Year |
Citation |
Score |
2024 |
Bachelart T, Kumar S, Jouin A, Yousef M, Kieffer B, Torbeev V. Design, Synthesis and Catalytic Activity of Protein Containing Thiotyrosine as an Active Site Residue. Chembiochem : a European Journal of Chemical Biology. e202400148. PMID 38629812 DOI: 10.1002/cbic.202400148 |
0.331 |
|
2021 |
Naudin EA, McEwen AG, Tan SK, Poussin-Courmontagne P, Schmitt JL, Birck C, DeGrado WF, Torbeev V. Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site. Journal of the American Chemical Society. PMID 33635059 DOI: 10.1021/jacs.0c10053 |
0.304 |
|
2020 |
Garcia AM, Giorgiutti C, El Khoury Y, Bauer V, Spiegelhalter C, Leize-Wagner E, Hellwig P, Potier N, Torbeev V. Aggregation and amyloidogenicity of nuclear coactivator binding domain of CREB-binding protein. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 32364648 DOI: 10.1002/Chem.202001847 |
0.403 |
|
2020 |
Torbeev V, Kent SBH. Chemical Synthesis of an Enzyme Containing an Artificial Catalytic Apparatus Australian Journal of Chemistry. 73: 321-326. DOI: 10.1071/Ch19460 |
0.42 |
|
2019 |
Baral A, Asokan A, Bauer V, Kieffer B, Torbeev V. Chemical synthesis of transactivation domain (TAD) of tumor suppressor protein p53 by native chemical ligation of three peptide segments Tetrahedron. 75: 703-708. DOI: 10.1016/J.Tet.2018.11.074 |
0.362 |
|
2018 |
Boehringer R, Kieffer B, Torbeev V. Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue. Chemical Science. 9: 5594-5599. PMID 30061991 DOI: 10.1039/C8Sc01790E |
0.416 |
|
2017 |
Schmidtgall B, Chaloin O, Bauer V, Sumyk M, Birck C, Torbeev V. Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues. Chemical Communications (Cambridge, England). PMID 28604862 DOI: 10.1039/C7Cc02276J |
0.351 |
|
2016 |
Ruiz J, Boehringer R, Grogg M, Raya J, Schirer A, Crucifix C, Hellwig P, Schultz P, Torbeev V. Covalent tethering and residues with bulky hydrophobic side chains enable to direct self-assembly of the distinct amyloid structures. Chembiochem : a European Journal of Chemical Biology. PMID 27717158 DOI: 10.1002/Cbic.201600440 |
0.406 |
|
2016 |
Torbeev V, Grogg M, Ruiz J, Boehringer R, Schirer A, Hellwig P, Jeschke G, Hilvert D. Chiral recognition in amyloid fiber growth. Journal of Peptide Science : An Official Publication of the European Peptide Society. PMID 26929241 DOI: 10.1002/Psc.2861 |
0.536 |
|
2015 |
Friedmann MP, Torbeev V, Zelenay V, Sobol A, Greenwald J, Riek R. Towards Prebiotic Catalytic Amyloids Using High Throughput Screening. Plos One. 10: e0143948. PMID 26650386 DOI: 10.1371/Journal.Pone.0143948 |
0.366 |
|
2015 |
Torbeev V, Ebert MO, Dolenc J, Hilvert D. Substitution of proline32 by α-methylproline preorganizes β2-microglobulin for oligomerization but not for aggregation into amyloids. Journal of the American Chemical Society. 137: 2524-35. PMID 25633201 DOI: 10.1021/Ja510109P |
0.572 |
|
2015 |
Torbeev V, Ebert MO, Dolenc J, Hilvert D. Substitution of proline32 by α-methylproline preorganizes β2-microglobulin for oligomerization but not for aggregation into amyloids Journal of the American Chemical Society. 137: 2524-2535. DOI: 10.1021/ja510109p |
0.347 |
|
2013 |
Torbeev VY, Hilvert D. Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly. Proceedings of the National Academy of Sciences of the United States of America. 110: 20051-6. PMID 24262149 DOI: 10.1073/Pnas.1310414110 |
0.515 |
|
2012 |
Torbeev VY, Kent SB. Ionization state of the catalytic dyad Asp25/25' in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis. Organic & Biomolecular Chemistry. 10: 5887-91. PMID 22659831 DOI: 10.1039/C2Ob25569C |
0.517 |
|
2012 |
Mandal K, Pentelute BL, Bang D, Gates ZP, Torbeev VY, Kent SB. Design, total chemical synthesis, and X-ray structure of a protein having a novel linear-loop polypeptide chain topology. Angewandte Chemie (International Ed. in English). 51: 1481-6. PMID 22213444 DOI: 10.1002/Anie.201107846 |
0.556 |
|
2012 |
Torbeev VY, Fumi E, Ebert MO, Schweizer WB, Hilvert D. Cis-trans peptide-bond isomerization in α-methylproline derivatives Helvetica Chimica Acta. 95: 2411-2420. DOI: 10.1002/Hlca.201200483 |
0.438 |
|
2011 |
Torbeev VY, Raghuraman H, Hamelberg D, Tonelli M, Westler WM, Perozo E, Kent SB. Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proceedings of the National Academy of Sciences of the United States of America. 108: 20982-7. PMID 22158985 DOI: 10.1073/Pnas.1111202108 |
0.582 |
|
2009 |
Torbeev VY, Raghuraman H, Mandal K, Senapati S, Perozo E, Kent SB. Dynamics of "flap" structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy. Journal of the American Chemical Society. 131: 884-5. PMID 19117390 DOI: 10.1021/Ja806526Z |
0.516 |
|
2008 |
Torbeev VY, Mandal K, Terechko VA, Kent SB. Reprint of "Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site" [Bioorg. Med. Chem. Lett. 18 (2008) 4554-4557]. Bioorganic & Medicinal Chemistry Letters. 18: 6012-5. PMID 18995173 DOI: 10.1016/S0960-894X(08)01314-0 |
0.544 |
|
2008 |
Torbeev VY, Mandal K, Terechko VA, Kent SB. Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site. Bioorganic & Medicinal Chemistry Letters. 18: 4554-7. PMID 18657969 DOI: 10.1016/J.Bmcl.2008.07.039 |
0.544 |
|
2007 |
Torbeev VY, Kent SB. Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule. Angewandte Chemie (International Ed. in English). 46: 1667-70. PMID 17397076 DOI: 10.1002/Anie.200604087 |
0.537 |
|
2007 |
Durek T, Torbeev VY, Kent SB. Convergent chemical synthesis and high-resolution x-ray structure of human lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 104: 4846-51. PMID 17360367 DOI: 10.1073/Pnas.0610630104 |
0.591 |
|
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