Iris Thamm

472 total citations
13 papers, 397 citations indexed

About

Iris Thamm is a scholar working on Molecular Biology, Molecular Medicine and Oncology. According to data from OpenAlex, Iris Thamm has authored 13 papers receiving a total of 397 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Molecular Medicine and 4 papers in Oncology. Recurrent topics in Iris Thamm's work include Antibiotic Resistance in Bacteria (6 papers), RNA and protein synthesis mechanisms (4 papers) and Glycosylation and Glycoproteins Research (2 papers). Iris Thamm is often cited by papers focused on Antibiotic Resistance in Bacteria (6 papers), RNA and protein synthesis mechanisms (4 papers) and Glycosylation and Glycoproteins Research (2 papers). Iris Thamm collaborates with scholars based in Belgium, France and Italy. Iris Thamm's co-authors include Moreno Galleni, Jean‐Marie Frère, Gian María Rossolini, Maria Letizia Riccio, Gianfranco Amicosante, Bernard Joris, Colette Duez, Bart Devreese, Jean‐Marie Ghuysen and Bart Samyn and has published in prestigious journals such as Journal of Biological Chemistry, Biochemical Journal and FEBS Letters.

In The Last Decade

Iris Thamm

12 papers receiving 391 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Iris Thamm Belgium 10 210 205 88 79 57 13 397
Kwang Hoon Sung South Korea 8 166 0.8× 227 1.1× 45 0.5× 84 1.1× 84 1.5× 12 393
Philippe Dehottay Belgium 10 172 0.8× 217 1.1× 33 0.4× 30 0.4× 100 1.8× 12 374
Vincenzo A. Rao United Kingdom 10 151 0.7× 201 1.0× 63 0.7× 166 2.1× 30 0.5× 11 444
Pablo E. Tomatis Argentina 11 274 1.3× 229 1.1× 42 0.5× 70 0.9× 106 1.9× 15 467
S Roychoudhury United States 10 130 0.6× 389 1.9× 54 0.6× 47 0.6× 58 1.0× 12 600
Alex A. Neyfakh United States 8 202 1.0× 323 1.6× 82 0.9× 28 0.4× 95 1.7× 9 554
Ashley T. Tucker United States 10 278 1.3× 384 1.9× 40 0.5× 161 2.0× 50 0.9× 18 674
Reiko Ohki Japan 14 136 0.6× 344 1.7× 42 0.5× 26 0.3× 56 1.0× 20 558
Jos A. M. van de Klundert Netherlands 10 108 0.5× 155 0.8× 58 0.7× 36 0.5× 40 0.7× 21 378
Hubing Lou United Kingdom 6 145 0.7× 187 0.9× 45 0.5× 48 0.6× 20 0.4× 7 364

Countries citing papers authored by Iris Thamm

Since Specialization
Citations

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

Fields of papers citing papers by Iris Thamm

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Iris Thamm

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

All Works

13 of 13 papers shown
1.
2.
Mercuri, Paola Sandra, I. Garcia-Saez, Iris Thamm, et al.. (2004). Probing the Specificity of the Subclass B3 FEZ-1 Metallo-β-lactamase by Site-directed Mutagenesis. Journal of Biological Chemistry. 279(32). 33630–33638. 27 indexed citations
3.
Filée, Patrice, Christelle Vreuls, R. Herman, et al.. (2003). Dimerization and DNA Binding Properties of theBacillus licheniformis 749/I BlaI Repressor. Journal of Biological Chemistry. 278(19). 16482–16487. 16 indexed citations
4.
Filée, Patrice, et al.. (2001). Use of an ALFexpress™ DNA Sequencer to Analyze Protein-Nucleic Acid Interactions by Band Shift Assay. BioTechniques. 30(5). 1044–1051. 14 indexed citations
5.
6.
Fanuel, Laurence, Iris Thamm, Vesna Kostanjevečki, et al.. (1999). Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide. Cellular and Molecular Life Sciences. 55(5). 812–818. 23 indexed citations
7.
Galleni, Moreno, Iris Thamm, Maria Letizia Riccio, et al.. (1999). Structure of In31, a bla IMP -Containing Pseudomonas aeruginosa Integron Phyletically Related to In5, Which Carries an Unusual Array of Gene Cassettes. Antimicrobial Agents and Chemotherapy. 43(4). 890–901. 134 indexed citations
8.
Thamm, Iris, et al.. (1998). The Division and Cell Wall Gene Cluster ofEnterococcus hiraeS185. DNA sequence. 9(3). 149–161. 13 indexed citations
9.
Ledent, Philippe, Colette Duez, Marc Vanhove, et al.. (1997). Unexpected influence of a C‐terminal‐fused His‐tag on the processing of an enzyme and on the kinetic and folding parameters. FEBS Letters. 413(2). 194–196. 57 indexed citations
10.
Lepage, S, Moreno Galleni, Bernard Lakaye, et al.. (1995). Kinetic properties of the Bacillus licheniformis penicillin-binding proteins. Biochemical Journal. 309(1). 49–53. 8 indexed citations
11.
Lepage, S, et al.. (1995). Saturation of penicillin‐binding protein 1 by β‐lactam antibiotics in growing cells of Bacillus licheniformis. Molecular Microbiology. 16(2). 365–372. 3 indexed citations
12.
Malissard, Martine, Colette Duez, Micheline Guinand, et al.. (1993). Sequence of a gene encoding a (poly ManA) alginate lyase active onPseudomonas aeruginosaalginate. FEMS Microbiology Letters. 110(1). 101–106. 38 indexed citations
13.
Galleni, Moreno, Bernard Lakaye, S Lepage, et al.. (1993). A new, highly sensitive method for the detection and quantification of penicillin-binding proteins. Biochemical Journal. 291(1). 19–21. 28 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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