Martin Sagermann

740 total citations
22 papers, 627 citations indexed

About

Martin Sagermann is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Martin Sagermann has authored 22 papers receiving a total of 627 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 8 papers in Materials Chemistry and 3 papers in Biotechnology. Recurrent topics in Martin Sagermann's work include Enzyme Structure and Function (8 papers), RNA and protein synthesis mechanisms (6 papers) and Protein Structure and Dynamics (4 papers). Martin Sagermann is often cited by papers focused on Enzyme Structure and Function (8 papers), RNA and protein synthesis mechanisms (6 papers) and Protein Structure and Dynamics (4 papers). Martin Sagermann collaborates with scholars based in United States, Japan and Canada. Martin Sagermann's co-authors include Brian W. Matthews, Kiel Nikolakakis, Tom H. Stevens, Akashi Ohtaki, Noriyuki Doukyu, Hiroyasu Ogino, Robert Aggeler, Roderick A. Capaldi, Edward P. Gogol and Walter A. Baase and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Martin Sagermann

21 papers receiving 619 citations

Peers

Martin Sagermann

ECOLO

PHARM

RESE

G. Reza Malmirchegini United States

Christopher T. Jurgenson United States

Marcel Meury Switzerland

Fabian Meyer Switzerland

Yakov Korkhin Israel

Miriam Kaltenbach United Kingdom

Fei Zhou United States

Jason J. Reddick United States

Mohsen Badiee United States

Jochen Strassner Switzerland

G. Reza Malmirchegini United States

Martin Sagermann

1.0k ×2.0

68 ×0.8

53 ×0.8

ECOLO

12 ×0.2

PHARM

29 ×0.6

RESE

Citations per year, relative to Martin Sagermann Martin Sagermann (= 1×) peers G. Reza Malmirchegini

Countries citing papers authored by Martin Sagermann

Since Specialization

Citations

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

Fields of papers citing papers by Martin Sagermann

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin Sagermann

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Sagermann. A scholar is included among the top collaborators of Martin Sagermann 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 Martin Sagermann. Martin Sagermann 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

Nikolakakis, Kiel, et al.. (2013). Crystallographic Insights into the Pore Structures and Mechanisms of the Eutl and Eutm Shell Proteins of the Eut-Bmc. Journal of Bacteriology.

Sagermann, Martin, et al.. (2013). A vaccine and diagnostic target for Clostridium bolteae, an autism-associated bacterium. Vaccine. 31(26). 2787–2790. 50 indexed citations

Monteiro, Mário A., Zuchao Ma, Luis G. Arroyo, et al.. (2013). Carbohydrate-basedClostridium difficilevaccines. Expert Review of Vaccines. 12(4). 421–431. 39 indexed citations

Sagermann, Martin, et al.. (2010). Structural characterization of the organic solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1. Journal of Structural Biology. 170(1). 32–40. 13 indexed citations

Chapleau, Richard R. & Martin Sagermann. (2009). Real-time in vivo imaging of mercury uptake in Caenorhabditis elegans through the foodchain. Toxicology. 261(3). 136–142. 5 indexed citations

Nikolakakis, Kiel, et al.. (2009). Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome ofEscherichia coli. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(2). 128–132. 2 indexed citations

Sagermann, Martin, et al.. (2008). Using affinity chromatography to engineer and characterize pH‐dependent protein switches. Protein Science. 18(1). 217–228. 9 indexed citations

Doukyu, Noriyuki, et al.. (2008). Cloning, sequence analysis, and expression of a gene encoding Chromobacterium sp. DS-1 cholesterol oxidase. Applied Microbiology and Biotechnology. 82(3). 479–490. 28 indexed citations

Doukyu, Noriyuki, et al.. (2008). Purification and characterization of Chromobacterium sp. DS-1 cholesterol oxidase with thermal, organic solvent, and detergent tolerance. Applied Microbiology and Biotechnology. 80(1). 59–70. 50 indexed citations

10.

Chapleau, Richard R., Rebecca Blomberg, Peter C. Ford, & Martin Sagermann. (2008). Design of a highly specific and noninvasive biosensor suitable for real‐time in vivo imaging of mercury (II) uptake. Protein Science. 17(4). 614–622. 34 indexed citations

11.

Sagermann, Martin, Walter A. Baase, & Brian W. Matthews. (2006). Sequential reorganization of β‐sheet topology by insertion of a single strand. Protein Science. 15(5). 1085–1092. 10 indexed citations

12.

Sagermann, Martin, Walter A. Baase, Blaine H. M. Mooers, Leslie Gay, & Brian W. Matthews. (2004). Relocation or Duplication of the Helix A Sequence of T4 Lysozyme Causes Only Modest Changes in Structure but Can Increase or Decrease the Rate of Folding. Biochemistry. 43(5). 1296–1301. 11 indexed citations

13.

Sagermann, Martin, Leslie Gay, & Brian W. Matthews. (2003). Long-distance conformational changes in a protein engineered by modulated sequence duplication. Proceedings of the National Academy of Sciences. 100(16). 9191–9195. 14 indexed citations

14.

Sagermann, Martin & Brian W. Matthews. (2002). Crystal Structures of a T4-lysozyme Duplication-extension Mutant Demonstrate that the Highly Conserved β-Sheet Region has Low Intrinsic Folding Propensity. Journal of Molecular Biology. 316(4). 931–940. 18 indexed citations

15.

Sagermann, Martin, Lars‐Göran Mårtensson, Walter A. Baase, & Brian W. Matthews. (2002). A test of proposed rules for helix capping: Implications for protein design. Protein Science. 11(3). 516–521. 13 indexed citations

16.

Sagermann, Martin, Tom H. Stevens, & Brian W. Matthews. (2001). Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences. 98(13). 7134–7139. 111 indexed citations

17.

Sagermann, Martin & Brian W. Matthews. (2000). Cloning, expression and crystallization of VMA13p, an essential subunit of the vacuolar H⁺-ATPase ofSaccharomyces cerevisiae. Acta Crystallographica Section D Biological Crystallography. 56(4). 475–477. 3 indexed citations

18.

Sagermann, Martin, Walter A. Baase, & Brian W. Matthews. (1999). Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proceedings of the National Academy of Sciences. 96(11). 6078–6083. 19 indexed citations

19.

Grüber, Gerhard, Andrew C. Hausrath, Martin Sagermann, & Roderick Capaldi. (1997). An improved purification of ECF₁ and ECF₁F₀ by using a cytochrome bo‐deficient strain of Escherichia coli facilitates crystallization of these complexes. FEBS Letters. 410(2-3). 165–168. 10 indexed citations

20.

Gogol, Edward P., Robert Aggeler, Martin Sagermann, & Roderick A. Capaldi. (1989). Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex. Biochemistry. 28(11). 4717–4724. 66 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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