T.R.M. Barends

2.1k total citations
24 papers, 1.0k citations indexed

About

T.R.M. Barends is a scholar working on Materials Chemistry, Molecular Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, T.R.M. Barends has authored 24 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Materials Chemistry, 15 papers in Molecular Biology and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in T.R.M. Barends's work include Enzyme Structure and Function (14 papers), Biochemical and Molecular Research (6 papers) and Enzyme Catalysis and Immobilization (4 papers). T.R.M. Barends is often cited by papers focused on Enzyme Structure and Function (14 papers), Biochemical and Molecular Research (6 papers) and Enzyme Catalysis and Immobilization (4 papers). T.R.M. Barends collaborates with scholars based in Germany, Netherlands and Switzerland. T.R.M. Barends's co-authors include Ilme Schlichting, Bauke W. Dijkstra, Michael F. Dunn, Dimitri Niks, Huu Ngo, Tatiana Domratcheva, M.J. Maul, Andreas F. Glas, Sabine Schneider and Thomas Carell and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

T.R.M. Barends

24 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
T.R.M. Barends Germany	17	638	375	207	142	118	24	1.0k
Akiko Kita Japan	18	1.0k 1.6×	341 0.9×	277 1.3×	178 1.3×	186 1.6×	66	1.5k
T. Arakawa Japan	21	1.1k 1.7×	195 0.5×	154 0.7×	177 1.2×	234 2.0×	53	1.6k
Franz Suter Switzerland	26	1.3k 2.0×	232 0.6×	155 0.7×	220 1.5×	77 0.7×	45	1.6k
Amrik Basran United Kingdom	12	541 0.8×	96 0.3×	176 0.9×	78 0.5×	56 0.5×	19	1.0k
Laura A. Andersson United States	19	689 1.1×	204 0.5×	147 0.7×	61 0.4×	77 0.7×	33	1.3k
Beata Myśliwa‐Kurdziel Poland	21	694 1.1×	186 0.5×	356 1.7×	100 0.7×	22 0.2×	54	1.1k
Konstantin M. Boyko Russia	19	661 1.0×	281 0.7×	74 0.4×	54 0.4×	33 0.3×	105	988
S.L. Edwards United States	8	604 0.9×	142 0.4×	628 3.0×	74 0.5×	262 2.2×	14	1.3k
T. Joseph Kappock United States	21	1.1k 1.7×	396 1.1×	64 0.3×	28 0.2×	61 0.5×	35	1.5k
Audrey L. Lamb United States	19	899 1.4×	288 0.8×	241 1.2×	21 0.1×	41 0.3×	54	1.7k

Countries citing papers authored by T.R.M. Barends

Since Specialization

Citations

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

Fields of papers citing papers by T.R.M. Barends

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T.R.M. Barends

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Akram, M., Joachim Reimann, Andreas Dietl, et al.. (2019). A nitric oxide–binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase. Journal of Biological Chemistry. 294(45). 16712–16728. 15 indexed citations

Maalcke, Wouter J., Joachim Reimann, Simon de Vries, et al.. (2016). Characterization of Anammox Hydrazine Dehydrogenase, a Key N2-producing Enzyme in the Global Nitrogen Cycle. Journal of Biological Chemistry. 291(33). 17077–17092. 102 indexed citations

Zarrine‐Afsar, Arash, T.R.M. Barends, Christina S. Müller, et al.. (2012). Crystallography on a chip. Acta Crystallographica Section D Biological Crystallography. 68(3). 321–323. 68 indexed citations

Lai, Jinfeng, Dimitri Niks, Tatiana Domratcheva, et al.. (2010). X-ray and NMR Crystallography in an Enzyme Active Site: The Indoline Quinonoid Intermediate in Tryptophan Synthase. Journal of the American Chemical Society. 133(1). 4–7. 71 indexed citations

Jaenicke, Elmar, et al.. (2009). Cupredoxin-like domains in haemocyanins. Biochemical Journal. 426(3). 373–378. 25 indexed citations

Dunn, Michael F., Dimitri Niks, Huu Ngo, T.R.M. Barends, & Ilme Schlichting. (2008). Tryptophan synthase: the workings of a channeling nanomachine. Trends in Biochemical Sciences. 33(6). 254–264. 137 indexed citations

