David Eisenberg

85.7k total citations · 39 hit papers
409 papers, 62.2k citations indexed

About

David Eisenberg is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, David Eisenberg has authored 409 papers receiving a total of 62.2k indexed citations (citations by other indexed papers that have themselves been cited), including 319 papers in Molecular Biology, 128 papers in Materials Chemistry and 90 papers in Physiology. Recurrent topics in David Eisenberg's work include Protein Structure and Dynamics (141 papers), Enzyme Structure and Function (124 papers) and Alzheimer's disease research and treatments (83 papers). David Eisenberg is often cited by papers focused on Protein Structure and Dynamics (141 papers), Enzyme Structure and Function (124 papers) and Alzheimer's disease research and treatments (83 papers). David Eisenberg collaborates with scholars based in United States, United Kingdom and Germany. David Eisenberg's co-authors include James U. Bowie, Roland Lüthy, M.R. Sawaya, Thomas C. Terwilliger, Todd O. Yeates, Edward M. Marcotte, Andrew D. McLachlan, Michael J. Thompson, Matteo Pellegrini and Rebecca A. Nelson and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David Eisenberg

404 papers receiving 60.8k citations

Hit Papers

Assessment of protein models with three-dimensional p... 1971 2026 1989 2007 1992 1991 1984 2007 2005 500 1000 1.5k 2.0k 2.5k
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. Assessment of protein models with three-dimensional profiles
    1992 2.9k citations David Eisenberg et al. Nature profile →
  2. A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure
    1991 2.3k citations David Eisenberg et al. Science profile →
  3. Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    1984 2.0k citations David Eisenberg et al. profile →
  4. Atomic structures of amyloid cross-β spines reveal varied steric zippers
    2007 1.9k citations M.R. Sawaya, David Eisenberg et al. Nature profile →
  5. Structure of the cross-β spine of amyloid-like fibrils
    2005 1.9k citations M.R. Sawaya, David Eisenberg et al. Nature profile →
  6. [20] VERIFY3D: Assessment of protein models with three-dimensional profiles
    1997 1.8k citations David Eisenberg et al. profile →
  7. Solvation energy in protein folding and binding
    1986 1.6k citations David Eisenberg et al. Nature profile →
  8. Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
    2012 1.5k citations M.R. Sawaya, David Eisenberg et al. profile →
  9. The Amyloid State of Proteins in Human Diseases
    2012 1.4k citations David Eisenberg et al. profile →
  10. Detecting Protein Function and Protein-Protein Interactions from Genome Sequences
    1999 1.3k citations Edward M. Marcotte, Todd O. Yeates et al. Science profile →
  11. Assigning protein functions by comparative genome analysis: Protein phylogenetic profiles
    1999 1.2k citations Edward M. Marcotte, David Eisenberg et al. Proceedings of the National Academy of Sciences profile →
  12. The helical hydrophobic moment: a measure of the amphiphilicity of a helix
    1982 891 citations David Eisenberg et al. Nature profile →
  13. Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules
    2009 872 citations Samir K. Maji, Marilyn H. Perrin et al. Science profile →
  14. The hydrophobic moment detects periodicity in protein hydrophobicity.
    1984 752 citations David Eisenberg et al. Proceedings of the National Academy of Sciences profile →
  15. Ferricytochrome c
    1971 744 citations David Eisenberg et al. Journal of Biological Chemistry profile →
  16. A combined algorithm for genome-wide prediction of protein function
    1999 706 citations Edward M. Marcotte, Todd O. Yeates et al. Nature profile →
  17. Identifying the amylome, proteins capable of forming amyloid-like fibrils
    2010 658 citations Lukasz Goldschmidt, Poh K. Teng et al. Proceedings of the National Academy of Sciences profile →
  18. 3D domain swapping: A mechanism for oligomer assembly
    1995 639 citations David Eisenberg et al. Protein Science profile →
  19. Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    2006 607 citations Michael Strong, M.R. Sawaya et al. Proceedings of the National Academy of Sciences profile →
  20. The primary mechanism of attenuation of bacillus Calmette–Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue
    2003 579 citations David Eisenberg et al. Proceedings of the National Academy of Sciences profile →
  21. 3D domain swapping: As domains continue to swap
    2002 569 citations David Eisenberg et al. Protein Science profile →
  22. Protein function in the post-genomic era
    2000 536 citations David Eisenberg, Edward M. Marcotte et al. Nature profile →
  23. The crystal structure of diphtheria toxin
    1992 527 citations David Eisenberg et al. Nature profile →
  24. Atomic View of a Toxic Amyloid Small Oligomer
    2012 490 citations Arthur Laganowsky, Cong Liu et al. Science profile →
  25. Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
    2018 470 citations Binsen Li, P. Ge et al. Nature Communications profile →
  26. The structure of melittin. II. Interpretation of the structure.
    1982 442 citations David Eisenberg et al. Journal of Biological Chemistry profile →
  27. Propagation of Tau Aggregates and Neurodegeneration
    2017 429 citations David Eisenberg et al. profile →
  28. Half a century of amyloids: past, present and future
    2020 425 citations Roland Riek, Ehud Gazit et al. profile →
  29. Structural Studies of Amyloid Proteins at the Molecular Level
    2017 424 citations David Eisenberg, M.R. Sawaya profile →
  30. Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee
    2018 396 citations David Eisenberg et al. profile →
  31. The activities of amyloids from a structural perspective
    2016 391 citations Roland Riek, David Eisenberg Nature profile →
  32. Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation
    2011 389 citations Lin Jiang, David Eisenberg et al. Nature profile →
  33. The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities
    1982 367 citations David Eisenberg et al. profile →
  34. Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks
    2018 343 citations Michael P. Hughes, M.R. Sawaya et al. Science profile →
  35. The 3D profile method for identifying fibril-forming segments of proteins
    2006 340 citations David Eisenberg et al. Proceedings of the National Academy of Sciences profile →
  36. Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee
    2020 268 citations David Eisenberg et al. profile →
  37. The expanding amyloid family: Structure, stability, function, and pathogenesis
    2021 267 citations M.R. Sawaya, Michael P. Hughes et al. profile →
  38. Reconstruction of glutamine synthetase using computer averaging
    1978 193 citations David Eisenberg et al. profile →
  39. Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee
    2022 184 citations David Eisenberg et al. profile →

