Vladimir Torbeev

2.0k total citations
39 papers, 1.6k citations indexed

About

Vladimir Torbeev is a scholar working on Molecular Biology, Materials Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, Vladimir Torbeev has authored 39 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 9 papers in Materials Chemistry and 7 papers in Physical and Theoretical Chemistry. Recurrent topics in Vladimir Torbeev's work include Chemical Synthesis and Analysis (16 papers), Crystallography and molecular interactions (6 papers) and Glycosylation and Glycoproteins Research (5 papers). Vladimir Torbeev is often cited by papers focused on Chemical Synthesis and Analysis (16 papers), Crystallography and molecular interactions (6 papers) and Glycosylation and Glycoproteins Research (5 papers). Vladimir Torbeev collaborates with scholars based in France, United States and Switzerland. Vladimir Torbeev's co-authors include Stephen B. H. Kent, Leslie Leiserowitz, Isabelle Weissbuch, Meir Lahav, Thomas Durek, Donald Hilvert, Thomas W. Ebbesen, Robrecht M. A. Vergauwe, Jino George and Thibault Chervy and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Vladimir Torbeev

39 papers receiving 1.6k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Vladimir Torbeev France 19 762 465 395 308 208 39 1.6k
Alessandro Moretto Italy 33 1.5k 2.0× 991 2.1× 993 2.5× 403 1.3× 168 0.8× 106 3.0k
Christopher M. Baker United Kingdom 21 1.1k 1.4× 517 1.1× 167 0.4× 393 1.3× 143 0.7× 32 1.8k
Lisa Emily Chirlian United States 9 518 0.7× 310 0.7× 390 1.0× 501 1.6× 335 1.6× 10 1.5k
Daniel Trzesniak Switzerland 12 1.2k 1.5× 445 1.0× 156 0.4× 483 1.6× 126 0.6× 16 1.7k
Giuliano Zanchetta Italy 21 869 1.1× 291 0.6× 206 0.5× 166 0.5× 74 0.4× 49 1.6k
Guangju Chen China 22 835 1.1× 510 1.1× 599 1.5× 163 0.5× 185 0.9× 143 1.9k
Lara Martínez‐Fernández Spain 25 1.1k 1.4× 465 1.0× 314 0.8× 527 1.7× 618 3.0× 96 1.8k
Dmitri Toptygin United States 23 794 1.0× 314 0.7× 120 0.3× 304 1.0× 280 1.3× 49 1.3k
A. Bonincontro Italy 23 787 1.0× 274 0.6× 429 1.1× 233 0.8× 309 1.5× 107 1.6k

Countries citing papers authored by Vladimir Torbeev

Since Specialization
Citations

This map shows the geographic impact of Vladimir Torbeev's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Vladimir Torbeev with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Vladimir Torbeev more than expected).

Fields of papers citing papers by Vladimir Torbeev

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Vladimir Torbeev. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Vladimir Torbeev. The network helps show where Vladimir Torbeev may publish in the future.

