Rokus Renirie

1.6k total citations
23 papers, 1.3k citations indexed

About

Rokus Renirie is a scholar working on Inorganic Chemistry, Molecular Biology and Materials Chemistry. According to data from OpenAlex, Rokus Renirie has authored 23 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Inorganic Chemistry, 6 papers in Molecular Biology and 6 papers in Materials Chemistry. Recurrent topics in Rokus Renirie's work include Vanadium and Halogenation Chemistry (19 papers), Metal-Catalyzed Oxygenation Mechanisms (15 papers) and Porphyrin and Phthalocyanine Chemistry (5 papers). Rokus Renirie is often cited by papers focused on Vanadium and Halogenation Chemistry (19 papers), Metal-Catalyzed Oxygenation Mechanisms (15 papers) and Porphyrin and Phthalocyanine Chemistry (5 papers). Rokus Renirie collaborates with scholars based in Netherlands, Germany and United States. Rokus Renirie's co-authors include Ron Wever, Wieger Hemrika, Frank Hollmann, Elena Fernández‐Fueyo, Sandra Macedo‐Ribeiro, Phil Barnett, Lukas Dekker, Yan Ni, Miguel Alcalde and Morten M. C. H. van Schie and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Rokus Renirie

23 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Rokus Renirie Netherlands	19	695	481	331	272	151	23	1.3k
Yoshihiko Kondo Japan	23	409 0.6×	258 0.5×	564 1.7×	437 1.6×	179 1.2×	76	1.7k
Katlyn K. Meier United States	22	1.1k 1.6×	476 1.0×	326 1.0×	598 2.2×	252 1.7×	32	1.6k
Joseph P. Emerson United States	18	863 1.2×	642 1.3×	241 0.7×	246 0.9×	189 1.3×	50	1.4k
Isabelle Artaud France	25	344 0.5×	544 1.1×	470 1.4×	274 1.0×	131 0.9×	75	1.6k
Matthew H. Sazinsky United States	21	1.1k 1.6×	911 1.9×	203 0.6×	478 1.8×	248 1.6×	40	1.8k
Xiaowei Yan China	21	244 0.4×	582 1.2×	188 0.6×	394 1.4×	53 0.4×	76	1.5k
Robert C. Scarrow United States	21	634 0.9×	429 0.9×	282 0.9×	341 1.3×	261 1.7×	31	1.4k
Jean-Louis Séris France	13	245 0.4×	177 0.4×	163 0.5×	345 1.3×	108 0.7×	20	884
Geng Dong China	17	240 0.3×	328 0.7×	86 0.3×	179 0.7×	250 1.7×	51	924
Miao Chen China	21	181 0.3×	557 1.2×	303 0.9×	342 1.3×	106 0.7×	43	1.5k

Countries citing papers authored by Rokus Renirie

Since Specialization

Citations

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

Fields of papers citing papers by Rokus Renirie

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rokus Renirie

This figure shows the co-authorship network connecting the top 25 collaborators of Rokus Renirie. A scholar is included among the top collaborators of Rokus Renirie 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 Rokus Renirie. Rokus Renirie 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

Wever, Ron, Bea E. Krenn, & Rokus Renirie. (2018). Marine Vanadium-Dependent Haloperoxidases, Their Isolation, Characterization, and Application. Methods in enzymology on CD-ROM/Methods in enzymology. 605. 141–201. 49 indexed citations

Dong, Jiajia, Elena Fernández‐Fueyo, Jingbo Li, et al.. (2017). Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis. Chemical Communications. 53(46). 6207–6210. 53 indexed citations

Zhang, Wuyuan, Elena Fernández‐Fueyo, Yan Ni, et al.. (2017). Selective aerobic oxidation reactions using a combination of photocatalytic water oxidation and enzymatic oxyfunctionalizations. Nature Catalysis. 1(1). 55–62. 300 indexed citations

Gupta, Rupal, Guangjin Hou, Rokus Renirie, Ron Wever, & Tatyana Polenova. (2015). ⁵¹V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site. Journal of the American Chemical Society. 137(16). 5618–5628. 27 indexed citations

Fernández‐Fueyo, Elena, Rokus Renirie, Ron Wever, et al.. (2015). Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis. ChemCatChem. 7(24). 4035–4038. 53 indexed citations

