M. Selmer

3.3k total citations · 2 hit papers
42 papers, 2.6k citations indexed

About

M. Selmer is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, M. Selmer has authored 42 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 12 papers in Materials Chemistry and 9 papers in Genetics. Recurrent topics in M. Selmer's work include RNA and protein synthesis mechanisms (28 papers), RNA modifications and cancer (19 papers) and Enzyme Structure and Function (12 papers). M. Selmer is often cited by papers focused on RNA and protein synthesis mechanisms (28 papers), RNA modifications and cancer (19 papers) and Enzyme Structure and Function (12 papers). M. Selmer collaborates with scholars based in Sweden, United Kingdom and United States. M. Selmer's co-authors include V. Ramakrishnan, Ann C. Kelley, C.M. Dunham, Albert Weixlbaumer, Sabine Petry, F.V. Murphy, John R. Weir, Yong‐Gui Gao, Anders Liljas and Salam Al‐Karadaghi and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

M. Selmer

42 papers receiving 2.5k citations

Hit Papers

Structure of the 70 S Ribosome Complexed with mRNA and tRNA 2006 2026 2012 2019 2006 2009 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M. Selmer Sweden 21 2.3k 593 218 205 145 42 2.6k
Joerg Harms Germany 19 2.3k 1.0× 712 1.2× 202 0.9× 203 1.0× 102 0.7× 24 2.6k
C.M. Dunham United States 27 3.0k 1.3× 947 1.6× 196 0.9× 420 2.0× 156 1.1× 59 3.4k
Thomas Hartsch Germany 16 2.7k 1.2× 795 1.3× 286 1.3× 465 2.3× 118 0.8× 22 3.1k
Albert Weixlbaumer United Kingdom 17 2.8k 1.2× 804 1.4× 152 0.7× 267 1.3× 170 1.2× 20 2.9k
B.S. Schuwirth United States 6 1.6k 0.7× 524 0.9× 115 0.5× 180 0.9× 107 0.7× 6 1.8k
Hans‐Joachim Wieden Canada 23 1.9k 0.8× 668 1.1× 118 0.5× 279 1.4× 90 0.6× 63 2.2k
M.J. Tarry United Kingdom 15 2.4k 1.0× 843 1.4× 120 0.6× 328 1.6× 147 1.0× 20 2.6k
Kurt Fredrick United States 35 2.7k 1.1× 1.1k 1.8× 112 0.5× 456 2.2× 143 1.0× 72 3.0k
T.M. Schmeing Canada 24 3.0k 1.3× 534 0.9× 155 0.7× 132 0.6× 144 1.0× 57 3.3k
Alexey A. Bogdanov Russia 31 2.4k 1.0× 562 0.9× 76 0.3× 297 1.4× 100 0.7× 132 2.7k

Countries citing papers authored by M. Selmer

Since Specialization
Citations

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

Fields of papers citing papers by M. Selmer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Selmer

