Kurt Wagschal

2.2k total citations
52 papers, 1.8k citations indexed

About

Kurt Wagschal is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, Kurt Wagschal has authored 52 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Biomedical Engineering, 31 papers in Biotechnology and 29 papers in Molecular Biology. Recurrent topics in Kurt Wagschal's work include Biofuel production and bioconversion (36 papers), Enzyme Production and Characterization (30 papers) and Enzyme Catalysis and Immobilization (12 papers). Kurt Wagschal is often cited by papers focused on Biofuel production and bioconversion (36 papers), Enzyme Production and Characterization (30 papers) and Enzyme Catalysis and Immobilization (12 papers). Kurt Wagschal collaborates with scholars based in United States, Canada and China. Kurt Wagschal's co-authors include Charles C. Lee, Douglas B. Jordan, Brian Tripet, Dominic W. S. Wong, George H. Robertson, Colin T. Mant, Robert S. Hodges, Pierre Lavigne, Jay D. Braker and William J. Orts and has published in prestigious journals such as Journal of Molecular Biology, Applied and Environmental Microbiology and PLANT PHYSIOLOGY.

In The Last Decade

Kurt Wagschal

52 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kurt Wagschal United States 22 1.1k 854 724 252 235 52 1.8k
Roberto Ruller Brazil 28 1.1k 1.0× 1.1k 1.3× 929 1.3× 233 0.9× 360 1.5× 74 1.9k
Edward J. Taylor United Kingdom 28 1.3k 1.1× 631 0.7× 859 1.2× 345 1.4× 462 2.0× 50 2.2k
Colin Mitchinson United States 22 1.5k 1.4× 1.2k 1.4× 762 1.1× 165 0.7× 420 1.8× 32 2.3k
Danica Mislovičová Slovakia 23 825 0.7× 433 0.5× 327 0.5× 172 0.7× 311 1.3× 66 1.4k
Motoo Arai Japan 27 1.4k 1.3× 813 1.0× 1.2k 1.7× 285 1.1× 518 2.2× 177 2.2k
G.R. Hemsworth United Kingdom 21 1.5k 1.4× 1.2k 1.5× 878 1.2× 366 1.5× 827 3.5× 35 2.6k
J.E. Flint United Kingdom 20 769 0.7× 618 0.7× 508 0.7× 195 0.8× 486 2.1× 21 1.5k
Hannu Maaheimo Finland 30 1.9k 1.8× 776 0.9× 397 0.5× 413 1.6× 575 2.4× 87 2.9k
Stephen G. Withers Canada 15 1.8k 1.7× 334 0.4× 791 1.1× 261 1.0× 398 1.7× 17 2.5k
Yoji Hata Japan 25 1.3k 1.2× 557 0.7× 671 0.9× 192 0.8× 330 1.4× 77 1.9k

