Margaret M. Condron

9.0k total citations · 6 hit papers
42 papers, 7.6k citations indexed

About

Margaret M. Condron is a scholar working on Physiology, Molecular Biology and Computational Theory and Mathematics. According to data from OpenAlex, Margaret M. Condron has authored 42 papers receiving a total of 7.6k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Physiology, 28 papers in Molecular Biology and 10 papers in Computational Theory and Mathematics. Recurrent topics in Margaret M. Condron's work include Alzheimer's disease research and treatments (34 papers), Protein Structure and Dynamics (15 papers) and Computational Drug Discovery Methods (10 papers). Margaret M. Condron is often cited by papers focused on Alzheimer's disease research and treatments (34 papers), Protein Structure and Dynamics (15 papers) and Computational Drug Discovery Methods (10 papers). Margaret M. Condron collaborates with scholars based in United States, Japan and Germany. Margaret M. Condron's co-authors include David B. Teplow, Dominic M. Walsh, Aleksey Lomakin, George B. Benedek, Kenjiro Ono, Marina Kirkitadze, Dennis J. Selkoe, Dean M. Hartley, Gal Bitan and Youcef Fezoui 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

Margaret M. Condron

42 papers receiving 7.4k citations

Hit Papers

Amyloid β-Protein Fibrill... 1997 2026 2006 2016 1997 2001 1999 2009 2009 250 500 750
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. Amyloid β-Protein Fibrillogenesis
    1997 963 citations Dominic M. Walsh, Aleksey Lomakin et al. Journal of Biological Chemistry profile →
  2. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
    2001 943 citations Camilla Nilsberth, Anita Westlind‐Danielsson et al. Nature Neuroscience profile →
  3. Amyloid β-Protein Fibrillogenesis
    1999 912 citations Dominic M. Walsh, Dean M. Hartley et al. Journal of Biological Chemistry profile →
  4. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    2009 803 citations Summer L. Bernstein, Nicholas Dupuis et al. Nature Chemistry profile →
  5. Structure–neurotoxicity relationships of amyloid β-protein oligomers
    2009 666 citations Kenjiro Ono, Margaret M. Condron et al. Proceedings of the National Academy of Sciences profile →
  6. Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen
    2001 589 citations Margaret M. Condron et al. Journal of Molecular Biology profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Margaret M. Condron United States 29 5.9k 4.4k 1.5k 1.4k 1.1k 42 7.6k
Gal Bitan United States 49 6.3k 1.1× 5.6k 1.3× 1.7k 1.1× 1.3k 0.9× 1.2k 1.0× 129 9.6k
Saskia Milton United States 21 5.5k 0.9× 4.3k 1.0× 919 0.6× 968 0.7× 910 0.8× 34 7.5k
Lars O. Tjernberg Sweden 34 4.3k 0.7× 3.5k 0.8× 759 0.5× 1.0k 0.7× 774 0.7× 107 6.3k
Jan Näslund Sweden 30 5.4k 0.9× 3.4k 0.8× 1.0k 0.7× 1.4k 1.0× 651 0.6× 51 7.0k
Brett A. Chromy United States 28 4.1k 0.7× 3.2k 0.7× 759 0.5× 1.0k 0.7× 473 0.4× 46 6.4k
Michael G. Zagorski United States 36 3.4k 0.6× 3.4k 0.8× 811 0.5× 806 0.6× 669 0.6× 67 6.0k
Harry LeVine United States 36 3.3k 0.6× 2.6k 0.6× 689 0.5× 776 0.6× 560 0.5× 72 5.3k
Christer Nordstedt Sweden 26 3.3k 0.6× 2.7k 0.6× 700 0.5× 821 0.6× 620 0.6× 51 4.7k
Jeffrey Brender United States 47 3.8k 0.6× 4.1k 0.9× 667 0.4× 460 0.3× 1.0k 0.9× 93 6.7k
W. Blaine Stine United States 17 4.0k 0.7× 2.2k 0.5× 747 0.5× 871 0.6× 451 0.4× 24 4.8k

Countries citing papers authored by Margaret M. Condron

Since Specialization
Citations

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

Fields of papers citing papers by Margaret M. Condron

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Margaret M. Condron. 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 Margaret M. Condron. The network helps show where Margaret M. Condron may publish in the future.