Peers

David Eisenberg
Comparison fields: 5 of 205
  • Molecular Biology 46.7k
  • Physiology 12.3k
  • Materials Chemistry 10.0k
  • Biomaterials 5.0k
  • Genetics 4.0k
Replace Vladimir N. Uversky with:
Vladimir N. Uversky United States
Ruth Nussinov United States
Erik Lindahl Sweden
Peter G. Schultz United States
Jeremy C. Smith United States
Tom Darden United States
David van der Spoel Sweden
Susan Lindquist United States
Michele Vendruscolo United Kingdom
Dmitri I. Svergun Germany
Vladimir N. Uversky United States View profile →
Citations per field, relative to David Eisenberg
David Eisenberg · 1×
Citations per year, relative to David Eisenberg
David Eisenberg · 1×

Countries citing papers authored by David Eisenberg

Since Specialization
Citations

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

Fields of papers citing papers by David Eisenberg

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Eisenberg

This figure shows the co-authorship network connecting the top 25 collaborators of David Eisenberg. A scholar is included among the top collaborators of David Eisenberg 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 David Eisenberg. David Eisenberg 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
# Work Indexed citations
1
How short peptides disassemble tau fibrils in Alzheimer’s disease
2025 ·Nature ·Ke Hou, P. Ge, M.R. Sawaya, (unknown), (unknown), Yuan Yang, Yi Xiao Jiang, David R. Boyer, Xinyi Cheng, (unknown), Jeffrey Zhang, Jiahui Lu, Romany Abskharon, Shixin Yang, Zhiheng Yu, Juli Feigon, David Eisenberg
3
2
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
2022 ·Nature ·Yi Xiao Jiang, Qin Cao, M.R. Sawaya, Romany Abskharon, P. Ge, Michael DeTure, Dennis W. Dickson, (unknown), Rachel R. Ogorzalek Loo, Joseph A. Loo, David Eisenberg
94
3
Micro-electron diffraction structure of the aggregation-driving N terminus of Drosophila neuronal protein Orb2A reveals amyloid-like β-sheets
2022 ·Journal of Biological Chemistry ·(unknown), M.R. Sawaya, David R. Boyer, Duilio Cascio, (unknown), David Eisenberg
6
4
The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure
2020 ·Proceedings of the National Academy of Sciences ·David R. Boyer, Binsen Li, Chuanqi Sun, (unknown), Kang Zhou, Michael P. Hughes, M.R. Sawaya, Lin Jiang, David Eisenberg
137
5
Intrinsic electronic conductivity of individual atomically resolved amyloid crystals reveals micrometer-long hole hopping via tyrosines
2020 ·Proceedings of the National Academy of Sciences ·(unknown), H. Ray Kelly, Peter Dahl, Sophia M. Yi, Dennis Vu, David R. Boyer, Calina Glynn, M.R. Sawaya, David Eisenberg, Víctor S. Batista, Nikhil S. Malvankar
52
6
CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
2020 ·Nature Communications ·Jiahui Lu, Qin Cao, Michael P. Hughes, M.R. Sawaya, David R. Boyer, Duilio Cascio, David Eisenberg
78
7
Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
2019 ·Nature Communications ·(unknown), David R. Boyer, Chih-Te Zee, (unknown), M.R. Sawaya, Duilio Cascio, Tamir Gonen, David Eisenberg, Steven Clarke
43
8
Mechanically rigid supramolecular assemblies formed from an Fmoc-guanine conjugated peptide nucleic acid
2019 ·Nature Communications ·Vasantha Basavalingappa, Santu Bera, Bin Xue, Ido Azuri, Yiming Tang, Kai Tao, Linda J. W. Shimon, M.R. Sawaya, Sofiya Kolusheva, David Eisenberg, Leeor Kronik, Yi Cao, Guanghong Wei, Ehud Gazit
29
9
Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp
