Focco van den Akker

4.6k total citations
80 papers, 3.3k citations indexed

About

Focco van den Akker is a scholar working on Molecular Biology, Molecular Medicine and Pharmacology. According to data from OpenAlex, Focco van den Akker has authored 80 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 37 papers in Molecular Medicine and 24 papers in Pharmacology. Recurrent topics in Focco van den Akker's work include Antibiotic Resistance in Bacteria (37 papers), Antibiotics Pharmacokinetics and Efficacy (20 papers) and Nitric Oxide and Endothelin Effects (10 papers). Focco van den Akker is often cited by papers focused on Antibiotic Resistance in Bacteria (37 papers), Antibiotics Pharmacokinetics and Efficacy (20 papers) and Nitric Oxide and Endothelin Effects (10 papers). Focco van den Akker collaborates with scholars based in United States, Italy and Germany. Focco van den Akker's co-authors include Robert A. Bonomo, Annie Beuve, Xiaolei Ma, Nazish Sayed, Steve Sarfaty, E.A. Merritt, Joseph Martial, Cécile L'Hoir, Christopher R. Bethel and Padmamalini Baskaran and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Focco van den Akker

80 papers receiving 3.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Focco van den Akker United States	33	1.6k	962	606	554	409	80	3.3k
Samy O. Meroueh United States	35	2.0k 1.3×	875 0.9×	479 0.8×	144 0.3×	175 0.4×	89	4.2k
Walter Fast United States	32	1.7k 1.1×	1.5k 1.6×	579 1.0×	298 0.5×	305 0.7×	80	3.5k
David A. Six United States	23	1.6k 1.0×	421 0.4×	320 0.5×	198 0.4×	278 0.7×	49	2.8k
Adrian R. Walmsley United Kingdom	34	1.8k 1.1×	451 0.5×	227 0.4×	184 0.3×	137 0.3×	89	3.6k
Daniel Lim United States	23	3.0k 1.9×	323 0.3×	192 0.3×	190 0.3×	141 0.3×	38	4.4k
Stephen Wood United States	33	2.1k 1.3×	234 0.2×	463 0.8×	1.9k 3.5×	92 0.2×	66	5.0k
Glenn E. Dale Switzerland	35	1.6k 1.0×	489 0.5×	462 0.8×	232 0.4×	50 0.1×	63	3.0k
C R Raetz United States	51	4.1k 2.5×	383 0.4×	163 0.3×	357 0.6×	501 1.2×	87	6.0k
Angela Wilks United States	43	3.8k 2.4×	440 0.5×	267 0.4×	127 0.2×	363 0.9×	97	4.9k
Isabelle Broutin France	28	1.4k 0.9×	677 0.7×	239 0.4×	71 0.1×	136 0.3×	80	2.5k

Countries citing papers authored by Focco van den Akker

Since Specialization

Citations

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

Fields of papers citing papers by Focco van den Akker

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Focco van den Akker. 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 Focco van den Akker. The network helps show where Focco van den Akker may publish in the future.

Co-authorship network of co-authors of Focco van den Akker

This figure shows the co-authorship network connecting the top 25 collaborators of Focco van den Akker. A scholar is included among the top collaborators of Focco van den Akker 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 Focco van den Akker. Focco van den Akker 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

Mack, Andrew R, Vijay Kumar, Christopher R. Bethel, et al.. (2025). Structure and mechanism of taniborbactam inhibition of the cefepime-hydrolyzing, partial R2-loop deletion Pseudomonas -derived cephalosporinase variant PDC-88. Antimicrobial Agents and Chemotherapy. 69(7). e0007825–e0007825. 1 indexed citations

Kumar, Vijay, et al.. (2023). Exploring the inhibition of the soluble lytic transglycosylase Cj0843c of Campylobacter jejuni via targeting different sites with different scaffolds. Protein Science. 32(7). e4683–e4683. 3 indexed citations

Papp‐Wallace, Krisztina M., et al.. (2023). Exploring avibactam and relebactam inhibition of Klebsiella pneumoniae carbapenemase D179N variant: role of the Ω loop-held deacylation water. Antimicrobial Agents and Chemotherapy. 67(10). e0035023–e0035023. 8 indexed citations

Mack, Andrew R, Vijay Kumar, Magdalena A. Taracila, et al.. (2023). Natural protein engineering in the Ω-loop: the role of Y221 in ceftazidime and ceftolozane resistance in Pseudomonas -derived cephalosporinase. Antimicrobial Agents and Chemotherapy. 67(11). e0079123–e0079123. 8 indexed citations

Rodríguez, M.M., Magdalena A. Taracila, María F. Mojica, et al.. (2023). Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses. Antimicrobial Agents and Chemotherapy. 67(1). e0093022–e0093022. 6 indexed citations

