Christina M. Payne

4.0k total citations · 2 hit papers
53 papers, 2.9k citations indexed

About

Christina M. Payne is a scholar working on Biomedical Engineering, Molecular Biology and Biotechnology. According to data from OpenAlex, Christina M. Payne has authored 53 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Biomedical Engineering, 29 papers in Molecular Biology and 27 papers in Biotechnology. Recurrent topics in Christina M. Payne's work include Biofuel production and bioconversion (30 papers), Enzyme Production and Characterization (25 papers) and Enzyme Catalysis and Immobilization (10 papers). Christina M. Payne is often cited by papers focused on Biofuel production and bioconversion (30 papers), Enzyme Production and Characterization (25 papers) and Enzyme Catalysis and Immobilization (10 papers). Christina M. Payne collaborates with scholars based in United States, Sweden and Norway. Christina M. Payne's co-authors include Gregg T. Beckham, Michael E. Himmel, Mats Sandgren, Michael F. Crowley, Jerry Ståhlberg, Brandon C. Knott, Henrik Hansson, Heather B. Mayes, Josh V. Vermaas and Morten Sørlie and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Christina M. Payne

53 papers receiving 2.9k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Fungal Cellulases

2015 603 citations Christina M. Payne, Brandon C. Knott et al. profile →
Characterization and engineering of a two-enzyme system for plastics depolymerization

2020 365 citations Brandon C. Knott, Erika Erickson et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Christina M. Payne United States	25	1.9k	1.4k	1.1k	734	684	53	2.9k
Kim Borch Denmark	29	1.4k 0.7×	1.2k 0.8×	581 0.5×	305 0.4×	766 1.1×	74	2.4k
Mats Sandgren Sweden	39	3.4k 1.8×	2.8k 2.0×	1.7k 1.5×	1.4k 1.9×	686 1.0×	108	5.3k
Qiu Cui China	28	1.1k 0.6×	1.4k 1.0×	344 0.3×	240 0.3×	331 0.5×	119	2.7k
Mary Ann Franden United States	22	1.7k 0.9×	1.4k 1.0×	503 0.4×	329 0.4×	369 0.5×	31	2.6k
Qingsheng Qi China	39	1.2k 0.6×	3.0k 2.1×	445 0.4×	171 0.2×	833 1.2×	147	4.0k
Brian F. Pfleger United States	41	2.0k 1.1×	4.2k 2.9×	268 0.2×	303 0.4×	473 0.7×	110	5.9k
Gotthard Kunze Germany	34	1.1k 0.6×	2.4k 1.7×	530 0.5×	699 1.0×	119 0.2×	167	3.6k
Katrina Cornish United States	39	613 0.3×	3.0k 2.1×	331 0.3×	1.4k 1.9×	778 1.1×	170	5.2k
Daniel Kracher Austria	21	1.7k 0.9×	1.2k 0.9×	839 0.7×	1.2k 1.6×	225 0.3×	45	2.6k
Anikó Várnai Norway	33	2.7k 1.5×	1.5k 1.1×	1.2k 1.1×	1.5k 2.0×	625 0.9×	62	3.5k

Countries citing papers authored by Christina M. Payne

Since Specialization

Citations

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

Fields of papers citing papers by Christina M. Payne

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christina M. Payne

This figure shows the co-authorship network connecting the top 25 collaborators of Christina M. Payne. A scholar is included among the top collaborators of Christina M. Payne 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 Christina M. Payne. Christina M. Payne 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

Gado, Japheth E., Brent Harrison, Mats Sandgren, et al.. (2021). Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases. Journal of Biological Chemistry. 297(2). 100931–100931. 19 indexed citations

Gado, Japheth E., Gregg T. Beckham, & Christina M. Payne. (2020). Improving Enzyme Optimum Temperature Prediction with Resampling Strategies and Ensemble Learning. Journal of Chemical Information and Modeling. 60(8). 4098–4107. 37 indexed citations

Knott, Brandon C., Erika Erickson, Mark D. Allen, et al.. (2020). Characterization and engineering of a two-enzyme system for plastics depolymerization. Proceedings of the National Academy of Sciences. 117(41). 25476–25485. 365 indexed citations breakdown →

Machovina, Melodie M., S.J.B. Mallinson, Brandon C. Knott, et al.. (2019). Enabling microbial syringol conversion through structure-guided protein engineering. Proceedings of the National Academy of Sciences. 116(28). 13970–13976. 52 indexed citations

