Inger Andersson

9.4k total citations
97 papers, 4.3k citations indexed

About

Inger Andersson is a scholar working on Molecular Biology, Materials Chemistry and Inorganic Chemistry. According to data from OpenAlex, Inger Andersson has authored 97 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 56 papers in Molecular Biology, 25 papers in Materials Chemistry and 18 papers in Inorganic Chemistry. Recurrent topics in Inger Andersson's work include Photosynthetic Processes and Mechanisms (29 papers), Enzyme Structure and Function (23 papers) and Metal-Catalyzed Oxygenation Mechanisms (18 papers). Inger Andersson is often cited by papers focused on Photosynthetic Processes and Mechanisms (29 papers), Enzyme Structure and Function (23 papers) and Metal-Catalyzed Oxygenation Mechanisms (18 papers). Inger Andersson collaborates with scholars based in Sweden, United Kingdom and United States. Inger Andersson's co-authors include Anders Backlund, Thomas C. Taylor, Stefan D. Knight, Carl‐Ivar Brändén, János Hajdu, K. Valegård, Christopher J. Schofield, Jack E. Baldwin, Anke C. Terwisscha van Scheltinga and Karl Harlos and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Inger Andersson

93 papers receiving 4.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Inger Andersson Sweden	31	2.9k	756	625	622	587	97	4.3k
Kazuo Kobayashi Japan	41	3.0k 1.0×	502 0.7×	450 0.7×	560 0.9×	413 0.7×	186	5.5k
M.A. Carrondo Portugal	37	3.0k 1.0×	960 1.3×	795 1.3×	633 1.0×	926 1.6×	165	5.7k
Keiichi Fukuyama Japan	39	3.0k 1.0×	796 1.1×	741 1.2×	1.1k 1.7×	766 1.3×	200	4.9k
Christian Obinger Austria	50	3.8k 1.3×	1.0k 1.4×	1.5k 2.5×	405 0.7×	778 1.3×	236	9.0k
Lewis M. Siegel United States	34	3.6k 1.2×	725 1.0×	625 1.0×	1.1k 1.7×	849 1.4×	63	6.0k
Stephen K. Chapman United Kingdom	45	3.2k 1.1×	1.2k 1.6×	195 0.3×	393 0.6×	601 1.0×	151	5.7k
E. Neil G. Marsh United States	49	4.4k 1.5×	720 1.0×	187 0.3×	554 0.9×	859 1.5×	175	7.1k
Hiroshi Sugimoto Japan	39	2.0k 0.7×	997 1.3×	331 0.5×	188 0.3×	804 1.4×	156	4.8k
Lev Weiner Israel	40	2.1k 0.7×	888 1.2×	1.2k 1.9×	502 0.8×	1.3k 2.2×	136	6.3k
Pedro M. Matias Portugal	34	2.4k 0.8×	612 0.8×	170 0.3×	692 1.1×	776 1.3×	117	4.4k

Countries citing papers authored by Inger Andersson

Since Specialization

Citations

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

Fields of papers citing papers by Inger Andersson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Inger Andersson

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

Andrikopoulos, Prokopis C., Yingliang Liu, Inger Andersson, et al.. (2023). Genetically encoded non‐canonical amino acids reveal asynchronous dark reversion of chromophore, backbone, and side‐chains in EL222. Protein Science. 32(4). e4590–e4590. 8 indexed citations

Snarski, Emilian, Jacqui Stringer, Małgorzata Mikulska, et al.. (2021). Risk of infectious complications in adult patients after allogeneic hematopoietic stem cell transplantation depending on the site of central venous catheter insertion—multicenter prospective observational study, from the IDWP EBMT and Nurses Group of EBMT. Bone Marrow Transplantation. 56(12). 2929–2933. 6 indexed citations

Liu, Yingliang, et al.. (2021). Site-Specific Photoinduced Dynamics of the LOV Protein EL222 Monitored by Multiple Genetically Encoded Infrared Probes. Biophysical Journal. 120(3). 124a–124a. 1 indexed citations

Hasse, Dirk, et al.. (2019). Structure and mechanism of piperideine-6-carboxylate dehydrogenase fromStreptomyces clavuligerus. Acta Crystallographica Section D Structural Biology. 75(12). 1107–1118. 2 indexed citations

Carlsson, Gunilla, Dirk Hasse, Francesca Cardinale, Cristina Prandi, & Inger Andersson. (2018). The elusive ligand complexes of the DWARF14 strigolactone receptor. Journal of Experimental Botany. 69(9). 2345–2354. 29 indexed citations

