Douglas M. Lublin

9.1k total citations
82 papers, 7.5k citations indexed

About

Douglas M. Lublin is a scholar working on Immunology, Molecular Biology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Douglas M. Lublin has authored 82 papers receiving a total of 7.5k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Immunology, 32 papers in Molecular Biology and 17 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Douglas M. Lublin's work include Complement system in diseases (26 papers), Monoclonal and Polyclonal Antibodies Research (17 papers) and Erythrocyte Function and Pathophysiology (12 papers). Douglas M. Lublin is often cited by papers focused on Complement system in diseases (26 papers), Monoclonal and Polyclonal Antibodies Research (17 papers) and Erythrocyte Function and Pathophysiology (12 papers). Douglas M. Lublin collaborates with scholars based in United States, United Kingdom and Australia. Douglas M. Lublin's co-authors include John P. Atkinson, Dennis J. Dietzen, Jacky M. K. Kwong, William R. Hastings, John P. Atkinson, Andréy S. Shaw, Youchun Zeng, Isabelle Rooney, T C Farries and Timothy Blackmore and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Douglas M. Lublin

82 papers receiving 7.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Douglas M. Lublin United States	49	2.9k	2.8k	1.7k	1.1k	1.0k	82	7.5k
Andrew J. Dorner United States	43	3.1k 1.1×	1.9k 0.7×	1.2k 0.7×	897 0.8×	408 0.4×	87	7.3k
M. Edward Medof United States	56	2.4k 0.8×	5.9k 2.1×	683 0.4×	1.6k 1.4×	1.2k 1.2×	183	9.9k
Jay C. Unkeless United States	49	4.3k 1.5×	5.3k 1.9×	632 0.4×	1.0k 0.9×	663 0.6×	89	11.1k
Eileen Remold‐O’Donnell United States	44	2.9k 1.0×	2.7k 1.0×	1.3k 0.8×	1.5k 1.3×	368 0.4×	116	7.4k
Alan Solomon United States	52	6.3k 2.2×	1.7k 0.6×	539 0.3×	1.2k 1.1×	1.7k 1.7×	201	9.3k
J. B. Natvig Norway	55	3.9k 1.4×	5.1k 1.8×	327 0.2×	1.4k 1.2×	1.3k 1.3×	287	11.0k
Henri S. Lichenstein United States	40	3.3k 1.1×	2.1k 0.8×	490 0.3×	346 0.3×	335 0.3×	59	6.3k
David W. Scott United States	49	2.8k 1.0×	4.2k 1.5×	420 0.2×	977 0.9×	351 0.3×	287	8.0k
Mehrdad Matloubian United States	31	3.4k 1.2×	6.4k 2.3×	568 0.3×	554 0.5×	461 0.4×	53	9.8k
Brian F. Tack United States	54	4.1k 1.4×	4.2k 1.5×	584 0.3×	1.2k 1.0×	750 0.7×	93	8.9k

Countries citing papers authored by Douglas M. Lublin

Since Specialization

Citations

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

Fields of papers citing papers by Douglas M. Lublin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Douglas M. Lublin. 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 Douglas M. Lublin. The network helps show where Douglas M. Lublin may publish in the future.

Co-authorship network of co-authors of Douglas M. Lublin

This figure shows the co-authorship network connecting the top 25 collaborators of Douglas M. Lublin. A scholar is included among the top collaborators of Douglas M. Lublin 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 Douglas M. Lublin. Douglas M. Lublin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Despotis, George J., Charles Eby, & Douglas M. Lublin. (2008). A review of transfusion risks and optimal management of perioperative bleeding with cardiac surgery. Transfusion. 48(s1). 2S–30S. 104 indexed citations

Lublin, Douglas M., D. Phelan, Sarah Boslaugh, et al.. (2007). Mortality and Morbidity in Pre-sensitized Pediatric Heart Transplant Recipients With a Positive Donor Crossmatch Utilizing Peri-operative Plasmapheresis and Cytolytic Therapy. The Journal of Heart and Lung Transplantation. 26(9). 876–882. 69 indexed citations

Hue‐Roye, Kim, Christine Lomas‐Francis, Larisa Belaygorod, et al.. (2007). Three new high‐prevalence antigens in the Cromer blood group system. Transfusion. 47(9). 1621–1629. 8 indexed citations

