Roberto Ruller

2.9k total citations
74 papers, 1.9k citations indexed

About

Roberto Ruller is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, Roberto Ruller has authored 74 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Biomedical Engineering, 45 papers in Biotechnology and 43 papers in Molecular Biology. Recurrent topics in Roberto Ruller's work include Biofuel production and bioconversion (50 papers), Enzyme Production and Characterization (42 papers) and Microbial Metabolic Engineering and Bioproduction (16 papers). Roberto Ruller is often cited by papers focused on Biofuel production and bioconversion (50 papers), Enzyme Production and Characterization (42 papers) and Microbial Metabolic Engineering and Bioproduction (16 papers). Roberto Ruller collaborates with scholars based in Brazil, United States and United Kingdom. Roberto Ruller's co-authors include Richard J. Ward, M.T. Murakami, Fábio M. Squina, A.H.C. de Oliveira, Lucimara Chioato, Juliana M. Sá, L.M. Zanphorlin, Júnio Cota, C.R. Santos and Zaira B. Hoffmam and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Hazardous Materials.

In The Last Decade

Roberto Ruller

72 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Roberto Ruller Brazil 28 1.1k 1.1k 929 360 286 74 1.9k
C.R. Santos Brazil 21 452 0.4× 520 0.5× 538 0.6× 250 0.7× 64 0.2× 38 944
Chieko Kumagai Japan 20 949 0.8× 422 0.4× 629 0.7× 263 0.7× 49 0.2× 47 1.3k
Shodo Hara Japan 21 1.1k 1.0× 440 0.4× 536 0.6× 351 1.0× 63 0.2× 82 1.5k
Yuzuru Iimura Japan 21 1.2k 1.0× 430 0.4× 562 0.6× 513 1.4× 51 0.2× 68 1.6k
Henri‐Pierre Fierobe France 32 1.4k 1.2× 1.9k 1.8× 1.4k 1.6× 820 2.3× 179 0.6× 68 2.8k
Rolf Morosoli Canada 29 1.4k 1.2× 1.3k 1.2× 1.3k 1.4× 547 1.5× 178 0.6× 81 2.3k
Colin Mitchinson United States 22 1.5k 1.3× 1.2k 1.1× 762 0.8× 420 1.2× 60 0.2× 32 2.3k
A. Belaich France 29 1.2k 1.0× 1.9k 1.8× 1.4k 1.5× 829 2.3× 170 0.6× 46 2.6k
Takeshi Uozumi Japan 27 1.5k 1.3× 486 0.5× 709 0.8× 425 1.2× 336 1.2× 138 2.1k
Katsuya Ozaki Japan 25 1.1k 1.0× 502 0.5× 1.1k 1.2× 415 1.2× 349 1.2× 67 1.8k

Countries citing papers authored by Roberto Ruller

Since Specialization
Citations

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

Fields of papers citing papers by Roberto Ruller

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Roberto Ruller. 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 Roberto Ruller. The network helps show where Roberto Ruller may publish in the future.