Larsson, A.M., Dirk Hasse, K. Valegård, & Inger Andersson. (2017). Crystal structures of β-carboxysome shell protein CcmP: ligand binding correlates with the closed or open central pore. Journal of Experimental Botany. 68(14). 3857–3867. 38 indexed citations

Valegård, K., Dirk Hasse, Inger Andersson, & Laura H. Gunn. (2017). Structure of Rubisco fromArabidopsis thalianain complex with 2-carboxyarabinitol-1,5-bisphosphate. Acta Crystallographica Section D Structural Biology. 74(1). 1–9. 16 indexed citations

Gunn, Laura H., K. Valegård, & Inger Andersson. (2017). A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic. Journal of Biological Chemistry. 292(16). 6838–6850. 15 indexed citations

Ankarberg‐Lindgren, Carina, Inger Andersson, Lena Björkman, et al.. (2016). Androgens in women after allogeneic hematopoietic cell transplantation: impact of chronic GvHD and glucocorticoid therapy. Bone Marrow Transplantation. 52(3). 431–437. 5 indexed citations

10.

Kapralov, Maxim V., David S. Kubien, Inger Andersson, & Dmitry A. Filatov. (2010). Changes in Rubisco Kinetics during the Evolution of C4 Photosynthesis in Flaveria (Asteraceae) Are Associated with Positive Selection on Genes Encoding the Enzyme. Molecular Biology and Evolution. 28(4). 1491–1503. 84 indexed citations

11.

MacKenzie, A.K., K. Valegård, Aman Iqbal, et al.. (2009). Crystal Structures of an Oligopeptide-Binding Protein from the Biosynthetic Pathway of the β-Lactamase Inhibitor Clavulanic Acid. Journal of Molecular Biology. 396(2). 332–344. 11 indexed citations

12.

Öster, Linda, et al.. (2006). Insights into Cephamycin Biosynthesis: the Crystal Structure of CmcI from Streptomyces clavuligerus. Journal of Molecular Biology. 358(2). 546–558. 19 indexed citations

13.

Öster, Linda, Anke C. Terwisscha van Scheltinga, K. Valegård, et al.. (2004). Conformational Flexibility of the C Terminus with Implications for Substrate Binding and Catalysis Revealed in a New Crystal Form of Deacetoxycephalosporin C Synthase. Journal of Molecular Biology. 343(1). 157–171. 20 indexed citations

14.

Valegård, K., Anke C. Terwisscha van Scheltinga, Alain Dubus, et al.. (2003). The structural basis of cephalosporin formation in a mononuclear ferrous enzyme. Nature Structural & Molecular Biology. 11(1). 95–101. 73 indexed citations

15.

Scheltinga, Anke C. Terwisscha van, K. Valegård, János Hajdu, & Inger Andersson. (2003). MIR phasing using merohedrally twinned crystals. Acta Crystallographica Section D Biological Crystallography. 59(11). 2017–2022. 8 indexed citations

16.

Taylor, Thomas C., Anders Backlund, Karin Björhall, Robert J. Spreitzer, & Inger Andersson. (2001). First Crystal Structure of Rubisco from a Green Alga,Chlamydomonas reinhardtii. Journal of Biological Chemistry. 276(51). 48159–48164. 85 indexed citations

17.

Andersson, Inger. (1996). Large Structures at High Resolution: The 1.6 Å Crystal Structure of Spinach Ribulose-1,5- Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol Bisphosphate. Journal of Molecular Biology. 259(1). 160–174. 137 indexed citations

18.

Taylor, Thomas C., et al.. (1996). A Common Structural Basis for the Inhibition of Ribulose 1,5-Bisphosphate Carboxylase by 4-Carboxyarabinitol 1,5-Bisphosphate and Xylulose 1,5-Bisphosphate. Journal of Biological Chemistry. 271(51). 32894–32899. 27 indexed citations

19.

Westlind‐Danielsson, Anita, et al.. (1994). Remoxipride shows low propensity to block functional striatal dopamine D2 receptors in vitro. European Journal of Pharmacology Molecular Pharmacology. 288(1). 89–95. 8 indexed citations

20.

Bauer, Rogert, et al.. (1991). Coordination geometry for cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase: studies by PAC spectroscopy. European Biophysics Journal. 20(4). 215–21. 18 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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