This figure shows the co-authorship network connecting the top 25 collaborators of M. Selmer. A scholar is included among the top collaborators of M. Selmer 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 M. Selmer. M. Selmer 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.
Ge, Xueliang, et al.. (2025). Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis. Nature Communications. 16(1). 3693–3693. 1 indexed citations
2.
González-López, Adrián, Daniel S. D. Larsson, Ravi Kiran Koripella, et al.. (2024). Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane. Scientific Reports. 14(1). 14253–14253. 5 indexed citations
3.
Isaksen, Geir Villy, Omar Warsi, Ulrich Eckhard, et al.. (2021). Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family. eLife. 10. 20 indexed citations
4.
Selmer, M., et al.. (2020). Structural Recognition of Spectinomycin by Resistance Enzyme ANT(9) from Enterococcus faecalis. Antimicrobial Agents and Chemotherapy. 64(6). 16 indexed citations
5.
Stsiapanava, Alena & M. Selmer. (2019). Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance. Scientific Reports. 9(1). 14607–14607. 16 indexed citations
6.
Jerlström-Hultqvist, Jon, Omar Warsi, Michael Knopp, et al.. (2018). A bacteriophage enzyme induces bacterial metabolic perturbation that confers a novel promiscuous function. Nature Ecology & Evolution. 2(8). 1321–1330. 16 indexed citations
7.
Chen, Yang, Joakim Näsvall, Shiying Wu, Dan I. Andersson, & M. Selmer. (2015). Structure of AadA fromSalmonella enterica: a monomeric aminoglycoside (3′′)(9) adenyltransferase. Acta Crystallographica Section D Biological Crystallography. 71(11). 2267–2277. 16 indexed citations
8.
Sun, Song, M. Selmer, & Dan I. Andersson. (2014). Resistance to β-Lactam Antibiotics Conferred by Point Mutations in Penicillin-Binding Proteins PBP3, PBP4 and PBP6 in Salmonella enterica. PLoS ONE. 9(5). e97202–e97202. 43 indexed citations
9.
Hultqvist, Greta, S. Raza Haq, N. Celestine, et al.. (2013). Energetic Pathway Sampling in a Protein Interaction Domain. Structure. 21(7). 1193–1202. 38 indexed citations
10.
Selmer, M., et al.. (2013). Purification, crystallization and preliminary X-ray diffraction analysis of the 23S rRNA methyltransferase RlmJ fromEscherichia coli. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(9). 1001–1003. 1 indexed citations
11.
Shepherd, Tyson R., et al.. (2012). Crystal structure of RlmM, the 2′O-ribose methyltransferase for C2498 of Escherichia coli 23S rRNA. Nucleic Acids Research. 40(20). 10507–10520. 11 indexed citations
12.
Selmer, M. & Anders Liljas. (2008). Exit Biology: Battle for the Nascent Chain. Structure. 16(4). 498–500. 6 indexed citations
13.
Weixlbaumer, Albert, Sabine Petry, C.M. Dunham, et al.. (2007). Crystal structure of the ribosome recycling factor bound to the ribosome. Nature Structural & Molecular Biology. 14(8). 733–737. 69 indexed citations
14.
Dunham, C.M., M. Selmer, Ann C. Kelley, et al.. (2007). Structures of tRNAs with an expanded anticodon loop in the decoding center of the 30S ribosomal subunit. RNA. 13(6). 817–823. 44 indexed citations
15.
Selmer, M., C.M. Dunham, F.V. Murphy, et al.. (2006). Structure of the 70 S Ribosome Complexed with mRNA and tRNA. Science. 313(5795). 1935–1942. 1036 indexed citations breakdown →
16.
Petry, Sabine, Ditlev E. Brodersen, F.V. Murphy, et al.. (2005). Crystal Structures of the Ribosome in Complex with Release Factors RF1 and RF2 Bound to a Cognate Stop Codon. Cell. 123(7). 1255–1266. 185 indexed citations
17.
Kristensen, O., Martin Laurberg, Anders Liljas, & M. Selmer. (2002). Is tRNA Binding or tRNA Mimicry Mandatory for Translation Factors?. Current Protein and Peptide Science. 3(1). 133–141. 8 indexed citations
18.
Selmer, M., et al.. (2002). Preparation of a crystallizable mRNA-binding fragment ofMoorella thermoaceticaelongation factor SelB. Acta Crystallographica Section D Biological Crystallography. 58(10). 1871–1873. 3 indexed citations
19.
Selmer, M.. (2002). Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. The EMBO Journal. 21(15). 4145–4153. 44 indexed citations
20.
Selmer, M., Salam Al‐Karadaghi, Go Hirokawa, Akira Kaji, & Anders Liljas. (1999). Crystallization and preliminary X-ray analysis of Thermotoga maritima ribosome recycling factor. Acta Crystallographica Section D Biological Crystallography. 55(12). 2049–2050. 5 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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