Despotis, George J., Lini Zhang, & Douglas M. Lublin. (2007). Transfusion Risks and Transfusion-related Pro-inflammatory Responses. Hematology/Oncology Clinics of North America. 21(1). 147–161. 30 indexed citations

Ren, Xiaoyan, et al.. (2004). Conformational Defects Slow Golgi Exit, Block Oligomerization, and Reduce Raft Affinity of Caveolin-1 Mutant Proteins. Molecular Biology of the Cell. 15(10). 4556–4567. 43 indexed citations

Hofling, A. Alex, Mark S. Sands, Douglas M. Lublin, Gerhard Bauer, & Steven M. Devine. (2004). Collection of a mobilized peripheral blood apheresis product from a patient with mucopolysaccharidosis type VII and subsequent CD34+ cell isolation. Journal of Clinical Apheresis. 19(3). 151–153. 5 indexed citations

Storry, Jill R., Kim Hue‐Roye, Morris A. Blajchman, et al.. (2003). GUTI: a new antigen in the Cromer blood group system. Transfusion. 43(3). 340–344. 14 indexed citations

Harris, Claire L., Douglas M. Lublin, & B. Paul Morgan. (2002). Efficient generation of monoclonal antibodies for specific protein domains using recombinant immunoglobulin fusion proteins: pitfalls and solutions. Journal of Immunological Methods. 268(2). 245–258. 23 indexed citations

Ostermeyer, Anne G., James M. Paci, Youchun Zeng, et al.. (2001). Accumulation of Caveolin in the Endoplasmic Reticulum Redirects the Protein to Lipid Storage Droplets. The Journal of Cell Biology. 152(5). 1071–1078. 222 indexed citations

10.

Blackmore, Timothy, Tania Sadlon, H. Marshall Ward, Douglas M. Lublin, & David Gordon. (1996). Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H. The Journal of Immunology. 157(12). 5422–5427. 161 indexed citations

11.

Farries, T C, et al.. (1996). Control of the Complement System. Advances in immunology. 61. 201–283. 375 indexed citations

12.

Kendall, G M, et al.. (1996). Activation of the gene encoding decay accelerating factor following nerve growth factor treatment of sensory neurons is mediated by promoter sequences within 206 bases of the transcriptional start site. Journal of Neuroscience Research. 45(2). 96–103. 7 indexed citations

13.

Tao, Nengbing, Steven J. Wagner, & Douglas M. Lublin. (1996). CD36 Is Palmitoylated on Both N- and C-terminal Cytoplasmic Tails. Journal of Biological Chemistry. 271(37). 22315–22320. 156 indexed citations

14.

Hart, Audrey, Pawel Goluszko, J. J. Moulds, et al.. (1995). dra-related X adhesins of gestational pyelonephritis-associated Escherichia coli recognize SCR-3 and SCR-4 domains of recombinant decay-accelerating factor. Infection and Immunity. 63(5). 1663–1668. 50 indexed citations

15.

Nickells, M W, et al.. (1994). Characterization of DAF-2, a high molecular weight form of decay-accelerating factor (DAF; CD55), as a covalently cross-linked dimer of DAF-1.. The Journal of Immunology. 152(2). 676–685. 20 indexed citations

16.

Dietzen, Dennis J., et al.. (1994). Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae.. The Journal of Cell Biology. 126(2). 353–363. 344 indexed citations

17.

Hall, Susan, Stephen Thompson, Taroh Kinoshita, et al.. (1992). Mapping of epitopes, glycosylation sites, and complement regulatory domains in human decay accelerating factor. The Journal of Immunology. 149(9). 2906–2913. 199 indexed citations

18.

Bora, Nalini S., et al.. (1989). Structural gene for human membrane cofactor protein (MCP) of complement maps to within 100 kb of the 3' end of the C3b/C4b receptor gene.. The Journal of Experimental Medicine. 169(2). 597–602. 51 indexed citations

19.

Lublin, Douglas M., M. Kathryn Liszewski, T W Post, et al.. (1988). Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins.. The Journal of Experimental Medicine. 168(1). 181–194. 180 indexed citations

20.

Lublin, Douglas M., Rogers C. Griffith, & John Atkinson. (1986). Influence of glycosylation on allelic and cell-specific Mr variation, receptor processing, and ligand binding of the human complement C3b/C4b receptor.. Journal of Biological Chemistry. 261(13). 5736–5744. 48 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