Ingrid R. Vetter

10.3k total citations · 1 hit paper
102 papers, 7.9k citations indexed

About

Ingrid R. Vetter is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Ingrid R. Vetter has authored 102 papers receiving a total of 7.9k indexed citations (citations by other indexed papers that have themselves been cited), including 89 papers in Molecular Biology, 32 papers in Cell Biology and 13 papers in Materials Chemistry. Recurrent topics in Ingrid R. Vetter's work include Protein Kinase Regulation and GTPase Signaling (22 papers), Microtubule and mitosis dynamics (19 papers) and Cellular transport and secretion (15 papers). Ingrid R. Vetter is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (22 papers), Microtubule and mitosis dynamics (19 papers) and Cellular transport and secretion (15 papers). Ingrid R. Vetter collaborates with scholars based in Germany, United States and Netherlands. Ingrid R. Vetter's co-authors include Alfred Wittinghofer, Herbert Waldmann, Rolf Breinbauer, Christian Herrmann, Roger S. Goody, Hans Robert Kalbitzer, Ilme Schlichting, Michael Spoerner, Andreas Arndt and Ulrike Kutay and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Ingrid R. Vetter

99 papers receiving 7.8k citations

Hit Papers

The Guanine Nucleotide-Binding Switch in Three Dimensions 2001 2026 2009 2017 2001 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ingrid R. Vetter Germany 48 6.4k 2.2k 909 747 519 102 7.9k
D.A.R. Sanders Canada 29 5.4k 0.8× 1.5k 0.7× 843 0.9× 988 1.3× 501 1.0× 89 7.1k
Simon E. V. Phillips United Kingdom 43 5.6k 0.9× 1.2k 0.6× 1.3k 1.4× 691 0.9× 711 1.4× 151 8.4k
Klaus Scheffzek Germany 43 5.2k 0.8× 1.5k 0.7× 797 0.9× 528 0.7× 991 1.9× 78 7.1k
Diana R. Tomchick United States 54 6.6k 1.0× 3.0k 1.4× 631 0.7× 571 0.8× 605 1.2× 115 9.6k
Matthias Wilmanns Germany 53 6.7k 1.1× 1.1k 0.5× 1.7k 1.9× 639 0.9× 469 0.9× 203 8.8k
Kalle Gehring Canada 53 7.0k 1.1× 1.8k 0.8× 601 0.7× 750 1.0× 598 1.2× 198 9.3k
Mischa Machius United States 47 4.4k 0.7× 1.6k 0.7× 695 0.8× 441 0.6× 369 0.7× 90 6.6k
Jacqueline Cherfils France 39 5.0k 0.8× 2.6k 1.2× 594 0.7× 402 0.5× 533 1.0× 108 6.4k
Timothy R. Dafforn United Kingdom 50 5.0k 0.8× 1.0k 0.5× 566 0.6× 477 0.6× 612 1.2× 152 7.4k
Chad A. Brautigam United States 47 5.1k 0.8× 1.5k 0.7× 508 0.6× 673 0.9× 418 0.8× 137 7.7k

Countries citing papers authored by Ingrid R. Vetter

Since Specialization
Citations

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

Fields of papers citing papers by Ingrid R. Vetter

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ingrid R. Vetter. 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 Ingrid R. Vetter. The network helps show where Ingrid R. Vetter may publish in the future.

