David A. Lomas

14.9k total citations · 4 hit papers
135 papers, 8.8k citations indexed

About

David A. Lomas is a scholar working on Cancer Research, Molecular Biology and Cell Biology. According to data from OpenAlex, David A. Lomas has authored 135 papers receiving a total of 8.8k indexed citations (citations by other indexed papers that have themselves been cited), including 78 papers in Cancer Research, 53 papers in Molecular Biology and 46 papers in Cell Biology. Recurrent topics in David A. Lomas's work include Protease and Inhibitor Mechanisms (78 papers), Peptidase Inhibition and Analysis (28 papers) and Endoplasmic Reticulum Stress and Disease (23 papers). David A. Lomas is often cited by papers focused on Protease and Inhibitor Mechanisms (78 papers), Peptidase Inhibition and Analysis (28 papers) and Endoplasmic Reticulum Stress and Disease (23 papers). David A. Lomas collaborates with scholars based in United Kingdom, United States and Italy. David A. Lomas's co-authors include Robin W. Carrell, Bibek Gooptu, Ravi Mahadeva, Elena Miranda, Stefan J. Marciniak, Peter R. Elliott, Timothy R. Dafforn, Noel G. McElvaney, James A. Irving and Damian C. Crowther and has published in prestigious journals such as Nature, New England Journal of Medicine and Proceedings of the National Academy of Sciences.

In The Last Decade

David A. Lomas

132 papers receiving 8.7k citations

Hit Papers

The Serpins Are an Expanding Superfamily of Structurally ... 1997 2026 2006 2016 2001 1997 2011 2020 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
David A. Lomas United Kingdom 44 4.3k 3.6k 2.0k 1.6k 1.5k 135 8.8k
Steven L. Gonias United States 60 5.0k 1.2× 3.6k 1.0× 1.7k 0.8× 2.0k 1.2× 1.7k 1.1× 223 11.0k
Magnus Abrahamson Sweden 52 3.9k 0.9× 2.5k 0.7× 723 0.4× 1.1k 0.7× 625 0.4× 178 9.4k
Luis Sánchez‐Pulido Spain 47 4.9k 1.1× 1.9k 0.5× 988 0.5× 1.5k 0.9× 534 0.4× 112 8.0k
Jian Cao United States 49 4.6k 1.1× 4.7k 1.3× 885 0.4× 3.9k 2.4× 1.3k 0.9× 131 9.9k
Sylvie Robine France 53 6.5k 1.5× 1.3k 0.4× 1.3k 0.6× 3.1k 1.9× 1.2k 0.8× 112 11.9k
Senji Shirasawa Japan 48 5.8k 1.4× 2.0k 0.6× 804 0.4× 2.7k 1.6× 375 0.3× 191 9.3k
Henry C. Krutzsch United States 48 6.3k 1.5× 2.3k 0.7× 1.3k 0.6× 1.8k 1.1× 790 0.5× 111 9.7k
Vivek Mittal United States 50 7.2k 1.7× 3.2k 0.9× 1.1k 0.5× 4.2k 2.5× 520 0.3× 130 12.9k
Alan L. Schwartz United States 66 9.2k 2.2× 1.8k 0.5× 3.5k 1.7× 2.4k 1.4× 1.3k 0.8× 176 14.3k
Giovanni Blandino Italy 61 9.2k 2.2× 4.0k 1.1× 1.9k 0.9× 5.2k 3.1× 320 0.2× 266 12.8k

