Tammo Diercks

2.9k total citations
74 papers, 2.1k citations indexed

About

Tammo Diercks is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Tammo Diercks has authored 74 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 62 papers in Molecular Biology, 15 papers in Spectroscopy and 12 papers in Materials Chemistry. Recurrent topics in Tammo Diercks's work include Glycosylation and Glycoproteins Research (19 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (11 papers). Tammo Diercks is often cited by papers focused on Glycosylation and Glycoproteins Research (19 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (11 papers). Tammo Diercks collaborates with scholars based in Spain, Germany and United States. Tammo Diercks's co-authors include Horst Kessler, M.P. Coles, Óscar Millet, Jesús Jiménez‐Barbero, Horst Kessler, Frank Siedler, Luis Moroder, Hans‐Joachim Gabius, Mark A. Daniëls and Gabriel Ortega and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Tammo Diercks

71 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tammo Diercks Spain 29 1.6k 307 263 220 171 74 2.1k
Hui Sun Lee United States 22 1.6k 1.0× 310 1.0× 224 0.9× 130 0.6× 130 0.8× 43 2.3k
Alexander Shekhtman United States 37 3.1k 2.0× 258 0.8× 301 1.1× 296 1.3× 185 1.1× 133 4.6k
Daniel O. Cicero Italy 25 1.3k 0.8× 317 1.0× 312 1.2× 223 1.0× 324 1.9× 122 2.3k
D. Bruce Fulton United States 29 1.6k 1.0× 251 0.8× 144 0.5× 120 0.5× 230 1.3× 64 2.7k
Diane Joseph‐McCarthy United States 32 1.7k 1.1× 310 1.0× 408 1.6× 192 0.9× 172 1.0× 78 2.8k
Daniel F. Wyss United States 31 1.6k 1.0× 382 1.2× 227 0.9× 164 0.7× 323 1.9× 58 3.4k
Bent W. Sigurskjold Denmark 25 1.3k 0.9× 303 1.0× 223 0.8× 151 0.7× 109 0.6× 40 2.0k
Robert X. Xu United States 22 1.5k 1.0× 251 0.8× 247 0.9× 168 0.8× 339 2.0× 30 2.3k
Debnath Pal India 21 1.7k 1.1× 347 1.1× 536 2.0× 285 1.3× 127 0.7× 102 2.4k
Bernard Gsell Switzerland 17 907 0.6× 302 1.0× 244 0.9× 115 0.5× 200 1.2× 19 1.7k