Co-authorship network of co-authors of Roberto Ruller

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

All Works

20 of 20 papers shown
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Silva, Denise Brentan, Adilson Beatriz, Fabiana Fonseca Zanoelo, et al.. (2022). N-acetylation of toxic aromatic amines by fungi: Strain screening, cytotoxicity and genotoxicity evaluation, and application in bioremediation of 3,4-dichloroaniline. Journal of Hazardous Materials. 441. 129887–129887. 8 indexed citations
4.
Contessoto, Vinícius G., Ricardo Rodrigues de Melo, Vinícius M. de Oliveira, et al.. (2021). Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases. Biophysical Journal. 120(11). 2172–2180. 8 indexed citations
5.
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
6.
Milessi, Thais S., Viviane Maimoni Gonçalves, Roberto Ruller, et al.. (2020). High stabilization and hyperactivation of a Recombinant β-Xylosidase through Immobilization Strategies. Enzyme and Microbial Technology. 145. 109725–109725. 15 indexed citations
7.
Tramontina, Robson, Lívia Beatriz Brenelli, Viviane Marcos Nascimento, et al.. (2019). Designing a cocktail containing redox enzymes to improve hemicellulosic hydrolysate fermentability by microorganisms. Enzyme and Microbial Technology. 135. 109490–109490. 13 indexed citations
8.
Hoffmam, Zaira B., L.M. Zanphorlin, Júnio Cota, et al.. (2016). Xylan-specific carbohydrate-binding module belonging to family 6 enhances the catalytic performance of a GH11 endo-xylanase. New Biotechnology. 33(4). 467–472. 29 indexed citations
9.
Lima, E.A., Carla Botelho Machado, L.M. Zanphorlin, et al.. (2016). GH53 Endo-Beta-1,4-Galactanase from a Newly Isolated Bacillus licheniformis CBMAI 1609 as an Enzymatic Cocktail Supplement for Biomass Saccharification. Applied Biochemistry and Biotechnology. 179(3). 415–426. 9 indexed citations
10.
Zanphorlin, L.M., Flávio Henrique Moreira Souza, José Diogo, et al.. (2015). A novel cold-adapted and glucose-tolerant GH1 β-glucosidase from Exiguobacterium antarcticum B7. International Journal of Biological Macromolecules. 82. 375–380. 59 indexed citations
11.
Santos, C.R., Zaira B. Hoffmam, L.M. Zanphorlin, et al.. (2014). Molecular Mechanisms Associated with Xylan Degradation by Xanthomonas Plant Pathogens. Journal of Biological Chemistry. 289(46). 32186–32200. 55 indexed citations
12.
Cota, Júnio, Leandro C. Oliveira, André Damásio, et al.. (2013). Assembling a xylanase–lichenase chimera through all-atom molecular dynamics simulations. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(8). 1492–1500. 32 indexed citations
13.
Ribeiro, Daniela A., Júnio Cota, Thabata M. Alvarez, et al.. (2012). The Penicillium echinulatum Secretome on Sugar Cane Bagasse. PLoS ONE. 7(12). e50571–e50571. 58 indexed citations
14.
Santos, C.R., Júnio Cota, Thabata M. Alvarez, et al.. (2011). Molecular insights into substrate specificity and thermal stability of a bacterial GH5-CBM27 endo-1,4-β-d-mannanase. Journal of Structural Biology. 177(2). 469–476. 37 indexed citations
15.
Souza, T.A.C.B., C.R. Santos, Roberto Ruller, et al.. (2011). Structure of a novel thermostable GH51 α‐L‐arabinofuranosidase from Thermotoga petrophila RKU‐1. Protein Science. 20(9). 1632–1637. 20 indexed citations
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Santos, C.R., Fábio M. Squina, Adriana Franco Paes Leme, et al.. (2010). Functional and biophysical characterization of a hyperthermostable GH51 α-l-arabinofuranosidase from Thermotoga petrophila. Biotechnology Letters. 33(1). 131–137. 18 indexed citations
18.
Squina, Fábio M., C.R. Santos, Daniela A. Ribeiro, et al.. (2010). Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila. Biochemical and Biophysical Research Communications. 399(4). 505–511. 22 indexed citations
19.
Murakami, M.T., Roberto Ruller, Richard J. Ward, & Raghuvir K. Arni. (2005). Crystallization and preliminary X-ray crystallographic studies of the mesophilic xylanase A fromBacillus subtilis1A1. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(2). 219–220. 8 indexed citations
20.
Ruller, Roberto, José Cesar Rosa, Vítor M. Faça, Lewis Joel Greene, & Richard J. Ward. (2005). Efficient constitutive expression of Bacillus subtilis xylanase A in Escherichia coli DH5α under the control of the Bacillus BsXA promoter. Biotechnology and Applied Biochemistry. 43(1). 9–15. 30 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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