Countries citing papers authored by David A. Lomas

Since Specialization
Citations

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

Fields of papers citing papers by David A. Lomas

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David A. Lomas

This figure shows the co-authorship network connecting the top 25 collaborators of David A. Lomas. A scholar is included among the top collaborators of David A. Lomas 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 A. Lomas. David A. Lomas 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.
Gangemi, Roberto, Riccardo Ronzoni, David A. Lomas, et al.. (2025). Identification of an exosite at the neutrophil elastase/alpha‐1‐antitrypsin interface. FEBS Journal. 292(8). 1887–1903. 1 indexed citations
2.
Waudby, Christopher A., Mattia Laffranchi, Annamaria Fra, et al.. (2025). High-resolution characterization of ex vivo AAT polymers by solution-state NMR spectroscopy. Science Advances. 11(19). eadu7064–eadu7064. 2 indexed citations
3.
Arold, Stefan T., et al.. (2025). The mechanism of pathogenic α 1 -antitrypsin aggregation in the human liver. Proceedings of the National Academy of Sciences. 122(46). e2507535122–e2507535122.
4.
Irving, James A., et al.. (2023). Native and Ion Mobility Mass Spectrometry Characterization of Alpha 1 Antitrypsin Variants and Oligomers. Methods in molecular biology. 2750. 41–55. 1 indexed citations
5.
Ronzoni, Riccardo, Ilaria Ferrarotti, Stefania Ottaviani, et al.. (2021). The Importance of N186 in the Alpha-1-Antitrypsin Shutter Region Is Revealed by the Novel Bologna Deficiency Variant. International Journal of Molecular Sciences. 22(11). 5668–5668. 9 indexed citations
6.
Raccosta, Samuele, Fabio Librizzi, Rosina Noto, et al.. (2021). Scaling Concepts in Serpin Polymer Physics. Materials. 14(10). 2577–2577. 3 indexed citations
7.
McKimpson, Wendy M., Yun Chen, James A. Irving, et al.. (2021). Conversion of the death inhibitor ARC to a killer activates pancreatic β cell death in diabetes. Developmental Cell. 56(6). 747–760.e6. 4 indexed citations
8.
Gooptu, Bibek, Adam Redzej, S. Tamir Rashid, et al.. (2020). The structural basis for Z α 1 -antitrypsin polymerization in the liver. Science Advances. 6(43). 31 indexed citations
9.
Laffranchi, Mattia, et al.. (2019). Characterisation of a type II functionally-deficient variant of alpha-1-antitrypsin discovered in the general population. PLoS ONE. 14(1). e0206955–e0206955. 15 indexed citations
10.
Raimondi, Sara, Loredana Marchese, Frederick A. Partridge, et al.. (2019). C. elegans expressing D76N β2-microglobulin: a model for in vivo screening of drug candidates targeting amyloidosis. Scientific Reports. 9(1). 19960–19960. 12 indexed citations
11.
Partridge, Frederick A., Steven D. Buckingham, Nicky J. Willis, et al.. (2017). An automated high-throughput system for phenotypic screening of chemical libraries on C. elegans and parasitic nematodes. International Journal for Parasitology Drugs and Drug Resistance. 8(1). 8–21. 62 indexed citations
12.
Haq, Imran Ul, James A. Irving, Aarash Saleh, et al.. (2015). Deficiency Mutations of Alpha-1 Antitrypsin. Effects on Folding, Function, and Polymerization. American Journal of Respiratory Cell and Molecular Biology. 54(1). 71–80. 29 indexed citations
13.
Lee, Jin Hwa, Michael H. Cho, Craig P. Hersh, et al.. (2014). IREB2 and GALC Are Associated with Pulmonary Artery Enlargement in Chronic Obstructive Pulmonary Disease. American Journal of Respiratory Cell and Molecular Biology. 52(3). 365–376. 23 indexed citations
14.
Khabirova, Eleonora, Aileen M. Moloney, Stefan J. Marciniak, et al.. (2014). The TRiC/CCT Chaperone Is Implicated in Alzheimer's Disease Based on Patient GWAS and an RNAi Screen in Aβ-Expressing Caenorhabditis elegans. PLoS ONE. 9(7). e102985–e102985. 29 indexed citations
15.
Lomas, David A.. (2013). Twenty Years of Polymers: A Personal Perspective on Alpha-1 Antitrypsin Deficiency. COPD Journal of Chronic Obstructive Pulmonary Disease. 10(sup1). 17–25. 18 indexed citations
16.
Dawwas, Muhammad F., Susan E. Davies, William J. Griffiths, David A. Lomas, & Graeme Alexander. (2012). Prevalence and Risk Factors for Liver Involvement in Individuals with PiZZ-related Lung Disease. American Journal of Respiratory and Critical Care Medicine. 187(5). 502–508. 39 indexed citations
17.
Takehara, Sayaka, Maki Onda, Juan Zhang, et al.. (2009). The 2.1-Å Crystal Structure of Native Neuroserpin Reveals Unique Structural Elements That Contribute to Conformational Instability. Journal of Molecular Biology. 388(1). 11–20. 37 indexed citations
18.
Munuswamy‐Ramanujam, Ganesh, Erbin Dai, Yuming Sun, et al.. (2007). Abstract 718: Mammalian Serine Protease Inhibitor (Serpin), Neuroserpin, Targets Thromblytic Proteases to Reduce Inflammation, Atherogenesis and T Helper Lymphocyte Activation. Circulation. 116.
19.
Belorgey, Didier, et al.. (2004). Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers. European Journal of Biochemistry. 271(16). 3360–3367. 42 indexed citations
20.
Lomas, David A. & Ravi Mahadeva. (2002). α1-Antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. Journal of Clinical Investigation. 110(11). 1585–1590. 167 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026