Countries citing papers authored by Tammo Diercks

Since Specialization
Citations

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

Fields of papers citing papers by Tammo Diercks

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tammo Diercks

This figure shows the co-authorship network connecting the top 25 collaborators of Tammo Diercks. A scholar is included among the top collaborators of Tammo Diercks 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 Tammo Diercks. Tammo Diercks 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.
Unione, Luca, Gerlof P. Bosman, Roosmarijn van der Woude, et al.. (2024). Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling. Nature Communications. 15(1). 2979–2979. 9 indexed citations
2.
Escobedo, Albert, Juan Aranda, Tammo Diercks, et al.. (2022). A glutamine-based single α-helix scaffold to target globular proteins. Nature Communications. 13(1). 7073–7073. 7 indexed citations
3.
Lesovoy, Dmitry, Tammo Diercks, Irena Matečko‐Burmann, et al.. (2021). Unambiguous Tracking of Protein Phosphorylation by Fast High‐Resolution FOSY NMR**. Angewandte Chemie International Edition. 60(44). 23540–23544. 4 indexed citations
4.
Lesovoy, Dmitry, Tammo Diercks, Irena Matečko‐Burmann, et al.. (2021). Unambiguous Tracking of Protein Phosphorylation by Fast High‐Resolution FOSY NMR**. Angewandte Chemie. 133(44). 23732–23736.
5.
Schedlbauer, Andreas, Anna‐Kristin Ludwig, Herbert Kaltner, et al.. (2021). Characterizing ligand-induced conformational changes in clinically relevant galectin-1 by HN/H2O (D2O) exchange. Biochimie. 187. 48–56. 4 indexed citations
6.
Blanco, Francisco J., et al.. (2020). Non‐Stationary Complementary Non‐Uniform Sampling (NOSCO NUS) for Fast Acquisition of Serial 2D NMR Titration Data. Angewandte Chemie. 132(52). 23702–23705. 2 indexed citations
7.
Blanco, Francisco J., et al.. (2020). Non‐Stationary Complementary Non‐Uniform Sampling (NOSCO NUS) for Fast Acquisition of Serial 2D NMR Titration Data. Angewandte Chemie International Edition. 59(52). 23496–23499. 2 indexed citations
8.
Bruzzone, Chiara, Maider Bizkarguenaga, Rubén Gil‐Redondo, et al.. (2020). SARS-CoV-2 Infection Dysregulates the Metabolomic and Lipidomic Profiles of Serum. iScience. 23(10). 101645–101645. 151 indexed citations
9.
Escobedo, Albert, Micha B. A. Kunze, Juan Aranda, et al.. (2019). Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor. Nature Communications. 10(1). 2034–2034. 78 indexed citations
10.
Embade, Nieves, Claire Cannet, Tammo Diercks, et al.. (2019). NMR-based newborn urine screening for optimized detection of inherited errors of metabolism. Scientific Reports. 9(1). 13067–13067. 29 indexed citations
11.
Oyenarte, Iker, Serge Hardy, Tilman Breiderhoff, et al.. (2016). Structural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2. Journal of Biological Chemistry. 292(3). 786–801. 45 indexed citations
12.
Ortega, Gabriel, Tammo Diercks, & Óscar Millet. (2015). Halophilic Protein Adaptation Results from Synergistic Residue-Ion Interactions in the Folded and Unfolded States. Chemistry & Biology. 22(12). 1597–1607. 44 indexed citations
13.
Echeverría, Begoña, Antonio Franconetti, Sonia Serna, et al.. (2015). Monitoring Glycan–Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH–π Interactions. Chemistry - A European Journal. 21(32). 11408–11416. 16 indexed citations
14.
Jong, Rob N. de, Vincent Truffault, Tammo Diercks, et al.. (2008). Structure and DNA Binding of the Human Rtf1 Plus3 Domain. Structure. 16(1). 149–159. 38 indexed citations
15.
Diercks, Tammo & Vladislav Orekhov. (2005). qTROSY – a novel scheme for recovery of the anti-TROSY magnetisation. Journal of Biomolecular NMR. 32(2). 113–127. 3 indexed citations
16.
Diercks, Tammo, Mark A. Daniëls, & Robert Kaptein. (2005). Extended Flip-back Schemes for Sensitivity Enhancement in Multidimensional HSQC-type Out-and-back Experiments. Journal of Biomolecular NMR. 33(4). 243–259. 42 indexed citations
17.
Kessler, Horst, Markus Heller, Gerd Gemmecker, et al.. (2003). NMR in Medicinal Chemistry. PubMed. 59–85.
18.
Robelek, Rudolf, Tammo Diercks, Stephan C. Schuster, et al.. (2002). Transcriptional Regulation by Antitermination. Interaction of RNA with NusB Protein and NusB/NusE Protein Complex of Escherichia coli. Journal of Molecular Biology. 316(4). 875–885. 29 indexed citations
19.
Klein, Christian, Eckart Planker, Tammo Diercks, et al.. (2001). NMR Spectroscopy Reveals the Solution Dimerization Interface of p53 Core Domains Bound to Their Consensus DNA. Journal of Biological Chemistry. 276(52). 49020–49027. 76 indexed citations
20.
Coles, M.P., Tammo Diercks, Beate Rockel, et al.. (1999). The solution structure of VAT-N reveals a ‘missing link’ in the evolution of complex enzymes from a simple βαββ element. Current Biology. 9(20). 1158–1168. 82 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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