Philipp Koldewey

1.1k total citations
18 papers, 720 citations indexed

About

Philipp Koldewey is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Philipp Koldewey has authored 18 papers receiving a total of 720 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 7 papers in Materials Chemistry and 4 papers in Cell Biology. Recurrent topics in Philipp Koldewey's work include Enzyme Structure and Function (7 papers), Protein Structure and Dynamics (6 papers) and Heat shock proteins research (5 papers). Philipp Koldewey is often cited by papers focused on Enzyme Structure and Function (7 papers), Protein Structure and Dynamics (6 papers) and Heat shock proteins research (5 papers). Philipp Koldewey collaborates with scholars based in United States, United Kingdom and Switzerland. Philipp Koldewey's co-authors include James C.A. Bardwell, Scott Horowitz, Frederick Stull, Ursula Jakob, Raoul Martin, E. Neil G. Marsh, Brandon T. Ruotolo, Sheena E. Radford, Joseph D. Eschweiler and Min Su and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Philipp Koldewey

17 papers receiving 712 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Philipp Koldewey United States 13 598 153 124 119 112 18 720
Haiping Ke United States 12 684 1.1× 100 0.7× 61 0.5× 112 0.9× 226 2.0× 22 879
Nathalie Sassoon France 14 500 0.8× 93 0.6× 51 0.4× 91 0.8× 222 2.0× 16 676
Melisa Merdanovic Germany 13 527 0.9× 130 0.8× 42 0.3× 160 1.3× 313 2.8× 15 869
Andrea Vera Spain 14 633 1.1× 91 0.6× 80 0.6× 94 0.8× 166 1.5× 32 1.1k
Serge Pérez France 8 525 0.9× 59 0.4× 31 0.3× 107 0.9× 49 0.4× 10 716
Sreedevi Nallamsetty United States 10 572 1.0× 72 0.5× 46 0.4× 87 0.7× 160 1.4× 10 711
Aymeric Audfray France 16 601 1.0× 55 0.4× 50 0.4× 111 0.9× 35 0.3× 21 782
Gautier Robin Australia 12 541 0.9× 99 0.6× 203 1.6× 122 1.0× 76 0.7× 25 786
Tiago Q. Faria Portugal 16 469 0.8× 71 0.5× 37 0.3× 49 0.4× 96 0.9× 28 661
Eaazhisai Kandiah France 16 376 0.6× 68 0.4× 76 0.6× 42 0.4× 41 0.4× 28 568

Countries citing papers authored by Philipp Koldewey

Since Specialization
Citations

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

Fields of papers citing papers by Philipp Koldewey

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Philipp Koldewey

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

All Works

18 of 18 papers shown
1.
Heinig, Katja, Filippo Sladojevich, Georg Jaeschke, et al.. (2022). Chemical, Analytical and Pharmacokinetic Characterisation of RO7304898, an API Consisting of Two Rapidly Interconverting Diastereoisomers. Pharmaceutical Research. 39(4). 653–667.
2.
Richter, Kirsten, Arne C. Rufer, Dominique Burger, et al.. (2020). Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. Journal of Biological Chemistry. 295(23). 7849–7864. 10 indexed citations
3.
Koldewey, Philipp, et al.. (2019). Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket. Journal of Biological Chemistry. 294(38). 14119–14134. 15 indexed citations
4.
An, Sojin, et al.. (2018). Mis16 Switches Function from a Histone H4 Chaperone to a CENP-ACnp1-Specific Assembly Factor through Eic1 Interaction. Structure. 26(7). 960–971.e4. 5 indexed citations
5.
Koldewey, Philipp, et al.. (2018). Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains. Protein Science. 27(11). 1893–1900. 13 indexed citations
6.
Horowitz, Scott, Philipp Koldewey, Frederick Stull, & James C.A. Bardwell. (2017). Folding while bound to chaperones. Current Opinion in Structural Biology. 48. 1–5. 34 indexed citations
7.
Koldewey, Philipp, Scott Horowitz, & James C.A. Bardwell. (2017). Chaperone-client interactions: Non-specificity engenders multifunctionality. Journal of Biological Chemistry. 292(29). 12010–12017. 52 indexed citations
8.
Badieyan, Somayesadat, et al.. (2017). Evaluation of de novo-designed coiled coils as off-the-shelf components for protein assembly. Molecular Systems Design & Engineering. 2(2). 140–148. 20 indexed citations
9.
Badieyan, Somayesadat, Joseph D. Eschweiler, Philipp Koldewey, et al.. (2017). Symmetry‐Directed Self‐Assembly of a Tetrahedral Protein Cage Mediated by de Novo‐Designed Coiled Coils. ChemBioChem. 18(19). 1888–1892. 38 indexed citations
10.
Horowitz, Scott, Loïc Salmon, Philipp Koldewey, et al.. (2016). Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. 23(7). 691–697. 43 indexed citations
11.
Koldewey, Philipp, Frederick Stull, Scott Horowitz, Raoul Martin, & James C.A. Bardwell. (2016). Forces Driving Chaperone Action. Cell. 166(2). 369–379. 83 indexed citations
12.
Su, Min, Philipp Koldewey, Joseph D. Eschweiler, et al.. (2016). Flexible, symmetry-directed approach to assembling protein cages. Proceedings of the National Academy of Sciences. 113(31). 8681–8686. 83 indexed citations
13.
Stull, Frederick, et al.. (2015). Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nature Structural & Molecular Biology. 23(1). 53–58. 71 indexed citations
14.
Dahl, Jan‐Ulrik, et al.. (2015). HdeB functions as an acid-protective chaperone in bacteria.. Journal of Biological Chemistry. 290(16). 9950–9950. 7 indexed citations
15.
Castro, Helena, Tânia Cruz, Eric Tse, et al.. (2015). Mitochondrial peroxiredoxin functions as crucial chaperone reservoir inLeishmania infantum. Proceedings of the National Academy of Sciences. 112(7). E616–24. 69 indexed citations
16.
Dahl, Jan‐Ulrik, Philipp Koldewey, Loïc Salmon, et al.. (2014). HdeB Functions as an Acid-protective Chaperone in Bacteria. Journal of Biological Chemistry. 290(1). 65–75. 48 indexed citations
17.
Horowitz, Scott, Philipp Koldewey, & James C.A. Bardwell. (2014). Undergraduates improve upon published crystal structure in class assignment. Biochemistry and Molecular Biology Education. 42(5). 398–404. 2 indexed citations
18.
Quan, Shu, Philipp Koldewey, Rong Shi, et al.. (2011). Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature Structural & Molecular Biology. 18(3). 262–269. 127 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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