Regine Koelsch

486 citations
26 papers · 377 indexed · h-index 12
Topics
Peptidase Inhibition and Analysis (10 papers)Neuropeptides and Animal Physiology (6 papers)Chemical Synthesis and Analysis (4 papers)

In The Last Decade

Regine Koelsch

26 papers receiving 352 citations

Peers

Regine Koelsch
Comparison fields: 5 of 67
  • Molecular Biology 276
  • Oncology 91
  • Cellular and Molecular Neuroscience 58
  • Organic Chemistry 38
  • Spectroscopy 34
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Citations per field
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Citations per year

Countries citing papers authored by Regine Koelsch

Since Specialization
Citations

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

Fields of papers citing papers by Regine Koelsch

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Regine Koelsch

This figure shows the co-authorship network connecting the top 25 collaborators of Regine Koelsch. A scholar is included among the top collaborators of Regine Koelsch 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 Regine Koelsch. Regine Koelsch 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
#WorkIndexed citations
1 11
2 22
3 33
4 19
5
Aminopeptidase P. A cell-surface antigen of endothelial and lymphoid cells.
2
6 12
7 28
8 18
9 2
10
Incorporation of chemically modified (hydrophobized) ferritin in liposomal membranes: electron microscopic studies.
3
11 4
12 12
13 33
14 62
15 3
16 35
17 29
18
An inexpensive device for sample stirring in VSU Zeiss spectrophotometers. Its use for kinetic measurements and active site titrations with immobilized enzymes.
1
19 4
20
[Studies on covalent and non-covalent binding of leucine amino peptidase from bovine eye lenses to water insoluble carriers].
7

About Regine Koelsch

Regine Koelsch is a scholar working on Oncology, Biotechnology and Cellular and Molecular Neuroscience, having authored 26 papers that have together received 377 indexed citations. Recurring topics across this work include Peptidase Inhibition and Analysis (10 papers), Neuropeptides and Animal Physiology (6 papers) and Chemical Synthesis and Analysis (4 papers). The work is most often cited by research in Molecular Biology (276 citations), Oncology (91 citations) and Cellular and Molecular Neuroscience (58 citations). Regine Koelsch has collaborated with scholars based in Germany, Czechia and South Korea. Frequent co-authors include Jürgen Lasch, J. Lasch, H Hanson, Klaus Neubert, M. Iwig, Heinz David, H.‐D. Taubert, Volkmar Weissig, Torsten Steinmetzer and Ulf P. Neumann. Their work appears in journals such as Analytical Biochemistry, FEBS Letters and Journal of Chromatography A.

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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