W. Steigemann

2.9k total citations · 2 hit papers
24 papers, 2.4k citations indexed

About

W. Steigemann is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, W. Steigemann has authored 24 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 9 papers in Materials Chemistry and 7 papers in Cell Biology. Recurrent topics in W. Steigemann's work include Protein Structure and Dynamics (10 papers), Enzyme Structure and Function (9 papers) and Hemoglobin structure and function (7 papers). W. Steigemann is often cited by papers focused on Protein Structure and Dynamics (10 papers), Enzyme Structure and Function (9 papers) and Hemoglobin structure and function (7 papers). W. Steigemann collaborates with scholars based in Germany, Switzerland and Israel. W. Steigemann's co-authors include J. Deisenhofer, Robert Huber, E. Weber, D. Kukla, Wolfram Bode, P. Schwager, Klaus Bartels, O. Epp, H. Hartmann and F. Parak and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Molecular Biology.

In The Last Decade

W. Steigemann

24 papers receiving 2.1k citations

Hit Papers

Structure of the complex formed by bovine trypsin and bov... 1974 2026 1991 2008 1974 1975 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
W. Steigemann Germany 17 1.8k 733 668 354 259 24 2.4k
Robert C. Ladner United States 29 2.1k 1.2× 404 0.6× 517 0.8× 257 0.7× 291 1.1× 48 3.3k
James B. Matthew United States 26 1.8k 1.0× 456 0.6× 530 0.8× 364 1.0× 394 1.5× 37 2.4k
D.R. Davies United States 22 2.3k 1.3× 463 0.6× 448 0.7× 216 0.6× 127 0.5× 51 3.2k
Nguyen‐Huu Xuong United States 30 3.2k 1.7× 1.0k 1.4× 489 0.7× 167 0.5× 128 0.5× 67 4.5k
Hilary Muirhead United Kingdom 27 2.3k 1.2× 961 1.3× 1.2k 1.8× 319 0.9× 133 0.5× 42 3.6k
P.J. Artymiuk United Kingdom 17 1.5k 0.8× 865 1.2× 181 0.3× 220 0.6× 134 0.5× 21 2.1k
Allen B. Edmundson United States 39 3.9k 2.1× 531 0.7× 725 1.1× 335 0.9× 95 0.4× 120 5.5k
John A. Rupley United States 23 1.9k 1.0× 712 1.0× 263 0.4× 402 1.1× 544 2.1× 42 2.6k
Eaton E. Lattman United States 32 3.1k 1.7× 1.2k 1.6× 625 0.9× 371 1.0× 310 1.2× 81 3.9k
B.W. Matthews United States 28 3.0k 1.6× 1.5k 2.1× 350 0.5× 264 0.7× 157 0.6× 39 3.8k

Countries citing papers authored by W. Steigemann

Since Specialization
Citations

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

Fields of papers citing papers by W. Steigemann

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of W. Steigemann

This figure shows the co-authorship network connecting the top 25 collaborators of W. Steigemann. A scholar is included among the top collaborators of W. Steigemann 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 W. Steigemann. W. Steigemann 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.
Messerschmidt, Albrecht, et al.. (1992). X‐ray crystallographic characterisation of type‐2‐depleted ascorbate oxidase from zucchini. European Journal of Biochemistry. 209(2). 597–602. 33 indexed citations
2.
Hartmann, H., et al.. (1987). Structural disorder in proteins. European Biophysics Journal. 14(6). 337–48. 14 indexed citations
3.
Parak, F., et al.. (1987). Low temperature X-ray investigation of structural distributions in myoglobin. European Biophysics Journal. 15(4). 237–249. 88 indexed citations
4.
Baur, Xaver, et al.. (1986). Structure, Antigenic Determinants of Some Clinically Important Insect Allergens: Chironomid Hemoglobins. Science. 233(4761). 351–354. 49 indexed citations
5.
Kilchherr, E., Hans Hofmann, W. Steigemann, & Jürgen Engel. (1985). Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices. Journal of Molecular Biology. 186(2). 403–415. 61 indexed citations
6.
Deisenhofer, J., S. James Remington, & W. Steigemann. (1985). Experience with various techniques for the refinement of protein structures. Methods in enzymology on CD-ROM/Methods in enzymology. 115. 303–323. 20 indexed citations
7.
Hartmann, H., F. Parak, W. Steigemann, et al.. (1982). Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K.. Proceedings of the National Academy of Sciences. 79(16). 4967–4971. 192 indexed citations
8.
Walter, J., W. Steigemann, T.P. Singh, et al.. (1982). On the disordered activation domain in trypsinogen: chemical labelling and low-temperature crystallography. Acta Crystallographica Section B. 38(5). 1462–1472. 177 indexed citations
9.
Steigemann, W.. (1981). Experiences in refinement with chain constraints in real space and energy restraints in reciprocal space. Acta Crystallographica Section A Foundations of Crystallography. 37(a1). C6–C6. 1 indexed citations
10.
Steigemann, W. & E. Weber. (1979). Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution. Journal of Molecular Biology. 127(3). 309–338. 275 indexed citations
11.
Straßburger, W., et al.. (1978). Calculation of the Circular Dichroism of Chironomus Hemoglobin in the Light of the Quality of Its X-Ray Structure. Zeitschrift für Naturforschung C. 33(11-12). 908–911. 6 indexed citations
12.
Weber, E., W. Steigemann, Thomas A. Jones, & Robert Huber. (1978). The structure of oxy-erythrocruorin at 1.4 Å resolution. Journal of Molecular Biology. 120(2). 327–336. 37 indexed citations
13.
Huber, Robert & W. Steigemann. (1974). Two cis‐prolines in the Bence‐Jones protein Rei and the cis‐pro‐bend. FEBS Letters. 48(2). 235–237. 52 indexed citations
14.
Epp, O., Walter Palm, Heinz Fehlhammer, et al.. (1972). Crystallographic evidence for structurally similar domains in the human κ-type Bence-Jones protein Rei. Journal of Molecular Biology. 69(2). 315–318. 5 indexed citations
15.
Blow, D. M., et al.. (1972). A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin. Journal of Molecular Biology. 69(1). 137–144. 88 indexed citations
16.
Huber, R., D. Kukla, Andreas Rühlmann, & W. Steigemann. (1972). Pancreatic Trypsin Inhibitor (Kunitz): Part I: Structure and function. Cold Spring Harbor Symposia on Quantitative Biology. 36(0). 141–150. 68 indexed citations
17.
Epp, O., W. Steigemann, H. Formanek, & Robert Huber. (1971). Crystallographic Evidence for the Tetrameric Subunit Structure of l‐Asparaginase from Escherichia coli. European Journal of Biochemistry. 20(3). 432–437. 49 indexed citations
19.
Schramm, Hans J., W. Steigemann, P. Schwager, R. Huber, & W. Hoppe. (1970). Crystallisation and X-ray investigationsn of immunoglobulin-fragments. Immunochemistry. 7(10). 872–872. 1 indexed citations
20.
Hoppe, W., et al.. (1969). New developments in the determination of the structure of complex organic molecules. Pure and Applied Chemistry. 18(4). 465–488. 11 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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