
(2011)
Appl Environ Microbiol
, vol.77
, pp. 6794-6801
-
-
Bosma, T.1
Kuipers, A.2
Bulten, E.3
de Vries, L.4
Rink, R.5
Moll, G.N.6
-
51
-
-
70349556387
-
Ribosomal synthesis of cyclic peptides with a fluorogenic oxidative coupling reaction
-
51 Yamagishi, Y., Ashigai, H., Goto, Y., Murakami, H., Suga, H., Ribosomal synthesis of cyclic peptides with a fluorogenic oxidative coupling reaction. ChemBioChem 10 (2009), 1469–1472.
-
(2009)
ChemBioChem
, vol.10
, pp. 1469-1472
-
-
Yamagishi, Y.1
Ashigai, H.2
Goto, Y.3
Murakami, H.4
Suga, H.5
-
52
-
-
44949231370
-
Ribosomal synthesis of bicyclic peptides via two orthogonal inter-side-chain reactions
-
52 Sako, Y., Morimoto, J., Murakami, H., Suga, H., Ribosomal synthesis of bicyclic peptides via two orthogonal inter-side-chain reactions. J Am Chem Soc 130 (2008), 7232–7234.
-
(2008)
J Am Chem Soc
, vol.130
, pp. 7232-7234
-
-
Sako, Y.1
Morimoto, J.2
Murakami, H.3
Suga, H.4
-
53
-
-
84880359790
-
A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells
-
53 Miranda, E., Nordgren, I.K., Male, A.L., Lawrence, C.E., Hoakwie, F., Cuda, F., Court, W., Fox, K.R., Townsend, P.A., Packham, G.K., et al. A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells. J Am Chem Soc 135 (2013), 10418–10425.
-
(2013)
J Am Chem Soc
, vol.135
, pp. 10418-10425
-
-
Miranda, E.1
Nordgren, I.K.2
Male, A.L.3
Lawrence, C.E.4
Hoakwie, F.5
Cuda, F.6
Court, W.7
Fox, K.R.8
Townsend, P.A.9
Packham, G.K.10
-
54
-
-
84974556085
-
Development of potent and selective S. aureus sortase A inhibitors based on peptide macrocycles
-
54 Rentero Rebollo, I., McCallin, S., Bertoldo, D., Entenza, J.M., Moreillon, P., Heinis, C., Development of potent and selective S. aureus sortase A inhibitors based on peptide macrocycles. ACS Med Chem Lett 7 (2016), 606–611.
-
(2016)
ACS Med Chem Lett
, vol.7
, pp. 606-611
-
-
Rentero Rebollo, I.1
McCallin, S.2
Bertoldo, D.3
Entenza, J.M.4
Moreillon, P.5
Heinis, C.6
-
55
-
-
84995793657
-
Allosteric inhibition of a Semaphorin 4D receptor Plexin B1 by a high-affinity macrocyclic peptide
-
The authors show the generation and characterisation of a macrocyclic peptide, which allosterically inhibits Semaphorin receptor Plexin B1.
-
55• Matsunaga, Y., Bashiruddin, N.K., Kitago, Y., Takagi, J., Suga, H., Allosteric inhibition of a Semaphorin 4D receptor Plexin B1 by a high-affinity macrocyclic peptide. Cell Chem Biol 23 (2016), 1341–1350 The authors show the generation and characterisation of a macrocyclic peptide, which allosterically inhibits Semaphorin receptor Plexin B1.
-
(2016)
Cell Chem Biol
, vol.23
, pp. 1341-1350
-
-
Matsunaga, Y.1
Bashiruddin, N.K.2
Kitago, Y.3
Takagi, J.4
Suga, H.5
-
56
-
-
85014117670
-
Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides
-
The authors use the RaPID system to identify a potent nonapeptide inhibitor of human pancreatic α-amylase with high selectivity over other glycosidases.
