David W. Colby

3.4k total citations
23 papers, 2.6k citations indexed

About

David W. Colby is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Nutrition and Dietetics. According to data from OpenAlex, David W. Colby has authored 23 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 6 papers in Cellular and Molecular Neuroscience and 6 papers in Nutrition and Dietetics. Recurrent topics in David W. Colby's work include Prion Diseases and Protein Misfolding (13 papers), Trace Elements in Health (6 papers) and Genetic Neurodegenerative Diseases (6 papers). David W. Colby is often cited by papers focused on Prion Diseases and Protein Misfolding (13 papers), Trace Elements in Health (6 papers) and Genetic Neurodegenerative Diseases (6 papers). David W. Colby collaborates with scholars based in United States, Germany and India. David W. Colby's co-authors include S. B. Prusiner, Stanley B. Prusiner, K. Dane Wittrup, Holger Wille, Giuseppe Legname, Christilyn Graff, Yik A. Yeung, Jeffrey S. Swers, Stephen J. DeArmond and Ilia V. Baskakov and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Biotechnology.

In The Last Decade

David W. Colby

23 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David W. Colby United States 21 2.2k 672 636 572 392 23 2.6k
Olga V. Bocharova Russia 25 1.9k 0.9× 648 1.0× 631 1.0× 178 0.3× 586 1.5× 59 2.2k
Jeff Zhiqiang Lu United States 32 838 0.4× 479 0.7× 234 0.4× 354 0.6× 60 0.2× 53 2.0k
Russell E. Martenson United States 31 2.0k 0.9× 536 0.8× 235 0.4× 436 0.8× 109 0.3× 78 3.4k
Frank Shewmaker United States 33 3.3k 1.5× 841 1.3× 666 1.0× 49 0.1× 462 1.2× 60 3.8k
Aurélien Olichon France 21 2.7k 1.2× 244 0.4× 90 0.1× 439 0.8× 57 0.1× 32 3.0k
Anat Yanai Canada 17 1.7k 0.8× 302 0.4× 413 0.6× 77 0.1× 258 0.7× 34 2.3k
Toshio Ariga United States 26 1.9k 0.9× 830 1.2× 110 0.2× 124 0.2× 76 0.2× 88 2.8k
John Goers United States 17 674 0.3× 449 0.7× 73 0.1× 243 0.4× 81 0.2× 24 1.6k
Randal Halfmann United States 20 2.8k 1.3× 457 0.7× 516 0.8× 22 0.0× 224 0.6× 38 3.1k
Valerie L. Sim Canada 20 1.6k 0.7× 507 0.8× 640 1.0× 35 0.1× 492 1.3× 51 2.0k

Countries citing papers authored by David W. Colby

Since Specialization
Citations

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

Fields of papers citing papers by David W. Colby

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David W. Colby

This figure shows the co-authorship network connecting the top 25 collaborators of David W. Colby. A scholar is included among the top collaborators of David W. Colby 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 W. Colby. David W. Colby 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.
Mirbaha, Hilda, Dailu Chen, Kiersten M. Ruff, et al.. (2018). Inert and seed-competent tau monomers suggest structural origins of aggregation. eLife. 7. 168 indexed citations
2.
Colby, David W., et al.. (2018). Designing well-defined photopolymerized synthetic matrices for three-dimensional culture and differentiation of induced pluripotent stem cells. Biomaterials Science. 6(6). 1358–1370. 32 indexed citations
3.
Wu, Bei, Alex J. McDonald, Celeste B. Rich, et al.. (2017). The N-terminus of the prion protein is a toxic effector regulated by the C-terminus. eLife. 6. 59 indexed citations
4.
Morozova, Olga A., Sharad Gupta, & David W. Colby. (2015). Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation. FEBS Letters. 589(15). 1897–1903. 15 indexed citations
5.
Barbaro, Brett A., Tamás Lukácsovich, Namita Agrawal, et al.. (2014). Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington's disease. Human Molecular Genetics. 24(4). 913–925. 63 indexed citations
6.
Colby, David W., et al.. (2014). Conformation-Dependent Epitopes Recognized by Prion Protein Antibodies Probed Using Mutational Scanning and Deep Sequencing. Journal of Molecular Biology. 427(2). 328–340. 35 indexed citations
7.
Ghaemmaghami, Sina, David W. Colby, Hoang-Oanh B. Nguyen, et al.. (2013). Convergent Replication of Mouse Synthetic Prion Strains. American Journal Of Pathology. 182(3). 866–874. 30 indexed citations
8.
Colby, David W. & Stanley B. Prusiner. (2011). De novo generation of prion strains. Nature Reviews Microbiology. 9(11). 771–777. 75 indexed citations
9.
Schiefner, A., Lorenz Chatwell, Irmgard Neumaier, et al.. (2011). A Disulfide-Free Single-Domain VL Intrabody with Blocking Activity towards Huntingtin Reveals a Novel Mode of Epitope Recognition. Journal of Molecular Biology. 414(3). 337–355. 27 indexed citations
10.
Gupta, Sharad, et al.. (2011). Protein Misfolding Detected Early in Pathogenesis of Transgenic Mouse Model of Huntington Disease Using Amyloid Seeding Assay. Journal of Biological Chemistry. 287(13). 9982–9989. 24 indexed citations
11.
Colby, David W. & S. B. Prusiner. (2011). Prions. Cold Spring Harbor Perspectives in Biology. 3(1). a006833–a006833. 373 indexed citations
12.
Wille, Holger, Wen Bian, Michele McDonald, et al.. (2010). X-Ray Fiber Diffraction Reveals Major Structural Differences Between Brain-Derived Prions and Recombinant Prion Protein Amyloid. Biophysical Journal. 98(3). 457a–457a. 3 indexed citations
13.
Colby, David W., Ilia V. Baskakov, Giuseppe Legname, et al.. (2010). Protease-Sensitive Synthetic Prions. PLoS Pathogens. 6(1). e1000736–e1000736. 127 indexed citations
14.
Wille, Holger, Wen Bian, Michele McDonald, et al.. (2009). Natural and synthetic prion structure from X-ray fiber diffraction. Proceedings of the National Academy of Sciences. 106(40). 16990–16995. 166 indexed citations
15.
Feng, Brian Y., Brandon H. Toyama, Holger Wille, et al.. (2008). Small-molecule aggregates inhibit amyloid polymerization. Nature Chemical Biology. 4(3). 197–199. 216 indexed citations
16.
Colby, David W., et al.. (2006). Stochastic kinetics of intracellular huntingtin aggregate formation. Nature Chemical Biology. 2(6). 319–323. 57 indexed citations
17.
Colby, David W., Ginger Chao, Jack M. Webster, et al.. (2004). Development of a Human Light Chain Variable Domain (VL) Intracellular Antibody Specific for the Amino Terminus of Huntingtin via Yeast Surface Display. Journal of Molecular Biology. 342(3). 901–912. 84 indexed citations
18.
Colby, David W., Brenda Kellogg, Christilyn Graff, et al.. (2004). Engineering Antibody Affinity by Yeast Surface Display. Methods in enzymology on CD-ROM/Methods in enzymology. 388. 348–358. 105 indexed citations
19.
Colby, David W., John P. Cassady, Martin L. Duennwald, et al.. (2004). Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody. Proceedings of the National Academy of Sciences. 101(51). 17616–17621. 149 indexed citations
20.
Feldhaus, Michael J., Robert W. Siegel, Lee K. Opresko, et al.. (2003). Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nature Biotechnology. 21(2). 163–170. 396 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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