Mandana Gruber‐Khadjawi

1.2k total citations
24 papers, 937 citations indexed

About

Mandana Gruber‐Khadjawi is a scholar working on Molecular Biology, Organic Chemistry and Biochemistry. According to data from OpenAlex, Mandana Gruber‐Khadjawi has authored 24 papers receiving a total of 937 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 9 papers in Organic Chemistry and 4 papers in Biochemistry. Recurrent topics in Mandana Gruber‐Khadjawi's work include Enzyme Catalysis and Immobilization (18 papers), Carbohydrate Chemistry and Synthesis (9 papers) and Microbial Metabolic Engineering and Bioproduction (7 papers). Mandana Gruber‐Khadjawi is often cited by papers focused on Enzyme Catalysis and Immobilization (18 papers), Carbohydrate Chemistry and Synthesis (9 papers) and Microbial Metabolic Engineering and Bioproduction (7 papers). Mandana Gruber‐Khadjawi collaborates with scholars based in Austria, Netherlands and Germany. Mandana Gruber‐Khadjawi's co-authors include Herfried Griengl, Thomas Purkarthofer, Wolfgang Skranc, Kateryna Fesko, Helmut Schwab, Karl Gruber, Kerstin Waich, Daniel Mink, Oliver May and Gernot A. Strohmeier and has published in prestigious journals such as Chemical Reviews, Angewandte Chemie International Edition and PLoS ONE.

In The Last Decade

Mandana Gruber‐Khadjawi

24 papers receiving 925 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mandana Gruber‐Khadjawi Austria 16 677 427 114 92 86 24 937
Wolfgang Skranc Austria 18 702 1.0× 362 0.8× 146 1.3× 91 1.0× 147 1.7× 29 986
Ioulia Smonou Greece 17 407 0.6× 469 1.1× 140 1.2× 60 0.7× 84 1.0× 44 833
Thomas Purkarthofer Austria 10 371 0.5× 296 0.7× 100 0.9× 79 0.9× 69 0.8× 11 576
Spiros Kambourakis Greece 17 409 0.6× 299 0.7× 86 0.8× 44 0.5× 96 1.1× 21 679
Anne Zaparucha France 18 488 0.7× 388 0.9× 123 1.1× 31 0.3× 48 0.6× 48 832
Eric C. Roos Netherlands 12 483 0.7× 298 0.7× 64 0.6× 83 0.9× 81 0.9× 22 664
James R. Marshall United Kingdom 18 648 1.0× 457 1.1× 229 2.0× 49 0.5× 156 1.8× 36 976
Chi‐Huey Wong United States 6 643 0.9× 925 2.2× 172 1.5× 52 0.6× 44 0.5× 8 1.1k
Naoyuki Shimada Japan 24 359 0.5× 1.5k 3.6× 252 2.2× 61 0.7× 51 0.6× 50 1.7k

Countries citing papers authored by Mandana Gruber‐Khadjawi

Since Specialization
Citations

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

Fields of papers citing papers by Mandana Gruber‐Khadjawi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mandana Gruber‐Khadjawi. 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 Mandana Gruber‐Khadjawi. The network helps show where Mandana Gruber‐Khadjawi may publish in the future.