-
56• Jongkees, S.A.K., Caner, S., Tysoe, C., Brayer, G.D., Withers, S.G., Suga, H., Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides. Cell Chem Biol, 2017, 10.1016/j.chembiol.2017.02.001 The authors use the RaPID system to identify a potent nonapeptide inhibitor of human pancreatic α-amylase with high selectivity over other glycosidases.
-
(2017)
Cell Chem Biol
-
-
Jongkees, S.A.K.1
Caner, S.2
Tysoe, C.3
Brayer, G.D.4
Withers, S.G.5
Suga, H.6
-
57
-
-
84859709933
-
Phage display screening without repetitious selection rounds
-
57 ‘t Hoen, P.C., Jirka, S.M., Ten Broeke, B.R., Schultes, E.A., Aguilera, B., Pang, K.H., Heemskerk, H., Aartsma-Rus, A., Van Ommen, G.J., den Dunnen, J.T., Phage display screening without repetitious selection rounds. Anal Biochem 421 (2012), 622–631.
-
(2012)
Anal Biochem
, vol.421
, pp. 622-631
-
-
t Hoen, P.C.1
Jirka, S.M.2
Ten Broeke, B.R.3
Schultes, E.A.4
Aguilera, B.5
Pang, K.H.6
Heemskerk, H.7
Aartsma-Rus, A.8
Van Ommen, G.J.9
den Dunnen, J.T.10
-
58
-
-
84870621677
-
Single-round, multiplexed antibody mimetic design through mRNA display
-
58 Olson, C.A., Nie, J., Diep, J., Al-Shyoukh, I., Takahashi, T.T., Al-Mawsawi, L.Q., Bolin, J.M., Elwell, A.L., Swanson, S., Stewart, R., et al. Single-round, multiplexed antibody mimetic design through mRNA display. Angew Chem Int Ed 51 (2012), 12449–12453.
-
(2012)
Angew Chem Int Ed
, vol.51
, pp. 12449-12453
-
-
Olson, C.A.1
Nie, J.2
Diep, J.3
Al-Shyoukh, I.4
Takahashi, T.T.5
Al-Mawsawi, L.Q.6
Bolin, J.M.7
Elwell, A.L.8
Swanson, S.9
Stewart, R.10
-
59
-
-
84960425701
-
High-throughput measurement of binding kinetics by mRNA display and next-generation sequencing
-
D of selected peptides in addition to the rank order by enrichment level. Their method allowed them to identify higher affinity, but less enriched peptides that would not have been identified by traditional screening methods.
-
D of selected peptides in addition to the rank order by enrichment level. Their method allowed them to identify higher affinity, but less enriched peptides that would not have been identified by traditional screening methods.
-
(2016)
Angew Chem Int Ed
, vol.55
, pp. 4007-4010
-
-
Jalali-Yazdi, F.1
Lai, L.H.2
Takahashi, T.T.3
Roberts, R.W.4
-
60
-
-
84985914489
-
Peptide synthesis on a next-generation DNA sequencing platform
-
On an Illumina sequencing chip, DNA clusters were transcribed into RNA and translated into peptides, both being immobilised to the original DNA cluster. This platform sets the stage for massive parallel peptide screening.
-
60•• Svensen, N., Peersen, O.B., Jaffrey, S.R., Peptide synthesis on a next-generation DNA sequencing platform. ChemBioChem 17 (2016), 1628–1635 On an Illumina sequencing chip, DNA clusters were transcribed into RNA and translated into peptides, both being immobilised to the original DNA cluster. This platform sets the stage for massive parallel peptide screening.
-
(2016)
ChemBioChem
, vol.17
, pp. 1628-1635
-
-
Svensen, N.1
Peersen, O.B.2
Jaffrey, S.R.3
-
61
-
-
84994009729
-
Passive membrane permeability in cyclic peptomer scaffolds is robust to extensive variation in side chain functionality and backbone geometry
-
61 Furukawa, A., Townsend, C.E., Schwochert, J., Pye, C.R., Bednarek, M.A., Lokey, R.S., Passive membrane permeability in cyclic peptomer scaffolds is robust to extensive variation in side chain functionality and backbone geometry. J Med Chem 59 (2016), 9503–9512.