Co-authorship network of co-authors of Vladimir Torbeev

This figure shows the co-authorship network connecting the top 25 collaborators of Vladimir Torbeev. A scholar is included among the top collaborators of Vladimir Torbeev based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Vladimir Torbeev. Vladimir Torbeev is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Sai, Masahiro, et al.. (2025). Single-molecule nanopore sensing of proline cis/trans amide isomers. Chemical Science. 16(22). 9730–9738. 1 indexed citations
2.
McEwen, Alastair G., Pierre Poussin‐Courmontagne, J.‐L. Schmitt, et al.. (2021). 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. 143(9). 3330–3339. 9 indexed citations
3.
Sinnaeve, Davy, Éva Erdmann, Bruno Linclau, et al.. (2021). Fluorine NMR study of proline-rich sequences using fluoroprolines. SHILAP Revista de lepidopterología. 2(2). 795–813. 8 indexed citations
4.
García, Ana M., et al.. (2021). Autofluorescence of Amyloids Determined by Enantiomeric Composition of Peptides. The Journal of Physical Chemistry B. 125(21). 5502–5510. 20 indexed citations
5.
García, Ana M., Youssef El Khoury, Coralie Spiegelhalter, et al.. (2020). Aggregation and Amyloidogenicity of the Nuclear Coactivator Binding Domain of CREB‐Binding Protein. Chemistry - A European Journal. 26(44). 9889–9899. 6 indexed citations
6.
Gógl, Gergő, Jožica Dolenc, Judit Ősz, et al.. (2020). Conformational editing of intrinsically disordered protein by α-methylation. Chemical Science. 12(3). 1080–1089. 10 indexed citations
7.
Kieffer, Bruno, et al.. (2018). Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue. Chemical Science. 9(25). 5594–5599. 4 indexed citations
8.
Chaloin, Olivier, et al.. (2017). Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues. Chemical Communications. 53(53). 7369–7372. 15 indexed citations
9.
Torbeev, Vladimir, et al.. (2015). Towards Prebiotic Catalytic Amyloids Using High Throughput Screening. PLoS ONE. 10(12). e0143948–e0143948. 69 indexed citations
10.
Torbeev, Vladimir & Stephen B. H. Kent. (2012). 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(30). 5887–5887. 23 indexed citations
11.
Torbeev, Vladimir, et al.. (2012). cis‐transPeptide‐Bond Isomerization inα‐Methylproline Derivatives. Helvetica Chimica Acta. 95(12). 2411–2420. 11 indexed citations
12.
Mandal, Kalyaneswar, Brad L. Pentelute, Duhee Bang, et al.. (2011). Design, Total Chemical Synthesis, and X‐Ray Structure of a Protein Having a Novel Linear‐Loop Polypeptide Chain Topology. Angewandte Chemie International Edition. 51(6). 1481–1486. 43 indexed citations
13.
14.
Torbeev, Vladimir, et al.. (2008). 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(16). 4554–4557. 12 indexed citations
15.
Torbeev, Vladimir & Stephen B. H. Kent. (2007). Convergent Chemical Synthesis and Crystal Structure of a 203 Amino Acid “Covalent Dimer” HIV‐1 Protease Enzyme Molecule. Angewandte Chemie International Edition. 46(10). 1667–1670. 144 indexed citations
16.
Torbeev, Vladimir & Stephen B. H. Kent. (2007). Convergent Chemical Synthesis and Crystal Structure of a 203 Amino Acid “Covalent Dimer” HIV‐1 Protease Enzyme Molecule. Angewandte Chemie. 119(10). 1697–1700. 43 indexed citations
17.
Weissbuch, Isabelle, Vladimir Torbeev, Leslie Leiserowitz, & Meir Lahav. (2005). Solvent Effect on Crystal Polymorphism: Why Addition of Methanol or Ethanol to Aqueous Solutions Induces the Precipitation of the Least Stable β Form of Glycine. Angewandte Chemie International Edition. 44(21). 3226–3229. 223 indexed citations
18.
Torbeev, Vladimir, Edna Shavit, Isabelle Weissbuch, Leslie Leiserowitz, & Meir Lahav. (2005). Control of Crystal Polymorphism by Tuning the Structure of Auxiliary Molecules as Nucleation Inhibitors. The β-Polymorph of Glycine Grown in Aqueous Solutions. Crystal Growth & Design. 5(6). 2190–2196. 122 indexed citations
19.
Kostyanovsky, Remir G., et al.. (2002). (±)-trans-1,2-Diaminocyclohexane crystallises as a conglomerate. Mendeleev Communications. 12(4). 147–148. 16 indexed citations
20.
Kostyanovsky, Remir G., Г. К. Кадоркина, Konstantin А. Lyssenko, et al.. (2002). Chiral drugs via the spontaneous resolution. Mendeleev Communications. 12(1). 6–8. 29 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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