Ingrid Mehlhorn

4.8k total citations · 3 hit papers
13 papers, 4.0k citations indexed

About

Ingrid Mehlhorn is a scholar working on Molecular Biology, Neurology and Nutrition and Dietetics. According to data from OpenAlex, Ingrid Mehlhorn has authored 13 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 8 papers in Neurology and 7 papers in Nutrition and Dietetics. Recurrent topics in Ingrid Mehlhorn's work include Prion Diseases and Protein Misfolding (13 papers), Neurological diseases and metabolism (8 papers) and Trace Elements in Health (7 papers). Ingrid Mehlhorn is often cited by papers focused on Prion Diseases and Protein Misfolding (13 papers), Neurological diseases and metabolism (8 papers) and Trace Elements in Health (7 papers). Ingrid Mehlhorn collaborates with scholars based in United States, Germany and Russia. Ingrid Mehlhorn's co-authors include Fred E. Cohen, Darlene Groth, Stanley B. Prusiner, Ziwei Huang, K M Pan, Ana Serban, Marı́a Gasset, R.J. Fletterick, M. A. Baldwin and Jack Nguyen and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Molecular Biology.

In The Last Decade

Ingrid Mehlhorn

13 papers receiving 3.9k citations

Hit Papers

Conversion of alpha-helices into beta-sheets features in ... 1993 2026 2004 2015 1993 1997 1997 500 1000 1.5k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
    1993 1.8k citations K M Pan, M. A. Baldwin et al. Proceedings of the National Academy of Sciences profile →
  2. Structure of the recombinant full-length hamster prion protein PrP(29–231): The N terminus is highly flexible
    1997 568 citations David G. Donne, John H. Viles et al. Proceedings of the National Academy of Sciences profile →
  3. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    1997 382 citations Thomas Leroy James, He Liu et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ingrid Mehlhorn United States 13 3.8k 1.9k 1.8k 481 297 13 4.0k
Ana Serban United States 15 3.3k 0.9× 1.6k 0.9× 1.5k 0.8× 462 1.0× 206 0.7× 17 3.5k
Stanley B. Prusiner United States 21 3.1k 0.8× 1.7k 0.9× 1.4k 0.8× 392 0.8× 245 0.8× 27 3.3k
Ralph Zahn Switzerland 27 3.3k 0.9× 903 0.5× 1.0k 0.6× 273 0.6× 989 3.3× 39 3.4k
Hana Serban United States 13 2.4k 0.6× 1.3k 0.7× 1.0k 0.6× 235 0.5× 77 0.3× 13 2.5k
K M Pan China 5 2.1k 0.5× 1.0k 0.5× 921 0.5× 291 0.6× 138 0.5× 10 2.2k
Natallia Makarava United States 32 2.3k 0.6× 1.2k 0.6× 729 0.4× 658 1.4× 154 0.5× 68 2.5k
Christine von Schroetter Switzerland 15 1.8k 0.5× 672 0.4× 709 0.4× 173 0.4× 229 0.8× 17 2.0k
Vitaly V. Kushnirov Russia 28 4.8k 1.3× 1.7k 0.9× 1.2k 0.7× 618 1.3× 341 1.1× 59 5.0k
Olga V. Bocharova Russia 25 1.9k 0.5× 631 0.3× 586 0.3× 648 1.3× 105 0.4× 59 2.2k
David W. Colby United States 21 2.2k 0.6× 636 0.3× 392 0.2× 672 1.4× 73 0.2× 23 2.6k

Countries citing papers authored by Ingrid Mehlhorn

Since Specialization
Citations

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

Fields of papers citing papers by Ingrid Mehlhorn

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ingrid Mehlhorn

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

All Works

13 of 13 papers shown
1.
Matsunaga, Yoichi, David Peretz, Dennis R. Burton, et al.. (2001). Cryptic epitopes in N‐terminally truncated prion protein are exposed in the full‐length molecule: Dependence of conformation on pH. Proteins Structure Function and Bioinformatics. 44(2). 110–118. 47 indexed citations
2.
Peretz, David, R. Anthony Williamson, Julie Vergara, et al.. (2001). Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature. 412(6848). 739–743. 420 indexed citations
3.
Supattapone, Surachai, Tamaki Muramoto, Giuseppe Legname, et al.. (2001). Identification of Two Prion Protein Regions That Modify Scrapie Incubation Time. Journal of Virology. 75(3). 1408–1413. 86 indexed citations
4.
Baskakov, Ilia V., Claus Aagaard, Ingrid Mehlhorn, et al.. (2000). Self-Assembly of Recombinant Prion Protein of 106 Residues. Biochemistry. 39(10). 2792–2804. 60 indexed citations
5.
Post, Karin, Martin Pitschke, Oliver Schäfer, et al.. (1998). Rapid Acquisition of β-Sheet Structure in the Prion Protein Prior to Multimer Formation. Biological Chemistry. 379(11). 1307–1318. 83 indexed citations
6.
Kaneko, Kiyotoshi, Holger Wille, Ingrid Mehlhorn, et al.. (1997). Molecular properties of complexes formed between the prion protein and synthetic peptides. Journal of Molecular Biology. 270(4). 574–586. 40 indexed citations
7.
James, Thomas Leroy, He Liu, Nikolai B. Ulyanov, et al.. (1997). Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proceedings of the National Academy of Sciences. 94(19). 10086–10091. 382 indexed citations breakdown →
8.
Donne, David G., John H. Viles, Ingrid Mehlhorn, et al.. (1997). Structure of the recombinant full-length hamster prion protein PrP(29–231): The N terminus is highly flexible. Proceedings of the National Academy of Sciences. 94(25). 13452–13457. 568 indexed citations breakdown →
9.
Zhang, Hong, Ingrid Mehlhorn, Darlene Groth, et al.. (1997). Physical Studies of Conformational Plasticity in a Recombinant Prion Protein. Biochemistry. 36(12). 3543–3553. 132 indexed citations
10.
Mehlhorn, Ingrid, Darlene Groth, Barbara Moffat, et al.. (1996). High-Level Expression and Characterization of a Purified 142-Residue Polypeptide of the Prion Protein. Biochemistry. 35(17). 5528–5537. 163 indexed citations
11.
Williamson, R. Anthony, David Peretz, Nechama I. Smorodinsky, et al.. (1996). Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein.. Proceedings of the National Academy of Sciences. 93(14). 7279–7282. 94 indexed citations
12.
Baldwin, M. A., K M Pan, Jack Nguyen, et al.. (1994). Spectroscopic characterization of conformational differences between PrPC and PrPSc: an α-helix to β-sheet transition. Philosophical Transactions of the Royal Society B Biological Sciences. 343(1306). 435–441. 34 indexed citations
13.
Pan, K M, M. A. Baldwin, Jack Nguyen, et al.. (1993). Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.. Proceedings of the National Academy of Sciences. 90(23). 10962–10966. 1843 indexed citations breakdown →

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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