Joseph A. Loo

32.4k total citations · 5 hit papers
346 papers, 23.8k citations indexed

About

Joseph A. Loo is a scholar working on Spectroscopy, Molecular Biology and Materials Chemistry. According to data from OpenAlex, Joseph A. Loo has authored 346 papers receiving a total of 23.8k indexed citations (citations by other indexed papers that have themselves been cited), including 184 papers in Spectroscopy, 167 papers in Molecular Biology and 32 papers in Materials Chemistry. Recurrent topics in Joseph A. Loo's work include Mass Spectrometry Techniques and Applications (170 papers), Advanced Proteomics Techniques and Applications (88 papers) and Analytical Chemistry and Chromatography (76 papers). Joseph A. Loo is often cited by papers focused on Mass Spectrometry Techniques and Applications (170 papers), Advanced Proteomics Techniques and Applications (88 papers) and Analytical Chemistry and Chromatography (76 papers). Joseph A. Loo collaborates with scholars based in United States, Australia and United Kingdom. Joseph A. Loo's co-authors include Richard Smith, Rachel R. Ogorzalek Loo, Harold R. Udseth, Charles G. Edmonds, David T. Wong, Shen Hu, Sheng Yin, Yongming Xie, Charles J. Barinaga and Pinmanee Boontheung and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Joseph A. Loo

341 papers receiving 23.0k citations

Hit Papers

Studying noncovalent protein complexes by electrospray io... 1990 2026 2002 2014 1997 1990 2009 1991 2024 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph A. Loo United States 82 11.8k 10.7k 2.7k 2.2k 1.5k 346 23.8k
Michael Karas Germany 80 12.8k 1.1× 15.9k 1.5× 2.3k 0.9× 1.4k 0.6× 4.1k 2.7× 320 28.3k
Joshua J. Coon United States 73 13.6k 1.2× 10.3k 1.0× 2.4k 0.9× 1.2k 0.6× 624 0.4× 359 22.0k
Lloyd M. Smith United States 64 10.8k 0.9× 3.7k 0.3× 3.3k 1.2× 1.3k 0.6× 509 0.3× 349 21.8k
Peter Roepstorff Denmark 81 14.2k 1.2× 8.1k 0.8× 1.3k 0.5× 1.1k 0.5× 782 0.5× 444 26.3k
Robert J. Cotter United States 78 8.4k 0.7× 6.0k 0.6× 836 0.3× 2.8k 1.3× 1.6k 1.1× 366 19.5k
Richard M. Caprioli United States 96 17.1k 1.4× 20.1k 1.9× 2.0k 0.7× 766 0.4× 4.3k 2.9× 469 31.6k
Carol V. Robinson United Kingdom 116 33.4k 2.8× 15.6k 1.5× 1.7k 0.6× 4.4k 2.0× 2.1k 1.4× 597 46.6k
Matthias Wilm Germany 73 26.1k 2.2× 7.5k 0.7× 1.4k 0.5× 1.7k 0.8× 404 0.3× 124 36.5k
Donald F. Hunt United States 106 25.0k 2.1× 9.4k 0.9× 1.2k 0.5× 739 0.3× 791 0.5× 407 40.0k
Roman A. Zubarev Sweden 64 8.6k 0.7× 11.3k 1.1× 707 0.3× 430 0.2× 1.4k 0.9× 361 17.1k

Countries citing papers authored by Joseph A. Loo

Since Specialization
Citations

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

Fields of papers citing papers by Joseph A. Loo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph A. Loo. 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 Joseph A. Loo. The network helps show where Joseph A. Loo may publish in the future.

