Udo Heinemann

12.7k total citations
227 papers, 10.1k citations indexed

About

Udo Heinemann is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Udo Heinemann has authored 227 papers receiving a total of 10.1k indexed citations (citations by other indexed papers that have themselves been cited), including 179 papers in Molecular Biology, 73 papers in Materials Chemistry and 37 papers in Genetics. Recurrent topics in Udo Heinemann's work include Enzyme Structure and Function (71 papers), RNA and protein synthesis mechanisms (67 papers) and Protein Structure and Dynamics (47 papers). Udo Heinemann is often cited by papers focused on Enzyme Structure and Function (71 papers), RNA and protein synthesis mechanisms (67 papers) and Protein Structure and Dynamics (47 papers). Udo Heinemann collaborates with scholars based in Germany, United States and United Kingdom. Udo Heinemann's co-authors include Wolfram Saenger, U. Müeller, Hermann Schindelin, Michael G. Hahn, Jürgen Müller, Claudia Alings, A. Schuetz, M.S. Weiss, Rainer Borriss and Yvette Roske and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Udo Heinemann

225 papers receiving 10.0k citations

Peers

Countries citing papers authored by Udo Heinemann

Since Specialization

Citations

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

Fields of papers citing papers by Udo Heinemann

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Udo Heinemann

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

All Works

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20 of 20 papers shown

#	Work	Indexed citations
1	The macromolecular crystallography beamlines of the Helmholtz-Zentrum Berlin at the BESSY II storage ring: history, current status and future directions 2025 ·Journal of Synchrotron Radiation ·U. Müeller, (unknown), (unknown), Volodymyr Bon, (unknown), (unknown), Ronald Förster, (unknown), Thomas Hauß, Udo Heinemann, Michael Hellmig, David T. James, F. Lennartz, (unknown), Ruslan Ovsyannikov, Pushpendra Singh, M.C. Wahl, Gert Weber, M.S. Weiss	0
2	Structural remodeling of AAA+ ATPase p97 by adaptor protein ASPL facilitates posttranslational methylation by METTL21D 2023 ·Proceedings of the National Academy of Sciences ·(unknown), Yvette Roske, (unknown), (unknown), Daniela Panáková, Udo Heinemann	5
3	PIN and CCCH Zn-finger domains coordinate RNA targeting in ZC3H12 family endoribonucleases 2021 ·Nucleic Acids Research ·Ankur Garg, Yvette Roske, Shinnosuke Yamada, Takuya Uehata, Osamu Takeuchi, Udo Heinemann	16
4	Pantoea stewartii WceF is a glycan biofilm-modifying enzyme with a bacteriophage tailspike-like fold 2021 ·Journal of Biological Chemistry ·(unknown), Yvette Roske, (unknown), Valentin Dunsing, Salvatore Chiantia, Udo Heinemann, Stefanie Barbirz	10
5	Small-molecule inhibitors of the PDZ domain of Dishevelled proteins interrupt Wnt signalling 2021 ·SHILAP Revista de lepidopterología ·(unknown), Yvette Roske, Dmytro Kovalskyy, Maxim O. Platonov, (unknown), Annika Kreuchwig, (unknown), Liang Fang, Anne Diehl, Peter Schmieder, Gerd Krause, Jörg Rademann, Udo Heinemann, Walter Birchmeier, Hartmut Oschkinat	8
6	Crystal structure of Q4D6Q6, a conserved kinetoplastid-specific protein from Trypanosoma cruzi 2020 ·Journal of Structural Biology ·(unknown), Yvette Roske, Guilherme A. P. de Oliveira, (unknown), Anne Diehl, Peter Schmieder, Udo Heinemann, Hartmut Oschkinat, José R. Pires	1
7	Symmetry in Nucleic-Acid Double Helices 2020 ·Symmetry ·Udo Heinemann, Yvette Roske	14
8	Structure‐Based Screening of Tetrazolylhydrazide Inhibitors versus KDM4 Histone Demethylases 2019 ·ChemMedChem ·P.H. Malecki, (unknown), Martin Roatsch, Oxana Krylova, Andreas Link, Manfred Jung, Udo Heinemann, M.S. Weiss	14
9	Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1 2019 ·Structure ·(unknown), Anup Arumughan, (unknown), David Schwefel, Erich E. Wanker, Yvette Roske, Udo Heinemann	13
10	Structure of the active GGEEF domain of a diguanylate cyclase from Vibrio cholerae 2019 ·Biochemical and Biophysical Research Communications ·(unknown), Yvette Roske, Udo Heinemann, Sumit Biswas	3
11	Roquin binding to target mRNAs involves a winged helix-turn-helix motif 2014 ·Nature Communications ·A. Schuetz, Yasuhiro Murakawa, Eva Rosenbaum, Markus Landthaler, Udo Heinemann	29
12	An Src Homology 3-like Domain Is Responsible for Dimerization of the Repressor Protein KorB Encoded by the Promiscuous IncP Plasmid RP4 2002 ·Journal of Biological Chemistry ·Heinrich Delbrück, Günter Ziegelin, Erich Lanka, Udo Heinemann	36
13	Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT) 2001 ·Acta Crystallographica Section D Biological Crystallography ·Erik Werner, Mathias Ziegler, Felicitas Lerner, Manfred Schweiger, Yves A. Muller, Udo Heinemann	3
14	Structure of adrenodoxin and function in mitochondrial steroid hydroxylation 1998 ·Endocrine Research ·Rita Bernhardt, Alexander J. Muller, Heike Uhlmann, Asya V. Grinberg, Jürgen Müller, Udo Heinemann	3
15	Crystal Structure and Site-directed Mutagenesis of Bacillus macerans Endo-1,3–1,4-β-glucanase 1995 ·Journal of Biological Chemistry ·Michael G. Hahn, Ole Olsen, Oliver Politz, Rainer Borriss, Udo Heinemann	98
16	Circular permutation of polypeptide chains: Implications for protein folding and stability 1995 ·Progress in Biophysics and Molecular Biology ·Udo Heinemann, Michael G. Hahn	78
17	Cation binding to a Bacillus (1,3–1,4)‐β‐glucanase Geometry, affinity and effect on protein stability 1994 ·European Journal of Biochemistry ·Thomas Keitel, Morten Meldgaard, Udo Heinemann	43
18	DNA helix structure and refinement algorithm: comparison of models for d(CCAGGCm5CTGG) derived from NUCLSQ, TNT and X-PLOR 1993 ·Acta Crystallographica Section D Biological Crystallography ·Michael G. Hahn, Udo Heinemann	21
19	Overproduction, crystallization, and preliminary X‐ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB 1992 ·Proteins Structure Function and Bioinformatics ·Hermann Schindelin, Michael Herrler, Gerald Willimsky, Mohamed A. Marahiel, Udo Heinemann	43
20	Ribonuclease T1 with free recognition and catalytic site: Crystal structure analysis at 1.5 Å resolution 1991 ·Journal of Molecular Biology ·José Martínez‐Oyanedel, Hui‐Woog Choe, Udo Heinemann, Wolfram Saenger	128

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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