Erik L. Snapp

7.9k total citations · 1 hit paper
73 papers, 5.8k citations indexed

About

Erik L. Snapp is a scholar working on Molecular Biology, Cell Biology and Biophysics. According to data from OpenAlex, Erik L. Snapp has authored 73 papers receiving a total of 5.8k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 46 papers in Cell Biology and 20 papers in Biophysics. Recurrent topics in Erik L. Snapp's work include Endoplasmic Reticulum Stress and Disease (31 papers), Cellular transport and secretion (22 papers) and Advanced Fluorescence Microscopy Techniques (20 papers). Erik L. Snapp is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (31 papers), Cellular transport and secretion (22 papers) and Advanced Fluorescence Microscopy Techniques (20 papers). Erik L. Snapp collaborates with scholars based in United States, Canada and Italy. Erik L. Snapp's co-authors include Jennifer Lippincott‐Schwartz, Anne K. Kenworthy, Maura Francolini, Lindsey M. Costantini, Patrick Lajoie, Ramanujan S. Hegde, Nica Borgese, Federica Brandizzí, Chris Hawes and Alison G. Roberts 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

Erik L. Snapp

70 papers receiving 5.7k citations

Hit Papers

Studying protein dynamics in living cells 2001 2026 2009 2017 2001 250 500 750

Peers

Erik L. Snapp
Kurt S. Thorn United States
Yeon‐Kyun Shin United States
Matilda Katan United Kingdom
Erik L. Snapp
Citations per year, relative to Erik L. Snapp Erik L. Snapp (= 1×) peers Marko Kaksonen

Countries citing papers authored by Erik L. Snapp

Since Specialization
Citations

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

Fields of papers citing papers by Erik L. Snapp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Erik L. Snapp. 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 Erik L. Snapp. The network helps show where Erik L. Snapp may publish in the future.

Co-authorship network of co-authors of Erik L. Snapp

This figure shows the co-authorship network connecting the top 25 collaborators of Erik L. Snapp. A scholar is included among the top collaborators of Erik L. Snapp 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 Erik L. Snapp. Erik L. Snapp 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.
Berg, Matthew D., Julie Genereaux, Robyn D. Moir, et al.. (2024). TUDCA modulates drug bioavailability to regulate resistance to acute ER stress in Saccharomyces cerevisiae. Molecular Biology of the Cell. 36(2). ar13–ar13.
2.
Lajoie, Patrick & Erik L. Snapp. (2020). Size‐dependent secretory protein reflux into the cytosol in association with acute endoplasmic reticulum stress. Traffic. 21(6). 419–429. 17 indexed citations
3.
Kaberniuk, Andrii A., Manuel Mohr, Vladislav V. Verkhusha, & Erik L. Snapp. (2018). moxMaple3: a Photoswitchable Fluorescent Protein for PALM and Protein Highlighting in Oxidizing Cellular Environments. Scientific Reports. 8(1). 14738–14738. 13 indexed citations
4.
Chorro, Laurent, Masako Suzuki, Tere Williams, et al.. (2018). Interleukin 2 modulates thymic-derived regulatory T cell epigenetic landscape. Nature Communications. 9(1). 5368–5368. 26 indexed citations
5.
Crissman, Jonathan, Silvère Pagant, Alenka Čopič, et al.. (2015). Traffic of p24 Proteins and COPII Coat Composition Mutually Influence Membrane Scaffolding. Current Biology. 25(10). 1296–1305. 28 indexed citations
6.
Stout, Randy F., Erik L. Snapp, & David C. Spray. (2015). Connexin Type and Fluorescent Protein Fusion Tag Determine Structural Stability of Gap Junction Plaques. Journal of Biological Chemistry. 290(39). 23497–23514. 27 indexed citations
7.
Lajoie, Patrick, Elena N. Fazio, & Erik L. Snapp. (2014). Approaches to imaging unfolded secretory protein stress in living cells. PubMed. 1(1). 27–39. 10 indexed citations
8.
Costantini, Lindsey M. & Erik L. Snapp. (2013). Fluorescent Proteins in Cellular Organelles: Serious Pitfalls and Some Solutions. DNA and Cell Biology. 32(11). 622–627. 46 indexed citations
9.
Lajoie, Patrick, Robyn D. Moir, Ian M. Willis, & Erik L. Snapp. (2012). Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells. Molecular Biology of the Cell. 23(5). 955–964. 71 indexed citations
10.
Haataja, Leena, Erik L. Snapp, J. J. Wright, et al.. (2012). Proinsulin Intermolecular Interactions during Secretory Trafficking in Pancreatic β Cells. Journal of Biological Chemistry. 288(3). 1896–1906. 67 indexed citations
11.
Windsor, Miriam, Philippa C. Hawes, Paul Monaghan, et al.. (2011). Mechanism of Collapse of Endoplasmic Reticulum Cisternae During African Swine Fever Virus Infection. Traffic. 13(1). 30–42. 15 indexed citations
12.
Naismith, Teresa V., et al.. (2011). Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum. The EMBO Journal. 30(16). 3217–3231. 42 indexed citations
13.
Müller, Linda, Patrick Lajoie, Martin Jung, et al.. (2010). Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans. Molecular Biology of the Cell. 21(5). 691–703. 76 indexed citations
14.
Lai, Chunwei W., et al.. (2010). BiP Availability Distinguishes States of Homeostasis and Stress in the Endoplasmic Reticulum of Living Cells. Molecular Biology of the Cell. 21(12). 1909–1921. 68 indexed citations
15.
Ostrovsky, Olga, Catherine A. Makarewich, Erik L. Snapp, & Yair Argon. (2009). An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proceedings of the National Academy of Sciences. 106(28). 11600–11605. 56 indexed citations
16.
Snapp, Erik L.. (2009). Fluorescent proteins: a cell biologist's user guide. Trends in Cell Biology. 19(11). 649–655. 131 indexed citations
17.
Snapp, Erik L., Ajay Sharma, Jennifer Lippincott‐Schwartz, & Ramanujan S. Hegde. (2006). Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells. Proceedings of the National Academy of Sciences. 103(17). 6536–6541. 104 indexed citations
18.
daSilva, Luis L. P., Erik L. Snapp, Jürgen Denecke, et al.. (2004). Endoplasmic Reticulum Export Sites and Golgi Bodies Behave as Single Mobile Secretory Units in Plant Cells[W]. The Plant Cell. 16(7). 1753–1771. 241 indexed citations
19.
Snapp, Erik L., et al.. (2004). Glycan-independent Role of Calnexin in the Intracellular Retention of Charcot-Marie-Tooth 1A Gas3/PMP22 Mutants. Journal of Biological Chemistry. 280(3). 2378–2387. 29 indexed citations
20.
Snapp, Erik L. & Scott M. Landfear. (1999). Characterization of a Targeting Motif for a Flagellar Membrane Protein in Leishmania enriettii. Journal of Biological Chemistry. 274(41). 29543–29548. 29 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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