Maul, M.J., T.R.M. Barends, Andreas F. Glas, et al.. (2008). Crystal Structure and Mechanism of a DNA (6‐4) Photolyase. Angewandte Chemie International Edition. 47(52). 10076–10080. 159 indexed citations

Brouns, Stan J. J., T.R.M. Barends, Petra Worm, et al.. (2008). Structural Insight into Substrate Binding and Catalysis of a Novel 2-Keto-3-deoxy-d-arabinonate Dehydratase Illustrates Common Mechanistic Features of the FAH Superfamily. Journal of Molecular Biology. 379(2). 357–371. 36 indexed citations

Straaten, K.E. Van, T.R.M. Barends, Bauke W. Dijkstra, & A.M.W.H. Thunnissen. (2007). Structure of Escherichia coli Lytic Transglycosylase MltA with Bound Chitohexaose. Journal of Biological Chemistry. 282(29). 21197–21205. 32 indexed citations

10.

Barends, T.R.M., Jelle B. Bultema, Thijs Kaper, et al.. (2007). Three-way Stabilization of the Covalent Intermediate in Amylomaltase, an α-Amylase-like Transglycosylase. Journal of Biological Chemistry. 282(23). 17242–17249. 64 indexed citations

11.

Casino, Patricia, Dimitri Niks, Huu Ngo, et al.. (2007). Allosteric Regulation of Tryptophan Synthase Channeling: The Internal Aldimine Probed bytrans-3-Indole-3‘-acrylate Binding. Biochemistry. 46(26). 7728–7739. 10 indexed citations

12.

Ngo, Huu, R. Harris, Patricia Casino, et al.. (2007). Synthesis and Characterization of Allosteric Probes of Substrate Channeling in the Tryptophan Synthase Bienzyme Complex^,. Biochemistry. 46(26). 7713–7727. 52 indexed citations

13.

Barends, T.R.M., René M. de Jong, K.E. Van Straaten, A.M.W.H. Thunnissen, & Bauke W. Dijkstra. (2005). Escherichia coliMltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure. Acta Crystallographica Section D Biological Crystallography. 61(5). 613–621. 9 indexed citations

14.

Barends, T.R.M., et al.. (2005). Acetobacter turbidans α-Amino Acid Ester Hydrolase. Journal of Biological Chemistry. 281(9). 5804–5810. 24 indexed citations

15.

Barends, T.R.M., Hiromi Yoshida, & Bauke W. Dijkstra. (2004). Three-dimensional structures of enzymes useful for β-lactam antibiotic production. Current Opinion in Biotechnology. 15(4). 356–363. 17 indexed citations

16.

Barends, T.R.M. & Bauke W. Dijkstra. (2003). Acetobacter turbidansα-amino acid ester hydrolase: merohedral twinning inP2₁obscured by pseudo-translational NCS. Acta Crystallographica Section D Biological Crystallography. 59(12). 2237–2241. 13 indexed citations

17.

Barends, T.R.M. & Bauke W. Dijkstra. (2003). Oils used in microbatch crystallization do not remove a detergent from the drops they cover. Acta Crystallographica Section D Biological Crystallography. 59(12). 2345–2347. 4 indexed citations

18.

Barends, T.R.M., Peter A. Jekel, Charles M. H. Hensgens, et al.. (2003). The Sequence and Crystal Structure of the α-Amino Acid Ester Hydrolase from Xanthomonas citri Define a New Family of β-Lactam Antibiotic Acylases. Journal of Biological Chemistry. 278(25). 23076–23084. 35 indexed citations

19.

Barends, T.R.M., et al.. (2002). X-ray analysis of two antibiotic-synthesizing bacterial ester hydrolases: preliminary results. Acta Crystallographica Section D Biological Crystallography. 59(1). 158–160. 4 indexed citations

20.

Bokma, Evert, T.R.M. Barends, Anke C. Terwisscha van Scheltinga, Bauke W. Dijkstra, & Jaap J. Beintema. (2000). Enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis. FEBS Letters. 478(1-2). 119–122. 34 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.

Explore authors with similar magnitude of impact