Mark J. Snider

2.2k total citations · 1 hit paper
48 papers, 1.9k citations indexed

About

Mark J. Snider is a scholar working on Molecular Biology, Materials Chemistry and Epidemiology. According to data from OpenAlex, Mark J. Snider has authored 48 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 10 papers in Materials Chemistry and 8 papers in Epidemiology. Recurrent topics in Mark J. Snider's work include Biochemical and Molecular Research (12 papers), Enzyme Structure and Function (9 papers) and Herpesvirus Infections and Treatments (7 papers). Mark J. Snider is often cited by papers focused on Biochemical and Molecular Research (12 papers), Enzyme Structure and Function (9 papers) and Herpesvirus Infections and Treatments (7 papers). Mark J. Snider collaborates with scholars based in United States, Canada and Netherlands. Mark J. Snider's co-authors include Richard Wolfenden, Brian G. Miller, Steven A. Short, Lorne A. Babiuk, Maria E. Baca‐Estrada, R. Norris Wolfenden, Dean Fraga, Stefan Gaunitz, Sylvia van Drunen Littel‐van den Hurk and Marianna Földvári and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Mark J. Snider

43 papers receiving 1.8k 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.

The Depth of Chemical Time and the Power of Enzymes as Catalysts

2001 737 citations Richard Wolfenden, Mark J. Snider profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Mark J. Snider United States	19	1.2k	436	233	197	177	48	1.9k
Anna Roujeinikova Australia	27	1.5k 1.3×	272 0.6×	398 1.7×	143 0.7×	108 0.6×	79	2.6k
Alejandro Panjkovich Germany	16	1.9k 1.6×	614 1.4×	125 0.5×	146 0.7×	91 0.5×	23	2.6k
Piotr Neumann Germany	31	2.2k 1.9×	322 0.7×	164 0.7×	121 0.6×	149 0.8×	87	2.8k
Rajan Sankaranarayanan India	30	2.4k 2.1×	363 0.8×	223 1.0×	162 0.8×	99 0.6×	94	2.9k
Kurt L. Krause United States	27	1.5k 1.3×	716 1.6×	187 0.8×	81 0.4×	176 1.0×	77	2.3k
Hideo Ago Japan	25	2.0k 1.7×	668 1.5×	114 0.5×	159 0.8×	171 1.0×	56	3.1k
Martin Högbom Sweden	31	2.3k 1.9×	499 1.1×	251 1.1×	106 0.5×	104 0.6×	103	3.3k
Bjørn Olav Brandsdal Norway	31	2.2k 1.9×	669 1.5×	357 1.5×	161 0.8×	74 0.4×	65	3.1k
M. Cristina Vega Spain	25	1.2k 1.0×	383 0.9×	135 0.6×	157 0.8×	54 0.3×	85	1.8k
Alice Vrielink Australia	30	2.5k 2.1×	563 1.3×	206 0.9×	110 0.6×	103 0.6×	86	3.3k

Countries citing papers authored by Mark J. Snider

Since Specialization

Citations

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

Fields of papers citing papers by Mark J. Snider

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark J. Snider

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

Perry, Kay, et al.. (2023). Ligand bound structure of a 6‐hydroxynicotinic acid 3‐monooxygenase provides mechanistic insights. Archives of Biochemistry and Biophysics. 752. 109859–109859.

Snider, Mark J., et al.. (2020). Two cryptosporidia species encode active creatine kinases that are not seen in other apicomplexa species. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 246-247. 110459–110459. 2 indexed citations

Fraga, Dean, et al.. (2019). Bacterial arginine kinases have a highly skewed distribution within the proteobacteria. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 233. 60–71. 1 indexed citations

Nakamoto, Kent, et al.. (2019). Mechanism of 6-Hydroxynicotinate 3-Monooxygenase, a Flavin-Dependent Decarboxylative Hydroxylase Involved in Bacterial Nicotinic Acid Degradation. Biochemistry. 58(13). 1751–1763. 9 indexed citations

