Christopher T. Lohans

2.4k total citations
53 papers, 1.6k citations indexed

About

Christopher T. Lohans is a scholar working on Molecular Biology, Molecular Medicine and Food Science. According to data from OpenAlex, Christopher T. Lohans has authored 53 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 19 papers in Molecular Medicine and 18 papers in Food Science. Recurrent topics in Christopher T. Lohans's work include Antibiotic Resistance in Bacteria (19 papers), Probiotics and Fermented Foods (18 papers) and Pneumocystis jirovecii pneumonia detection and treatment (11 papers). Christopher T. Lohans is often cited by papers focused on Antibiotic Resistance in Bacteria (19 papers), Probiotics and Fermented Foods (18 papers) and Pneumocystis jirovecii pneumonia detection and treatment (11 papers). Christopher T. Lohans collaborates with scholars based in Canada, United Kingdom and United States. Christopher T. Lohans's co-authors include John C. Vederas, Christopher J. Schofield, Marco J. van Belkum, Stephen A. Cochrane, Jürgen Brem, Clarissa S. Sit, Mark Miskolzie, James Spencer, M.A. McDonough and Jeella Z. Acedo and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Christopher T. Lohans

50 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Christopher T. Lohans Canada	26	880	456	430	399	224	53	1.6k
Dongwoo Shin South Korea	31	1.1k 1.3×	322 0.7×	519 1.2×	206 0.5×	147 0.7×	53	2.1k
Jean‐Michel Bolla France	29	957 1.1×	1.1k 2.4×	715 1.7×	289 0.7×	175 0.8×	81	2.7k
Michael J. Pucci United States	30	1.4k 1.6×	625 1.4×	776 1.8×	533 1.3×	229 1.0×	72	3.0k
Shangshang Qin China	28	607 0.7×	376 0.8×	793 1.8×	252 0.6×	273 1.2×	84	2.0k
Gary R. Eldridge United States	17	1.0k 1.2×	214 0.5×	199 0.5×	221 0.6×	185 0.8×	40	1.7k
Luís Octávio Regasini Brazil	30	706 0.8×	388 0.9×	113 0.3×	313 0.8×	119 0.5×	110	2.5k
Inshad Ali Khan India	32	1.4k 1.6×	461 1.0×	541 1.3×	519 1.3×	129 0.6×	97	3.1k
Dijun Du United Kingdom	16	1.1k 1.2×	161 0.4×	1.2k 2.7×	326 0.8×	122 0.5×	22	2.3k
Zeeshan Fatima India	21	449 0.5×	299 0.7×	191 0.4×	148 0.4×	91 0.4×	72	1.5k
Mona I. Shaaban Egypt	29	1.0k 1.2×	159 0.3×	358 0.8×	232 0.6×	141 0.6×	61	2.0k

Countries citing papers authored by Christopher T. Lohans

Since Specialization

Citations

This map shows the geographic impact of Christopher T. Lohans'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 Christopher T. Lohans with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Christopher T. Lohans more than expected).

Fields of papers citing papers by Christopher T. Lohans

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Christopher T. Lohans. 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 Christopher T. Lohans. The network helps show where Christopher T. Lohans may publish in the future.

Co-authorship network of co-authors of Christopher T. Lohans

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher T. Lohans. A scholar is included among the top collaborators of Christopher T. Lohans 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 Christopher T. Lohans. Christopher T. Lohans 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

Bhat, Shreyas, et al.. (2025). Rapid Detection of Carbapenemase-Producing Enterobacterales Using a Luminescent Whole-Cell Biosensor. ACS Infectious Diseases. 12(1). 64–73. 1 indexed citations

Zhang, Zhihong, et al.. (2024). Substitution of 2-oxoglutarate alters reaction outcomes of the Pseudomonas savastanoi ethylene-forming enzyme. Journal of Biological Chemistry. 300(8). 107546–107546. 5 indexed citations

Lohans, Christopher T., et al.. (2021). β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates. RSC Medicinal Chemistry. 12(10). 1623–1639. 125 indexed citations

Hinchliffe, Philip, Tika R. Malla, Catherine L. Tooke, et al.. (2021). Faropenem reacts with serine and metallo-β-lactamases to give multiple products. European Journal of Medicinal Chemistry. 215. 113257–113257. 15 indexed citations

