M.T. Murakami

10.2k total citations · 1 hit paper
210 papers, 8.0k citations indexed

About

M.T. Murakami is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, M.T. Murakami has authored 210 papers receiving a total of 8.0k indexed citations (citations by other indexed papers that have themselves been cited), including 108 papers in Molecular Biology, 60 papers in Biotechnology and 60 papers in Biomedical Engineering. Recurrent topics in M.T. Murakami's work include Biofuel production and bioconversion (56 papers), Enzyme Production and Characterization (52 papers) and Venomous Animal Envenomation and Studies (47 papers). M.T. Murakami is often cited by papers focused on Biofuel production and bioconversion (56 papers), Enzyme Production and Characterization (52 papers) and Venomous Animal Envenomation and Studies (47 papers). M.T. Murakami collaborates with scholars based in Brazil, Japan and United States. M.T. Murakami's co-authors include Raghuvir K. Arni, Yu Matsumoto, Kazunori Kataoka, Kazue Mizuno, Horacio Cabral, Masanari Kimura, Mitsunobu R. Kano, Kohei Miyazono, Yasuko Terada and Nobuhiro Nishiyama and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

M.T. Murakami

206 papers receiving 7.9k citations

Hit Papers

align trajectories sort by overperformance

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.

Accumulation of sub-100 nm polymeric micelles in poorly permeable tumours depends on size

2011 2.1k citations M.T. Murakami et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
M.T. Murakami	3.4k	2.6k	1.5k	1.5k	1.4k	210	8.0k
Laura L. Kiessling	10.9k 3.2×	1.5k 0.6×	1.6k 1.1×	621 0.4×	471 0.3×	195	15.5k
Kirsten Sandvig	14.1k 4.1×	1.7k 0.6×	1.2k 0.8×	1.3k 0.9×	3.5k 2.5×	315	23.3k
Joel A. Swanson	7.0k 2.0×	918 0.4×	912 0.6×	951 0.6×	729 0.5×	137	14.6k
Antonio Villaverde	7.6k 2.2×	1.2k 0.5×	1.3k 0.9×	1.9k 1.3×	1.7k 1.2×	348	10.5k
François Baneyx	5.2k 1.5×	878 0.3×	1.6k 1.1×	1.2k 0.8×	626 0.4×	113	7.5k
Meir Wilchek	9.3k 2.7×	1.3k 0.5×	721 0.5×	570 0.4×	623 0.4×	349	16.4k
Wei‐Chiang Shen	4.5k 1.3×	469 0.2×	658 0.4×	535 0.4×	478 0.3×	131	6.8k
Kouhei Tsumoto	7.6k 2.2×	879 0.3×	524 0.3×	670 0.5×	574 0.4×	419	11.5k
Norma J. Greenfield	8.2k 2.4×	541 0.2×	1.2k 0.8×	635 0.4×	380 0.3×	83	12.2k
Stefan Tenzer	5.3k 1.6×	1.5k 0.6×	2.3k 1.5×	478 0.3×	172 0.1×	178	10.9k

Countries citing papers authored by M.T. Murakami

Since Specialization

Citations

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

Fields of papers citing papers by M.T. Murakami

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M.T. Murakami

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

Li, Si, et al.. (2026). A disulfide redox switch mechanism regulates glycoside hydrolase function. Nature Communications. 17(1). 45–45.

Minsavage, Gerald V., Joachim Kilian, Nan Wang, et al.. (2025). Xanthomonas coordinates type III–type II effector synergy by activating fruit-ripening pathway. Science. 390(6779). 1292–1298.

Rodrigues, Maria Isabel, et al.. (2025). Pilot-scale high-consistency mechanical refining improves enzymatic saccharification of lignocellulosic feedstock. Scientific Reports. 15(1). 10514–10514. 1 indexed citations

Generoso, Wesley Cardoso, Ricardo Rodrigues de Melo, F Mandelli, et al.. (2025). Coordinated conformational changes in P450 decarboxylases enable hydrocarbons production from renewable feedstocks. Nature Communications. 16(1). 945–945. 3 indexed citations

Mandelli, F, E.A. Lima, M.A.B. Morais, et al.. (2024). A functionally augmented carbohydrate utilization locus from herbivore gut microbiota fueled by dietary β-glucans. npj Biofilms and Microbiomes. 10(1). 105–105. 1 indexed citations

