Monika Timmer

538 total citations
24 papers, 389 citations indexed

About

Monika Timmer is a scholar working on Molecular Biology, Materials Chemistry and Molecular Medicine. According to data from OpenAlex, Monika Timmer has authored 24 papers receiving a total of 389 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 10 papers in Materials Chemistry and 7 papers in Molecular Medicine. Recurrent topics in Monika Timmer's work include Protein Structure and Dynamics (7 papers), Antibiotic Resistance in Bacteria (7 papers) and Lanthanide and Transition Metal Complexes (5 papers). Monika Timmer is often cited by papers focused on Protein Structure and Dynamics (7 papers), Antibiotic Resistance in Bacteria (7 papers) and Lanthanide and Transition Metal Complexes (5 papers). Monika Timmer collaborates with scholars based in Netherlands, Germany and Taiwan. Monika Timmer's co-authors include Marcellus Ubbink, Anneloes Blok, Aleksandra Zambrowicz, Tadeusz Trziszka, Gert Lübec, Antoni Polanowski, Wei‐Min Liu, Mathias A. S. Hass, Mark Overhand and Simon P. Skinner and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Monika Timmer

24 papers receiving 385 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Monika Timmer Netherlands	11	240	107	102	80	45	24	389
Dong‐Kuk Lee United States	15	484 2.0×	223 2.1×	113 1.1×	43 0.5×	15 0.3×	22	778
Qing Yao United States	17	457 1.9×	34 0.3×	60 0.6×	30 0.4×	29 0.6×	38	701
S. Lopes Portugal	16	302 1.3×	75 0.7×	59 0.6×	18 0.2×	38 0.8×	24	473
Zhilun Zhao United States	13	425 1.8×	56 0.5×	42 0.4×	509 6.4×	148 3.3×	19	1000
Stéphanie Ravaud France	16	522 2.2×	60 0.6×	122 1.2×	9 0.1×	24 0.5×	34	752
Michel Juy France	17	486 2.0×	217 2.0×	202 2.0×	34 0.4×	5 0.1×	23	957
Jie Heng China	10	363 1.5×	40 0.4×	34 0.3×	19 0.2×	133 3.0×	14	590
Diana E. Schlamadinger United States	15	530 2.2×	42 0.4×	62 0.6×	37 0.5×	6 0.1×	24	708
Inokentijs Josts Germany	18	511 2.1×	46 0.4×	149 1.5×	28 0.3×	71 1.6×	29	734
Nicholas G. Rutherford United Kingdom	11	534 2.2×	92 0.9×	65 0.6×	28 0.3×	28 0.6×	15	806

Countries citing papers authored by Monika Timmer

Since Specialization

Citations

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

Fields of papers citing papers by Monika Timmer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Monika Timmer

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

1.

Timmer, Monika, et al.. (2025). A glycine at position 105 leads to clavulanic acid and avibactam resistance in class A β-lactamases. Journal of Biological Chemistry. 301(7). 110347–110347. 1 indexed citations

2.

Timmer, Monika, et al.. (2025). Stabilizing Mutations Enhance Evolvability of BlaC β-lactamase by Widening the Mutational Landscape. Journal of Molecular Biology. 437(9). 168999–168999. 2 indexed citations

3.

Bdira, Fredj Ben, et al.. (2024). Bimodal substrate binding in the active site of the glycosidase B c X. FEBS Journal. 291(19). 4222–4239. 1 indexed citations

4.

Timmer, Monika, et al.. (2023). Asp179 in the class A β‐lactamase from Mycobacterium tuberculosis is a conserved yet not essential residue due to epistasis. FEBS Journal. 290(20). 4933–4949. 7 indexed citations

5.

Boyle, Aimee L., et al.. (2023). Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase. International Journal of Biological Macromolecules. 250. 126160–126160. 8 indexed citations

6.

Zhou, Juan, et al.. (2021). Protein Dynamics Influence the Enzymatic Activity of Phospholipase A/Acyltransferases 3 and 4. Biochemistry. 60(15). 1178–1190. 6 indexed citations

7.

Blok, Anneloes, et al.. (2021). Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics. Antimicrobial Agents and Chemotherapy. 65(8). e0262820–e0262820. 9 indexed citations

8.

Blok, Anneloes, et al.. (2020). Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site. Angewandte Chemie International Edition. 59(51). 23239–23243. 10 indexed citations

9.

Blok, Anneloes, et al.. (2020). Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site. Angewandte Chemie. 132(51). 23439–23443. 1 indexed citations

10.

Valk, Ramon A. van der, et al.. (2020). Mechanical and structural properties of archaeal hypernucleosomes. Nucleic Acids Research. 49(8). 4338–4349. 24 indexed citations

11.

Blok, Anneloes, et al.. (2019). β-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding. Antimicrobial Agents and Chemotherapy. 64(3). 5 indexed citations

12.

Liu, Wei‐Min, et al.. (2019). A Double‐Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe. Angewandte Chemie International Edition. 58(37). 13093–13100. 17 indexed citations

13.

Ahuja, Puneet, et al.. (2018). Methyl group reorientation under ligand binding probed by pseudocontact shifts. Journal of Biomolecular NMR. 71(4). 275–285. 13 indexed citations

14.

Blok, Anneloes, et al.. (2017). Phosphate Promotes the Recovery of Mycobacterium tuberculosis β-Lactamase from Clavulanic Acid Inhibition. Biochemistry. 56(47). 6257–6267. 18 indexed citations

15.

Skinner, Simon P., Anneloes Blok, Monika Timmer, et al.. (2017). Methyl group assignment using pseudocontact shifts with PARAssign. Journal of Biomolecular NMR. 69(4). 183–195. 20 indexed citations

16.

Drijfhout, Jan W., et al.. (2014). An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein–Peptide Complexes Characterized by NMR Spectroscopy. ChemBioChem. 15(4). 556–566. 10 indexed citations

17.

Liu, Wei‐Min, Simon P. Skinner, Monika Timmer, et al.. (2014). A Two‐Armed Lanthanoid‐Chelating Paramagnetic NMR Probe Linked to Proteins via Thioether Linkages. Chemistry - A European Journal. 20(21). 6256–6258. 26 indexed citations

18.

Zambrowicz, Aleksandra, Monika Timmer, Ewelina Eckert, & Tadeusz Trziszka. (2013). Evaluation of the ACE-Inhibitory Activity of Egg-White Proteins Degraded with Pepsin. Polish Journal of Food and Nutrition Sciences. 63(2). 103–108. 7 indexed citations

19.

Zambrowicz, Aleksandra, Monika Timmer, Antoni Polanowski, Gert Lübec, & Tadeusz Trziszka. (2012). Manufacturing of peptides exhibiting biological activity. Amino Acids. 44(2). 315–320. 92 indexed citations

20.

Liu, Wei‐Min, Peter H. J. Keizers, Mathias A. S. Hass, et al.. (2012). A pH-Sensitive, Colorful, Lanthanide-Chelating Paramagnetic NMR Probe. Journal of the American Chemical Society. 134(41). 17306–17313. 58 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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