Heidi Erlandsen

2.6k total citations
39 papers, 2.0k citations indexed

About

Heidi Erlandsen is a scholar working on Molecular Biology, Clinical Biochemistry and Materials Chemistry. According to data from OpenAlex, Heidi Erlandsen has authored 39 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 15 papers in Clinical Biochemistry and 8 papers in Materials Chemistry. Recurrent topics in Heidi Erlandsen's work include Metabolism and Genetic Disorders (15 papers), Biochemical and Molecular Research (8 papers) and RNA and protein synthesis mechanisms (7 papers). Heidi Erlandsen is often cited by papers focused on Metabolism and Genetic Disorders (15 papers), Biochemical and Molecular Research (8 papers) and RNA and protein synthesis mechanisms (7 papers). Heidi Erlandsen collaborates with scholars based in United States, Norway and Sweden. Heidi Erlandsen's co-authors include Raymond C. Stevens, Torgeir Flatmark, Nenad Blau, Fabrizia Fusetti, Aurora Martı́nez, Edward Hough, Alejandra Gámez, Per M. Knappskog, Jan Haavik and Lin Wang and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Heidi Erlandsen

38 papers receiving 2.0k citations

Peers

Heidi Erlandsen

PHYSI

RHEUM

Michael J. McLeish United States

Martino L. di Salvo Italy

Judith L. Fridovich‐Keil United States

Toshio Yoshida Japan

Faik N. Musayev United States

Guy J.‐M. Lauquin France

Roberto Contestabile Italy

Kazuto Nosaka Japan

Subramanyam Swaminathan United States

François Collard Belgium

Michael J. McLeish United States

Heidi Erlandsen

1.3k ×0.9

420 ×0.4

77 ×0.3

PHYSI

69 ×0.3

RHEUM

224 ×1.0

Citations per year, relative to Heidi Erlandsen Heidi Erlandsen (= 1×) peers Michael J. McLeish

Countries citing papers authored by Heidi Erlandsen

Since Specialization

Citations

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

Fields of papers citing papers by Heidi Erlandsen

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Heidi Erlandsen

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

Krucinska, J., Heidi Erlandsen, Andrea M. Makkay, et al.. (2025). Two distinct protein-protein interfaces drive cooperative binding of the herpes simplex virus protein ICP8 to ssDNA, filament formation and annealing essential for viral replication. Journal of Biological Chemistry. 301(9). 110498–110498.

Correia, John J., Walter F. Stafford, Heidi Erlandsen, et al.. (2024). Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin. Biophysical Journal. 123(16). 2506–2521. 1 indexed citations

Krucinska, J., et al.. (2022). Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens. Communications Biology. 5(1). 459–459. 18 indexed citations

Rizzo, Alessandro A., et al.. (2022). Evolution of Rev7 interactions in eukaryotic TLS DNA polymerase Polζ. Journal of Biological Chemistry. 299(2). 102859–102859. 2 indexed citations

Hajian, Behnoush, Carolyn Shoen, J. Krucinska, et al.. (2019). Drugging the Folate Pathway in Mycobacterium tuberculosis: The Role of Multi-targeting Agents. Cell chemical biology. 26(6). 781–791.e6. 50 indexed citations

Krucinska, J., Michael N. Lombardo, Heidi Erlandsen, et al.. (2019). Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate. Scientific Reports. 9(1). 17106–17106. 9 indexed citations

Lipper, Colin H., Heidi Erlandsen, James L. Cole, et al.. (2019). Design of High-Affinity Metal-Controlled Protein Dimers. Biochemistry. 58(17). 2199–2207. 9 indexed citations

Rutsch, Frank, Mary MacDougall, Changming Lu, et al.. (2015). A Specific IFIH1 Gain-of-Function Mutation Causes Singleton-Merten Syndrome. The American Journal of Human Genetics. 96(2). 275–282. 156 indexed citations

Zhang, Hua, Fan Zhu, Lei Ding, et al.. (2014). The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold. Nature Communications. 5(1). 4339–4339. 61 indexed citations

10.

Zhu, Fan, Heidi Erlandsen, Lei Ding, et al.. (2011). Structural and Functional Analysis of a New Subfamily of Glycosyltransferases Required for Glycosylation of Serine-rich Streptococcal Adhesins. Journal of Biological Chemistry. 286(30). 27048–27057. 25 indexed citations

11.

Lu, Jun, et al.. (2008). The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins. Proteins Structure Function and Bioinformatics. 74(1). 18–31. 21 indexed citations

12.

Erlandsen, Heidi, Sankar Surendran, Raymond C. Stevens, et al.. (2004). Trends in Enzyme Therapy for Phenylketonuria. Molecular Therapy. 10(2). 220–224. 51 indexed citations

13.

Pey, Ángel L., Belén Pérez, Lourdes R. Desviat, et al.. (2004). Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations. Human Mutation. 24(5). 388–399. 103 indexed citations

14.

Matalon, Reuben, Richard Koch, Kimberlee Michals‐Matalon, et al.. (2004). Biopterin responsive phenylalanine hydroxylase deficiency. Genetics in Medicine. 6(1). 27–32. 50 indexed citations

15.

Erlandsen, Heidi, Ángel L. Pey, Alejandra Gámez, et al.. (2004). Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proceedings of the National Academy of Sciences. 101(48). 16903–16908. 138 indexed citations

16.

Grynberg, Marcin, Heidi Erlandsen, & Adam Godzik. (2003). HEPN: a common domain in bacterial drug resistance and human neurodegenerative proteins. Trends in Biochemical Sciences. 28(5). 224–226. 51 indexed citations

17.

Erlandsen, Heidi, et al.. (2002). Structural Comparison of Bacterial and Human Iron-dependent Phenylalanine Hydroxylases: Similar Fold, Different Stability and Reaction Rates. Journal of Molecular Biology. 320(3). 645–661. 64 indexed citations

18.

Fusetti, Fabrizia, Heidi Erlandsen, Torgeir Flatmark, & Raymond C. Stevens. (1998). Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria. Journal of Biological Chemistry. 273(27). 16962–16967. 129 indexed citations

19.

Erlandsen, Heidi, Torgeir Flatmark, Raymond C. Stevens, & Edward Hough. (1998). Crystallographic Analysis of the Human Phenylalanine Hydroxylase Catalytic Domain with Bound Catechol Inhibitors at 2.0 Å Resolution^,. Biochemistry. 37(45). 15638–15646. 48 indexed citations

20.

Erlandsen, Heidi, Aurora Martı́nez, Per M. Knappskog, et al.. (1997). Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase. FEBS Letters. 406(1-2). 171–174. 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.

Explore authors with similar magnitude of impact