Rime Kerfah

525 total citations
11 papers, 355 citations indexed

About

Rime Kerfah is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Rime Kerfah has authored 11 papers receiving a total of 355 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 5 papers in Materials Chemistry and 3 papers in Oncology. Recurrent topics in Rime Kerfah's work include Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and Peptidase Inhibition and Analysis (3 papers). Rime Kerfah is often cited by papers focused on Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and Peptidase Inhibition and Analysis (3 papers). Rime Kerfah collaborates with scholars based in France, United Kingdom and Germany. Rime Kerfah's co-authors include Jérôme Boisbouvier, Pierre Gans, Michael J. Plevin, Rémy Sounier, Olivier Hamelin, Pavel Macek, Elodie Crublet, Guy Schoehn, Paul Schanda and Diego F. Gauto and has published in prestigious journals such as Nature Communications, Chemical Communications and Science Advances.

In The Last Decade

Rime Kerfah

11 papers receiving 353 citations

Peers

Rime Kerfah
Thibault Viennet United States
Tomas Jacso Germany
Anne Schuetz Germany
Neil R. Birkett United Kingdom
Brian Fuglestad United States
Toni Vagt Germany
Rime Kerfah
Citations per year, relative to Rime Kerfah Rime Kerfah (= 1×) peers Venita Daebel

Countries citing papers authored by Rime Kerfah

Since Specialization
Citations

This map shows the geographic impact of Rime Kerfah'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 Rime Kerfah with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Rime Kerfah more than expected).

Fields of papers citing papers by Rime Kerfah

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rime Kerfah. 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 Rime Kerfah. The network helps show where Rime Kerfah may publish in the future.

Co-authorship network of co-authors of Rime Kerfah

This figure shows the co-authorship network connecting the top 25 collaborators of Rime Kerfah. A scholar is included among the top collaborators of Rime Kerfah 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 Rime Kerfah. Rime Kerfah is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

11 of 11 papers shown
1.
Crublet, Elodie, et al.. (2022). Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation. Biochemical Society Transactions. 50(6). 1555–1567. 8 indexed citations
2.
Kerfah, Rime, Ricarda Törner, Pavel Macek, et al.. (2021). Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain. Journal of Biomolecular NMR. 75(6-7). 221–232. 5 indexed citations
3.
Imbert, Lionel, Elodie Crublet, Isabel Ayala, et al.. (2020). In Vitro Production of Perdeuterated Proteins in H2O for Biomolecular NMR Studies. Methods in molecular biology. 127–149. 11 indexed citations
4.
Ayala, Isabel, et al.. (2020). Asymmetric Synthesis of Methyl Specifically Labelled L ‐Threonine and Application to the NMR Studies of High Molecular Weight Proteins. ChemistrySelect. 5(17). 5092–5098. 10 indexed citations
5.
Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, et al.. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10(1). 2697–2697. 76 indexed citations
6.
Macek, Pavel, Rime Kerfah, Elisabetta Boeri Erba, et al.. (2017). Unraveling self-assembly pathways of the 468-kDa proteolytic machine TET2. Science Advances. 3(4). e1601601–e1601601. 25 indexed citations
7.
Kurauskas, Vilius, Elodie Crublet, Pavel Macek, et al.. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: application to the 50S ribosome subunit. Chemical Communications. 52(61). 9558–9561. 23 indexed citations
8.
Kerfah, Rime, Olivier Hamelin, Jérôme Boisbouvier, & Dominique Marion. (2015). CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. Journal of Biomolecular NMR. 63(4). 389–402. 25 indexed citations
9.
Kerfah, Rime, Michael J. Plevin, Rémy Sounier, Pierre Gans, & Jérôme Boisbouvier. (2015). Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins. Current Opinion in Structural Biology. 32. 113–122. 130 indexed citations
10.
11.
Crublet, Elodie, Rime Kerfah, Guillaume Mas, et al.. (2013). A Cost-Effective Protocol for the Parallel Production of Libraries of 13CH3-Specifically Labeled Mutants for NMR Studies of High Molecular Weight Proteins. Methods in molecular biology. 1091. 229–244. 8 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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