2018 ·Nature Structural & Molecular Biology ·Marcus Gallagher-Jones, Calina Glynn, David R. Boyer, Michael W. Martynowycz, (unknown), (unknown), Chih-Te Zee, Irina Novikova, Lukasz Goldschmidt, (unknown), Gustavo Helguera, James Evans, M.R. Sawaya, Duilio Cascio, David Eisenberg, Tamir Gonen, José A. Rodríguez
67
10
Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks breakdown →
2018 ·Science ·Michael P. Hughes, M.R. Sawaya, David R. Boyer, Lukasz Goldschmidt, José A. Rodríguez, Duilio Cascio, Lisa D. Chong, Tamir Gonen, David Eisenberg
343
11
Atomic View of a Toxic Amyloid Small Oligomer breakdown →
2012 ·Science ·Arthur Laganowsky, Cong Liu, M.R. Sawaya, Julian P. Whitelegge, Jiyong Park, Minglei Zhao, Anna Pensalfini, A.B. Soriaga, Meytal Landau, Poh K. Teng, Duilio Cascio, Charles Glabe, David Eisenberg
490
12
Identifying the amylome, proteins capable of forming amyloid-like fibrils breakdown →
2010 ·Proceedings of the National Academy of Sciences ·Lukasz Goldschmidt, Poh K. Teng, Roland Riek, David Eisenberg
658
13
Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules breakdown →
2009 ·Science ·Samir K. Maji, Marilyn H. Perrin, M.R. Sawaya, Sebastian Jessberger, Krishna C. Vadodaria, Robert A. Rissman, Praful S. Singru, K. Peter R. Nilsson, Rozalyn Simon, David Schubert, David Eisenberg, Jean Rivier, Paul E. Sawchenko, Wylie Vale, Roland Riek
872
14
Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis breakdown →
2006 ·Proceedings of the National Academy of Sciences ·Michael Strong, M.R. Sawaya, Shuishu Wang, Martin L. Phillips, Duilio Cascio, David Eisenberg
607
15
Unique Transcriptome Signature of Mycobacterium tuberculosis in Pulmonary Tuberculosis
2006 ·Infection and Immunity ·Helmy Rachman, Michael Strong, Timo Ulrichs, Leander Grode, Johannes Schuchhardt, Hans‐Joachim Mollenkopf, George A. Kosmiadi, David Eisenberg, Stefan H. E. Kaufmann
195
16
Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I
2006 ·Proceedings of the National Academy of Sciences ·Zhefeng Guo, David Eisenberg
77
17
Use of Logic Relationships to Decipher Protein Network Organization
2004 ·Science ·Peter M. Bowers, Shawn Cokus, David Eisenberg, Todd O. Yeates
105
18
Sharing Publication-Related Data and Materials: Responsibilities of Authorship in the Life Sciences
2003 ·PLANT PHYSIOLOGY ·Thomas R. Cech, Sean R. Eddy, David Eisenberg, Karen Hersey, (unknown), George Poste, Natasha V. Raikhel, Richard H. Scheller, (unknown), (unknown), (unknown)
92
19
Motif‐based fold assignment
2001 ·Protein Science ·Łukasz Salwiński, David Eisenberg
9
20
Localizing proteins in the cell from their phylogenetic profiles
2000 ·Proceedings of the National Academy of Sciences ·Edward M. Marcotte, Ioannis Xénarios, Alexander M. van der Bliek, David Eisenberg
174

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

Breakdown of academic impact, for papers by Vladimir N. Uversky Breakdown of academic impact, for papers by Ruth Nussinov Breakdown of academic impact, for papers by Erik Lindahl Breakdown of academic impact, for papers by Peter G. Schultz Breakdown of academic impact, for papers by Jeremy C. Smith Breakdown of academic impact, for papers by Tom Darden Breakdown of academic impact, for papers by David van der Spoel Breakdown of academic impact, for papers by Susan Lindquist Breakdown of academic impact, for papers by Michele Vendruscolo Breakdown of academic impact, for papers by Dmitri I. Svergun
Rankless by CCL
2026