Co-authorship network of co-authors of Ingrid R. Vetter

This figure shows the co-authorship network connecting the top 25 collaborators of Ingrid R. Vetter. A scholar is included among the top collaborators of Ingrid R. Vetter 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 Ingrid R. Vetter. Ingrid R. Vetter 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.
2.
Stege, Patricia, et al.. (2024). How Do Molecular Tweezers Bind to Proteins? Lessons from X-ray Crystallography. Molecules. 29(8). 1764–1764. 2 indexed citations
3.
Raisch, Tobias, Sabrina Ghetti, Marie Körner, et al.. (2024). Structure of the human KMN complex and implications for regulation of its assembly. Nature Structural & Molecular Biology. 31(6). 861–873. 13 indexed citations
4.
Pesenti, Marion E., et al.. (2024). Role of protein kinase PLK1 in the epigenetic maintenance of centromeres. Science. 385(6713). 1091–1097. 12 indexed citations
5.
Antoni, Anna De, et al.. (2023). Stable kinetochore‐microtubule attachment requires loop‐dependent Ndc80‐Ndc80 binding. The EMBO Journal. 42(13). e112504–e112504. 20 indexed citations
6.
Raisch, Tobias, Giuseppe Ciossani, Stefano Maffini, et al.. (2022). Structure of the RZZ complex and molecular basis of Spindly‐driven corona assembly at human kinetochores. The EMBO Journal. 41(9). e110411–e110411. 27 indexed citations
7.
Girbig, Mathias, Franziska Müller, Sabine Wohlgemuth, et al.. (2022). Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin. The Journal of Cell Biology. 221(11). 16 indexed citations
8.
Walstein, Kai, et al.. (2021). Assembly principles and stoichiometry of a complete human kinetochore module. Science Advances. 7(27). 40 indexed citations
9.
Rondelet, Arnaud, Yu‐Chih Lin, Andreas Hecker, et al.. (2020). Clathrin’s adaptor interaction sites are repurposed to stabilize microtubules during mitosis. The Journal of Cell Biology. 219(2). 25 indexed citations
10.
Piano, Valentina, et al.. (2020). CDC20 assists its catalytic incorporation in the mitotic checkpoint complex. Science. 371(6524). 67–71. 57 indexed citations
11.
Vetter, Ingrid R., Patricia Stege, Farnusch Kaschani, et al.. (2018). Identification of Noncatalytic Lysine Residues from Allosteric Circuits via Covalent Probes. ACS Chemical Biology. 13(5). 1307–1312. 8 indexed citations
12.
Rudack, Till, et al.. (2015). Catalysis of GTP Hydrolysis by Small GTPases at Atomic Detail by Integration of X-ray Crystallography, Experimental, and Theoretical IR Spectroscopy. Journal of Biological Chemistry. 290(40). 24079–24090. 20 indexed citations
13.
Pantoom, Supansa, Ingrid R. Vetter, Heino Prinz, & Wipa Suginta. (2011). Potent Family-18 Chitinase Inhibitors. Journal of Biological Chemistry. 286(27). 24312–24323. 30 indexed citations
14.
Ismail, Shehab, Ingrid R. Vetter, Begoña Sot, & Alfred Wittinghofer. (2010). The Structure of an Arf-ArfGAP Complex Reveals a Ca2+ Regulatory Mechanism. Cell. 143(7). 1190–1190. 2 indexed citations
15.
Shimada, Atsushi, Miklós Nyitrai, Ingrid R. Vetter, et al.. (2004). The Core FH2 Domain of Diaphanous-Related Formins Is an Elongated Actin Binding Protein that Inhibits Polymerization. Molecular Cell. 13(4). 511–522. 123 indexed citations
16.
Breinbauer, Rolf, Ingrid R. Vetter, & Herbert Waldmann. (2002). From Protein Domains to Drug CandidatesâNatural Products as Guiding Principles in the Design and Synthesis of Compound Libraries. Angewandte Chemie International Edition. 41(16). 2878–2878. 378 indexed citations
17.
Vetter, Ingrid R., Fred Hofmann, Sabine Wohlgemuth, Christian Herrmann, & Ingo Just. (2000). Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin. Journal of Molecular Biology. 301(5). 1091–1095. 51 indexed citations
18.
Hillig, R.C., Louis Renault, Ingrid R. Vetter, et al.. (1999). The Crystal Structure of rna1p. Molecular Cell. 3(6). 781–791. 96 indexed citations
19.
Vetter, Ingrid R., Michael W. Parker, Alec D. Tucker, et al.. (1998). Crystal structure of a colicin N fragment suggests a model for toxicity. Structure. 6(7). 863–874. 109 indexed citations
20.
Lavie, Arnon, et al.. (1997). The bottleneck in AZT activation. Nature Medicine. 3(8). 922–924. 110 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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