Mark D. Distefano

7.5k total citations · 1 hit paper
169 papers, 6.0k citations indexed

About

Mark D. Distefano is a scholar working on Molecular Biology, Organic Chemistry and Cell Biology. According to data from OpenAlex, Mark D. Distefano has authored 169 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 130 papers in Molecular Biology, 73 papers in Organic Chemistry and 31 papers in Cell Biology. Recurrent topics in Mark D. Distefano's work include Click Chemistry and Applications (67 papers), Chemical Synthesis and Analysis (41 papers) and Ubiquitin and proteasome pathways (27 papers). Mark D. Distefano is often cited by papers focused on Click Chemistry and Applications (67 papers), Chemical Synthesis and Analysis (41 papers) and Ubiquitin and proteasome pathways (27 papers). Mark D. Distefano collaborates with scholars based in United States, Switzerland and Canada. Mark D. Distefano's co-authors include Jonathan K. Dozier, Mohammad Rashidian, Charuta C. Palsuledesai, Kiall F. Suazo, Melissa J. Moore, Keun‐Young Park, Christopher T. Walsh, Dongfeng Qi, Dietmar Häring and Joshua D. Ochocki and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Mark D. Distefano

168 papers receiving 5.9k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Directed cell migration towards softer environments

2022 151 citations Mark D. Distefano et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Mark D. Distefano United States	42	4.0k	1.9k	810	807	776	169	6.0k
Peng R. Chen China	52	6.0k 1.5×	3.3k 1.7×	600 0.7×	963 1.2×	794 1.0×	159	8.2k
Eranthie Weerapana United States	52	5.6k 1.4×	2.7k 1.4×	688 0.8×	509 0.6×	1.2k 1.6×	128	9.3k
Katsunori Tanaka Japan	41	3.7k 0.9×	2.7k 1.4×	272 0.3×	744 0.9×	373 0.5×	291	6.4k
Andrew J. Wilson United Kingdom	50	5.2k 1.3×	2.9k 1.5×	292 0.4×	420 0.5×	1.4k 1.8×	172	8.4k
Eric J. Toone United States	38	4.4k 1.1×	2.6k 1.3×	297 0.4×	591 0.7×	306 0.4×	114	6.7k
Dieter H. Klaubert United States	28	3.5k 0.9×	1.1k 0.6×	484 0.6×	372 0.5×	280 0.4×	59	5.2k
Nediljko Budiša Germany	46	5.9k 1.5×	1.8k 0.9×	266 0.3×	555 0.7×	363 0.5×	220	7.3k
Knud J. Jensen Denmark	39	3.8k 1.0×	2.2k 1.2×	246 0.3×	488 0.6×	422 0.5×	199	5.6k
Dirk T. S. Rijkers Netherlands	41	3.7k 0.9×	1.8k 0.9×	357 0.4×	403 0.5×	306 0.4×	121	5.4k
Maarten Merkx Netherlands	50	3.9k 1.0×	694 0.4×	392 0.5×	561 0.7×	640 0.8×	167	7.0k

Countries citing papers authored by Mark D. Distefano

Since Specialization

Citations

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

Fields of papers citing papers by Mark D. Distefano

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mark D. Distefano. 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 Mark D. Distefano. The network helps show where Mark D. Distefano may publish in the future.

Co-authorship network of co-authors of Mark D. Distefano

This figure shows the co-authorship network connecting the top 25 collaborators of Mark D. Distefano. A scholar is included among the top collaborators of Mark D. Distefano 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 Mark D. Distefano. Mark D. Distefano 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

Wagner, Carston R., et al.. (2025). Engineering protein prenylation: an emerging tool for selective protein modification. Biochemical Society Transactions. 53(4). 1129–1149. 1 indexed citations

Kumar, Vikas, et al.. (2024). The utility of Streptococcus mutans undecaprenol kinase for the chemoenzymatic synthesis of diverse non-natural isoprenoids. Bioorganic Chemistry. 151. 107707–107707. 2 indexed citations

Suazo, Kiall F., Vartika Mishra, Linda Ottoboni, et al.. (2024). Improved synthesis and application of an alkyne-functionalized isoprenoid analogue to study the prenylomes of motor neurons, astrocytes and their stem cell progenitors. Bioorganic Chemistry. 147. 107365–107365. 1 indexed citations