Côrrea, Thamy Lívia Ribeiro, Carlos Alberto Rodrigues Costa, Lúcia D. Wolf, et al.. (2024). On the Non‐Catalytic Role of Lytic Polysaccharide Monooxygenases in Boosting the Action of PETases on PET Polymers. ChemSusChem. 18(4). e202401350–e202401350. 2 indexed citations

Generoso, Wesley Cardoso, Suman Das, Amanda S. Souza, et al.. (2023). Dimer-assisted mechanism of (un)saturated fatty acid decarboxylation for alkene production. Proceedings of the National Academy of Sciences. 120(22). e2221483120–e2221483120. 15 indexed citations

Morais, M.A.B., et al.. (2023). Molecular plasticity of CBM3 ancillary domain leads to conformational changes in the cellulose binding interface. Biochemical and Biophysical Research Communications. 645. 71–78. 1 indexed citations

Murakami, M.T., et al.. (2023). Effect of pH on the secondary structure and thermostability of beetle luciferases: structural origin of pH-insensitivity. Photochemical & Photobiological Sciences. 22(4). 893–904. 2 indexed citations

10.

Terrasan, César Rafael Fanchini, Jaqueline Aline Gerhardt, João Paulo L. Franco Cairo, et al.. (2022). Deletion of AA9 Lytic Polysaccharide Monooxygenases Impacts A. nidulans Secretome and Growth on Lignocellulose. Microbiology Spectrum. 10(3). e0212521–e0212521. 7 indexed citations

11.

Melo, Ricardo Rodrigues de, E.A. Lima, Gabriela Félix Persinoti, et al.. (2020). Identification of a cold-adapted and metal-stimulated β-1,4-glucanase with potential use in the extraction of bioactive compounds from plants. International Journal of Biological Macromolecules. 166. 190–199. 11 indexed citations

12.

Lancheros, César Armando Contreras, et al.. (2019). In-solution behavior and protective potential of asparagine synthetase A from Trypanosoma cruzi. Molecular and Biochemical Parasitology. 230. 1–7. 2 indexed citations

13.

Murakami, M.T., et al.. (2019). Targeting Loxosceles spider Sphingomyelinase D with small-molecule inhibitors as a potential therapeutic approach for loxoscelism. Journal of Enzyme Inhibition and Medicinal Chemistry. 34(1). 310–321. 16 indexed citations

14.

Zanphorlin, L.M., P.O. Giuseppe, Rodrigo V. Honorato, et al.. (2016). Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7. Scientific Reports. 6(1). 23776–23776. 53 indexed citations

15.

Souza, Flávio Henrique Moreira, Luana Parras Meleiro, Carla Botelho Machado, et al.. (2014). Gene cloning, expression and biochemical characterization of a glucose- and xylose-stimulated β-glucosidase from Humicola insolens RP86. Journal of Molecular Catalysis B Enzymatic. 106. 1–10. 33 indexed citations

16.

Souza, T.A.C.B., Daniel Maragno Trindade, C.C.C. Tonoli, et al.. (2011). Molecular adaptability of nucleoside diphosphate kinase b from trypanosomatid parasites: stability, oligomerization and structural determinants of nucleotide binding. Molecular BioSystems. 7(7). 2189–2195. 37 indexed citations

17.

Oliveira, Rui, M.T. Murakami, Renato Vicentini, et al.. (2011). Expression, purification and spectroscopic analysis of an HdrC: An iron–sulfur cluster-containing protein from Acidithiobacillus ferrooxidans. Process Biochemistry. 46(6). 1335–1341. 12 indexed citations

18.

Georgieva, Dessislava, et al.. (2010). The structure of a native l -amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions. Molecular BioSystems. 7(2). 379–384. 22 indexed citations

19.

Tonoli, C.C.C., et al.. (2009). Structural studies of BmooMPα-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom. Toxicon. 55(2-3). 361–368. 33 indexed citations

20.

Ido, T., et al.. (1982). Metabolic Investigation of 18F-5-Fluorouracil, 18F-5-Fluoro-2'-Deoxyuridine and 18F-5-Fluorouridine in Rats. 1982. 145–149. 3 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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