Taracila, Magdalena A., Christopher R. Bethel, Andrea M. Hujer, et al.. (2022). Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC β-Lactamase. Antimicrobial Agents and Chemotherapy. 66(4). e0212421–e0212421. 17 indexed citations

Kumar, Vijay, Magdalena A. Taracila, Christopher R. Bethel, et al.. (2022). Structural Characterization of the D179N and D179Y Variants of KPC-2 β-Lactamase: Ω-Loop Destabilization as a Mechanism of Resistance to Ceftazidime-Avibactam. Antimicrobial Agents and Chemotherapy. 66(4). e0241421–e0241421. 41 indexed citations

Kumar, Vijay, Mijoon Lee, Ximin Zeng, et al.. (2021). Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase of Campylobacter jejuni. Biochemistry. 60(14). 1133–1144. 5 indexed citations

Goldberg, Joel, Vijay Kumar, Daniël Hoyer, et al.. (2021). A γ-lactam siderophore antibiotic effective against multidrug-resistant Pseudomonas aeruginosa, Klebsiella pneumoniae, and Acinetobacter spp.. European Journal of Medicinal Chemistry. 220. 113436–113436. 18 indexed citations

10.

Kumar, Vijay, Steven H. Marshall, Krisztina M. Papp‐Wallace, et al.. (2021). Structural Characterization of Diazabicyclooctane β-Lactam “Enhancers” in Complex with Penicillin-Binding Proteins PBP2 and PBP3 of Pseudomonas aeruginosa. mBio. 12(1). 26 indexed citations

11.

Papp‐Wallace, Krisztina M., Nhu Q. Nguyen, Michael R. Jacobs, et al.. (2018). Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234. Journal of Medicinal Chemistry. 61(9). 4067–4086. 125 indexed citations

12.

Kumar, Vijay, et al.. (2018). Structural studies and molecular dynamics simulations suggest a processive mechanism of exolytic lytic transglycosylase from Campylobacter jejuni. PLoS ONE. 13(5). e0197136–e0197136. 8 indexed citations

13.

Stomberski, Colin T., Hua‐Lin Zhou, Liwen Wang, Focco van den Akker, & Jonathan S. Stamler. (2018). Molecular recognition of S-nitrosothiol substrate by its cognate protein denitrosylase. Journal of Biological Chemistry. 294(5). 1568–1578. 26 indexed citations

14.

Winkler, Marisa, Magdalena A. Taracila, Sarah M. Drawz, et al.. (2012). Design and Exploration of Novel Boronic Acid Inhibitors Reveals Important Interactions with a Clavulanic Acid-Resistant Sulfhydryl-Variable (SHV) β-Lactamase. Journal of Medicinal Chemistry. 56(3). 1084–1097. 39 indexed citations

15.

Martin, Emil, Padmamalini Baskaran, Xiaolei Ma, et al.. (2010). Structure of Cinaciguat (BAY 58–2667) Bound to Nostoc H-NOX Domain Reveals Insights into Heme-mimetic Activation of the Soluble Guanylyl Cyclase. Journal of Biological Chemistry. 285(29). 22651–22657. 90 indexed citations

16.

Bethel, Christopher R., Andrea M. Hujer, Kristine M. Hujer, et al.. (2008). Strategic Design of an Effective β-Lactamase Inhibitor. Journal of Biological Chemistry. 284(2). 945–953. 45 indexed citations

17.

Padayatti, Pius S., Marion S. Helfand, Monica A. Totir, et al.. (2005). High Resolution Crystal Structures of the trans-Enamine Intermediates Formed by Sulbactam and Clavulanic Acid and E166A SHV-1 β-Lactamase. Journal of Biological Chemistry. 280(41). 34900–34907. 55 indexed citations

18.

Hall, Pamela R., Run Zheng, Marianne Pusztai‐Carey, et al.. (2004). Expression and crystallization of several forms of thePropionibacterium shermaniitranscarboxylase 5S subunit. Acta Crystallographica Section D Biological Crystallography. 60(3). 521–523. 4 indexed citations

19.

Akker, Focco van den, Mariagrazia Pizza, Rino Rappuoli, & W.G.J. Hol. (1997). Crystal structure of a non‐toxic mutant of heat‐labile enterotoxin, which is a potent mucosal adjuvant. Protein Science. 6(12). 2650–2654. 20 indexed citations

20.

Akker, Focco van den, Elles Steensma, & Wim G. J. Hol. (1996). Tumor marker disaccharide D‐Gal‐β1,3‐GalNAc complexed to heat‐labile enterotoxin from Escherichia coli. Protein Science. 5(6). 1184–1188. 22 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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