Countries citing papers authored by Kurt Wagschal

Since Specialization
Citations

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

Fields of papers citing papers by Kurt Wagschal

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kurt Wagschal

This figure shows the co-authorship network connecting the top 25 collaborators of Kurt Wagschal. A scholar is included among the top collaborators of Kurt Wagschal 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 Kurt Wagschal. Kurt Wagschal 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
1.
Wagschal, Kurt, Victor J. Chan, J.H. Pereira, Peter H. Zwart, & Banumathi Sankaran. (2020). Chromohalobacter salixigens uronate dehydrogenase: Directed evolution for improved thermal stability and mutant CsUDH-inc X-ray crystal structure. Process Biochemistry. 114. 185–192. 2 indexed citations
2.
Wagschal, Kurt, Douglas B. Jordan, William Hart‐Cooper, & Victor J. Chan. (2019). Penicillium camemberti galacturonate reductase: C-1 oxidation/reduction of uronic acids and substrate inhibition mitigation by aldonic acids. International Journal of Biological Macromolecules. 153. 1090–1098. 1 indexed citations
3.
Jordan, Douglas B., et al.. (2018). Absence or presence of metal ion activation in two structurally similar GH43 β-xylosidases. Enzyme and Microbial Technology. 114. 29–32. 3 indexed citations
4.
Lee, Charles C., et al.. (2018). Biochemical characterization of Caulobacter crescentus xylose dehydrogenase. International Journal of Biological Macromolecules. 118(Pt A). 1362–1367. 9 indexed citations
5.
6.
Lee, Charles C., et al.. (2016). Production of Glucaric Acid from Hemicellulose Substrate by Rosettasome Enzyme Assemblies. Molecular Biotechnology. 58(7). 489–496. 17 indexed citations
7.
Jordan, Douglas B., et al.. (2015). Isolation and divalent-metal activation of a β-xylosidase, RUM630-BX. Enzyme and Microbial Technology. 82. 158–163. 10 indexed citations
8.
Jordan, Douglas B., Charles C. Lee, Kurt Wagschal, & Jay D. Braker. (2013). Activation of a GH43 β-xylosidase by divalent metal cations: Slow binding of divalent metal and high substrate specificity. Archives of Biochemistry and Biophysics. 533(1-2). 79–87. 13 indexed citations
9.
Mao, Zichao, et al.. (2012). Designer Xylanosomes: Protein Nanostructures for Enhanced Xylan Hydrolysis. Applied Biochemistry and Biotechnology. 167(3). 395–411. 14 indexed citations
10.
Jordan, Douglas B., Kurt Wagschal, Arabela A. Grigorescu, & Jay D. Braker. (2012). Highly active β-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates. Applied Microbiology and Biotechnology. 97(10). 4415–4428. 45 indexed citations
11.
Jordan, Douglas B. & Kurt Wagschal. (2010). Properties and applications of microbial β-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium. Applied Microbiology and Biotechnology. 86(6). 1647–1658. 66 indexed citations
12.
Wong, Dominic W. S., et al.. (2010). ORIGINAL RESEARCH: Chromosomal integration of both an α-amylase and a glucoamylase gene in Saccharomyces cerevisiae for starch conversion. Industrial Biotechnology. 6(2). 112–118. 7 indexed citations
13.
Wagschal, Kurt, et al.. (2008). Purification and Characterization of a Glycoside Hydrolase Family 43 β-xylosidase from Geobacillus thermoleovorans IT-08. Applied Biochemistry and Biotechnology. 155(1-3). 1–10. 40 indexed citations
14.
Wagschal, Kurt, Charles C. Lee, Que Kong, et al.. (2008). The construction and characterization of two xylan‐degrading chimeric enzymes. Biotechnology and Bioengineering. 102(3). 684–692. 38 indexed citations
15.
Lee, Charles C., et al.. (2008). An α-Glucuronidase Enzyme Activity Assay Adaptable for Solid Phase Screening. Applied Biochemistry and Biotechnology. 155(1-3). 11–17. 10 indexed citations
16.
Wagschal, Kurt, et al.. (2007). Cloning, Expression and Characterization of a Glycoside Hydrolase Family 39 Xylosidase from Bacillus Halodurans C-125. Applied Biochemistry and Biotechnology. 146(1-3). 69–78. 17 indexed citations
17.
Wong, Dominic W. S., et al.. (2007). Synergistic Action of Recombinant α-Amylase and Glucoamylase on the Hydrolysis of Starch Granules. The Protein Journal. 26(3). 159–164. 30 indexed citations
18.
Wagschal, Kurt, Brian Tripet, Colin T. Mant, Robert S. Hodges, & Pierre Lavigne. (1999). The role of position a in determining the stability and oligomerization state of α‐helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. Protein Science. 8(11). 2312–2329. 147 indexed citations
19.
Wagschal, Kurt, Hyung‐Jung Pyun, Robert M. Coates, & Rodney Croteau. (1994). Monoterpene Biosynthesis: Isotope Effects Associated with Bicyclic Olefin Formation Catalyzed by Pinene Synthases from Sage (Salvia officinalis). Archives of Biochemistry and Biophysics. 308(2). 477–487. 28 indexed citations
20.
Pyun, Hyung‐Jung, et al.. (1994). Stereochemistry of the Proton Elimination in the Formation of (+)- and (−)-α-Pinene by Monoterpene Cyclases from Sage (Salvia officinalis). Archives of Biochemistry and Biophysics. 308(2). 488–496. 15 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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