Stephen J. Demarest

2.7k total citations
50 papers, 2.0k citations indexed

About

Stephen J. Demarest is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Stephen J. Demarest has authored 50 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 32 papers in Radiology, Nuclear Medicine and Imaging and 12 papers in Immunology. Recurrent topics in Stephen J. Demarest's work include Monoclonal and Polyclonal Antibodies Research (32 papers), Glycosylation and Glycoproteins Research (27 papers) and Protein purification and stability (17 papers). Stephen J. Demarest is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (32 papers), Glycosylation and Glycoproteins Research (27 papers) and Protein purification and stability (17 papers). Stephen J. Demarest collaborates with scholars based in United States, Iran and Switzerland. Stephen J. Demarest's co-authors include Ellen A. Garber, Scott Glaser, Daniel P. Raleigh, Xiufeng Wu, Peter E. Wright, H. Jane Dyson, Ronald M. Evans, Flora Huang, Maria A. Martinez‐Yamout and Wei Xu and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Stephen J. Demarest

49 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Stephen J. Demarest United States	25	1.6k	1.0k	364	315	309	50	2.0k
Boopathy Ramakrishnan United States	24	1.6k 1.0×	479 0.5×	351 1.0×	139 0.4×	271 0.9×	44	2.0k
Sandeep Kumar United States	32	2.4k 1.5×	1.8k 1.7×	406 1.1×	153 0.5×	222 0.7×	82	2.8k
Bassil I. Dahiyat United States	13	2.2k 1.4×	682 0.7×	343 0.9×	798 2.5×	240 0.8×	16	2.8k
Michael T. Stumpp Switzerland	18	1.7k 1.1×	1.0k 1.0×	224 0.6×	132 0.4×	310 1.0×	26	2.3k
Michael G. Mulkerrin United States	18	1.6k 1.0×	898 0.9×	569 1.6×	104 0.3×	315 1.0×	24	2.7k
Alexey Schulga Russia	22	880 0.6×	425 0.4×	106 0.3×	157 0.5×	260 0.8×	73	1.4k
Rafael de Llorens Spain	32	1.7k 1.1×	316 0.3×	475 1.3×	143 0.5×	690 2.2×	61	2.4k
Galina Obmolova United States	25	1.6k 1.0×	375 0.4×	275 0.8×	261 0.8×	235 0.8×	60	2.2k
David B. Langley Australia	22	987 0.6×	332 0.3×	310 0.9×	240 0.8×	126 0.4×	46	1.6k
Tilman Schlothauer Germany	23	1.6k 1.0×	1.3k 1.3×	570 1.6×	90 0.3×	242 0.8×	45	2.2k

Countries citing papers authored by Stephen J. Demarest

Since Specialization

Citations

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

Fields of papers citing papers by Stephen J. Demarest

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Stephen J. Demarest. 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 Stephen J. Demarest. The network helps show where Stephen J. Demarest may publish in the future.

Co-authorship network of co-authors of Stephen J. Demarest

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

All Works

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20 of 20 papers shown

Köester, Anja, Derrick R. Witcher, Mark Lee, et al.. (2025). Ucenprubart is an agonistic antibody to CD200R with the potential to treat inflammatory skin disease: preclinical development and a phase 1 clinical study. Nature Communications. 16(1). 4082–4082. 1 indexed citations

Poussin, Mathilde, Arlene Sereno, Xiufeng Wu, et al.. (2021). Dichotomous impact of affinity on the function of T cell engaging bispecific antibodies. Journal for ImmunoTherapy of Cancer. 9(7). e002444–e002444. 21 indexed citations

Potter, Sally, et al.. (2020). LB947 Development of LY3454738, an agonistic antibody to human CD200R. Journal of Investigative Dermatology. 140(7). B11–B11. 1 indexed citations

Leaver‐Fay, Andrew, Karen Froning, S. Atwell, et al.. (2016). Computationally Designed Bispecific Antibodies using Negative State Repertoires. Structure. 24(4). 641–651. 49 indexed citations