Co-authorship network of co-authors of Mandana Gruber‐Khadjawi

This figure shows the co-authorship network connecting the top 25 collaborators of Mandana Gruber‐Khadjawi. A scholar is included among the top collaborators of Mandana Gruber‐Khadjawi 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 Mandana Gruber‐Khadjawi. Mandana Gruber‐Khadjawi 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.
Pavkov‐Keller, Tea, Kerstin Steiner, Barbara Darnhofer, et al.. (2017). Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily. Scientific Reports. 7(1). 46738–46738. 28 indexed citations
2.
Pavkov‐Keller, Tea, et al.. (2017). Crystal Structure and Catalytic Mechanism of CouO, a Versatile C-Methyltransferase from Streptomyces rishiriensis. PLoS ONE. 12(2). e0171056–e0171056. 23 indexed citations
3.
Gutmann, Alexander, et al.. (2017). An ortho C-methylation/O-glycosylation motif on a hydroxy-coumarin scaffold, selectively installed by biocatalysis. Organic & Biomolecular Chemistry. 15(37). 7917–7924. 11 indexed citations
4.
Weber, Hansjörg, et al.. (2016). Methyltransferases: Green Catalysts for Friedel–Crafts Alkylations. ChemCatChem. 8(7). 1354–1360. 26 indexed citations
5.
Gruber‐Khadjawi, Mandana, et al.. (2016). (R)‐Selective Nitroaldol Reaction Catalyzed by Metal‐Dependent Bacterial Hydroxynitrile Lyases. ChemCatChem. 8(13). 2214–2216. 18 indexed citations
6.
Gruber‐Khadjawi, Mandana, et al.. (2016). High-level biosynthesis of norleucine in E. coli for the economic labeling of proteins. Journal of Biotechnology. 235. 100–111. 20 indexed citations
7.
Gruber‐Khadjawi, Mandana, et al.. (2014). Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum. Computational and Structural Biotechnology Journal. 10(16). 58–62. 23 indexed citations
8.
Fesko, Kateryna & Mandana Gruber‐Khadjawi. (2013). Biocatalytic Methods for CC Bond Formation. ChemCatChem. 5(6). 1248–1272. 109 indexed citations
9.
Łyskowski, Andrzej, et al.. (2012). Crystallization of the novelS-adenosyl-L-methionine-dependentC-methyltransferase CouO fromStreptomyces rishiriensisand preliminary diffraction data analysis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(6). 698–700. 1 indexed citations
10.
Remler, Peter, et al.. (2012). Molecular characterization of the C-methyltransferase NovO of Streptomyces spheroides, a valuable enzyme for performing Friedel–Crafts alkylation. Journal of Molecular Catalysis B Enzymatic. 84. 2–8. 15 indexed citations
11.
Strohmeier, Gernot A., Harald Pichler, Oliver May, & Mandana Gruber‐Khadjawi. (2011). Application of Designed Enzymes in Organic Synthesis. Chemical Reviews. 111(7). 4141–4164. 120 indexed citations
12.
Strohmeier, Gernot A., Harald Pichler, Oliver May, & Mandana Gruber‐Khadjawi. (2011). ChemInform Abstract: Application of Designed Enzymes in Organic Synthesis. ChemInform. 42(45). 1 indexed citations
13.
Gruber‐Khadjawi, Mandana, et al.. (2010). Asymmetric Retro‐Henry Reaction Catalyzed by Hydroxynitrile Lyase from Hevea brasiliensis. ChemCatChem. 2(8). 981–986. 27 indexed citations
14.
Ueberbacher, Bernhard J., et al.. (2009). Biocatalytic Friedel–Crafts Alkylation Using Non‐natural Cofactors. Angewandte Chemie. 121(50). 9710–9712. 41 indexed citations
15.
Ueberbacher, Bernhard J., et al.. (2009). Biocatalytic Friedel–Crafts Alkylation Using Non‐natural Cofactors. Angewandte Chemie International Edition. 48(50). 9546–9548. 116 indexed citations
16.
Gruber‐Khadjawi, Mandana, Thomas Purkarthofer, Wolfgang Skranc, & Herfried Griengl. (2007). Hydroxynitrile Lyase‐Catalyzed Enzymatic Nitroaldol (Henry) Reaction. Advanced Synthesis & Catalysis. 349(8-9). 1445–1450. 103 indexed citations
17.
Purkarthofer, Thomas, Karl Gruber, Mandana Gruber‐Khadjawi, et al.. (2006). A Biocatalytic Henry Reaction—The Hydroxynitrile Lyase from Hevea brasiliensis Also Catalyzes Nitroaldol Reactions. Angewandte Chemie International Edition. 45(21). 3454–3456. 158 indexed citations
18.
Gruber‐Khadjawi, Mandana, et al.. (1996). Chemoenzymatic methods for the preparation of optically active cyclic polyazido alcohols from easily available achiral starting materials. Tetrahedron Asymmetry. 7(3). 807–814. 4 indexed citations
19.
Gruber‐Khadjawi, Mandana & Helmut Hönig. (1993). A Contribution to Evaluate the Size of the Active Site of Lipases from Candida rugosa and Pseudomonas cepacia. 2 indexed citations
20.
Gruber‐Khadjawi, Mandana, Helmut Hönig, & Hansjörg Weber. (1992). Enzymatic resolutions of α‐ and β‐hydroxypropionic acid esters. Chirality. 4(2). 103–109. 6 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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