Co-authorship network of co-authors of Margaret M. Condron

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

All Works

20 of 20 papers shown
1.
Roychaudhuri, Robin, Xueyun Zheng, Aleksey Lomakin, et al.. (2015). Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity. ACS Chemical Neuroscience. 6(12). 1941–1955. 25 indexed citations
2.
Roychaudhuri, Robin, Aleksey Lomakin, Summer L. Bernstein, et al.. (2014). Gly25-Ser26 Amyloid β-Protein Structural Isomorphs Produce Distinct Aβ42 Conformational Dynamics and Assembly Characteristics. Journal of Molecular Biology. 426(13). 2422–2441. 28 indexed citations
3.
Lv, Zhengjian, Margaret M. Condron, David B. Teplow, & Yuri L. Lyubchenko. (2013). Nanoprobing of the Effect of Cu2+ Cations on Misfolding, Interaction and Aggregation of Amyloid Beta Peptide. Biophysical Journal. 104(2). 513a–514a. 2 indexed citations
4.
Lv, Zhengjian, Robin Roychaudhuri, Margaret M. Condron, David B. Teplow, & Yuri L. Lyubchenko. (2013). Mechanism of amyloid β−protein dimerization determined using single−molecule AFM force spectroscopy. Scientific Reports. 3(1). 2880–2880. 67 indexed citations
5.
Lv, Zhengjian, Yuliang Zhang, Robin Roychaudhuri, et al.. (2013). Misfolding and interactions of Aß proteins: Insight from single molecule experiments and computational analyses. Molecular Neurodegeneration. 8(S1). 1 indexed citations
6.
Ono, Kenjiro, Margaret M. Condron, & David B. Teplow. (2010). Effects of the English (H6R) and Tottori (D7N) Familial Alzheimer Disease Mutations on Amyloid β-Protein Assembly and Toxicity. Journal of Biological Chemistry. 285(30). 23186–23197. 134 indexed citations
7.
Bernstein, Summer L., Andrij Baumketner, Margaret M. Condron, et al.. (2009). Amyloid β-Protein: Experiment and Theory on the 21−30 Fragment. The Journal of Physical Chemistry B. 113(17). 6041–6046. 43 indexed citations
8.
Bernstein, Summer L., Nicholas Dupuis, Noel D. Lazo, et al.. (2009). Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chemistry. 1(4). 326–331. 803 indexed citations breakdown →
9.
Ono, Kenjiro, Margaret M. Condron, & David B. Teplow. (2009). Structure–neurotoxicity relationships of amyloid β-protein oligomers. Proceedings of the National Academy of Sciences. 106(35). 14745–14750. 666 indexed citations breakdown →
10.
Maji, Samir K., Rachel R. Ogorzalek Loo, Mohammed Inayathullah, et al.. (2009). Amino Acid Position-specific Contributions to Amyloid β-Protein Oligomerization. Journal of Biological Chemistry. 284(35). 23580–23591. 70 indexed citations
11.
Ren, Yuhao, Gary A. Strobel, Mark A. Jutila, et al.. (2008). Colutellin A, an immunosuppressive peptide from Colletotrichum dematium. Microbiology. 154(7). 1973–1979. 34 indexed citations
12.
Hori, Yukiko, Tadafumi Hashimoto, Yosuke Wakutani, et al.. (2006). The Tottori (D7N) and English (H6R) Familial Alzheimer Disease Mutations Accelerate Aβ Fibril Formation without Increasing Protofibril Formation. Journal of Biological Chemistry. 282(7). 4916–4923. 99 indexed citations
13.
Fluhrer, Regina, Lars Israel, Margaret M. Condron, et al.. (2006). A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b. Nature Cell Biology. 8(8). 894–896. 115 indexed citations
14.
Maji, Samir K., Gal Bitan, Sabrina S. Vollers, et al.. (2004). P1-236 Site-specific analysis of Abeta oligomerization using photochemical cross-linking. Neurobiology of Aging. 25. S163–S163. 1 indexed citations
15.
Leissring, Malcolm A., Alice Lu, Margaret M. Condron, et al.. (2003). Kinetics of Amyloid β-Protein Degradation Determined by Novel Fluorescence- and Fluorescence Polarization-based Assays. Journal of Biological Chemistry. 278(39). 37314–37320. 98 indexed citations
16.
Fluhrer, Regina, Anja Capell, Gil G. Westmeyer, et al.. (2002). A non‐amyloidogenic function of BACE‐2 in the secretory pathway. Journal of Neurochemistry. 81(5). 1011–1020. 87 indexed citations
17.
Nilsberth, Camilla, Anita Westlind‐Danielsson, Christopher B. Eckman, et al.. (2001). The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nature Neuroscience. 4(9). 887–893. 943 indexed citations breakdown →
18.
Fezoui, Youcef, Dean M. Hartley, James D. Harper, et al.. (2000). An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments. Amyloid. 7(3). 166–178. 233 indexed citations
19.
Strobel, Gary A., et al.. (1999). Cryptocandin, a potent antimycotic from the endophytic fungus Cryptosporiopsis cf. quercina. Microbiology. 145(8). 1919–1926. 155 indexed citations
20.
Walsh, Dominic M., Aleksey Lomakin, George B. Benedek, Margaret M. Condron, & David B. Teplow. (1997). Amyloid β-Protein Fibrillogenesis. Journal of Biological Chemistry. 272(35). 22364–22372. 963 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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