Cankar, Katarina, Adèle van Houwelingen, Miriam Goedbloed, et al.. (2014). Valencene oxidase CYP706M1 from Alaska cedar (Callitropsis nootkatensis). FEBS Letters. 588(6). 1001–1007. 47 indexed citations

Renirie, Rokus, John Charnock, C. David Garner, & Ron Wever. (2010). Vanadium K-edge XAS studies on the native and peroxo-forms of vanadium chloroperoxidase from Curvularia inaequalis. Journal of Inorganic Biochemistry. 104(6). 657–664. 20 indexed citations

Hoogenkamp, Michel A., W. Crielaard, J.M. ten Cate, et al.. (2009). Antimicrobial Activity of Vanadium Chloroperoxidase on Planktonic <i>Streptococcus mutans</i> Cells and <i>Streptococcus mutans</i> Biofilms. Caries Research. 43(5). 334–338. 15 indexed citations

Renirie, Rokus, et al.. (2008). Bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase. Journal of Applied Microbiology. 105(1). 264–270. 20 indexed citations

10.

Macedo‐Ribeiro, Sandra, Rokus Renirie, Ron Wever, & Albrecht Messerschmidt. (2007). Crystal Structure of a Trapped Phosphate Intermediate in Vanadium Apochloroperoxidase Catalyzing a Dephosphorylation Reaction. Biochemistry. 47(3). 929–934. 16 indexed citations

11.

Renirie, Rokus, et al.. (2006). Laboratory-evolved Vanadium Chloroperoxidase Exhibits 100-Fold Higher Halogenating Activity at Alkaline pH. Journal of Biological Chemistry. 281(14). 9738–9744. 66 indexed citations

12.

Renirie, Rokus, et al.. (2006). ⁵¹V Solid-State Magic Angle Spinning NMR Spectroscopy of Vanadium Chloroperoxidase. Journal of the American Chemical Society. 128(15). 5190–5208. 57 indexed citations

13.

Renirie, Rokus, Christel Pierlot, Jean‐Marie Aubry, et al.. (2003). Vanadium Chloroperoxidase as a Catalyst for Hydrogen Peroxide Disproportionation to Singlet Oxygen in Mildly Acidic Aqueous Environment. Advanced Synthesis & Catalysis. 345(6-7). 849–858. 48 indexed citations

14.

Renirie, Rokus, Wieger Hemrika, & Ron Wever. (2000). Peroxidase and Phosphatase Activity of Active-site Mutants of Vanadium Chloroperoxidase from the Fungus Curvularia inaequalis. Journal of Biological Chemistry. 275(16). 11650–11657. 59 indexed citations

15.

Renirie, Rokus, Wieger Hemrika, Sander R. Piersma, & Ron Wever. (2000). Cofactor and Substrate Binding to Vanadium Chloroperoxidase Determined by UV−VIS Spectroscopy and Evidence for High Affinity for Pervanadate. Biochemistry. 39(5). 1133–1141. 41 indexed citations

16.

Hemrika, Wieger, Rokus Renirie, Sandra Macedo‐Ribeiro, Albrecht Messerschmidt, & Ron Wever. (1999). Heterologous Expression of the Vanadium-containing Chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490. Journal of Biological Chemistry. 274(34). 23820–23827. 89 indexed citations

17.

Macedo‐Ribeiro, Sandra, et al.. (1999). X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis. JBIC Journal of Biological Inorganic Chemistry. 4(2). 209–219. 103 indexed citations

18.

Barnett, Phil, Wieger Hemrika, Lukas Dekker, et al.. (1998). Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora. Journal of Biological Chemistry. 273(36). 23381–23387. 41 indexed citations

19.

Hemrika, Wieger, Rokus Renirie, Lukas Dekker, Phil Barnett, & Ron Wever. (1997). From phosphatases to vanadium peroxidases: A similar architecture of the active site. Proceedings of the National Academy of Sciences. 94(6). 2145–2149. 140 indexed citations

20.

Floris, René, Nicole Moguilevsky, Gerwin J. Puppels, et al.. (1995). Heme-Protein Interaction in Myeloperoxidase: Modification of Spectroscopic Properties and Catalytic Activity by Single Residue Mutation. Journal of the American Chemical Society. 117(14). 3907–3912. 21 indexed citations

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