Fraga, Dean, et al.. (2015). Characterization of the arginine kinase isoforms in Caenorhabditis elegans. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 187. 85–101. 10 indexed citations

Palmer, Allyson K., et al.. (2013). Characterization of a putative oomycete taurocyamine kinase: Implications for the evolution of the phosphagen kinase family. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 166(3-4). 173–181. 14 indexed citations

Bragg, Jason G., Aleksandar Rajkovic, Carl W. Anderson, et al.. (2012). Identification and Characterization of a Putative Arginine Kinase Homolog from Myxococcus xanthus Required for Fruiting Body Formation and Cell Differentiation. Journal of Bacteriology. 194(10). 2668–2676. 27 indexed citations

Labiuk, Shaunivan, et al.. (2009). Bovine herpesvirus-1 US3 protein kinase: critical residues and involvement in the phosphorylation of VP22. Journal of General Virology. 91(5). 1117–1126. 12 indexed citations

Andrews, Logan D., et al.. (2008). Characterization of a novel bacterial arginine kinase from Desulfotalea psychrophila. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 150(3). 312–319. 43 indexed citations

10.

Hurk, Sylvia van Drunen Littel‐van den, et al.. (2008). Strategies for induction of protective immunity to bovine herpesvirus-1 in newborn calves with maternal antibodies. Vaccine. 26(25). 3103–3111. 13 indexed citations

11.

Clarke, Callisia N., et al.. (2007). Changing the substrate specificity of creatine kinase from creatine to glycocyamine: Evidence for a highly evolved active site. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774(12). 1519–1527. 13 indexed citations

12.

Thomenius, Michael J., et al.. (2005). Transition state stabilization by six arginines clustered in the active site of creatine kinase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1751(2). 178–183. 11 indexed citations

13.

Snider, Mark J., Brenda Temple, & Richard Wolfenden. (2004). The path to the transition state in enzyme reactions: a survey of catalytic efficiencies. Journal of Physical Organic Chemistry. 17(6-7). 586–591. 32 indexed citations

14.

Borders, C.L., et al.. (2003). Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase. Protein Science. 12(3). 532–537. 8 indexed citations

15.

Miller, Brian G., Mark J. Snider, Richard Wolfenden, & Steven A. Short. (2001). Dissecting a Charged Network at the Active Site of Orotidine-5′-phosphate Decarboxylase. Journal of Biological Chemistry. 276(18). 15174–15176. 45 indexed citations

16.

Wolfenden, R. Norris, et al.. (1999). The Temperature Dependence of Enzyme Rate Enhancements. Journal of the American Chemical Society. 121(32). 7419–7420. 109 indexed citations

17.

Baca‐Estrada, Maria E., Marianna Földvári, Mark J. Snider, Sylvia van Drunen Littel‐van den Hurk, & Lorne A. Babiuk. (1997). Effect of IL-4 and IL-12 liposomal formulations on the induction of immune response to bovine herpesvirus type-1 glycoprotein D. Vaccine. 15(16). 1753–1760. 44 indexed citations

18.

Baca‐Estrada, Maria E., Mark J. Snider, Suresh K. Tikoo, et al.. (1996). Immunogenicity of Bovine Herpes virus 1 Glycoprotein D in Mice: Effect of Antigen Form on the Induction of Cellular and Humoral Immune Responses. Viral Immunology. 9(1). 11–22. 30 indexed citations

19.

Sordillo, Lorraine M., et al.. (1991). Pathological Changes in Bovine Mammary Glands Following Intramammary Infusion of Recombinant Interleukin-2. Journal of Dairy Science. 74(12). 4164–4174. 23 indexed citations

20.

Fitzpatrick, David, et al.. (1990). Molecular mimicry: a herpes virus glycoprotein antigenically related to a cell-surface glycoprotein expressed by macrophages, polymorphonuclear leucocytes, and platelets.. PubMed. 70(4). 504–12. 17 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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