Co-authorship network of co-authors of Joseph A. Loo

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph A. Loo. A scholar is included among the top collaborators of Joseph A. Loo 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 Joseph A. Loo. Joseph A. Loo 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.
Chiang, Chen‐Yu, Masao Ōhashi, Pan‐Pan Chen, et al.. (2025). Copper-dependent halogenase catalyses unactivated C−H bond functionalization. Nature. 638(8049). 126–132. 12 indexed citations
2.
Campuzano, Iain D. G. & Joseph A. Loo. (2025). Evolution of Mass Spectrometers for High m/z Biological Ion Formation, Transmission, Analysis and Detection: A Personal Perspective. Journal of the American Society for Mass Spectrometry. 36(4). 632–652. 4 indexed citations
3.
Loo, Rachel R. Ogorzalek, et al.. (2024). Insight into the autoproteolysis mechanism of the RsgI9 anti‐σ factor from Clostridium thermocellum. Proteins Structure Function and Bioinformatics. 92(8). 946–958. 1 indexed citations
4.
Hou, Ke, Hope Pan, Romany Abskharon, et al.. (2024). D-peptide-magnetic nanoparticles fragment tau fibrils and rescue behavioral deficits in a mouse model of Alzheimer’s disease. Science Advances. 10(18). eadl2991–eadl2991. 9 indexed citations
5.
Doud, Evan A., Yu Chen, Arnold L. Rheingold, et al.. (2024). Ultrafast Au(III)-Mediated Arylation of Cysteine. Journal of the American Chemical Society. 146(18). 12365–12374. 24 indexed citations
6.
7.
Samanta, Nirnay, Yasser B. Ruiz‐Blanco, David Gnutt, et al.. (2022). Superoxide Dismutase 1 Folding Stability as a Target for Molecular Tweezers in SOD1‐Related Amyotrophic Lateral Sclerosis. ChemBioChem. 23(21). e202200396–e202200396. 10 indexed citations
8.
Nguyen, Hong Hanh, Neil Q. Wofford, Housna Mouttaki, et al.. (2022). The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation. Molecular & Cellular Proteomics. 21(4). 100215–100215. 8 indexed citations
9.
Smith, Lloyd M., Jeffrey N. Agar, Julia Chamot‐Rooke, et al.. (2021). The Human Proteoform Project: Defining the human proteome. Science Advances. 7(46). eabk0734–eabk0734. 145 indexed citations
10.
Cascio, Duilio, Martin L. Phillips, Musleh M. Muthana, et al.. (2021). Insight into the molecular basis of substrate recognition by the wall teichoic acid glycosyltransferase TagA. Journal of Biological Chemistry. 298(2). 101464–101464. 3 indexed citations
11.
Campuzano, Iain D. G., John H. Robinson, John O. Hui, et al.. (2019). Native and Denaturing MS Protein Deconvolution for Biopharma: Monoclonal Antibodies and Antibody–Drug Conjugates to Polydisperse Membrane Proteins and Beyond. Analytical Chemistry. 91(15). 9472–9480. 33 indexed citations
12.
Wofford, Neil Q., Housna Mouttaki, Jessica R. Sieber, et al.. (2016). Pyrophosphate-Dependent ATP Formation from Acetyl Coenzyme A in Syntrophus aciditrophicus, a New Twist on ATP Formation. mBio. 7(4). 21 indexed citations
13.
AhYoung, Andrew P., Jiansen Jiang, Jiang Zhang, et al.. (2015). Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly. Proceedings of the National Academy of Sciences. 112(25). E3179–88. 157 indexed citations
14.
Zhu, Weidong, Quynh T. Phan, Pinmanee Boontheung, et al.. (2012). EGFR and HER2 receptor kinase signaling mediate epithelial cell invasion by Candida albicans during oropharyngeal infection. Proceedings of the National Academy of Sciences. 109(35). 14194–14199. 142 indexed citations
15.
Lu, Qing‐Yi, Yanan Yang, Zuo‐Feng Zhang, et al.. (2009). Effects of green tea extract on lung cancer A549 cells: Proteomic identification of proteins associated with cell migration. PROTEOMICS. 9(3). 757–767. 36 indexed citations
16.
Mosessian, Sherly, Nuraly K. Avliyakulov, David J. Mulholland, et al.. (2009). Analysis of PTEN Complex Assembly and Identification of Heterogeneous Nuclear Ribonucleoprotein C as a Component of the PTEN-associated Complex. Journal of Biological Chemistry. 284(44). 30159–30166. 18 indexed citations
17.
Hu, Shen, Martha Arellano, Pinmanee Boontheung, et al.. (2008). Salivary Proteomics for Oral Cancer Biomarker Discovery. Clinical Cancer Research. 14(19). 6246–6252. 425 indexed citations
18.
Hu, Shen, et al.. (2005). Quantitative proteome analysis of oral tongue squamous cell carcinoma by laser capture microdissection, stable isotope labeling and liquid chromatography-mass spectrometry.. Cancer Research. 65. 93–93. 1 indexed citations
19.
Fry, David W., Alexander J. Bridges, William A. Denny, et al.. (1998). Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor. Proceedings of the National Academy of Sciences. 95(20). 12022–12027. 344 indexed citations
20.
Loo, Joseph A., Tod P. Holler, Susan K. Foltin, et al.. (1998). Application of electrospray ionization mass spectrometry for studying human immunodeficiency virus protein complexes. Proteins Structure Function and Bioinformatics. 33(S2). 28–37. 2 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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