Brian C. Bryksa

538 total citations
20 papers, 350 citations indexed

About

Brian C. Bryksa is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Brian C. Bryksa has authored 20 papers receiving a total of 350 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Biotechnology and 4 papers in Plant Science. Recurrent topics in Brian C. Bryksa's work include Biochemical and Structural Characterization (7 papers), Enzyme Production and Characterization (4 papers) and Protein Structure and Dynamics (3 papers). Brian C. Bryksa is often cited by papers focused on Biochemical and Structural Characterization (7 papers), Enzyme Production and Characterization (4 papers) and Protein Structure and Dynamics (3 papers). Brian C. Bryksa collaborates with scholars based in Canada, United States and India. Brian C. Bryksa's co-authors include Rickey Y. Yada, Masahiro Ogawa, Robert A. B. Keates, Takuji Tanaka, Huogen Xiao, Prasenjit Bhaumik, Alexander Wlodawer, John H. Dupuis, Alexander Zdanov and Susan E. Douglas and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

Brian C. Bryksa

20 papers receiving 349 citations

Peers

Brian C. Bryksa

BIOTE

PHEOH

MICRO

Wei Zhong China

Ana Yepes Germany

Xiang-He Lei United States

Muhammad Saleem United Kingdom

Eiji Tamai Japan

Patrick Yip Canada

Vaibhav Bhandari Canada

Renate Hanschke Germany

Xiaobo Liang China

Seok-Min Lee South Korea

Wei Zhong China

Brian C. Bryksa

326 ×1.6

36 ×0.5

46 ×1.0

BIOTE

22 ×0.5

PHEOH

21 ×0.6

MICRO

Citations per year, relative to Brian C. Bryksa Brian C. Bryksa (= 1×) peers Wei Zhong

Countries citing papers authored by Brian C. Bryksa

Since Specialization

Citations

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

Fields of papers citing papers by Brian C. Bryksa

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Brian C. Bryksa. 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 Brian C. Bryksa. The network helps show where Brian C. Bryksa may publish in the future.

Co-authorship network of co-authors of Brian C. Bryksa

This figure shows the co-authorship network connecting the top 25 collaborators of Brian C. Bryksa. A scholar is included among the top collaborators of Brian C. Bryksa 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 Brian C. Bryksa. Brian C. Bryksa 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

Dupuis, John H., et al.. (2021). Improving the alkaline stability of pepsin through rational protein design using renin, an alkaline-stable aspartic protease, as a structural and functional reference. Enzyme and Microbial Technology. 150. 109871–109871. 4 indexed citations

Dupuis, John H., et al.. (2020). Roles of Plant-Specific Inserts in Plant Defense. Trends in Plant Science. 25(7). 682–694. 9 indexed citations

Zhao, Xiaoli, Hua Yu, Brian C. Bryksa, et al.. (2020). Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert. Journal of Biological Chemistry. 295(43). 14548–14562. 6 indexed citations

Dupuis, John H., et al.. (2020). Comparative bioinformatic and structural analyses of pepsin and renin. Enzyme and Microbial Technology. 141. 109632–109632. 9 indexed citations

Bryksa, Brian C. & Rickey Y. Yada. (2020). Challenges in food nanoscale science and technology. Journal of Food and Drug Analysis. 20(1). 1 indexed citations

Bryksa, Brian C., et al.. (2017). Comparative structure-function characterization of the saposin-like domains from potato, barley, cardoon and Arabidopsis aspartic proteases. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859(5). 1008–1018. 10 indexed citations

Bryksa, Brian C. & Rickey Y. Yada. (2017). Protein Structure Insights into the Bilayer Interactions of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease. Scientific Reports. 7(1). 16911–16911. 8 indexed citations

Xiao, Huogen, et al.. (2016). The prosegment catalyzes native folding of Plasmodium falciparum plasmepsin II. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864(10). 1356–1362. 2 indexed citations

Rogers, Michael A., Qi Feng, Vladimir Ladizhansky, et al.. (2016). Self-assembled fibrillar networks comprised of a naturally-occurring cyclic peptide—LOB3. RSC Advances. 6(47). 40765–40776. 11 indexed citations

10.

Bryksa, Brian C., et al.. (2016). Feeding the world into the future – food and nutrition security: the role of food science and technology. 9(3). 155–166. 68 indexed citations

11.

Bryksa, Brian C., et al.. (2014). In Silico Insights into Protein-Protein Interactions and Folding Dynamics of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease. PLoS ONE. 9(9). e104315–e104315. 19 indexed citations

12.

Xiao, Huogen, Brian C. Bryksa, Prasenjit Bhaumik, et al.. (2014). The zymogen of plasmepsin V from Plasmodium falciparum is enzymatically active. Molecular and Biochemical Parasitology. 197(1-2). 56–63. 17 indexed citations

13.

Bryksa, Brian C. & Rickey Y. Yada. (2012). Nanotechnology: the word is new but the concept is old. An overview of the science and technology in food and food products at the nanoscale level. SHILAP Revista de lepidopterología. 1(2). 188–210. 1 indexed citations

14.

Bryksa, Brian C., Prasenjit Bhaumik, Eugenia Magracheva, et al.. (2011). Structure and Mechanism of the Saposin-like Domain of a Plant Aspartic Protease. Journal of Biological Chemistry. 286(32). 28265–28275. 39 indexed citations

15.

Bryksa, Brian C., et al.. (2010). Rational redesign of porcine pepsinogen containing an antimicrobial peptide. Protein Engineering Design and Selection. 23(9). 711–719. 2 indexed citations

16.

Keates, Robert A. B., et al.. (2007). The structure and function of Saccharomyces cerevisiae proteinase A. Yeast. 24(6). 467–480. 70 indexed citations

17.

Xiao, Huogen, et al.. (2006). Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum. Protein Expression and Purification. 49(1). 88–94. 28 indexed citations

18.

Bryksa, Brian C., et al.. (2006). Understanding the structure–function role of specific catalytic residues in a model food related enzyme: Pepsin. Enzyme and Microbial Technology. 40(5). 1175–1180. 15 indexed citations

19.

Bryksa, Brian C., et al.. (2005). A C-terminal glycine suppresses production of pleurocidin as a fusion peptide in Escherichia coli. Protein Expression and Purification. 45(1). 88–98. 19 indexed citations

20.

Bryksa, Brian C., Takuji Tanaka, & Rickey Y. Yada. (2003). N-Terminal Modifications Increase the Neutral-pH Stability of Pepsin. Biochemistry. 42(45). 13331–13338. 12 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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