Hanno Sjuts

898 total citations
13 papers, 690 citations indexed

About

Hanno Sjuts is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Rheumatology. According to data from OpenAlex, Hanno Sjuts has authored 13 papers receiving a total of 690 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 4 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Rheumatology. Recurrent topics in Hanno Sjuts's work include Porphyrin Metabolism and Disorders (5 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Antibiotic Resistance in Bacteria (3 papers). Hanno Sjuts is often cited by papers focused on Porphyrin Metabolism and Disorders (5 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Antibiotic Resistance in Bacteria (3 papers). Hanno Sjuts collaborates with scholars based in Germany, United Kingdom and United States. Hanno Sjuts's co-authors include David Leys, Karl Fisher, Mark S. Dunstan, Stephen E. J. Rigby, Klaas M. Pos, Sam Hay, K.A.P. Payne, Colin Levy, Carolina Paz Quezada and Attilio V. Vargiu and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Hanno Sjuts

13 papers receiving 680 citations

Peers

Hanno Sjuts

POLLU

PHARM

Stefan Siemann Canada

Dorothe Ankel‐Fuchs Germany

Jos J. A. G. Kamps United Kingdom

Geneviève Labbé Canada

Fernanda Ely Australia

Thammaiah Viswanatha Canada

Deenah Osman United Kingdom

Charles M. H. Hensgens Netherlands

Kathleen M. Holtz United States

Bryan W. Lepore United States

Stefan Siemann Canada

Hanno Sjuts

230 ×0.8

206 ×0.8

62 ×0.5

POLLU

81 ×0.8

PHARM

100 ×1.4

Citations per year, relative to Hanno Sjuts Hanno Sjuts (= 1×) peers Stefan Siemann

Countries citing papers authored by Hanno Sjuts

Since Specialization

Citations

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

Fields of papers citing papers by Hanno Sjuts

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hanno Sjuts

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

All Works

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13 of 13 papers shown

Sjuts, Hanno, Christian Lange, Jennifer Jung, et al.. (2022). A multivalent antibody assembled from different building blocks using tag/catcher systems: a case study. Protein Engineering Design and Selection. 35. 5 indexed citations

Wilhelm, Júlia, Hanno Sjuts, Attilio V. Vargiu, et al.. (2021). Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nature Communications. 12(1). 6919–6919. 33 indexed citations

Clark, Jennifer, et al.. (2020). Direct Comparison of Label-Free Biosensor Binding Kinetics Obtained on the Biacore 8K and the Carterra LSA. SLAS DISCOVERY. 25(9). 977–984. 11 indexed citations

Amaral, Marta Gonçalves, Soraya Hölper, Christian E. Lange, et al.. (2020). Engineered Technologies and Bioanalysis of multispecific Antibody Formats. SHILAP Revista de lepidopterología. 6(1). 26–51. 5 indexed citations

Sjuts, Hanno, Herman Schreuder, Christian K. Engel, Till Bussemer, & Yatin R. Gokarn. (2019). Matching pH values for antibody stabilization and crystallization suggest rationale for accelerated development of biotherapeutic drugs. Drug Development Research. 81(3). 329–337. 1 indexed citations

Sjuts, Hanno, Attilio V. Vargiu, Steven M. Kwasny, et al.. (2016). Molecular basis for inhibition of AcrB multidrug efflux pump by novel and powerful pyranopyridine derivatives. Proceedings of the National Academy of Sciences. 113(13). 3509–3514. 161 indexed citations

Sjuts, Hanno, Mark S. Dunstan, Karl Fisher, & David Leys. (2015). Structures of the methyltransferase component ofDesulfitobacterium hafnienseDCB-2O-demethylase shed light on methyltetrahydrofolate formation. Acta Crystallographica Section D Biological Crystallography. 71(9). 1900–1908. 5 indexed citations

Payne, K.A.P., Karl Fisher, Hanno Sjuts, et al.. (2015). Epoxyqueuosine Reductase Structure Suggests a Mechanism for Cobalamin-dependent tRNA Modification. Journal of Biological Chemistry. 290(46). 27572–27581. 33 indexed citations

Klingler, Franca‐Maria, Thomas A. Wichelhaus, Denia Frank, et al.. (2015). Approved Drugs Containing Thiols as Inhibitors of Metallo-β-lactamases: Strategy To Combat Multidrug-Resistant Bacteria. Journal of Medicinal Chemistry. 58(8). 3626–3630. 129 indexed citations

10.

Payne, K.A.P., Carolina Paz Quezada, Karl Fisher, et al.. (2014). Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation. Nature. 517(7535). 513–516. 238 indexed citations

11.

Sjuts, Hanno, Mark S. Dunstan, Karl Fisher, & David Leys. (2013). Structure of the cobalamin-binding protein of a putativeO-demethylase fromDesulfitobacterium hafnienseDCB-2. Acta Crystallographica Section D Biological Crystallography. 69(8). 1609–1616. 7 indexed citations

12.

Sjuts, Hanno, Karl Fisher, Mark S. Dunstan, Stephen E. J. Rigby, & David Leys. (2012). Heterologous expression, purification and cofactor reconstitution of the reductive dehalogenase PceA from Dehalobacter restrictus. Protein Expression and Purification. 85(2). 224–229. 21 indexed citations

13.

Meyer, Danilo, P. Neumann, Eline J. Koers, et al.. (2012). Unexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of thiamin. Proceedings of the National Academy of Sciences. 109(27). 10867–10872. 41 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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