Suazo, Kiall F., Yiao Wang, Jonas V. Schaefer, et al.. (2024). Broadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene–Tetrazine Click Chemistry. Bioconjugate Chemistry. 35(7). 922–933. 3 indexed citations

Wang, Yiao, et al.. (2024). Targeted Drug Delivery by MMAE Farnesyl-Bioconjugated Multivalent Chemically Self-Assembled Nanorings Induces Potent Receptor-Dependent Immunogenic Cell Death. Bioconjugate Chemistry. 35(5). 582–592. 3 indexed citations

Milosevic, Jelena, Abirami Kugadas, Xiaoxiao Lu, et al.. (2023). Prenylcysteine oxidase 1 like protein is required for neutrophil bactericidal activities. Nature Communications. 14(1). 2761–2761. 9 indexed citations

Lorimer, Ellen, et al.. (2023). GTPase splice variants RAC1 and RAC1B display isoform-specific differences in localization, prenylation, and interaction with the chaperone protein SmgGDS. Journal of Biological Chemistry. 299(6). 104698–104698. 9 indexed citations

Morstein, Johannes, et al.. (2022). Photoswitchable Isoprenoid Lipids Enable Optical Control of Peptide Lipidation. ACS Chemical Biology. 17(10). 2945–2953. 9 indexed citations

Wang, Yiao, et al.. (2022). Engineering Biomimetic Trogocytosis with Farnesylated Chemically Self-Assembled Nanorings. Biomacromolecules. 23(12). 5018–5035. 6 indexed citations

10.

Wang, Yiao, Carston R. Wagner, & Mark D. Distefano. (2022). Manipulating Cell Fates with Protein Conjugates. Bioconjugate Chemistry. 33(10). 1771–1784. 5 indexed citations

11.

Wang, Yiao, et al.. (2020). Engineering reversible cell–cell interactions using enzymatically lipidated chemically self-assembled nanorings. Chemical Science. 12(1). 331–340. 17 indexed citations

12.

Wang, Yiao, et al.. (2020). Anti-EGFR Fibronectin Bispecific Chemically Self-Assembling Nanorings (CSANs) Induce Potent T Cell-Mediated Antitumor Responses and Downregulation of EGFR Signaling and PD-1/PD-L1 Expression. Journal of Medicinal Chemistry. 63(18). 10235–10245. 8 indexed citations

13.

Zhang, Yi, et al.. (2019). Site-Selective Enzymatic Labeling of Designed Ankyrin Repeat Proteins Using Protein Farnesyltransferase. Methods in molecular biology. 2033. 207–219. 6 indexed citations

14.

Veglia, Gianluigi, et al.. (2018). Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor. Methods in enzymology on CD-ROM/Methods in enzymology. 614. 207–238. 2 indexed citations

15.

Palsuledesai, Charuta C., Joshua D. Ochocki, Todd W. Markowski, & Mark D. Distefano. (2014). A combination of metabolic labeling and 2D-DIGE analysis in response to a farnesyltransferase inhibitor facilitates the discovery of new prenylated proteins. Molecular BioSystems. 10(5). 1094–1103. 28 indexed citations

16.

Rashidian, Mohammad, et al.. (2012). Chemoenzymatic Reversible Immobilization and Labeling of Proteins without Prior Purification. Journal of the American Chemical Society. 134(20). 8455–8467. 82 indexed citations

17.

Mullen, Daniel G., et al.. (2012). Covalent protein–oligonucleotide conjugates by copper-free click reaction. Bioorganic & Medicinal Chemistry. 20(14). 4532–4539. 39 indexed citations

18.

Ochocki, Joshua D. & Mark D. Distefano. (2012). Prenyltransferase inhibitors: treating human ailments from cancer to parasitic infections. MedChemComm. 4(3). 476–492. 58 indexed citations

19.

Duckworth, Benjamin P., et al.. (2006). Selective Labeling of Proteins by Using Protein Farnesyltransferase. ChemBioChem. 8(1). 98–105. 98 indexed citations

20.

Miller, Susan M., Melissa J. Moore, Vincent Massey, et al.. (1989). Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 28(3). 1194–1205. 69 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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