-
(2016)
J Med Chem
, vol.59
, pp. 9503-9512
-
-
Furukawa, A.1
Townsend, C.E.2
Schwochert, J.3
Pye, C.R.4
Bednarek, M.A.5
Lokey, R.S.6
-
62
-
-
0026546880
-
Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor
-
62 Cull, M.G., Miller, J.F., Schatz, P.J., Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor. Proc Natl Acad Sci U S A 89 (1992), 1865–1869.
-
(1992)
Proc Natl Acad Sci U S A
, vol.89
, pp. 1865-1869
-
-
Cull, M.G.1
Miller, J.F.2
Schatz, P.J.3
-
63
-
-
0035006427
-
Surface display on gram positive bacteria
-
63 Hansson, M., Samuelson, P., Gunneriusso, E., Ståhl, S., Surface display on gram positive bacteria. Comb Chem High Throughput Screen 4 (2001), 171–184.
-
(2001)
Comb Chem High Throughput Screen
, vol.4
, pp. 171-184
-
-
Hansson, M.1
Samuelson, P.2
Gunneriusso, E.3
Ståhl, S.4
-
64
-
-
0030994634
-
Yeast surface display for screening combinatorial polypeptide libraries
-
64 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
-
65
-
-
0021818675
-
Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
-
65 Smith, G.P., Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228 (1985), 1315–1317.
-
(1985)
Science
, vol.228
, pp. 1315-1317
-
-
Smith, G.P.1
-
66
-
-
1542297763
-
CIS display: in vitro selection of peptides from libraries of protein–DNA complexes
-
66 Odegrip, R., Coomber, D., Eldridge, B., Hederer, R., Kuhlman, P.A., Ullman, C., FitzGerald, K., McGregor, D., CIS display: in vitro selection of peptides from libraries of protein–DNA complexes. Proc Natl Acad Sci U S A 101 (2004), 2806–2810.
-
(2004)
Proc Natl Acad Sci U S A
, vol.101
, pp. 2806-2810
-
-
Odegrip, R.1
Coomber, D.2
Eldridge, B.3
Hederer, R.4
Kuhlman, P.A.5
Ullman, C.6
FitzGerald, K.7
McGregor, D.8
-
67
-
-
0028592703
-
An in vitro polysome display system for identifying ligands from very large peptide libraries
-
67 Mattheakis, L.C., Bhattt, R.R., Dower, W.J., An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci U S A 91 (1994), 9022–9026.
-
(1994)
Proc Natl Acad Sci U S A
, vol.91
, pp. 9022-9026
-
-
Mattheakis, L.C.1
Bhattt, R.R.2
Dower, W.J.3
-
68
-
-
84555190565
-
Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library
-
68 Yamagishi, Y., Shoji, I., Miyagawa, S., Kawakami, T., Katoh, T., Goto, Y., Suga, H., Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library. Chem Biol 18 (2011), 1562–1570.
-
(2011)
Chem Biol
, vol.18
, pp. 1562-1570
-
-
Yamagishi, Y.1
Shoji, I.2
Miyagawa, S.3
Kawakami, T.4
Katoh, T.5
Goto, Y.6
Suga, H.7
-
69
-
-
84876021006
-
TRAP display: a high-speed selection method for the generation of functional polypeptides
-
69 Ishizawa, T., Kawakami, T., Reid, P.C., Murakami, H., TRAP display: a high-speed selection method for the generation of functional polypeptides. J Am Chem Soc 135 (2013), 5433–5440.
-
(2013)
J Am Chem Soc
, vol.135
, pp. 5433-5440
-
-
Ishizawa, T.1
Kawakami, T.2
Reid, P.C.3
Murakami, H.4
|