Abboud, Martine I., Rasheduzzaman Chowdhury, Anthony Tumber, et al.. (2020). Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii. Journal of Biological Chemistry. 295(49). 16545–16561. 13 indexed citations

Lohans, Christopher T., et al.. (2020). Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism. Journal of Biological Chemistry. 295(49). 16604–16613. 13 indexed citations

Cochrane, Stephen A. & Christopher T. Lohans. (2020). Breaking down the cell wall: Strategies for antibiotic discovery targeting bacterial transpeptidases. European Journal of Medicinal Chemistry. 194. 112262–112262. 40 indexed citations

Lohans, Christopher T., et al.. (2019). A Fluorescence‐Based Assay for Screening β‐Lactams Targeting the Mycobacterium tuberculosis Transpeptidase Ldt_Mt2. ChemBioChem. 21(3). 368–372. 18 indexed citations

Cahill, Samuel T., Jonathan M. Tyrrell, Iva Navrátilová, et al.. (2019). Studies on the inhibition of AmpC and other β-lactamases by cyclic boronates. Biochimica et Biophysica Acta (BBA) - General Subjects. 1863(4). 742–748. 25 indexed citations

10.

Lohans, Christopher T., Catherine L. Tooke, Philip Hinchliffe, et al.. (2019). Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation. Scientific Reports. 9(1). 13608–13608. 30 indexed citations

11.

Shaikh, Faraz, Yuguang Zhao, Luis Álvarez, et al.. (2019). Structure-Based in Silico Screening Identifies a Potent Ebolavirus Inhibitor from a Traditional Chinese Medicine Library. Journal of Medicinal Chemistry. 62(6). 2928–2937. 31 indexed citations

12.

Abboud, Martine I., et al.. (2019). Inhibition of a viral prolyl hydroxylase. Bioorganic & Medicinal Chemistry. 27(12). 2405–2412. 4 indexed citations

13.

Lohans, Christopher T., Tika R. Malla, Kiran Kumar, et al.. (2018). Non‐Hydrolytic β‐Lactam Antibiotic Fragmentation by l,d‐Transpeptidases and Serine β‐Lactamase Cysteine Variants. Angewandte Chemie International Edition. 58(7). 1990–1994. 24 indexed citations

14.

Lohans, Christopher T., David Y. Wang, Christian Jorgensen, et al.. (2017). ¹³C-Carbamylation as a mechanistic probe for the inhibition of class D β-lactamases by avibactam and halide ions. Organic & Biomolecular Chemistry. 15(28). 6024–6032. 19 indexed citations

15.

Li, Guo‐Bo, Zhujun Yu, Luyi Huang, et al.. (2017). IFPTarget: A Customized Virtual Target Identification Method Based on Protein–Ligand Interaction Fingerprinting Analyses. Journal of Chemical Information and Modeling. 57(7). 1640–1651. 24 indexed citations

16.

Acedo, Jeella Z., et al.. (2016). Nuclear Magnetic Resonance Solution Structures of Lacticin Q and Aureocin A53 Reveal a Structural Motif Conserved among Leaderless Bacteriocins with Broad-Spectrum Activity. Biochemistry. 55(4). 733–742. 46 indexed citations

17.

Lin, Xiaoxi B., Christopher T. Lohans, Rebbeca M. Duar, et al.. (2015). Genetic Determinants of Reutericyclin Biosynthesis in Lactobacillus reuteri. Applied and Environmental Microbiology. 81(6). 2032–2041. 53 indexed citations

18.

Arbulu, Sara, Christopher T. Lohans, Marco J. van Belkum, et al.. (2015). Solution Structure of Enterocin HF, an Antilisterial Bacteriocin Produced by Enterococcus faecium M3K31. Journal of Agricultural and Food Chemistry. 63(49). 10689–10695. 19 indexed citations

19.

Lohans, Christopher T. & John C. Vederas. (2013). Structural characterization of thioether-bridged bacteriocins. The Journal of Antibiotics. 67(1). 23–30. 48 indexed citations

20.

Lohans, Christopher T., Marco J. van Belkum, Stephen A. Cochrane, et al.. (2013). Biochemical, Structural, and Genetic Characterization of Tridecaptin A₁, an Antagonist of Campylobacter jejuni. ChemBioChem. 15(2). 243–249. 60 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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