Wu, Xiufeng, Arlene Sereno, Flora Huang, et al.. (2015). Protein design of IgG/TCR chimeras for the co-expression of Fab-like moieties within bispecific antibodies. mAbs. 7(2). 364–376. 22 indexed citations

Wu, Xiufeng, Arlene Sereno, Flora Huang, et al.. (2015). Fab-based bispecific antibody formats with robust biophysical properties and biological activity. mAbs. 7(3). 470–482. 52 indexed citations

Lewis, Steven M., Xiufeng Wu, Anna Pustilnik, et al.. (2014). Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface. Nature Biotechnology. 32(2). 191–198. 196 indexed citations

Proctor, Elizabeth A., Pradeep Kota, Stephen J. Demarest, Justin A. Caravella, & Nikolay V. Dokholyan. (2013). Highly covarying residues have a functional role in antibody constant domains. Proteins Structure Function and Bioinformatics. 81(5). 884–895. 5 indexed citations

Snyder, William B., Flora Huang, Allan D. Capili, et al.. (2012). Secretion from bacterial versus mammalian cells yields a recombinant scFv with variable folding properties. Archives of Biochemistry and Biophysics. 526(2). 188–193. 24 indexed citations

10.

Houde, Damian J. & Stephen J. Demarest. (2011). Fine Details of IGF-1R Activation, Inhibition, and Asymmetry Determined by Associated Hydrogen /Deuterium-Exchange and Peptide Mass Mapping. Structure. 19(6). 890–900. 24 indexed citations

11.

Dong, Jianying, Stephen J. Demarest, Arlene Sereno, et al.. (2010). Combination of Two Insulin-Like Growth Factor-I Receptor Inhibitory Antibodies Targeting Distinct Epitopes Leads to an Enhanced Antitumor Response. Molecular Cancer Therapeutics. 9(9). 2593–2604. 48 indexed citations

12.

Arndt, Joseph W., Guohui Li, Stephen J. Demarest, et al.. (2009). Structural understanding of stabilization patterns in engineered bispecific Ig‐like antibody molecules. Proteins Structure Function and Bioinformatics. 77(4). 832–841. 28 indexed citations

13.

Miller, Brian, Scott Glaser, & Stephen J. Demarest. (2008). Rapid Screening Platform for Stabilization of scFvs in Escherichia coli. Methods in molecular biology. 525. 279–289. 8 indexed citations

14.

Garber, Ellen A. & Stephen J. Demarest. (2007). A broad range of Fab stabilities within a host of therapeutic IgGs. Biochemical and Biophysical Research Communications. 355(3). 751–757. 184 indexed citations

15.

Demarest, Stephen J., Elisabeth Mertsching, Konrad Miatkowski, et al.. (2006). An Intermediate pH Unfolding Transition Abrogates the Ability of IgE to Interact with Its High Affinity Receptor FcϵRIα. Journal of Biological Chemistry. 281(41). 30755–30767. 14 indexed citations

16.

Demarest, Stephen J., Gang Chen, Bruce E. Kimmel, et al.. (2006). Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression. Protein Engineering Design and Selection. 19(7). 325–336. 37 indexed citations

17.

Demarest, Stephen J., Songpon Deechongkit, H. Jane Dyson, Ronald M. Evans, & Peter E. Wright. (2003). Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB‐binding protein. Protein Science. 13(1). 203–210. 60 indexed citations

18.

Demarest, Stephen J., Maria A. Martinez‐Yamout, John Y. L. Chung, et al.. (2002). Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature. 415(6871). 549–553. 371 indexed citations

19.

Demarest, Stephen J. & Daniel P. Raleigh. (2000). Solution structure of a peptide model of a region important for the folding of ?-lactalbumin provides evidence for the formation of nonnative structure in the denatured state. Proteins Structure Function and Bioinformatics. 38(2). 189–196. 13 indexed citations

20.

Demarest, Stephen J., et al.. (2000). Local interactions and the role of the 6-120 disulfide bond in α-lactalbumin: implications for formation of the molten globule state. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1476(1). 9–19. 7 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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