Japheth E. Gado

958 total citations · 1 hit paper
9 papers, 537 citations indexed

About

Japheth E. Gado is a scholar working on Molecular Biology, Biomedical Engineering and Pollution. According to data from OpenAlex, Japheth E. Gado has authored 9 papers receiving a total of 537 indexed citations (citations by other indexed papers that have themselves been cited), including 6 papers in Molecular Biology, 4 papers in Biomedical Engineering and 3 papers in Pollution. Recurrent topics in Japheth E. Gado's work include Microplastics and Plastic Pollution (3 papers), Biofuel production and bioconversion (3 papers) and biodegradable polymer synthesis and properties (3 papers). Japheth E. Gado is often cited by papers focused on Microplastics and Plastic Pollution (3 papers), Biofuel production and bioconversion (3 papers) and biodegradable polymer synthesis and properties (3 papers). Japheth E. Gado collaborates with scholars based in United States, Sweden and United Kingdom. Japheth E. Gado's co-authors include Gregg T. Beckham, Christina M. Payne, Erika Erickson, Christopher W. Johnson, Brandon C. Knott, J.E. McGeehan, Rosie Graham, Harry P. Austin, Bryon S. Donohoe and H. Lee Woodcock and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Japheth E. Gado

7 papers receiving 528 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.

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

Japheth E. Gado

POLLU

BIOMA

IME

MB

BE

Alexander Bollinger Germany

Christian Sonnendecker Germany

Leona Berndt Germany

Tae Uk Khang South Korea

Yingying Qu China

Jenny Arnling Bååth Denmark

Abhijit N. Shirke United States

Felipe Engelberger Chile

Wantae Kim United States

Ruth Schwerdtfeger Germany

Alexander Bollinger Germany

Japheth E. Gado

384 ×1.2

POLLU

267 ×1.0

BIOMA

128 ×0.8

IME

187 ×1.4

MB

92 ×0.7

BE

Citations per year, relative to Japheth E. Gado Japheth E. Gado (= 1×) peers Alexander Bollinger

Countries citing papers authored by Japheth E. Gado

Since Specialization

Citations

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

Fields of papers citing papers by Japheth E. Gado

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Japheth E. Gado. 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 Japheth E. Gado. The network helps show where Japheth E. Gado may publish in the future.

Co-authorship network of co-authors of Japheth E. Gado

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

All Works

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9 of 9 papers shown

1.

Gado, Japheth E., et al.. (2025). Machine learning prediction of enzyme optimum pH. Nature Machine Intelligence. 7(5). 716–729. 10 indexed citations

2.

Norton‐Baker, Brenna, Japheth E. Gado, Irimpan I. Mathews, et al.. (2025). Machine Learning-Guided Identification of PET Hydrolases from Natural Diversity. ACS Catalysis. 15(18). 16070–16083.

3.

Gomez-Uribe, Carlos Alberto, et al.. (2025). Designing diverse and high-performance proteins with a large language model in the loop. PLoS Computational Biology. 21(6). e1013119–e1013119.

4.

Bell, Elizabeth L., Gloria Rosetto, Morgan A. Ingraham, et al.. (2024). Natural diversity screening, assay development, and characterization of nylon-6 enzymatic depolymerization. Nature Communications. 15(1). 1217–1217. 50 indexed citations

5.

Gado, Japheth E., Anu Nutt, Mikael Nilsson, et al.. (2022). Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non‐productive binding: insights from crystal structures and MD simulation. FEBS Journal. 290(2). 379–399. 4 indexed citations

6.

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

7.

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 →

8.

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

9.

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

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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