Geronimo, Inacrist, Kathleen Piens, Mikael Gudmundsson, et al.. (2019). Kinetic and molecular dynamics study of inhibition and transglycosylation in Hypocrea jecorina family 3 β-glucosidases. Journal of Biological Chemistry. 294(9). 3169–3180. 9 indexed citations

Yu, Yue, et al.. (2019). Inhibition Mechanisms of Rhodococcus Erythropolis 2′-Hydroxybiphenyl-2-sulfinate Desulfinase (DszB). The Journal of Physical Chemistry B. 123(43). 9054–9065. 6 indexed citations

Liu, Bing, Abhishek A. Kognole, Miao Wu, et al.. (2018). Structural and molecular dynamics studies of a C1‐oxidizing lytic polysaccharide monooxygenase from Heterobasidion irregulare reveal amino acids important for substrate recognition. FEBS Journal. 285(12). 2225–2242. 34 indexed citations

Geronimo, Inacrist, Christina M. Payne, & Mats Sandgren. (2018). Hydrolysis and Transglycosylation Transition States of Glycoside Hydrolase Family 3 β-Glucosidases Differ in Charge and Puckering Conformation. The Journal of Physical Chemistry B. 122(41). 9452–9459. 12 indexed citations

Geronimo, Inacrist, et al.. (2017). Desulfination by 2′-hydroxybiphenyl-2-sulfinate desulfinase proceeds via electrophilic aromatic substitution by the cysteine-27 proton. Chemical Science. 8(7). 5078–5086. 9 indexed citations

10.

Geronimo, Inacrist, Christina M. Payne, & Mats Sandgren. (2017). The role of catalytic residue pK_a on the hydrolysis/transglycosylation partition in family 3 β-glucosidases. Organic & Biomolecular Chemistry. 16(2). 316–324. 13 indexed citations

11.

Kognole, Abhishek A. & Christina M. Payne. (2017). Inhibition of Mammalian Glycoprotein YKL-40. Journal of Biological Chemistry. 292(7). 2624–2636. 27 indexed citations

12.

Yu, Yue, et al.. (2016). CHARMM force field parameters for 2′-hydroxybiphenyl-2-sulfinate, 2-hydroxybiphenyl, and related analogs. Journal of Molecular Graphics and Modelling. 72. 32–42. 10 indexed citations

13.

Geronimo, Inacrist, William E. Rogers, Tom Huxford, et al.. (2016). Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450_BM3 Variants. Biochemistry. 55(25). 3594–3606. 13 indexed citations

14.

Vermaas, Josh V., Michael F. Crowley, Gregg T. Beckham, & Christina M. Payne. (2015). Effects of Lytic Polysaccharide Monooxygenase Oxidation on Cellulose Structure and Binding of Oxidized Cellulose Oligomers to Cellulases B. The Journal of Physical Chemistry. 43 indexed citations

15.

Kognole, Abhishek A. & Christina M. Payne. (2015). Cello-oligomer-binding dynamics and directionality in family 4 carbohydrate-binding modules. Glycobiology. 25(10). 1100–1111. 3 indexed citations

16.

Mathiesen, Geir, et al.. (2015). Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases. The Journal of Physical Chemistry B. 119(30). 9601–9613. 19 indexed citations

17.

Kern, Marcelo, J.E. McGeehan, S.D. Streeter, et al.. (2013). Structural characterization of a unique marine animal family 7 cellobiohydrolase suggests a mechanism of cellulase salt tolerance. Proceedings of the National Academy of Sciences. 110(25). 10189–10194. 82 indexed citations

18.

Wu, Miao, Gregg T. Beckham, A.M. Larsson, et al.. (2013). Crystal Structure and Computational Characterization of the Lytic Polysaccharide Monooxygenase GH61D from the Basidiomycota Fungus Phanerochaete chrysosporium. Journal of Biological Chemistry. 288(18). 12828–12839. 148 indexed citations

19.

Payne, Christina M., Wei Jiang, Michael R. Shirts, et al.. (2013). Glycoside Hydrolase Processivity Is Directly Related to Oligosaccharide Binding Free Energy. Journal of the American Chemical Society. 135(50). 18831–18839. 81 indexed citations

20.

Payne, Christina M., Svein Jarle Horn, Paul Hoff Backe, et al.. (2012). Hallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens Chitinases. Journal of Biological Chemistry. 287(43). 36322–36330. 88 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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