Jack J. Skalicky

4.2k total citations · 1 hit paper
54 papers, 3.4k citations indexed

About

Jack J. Skalicky is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Jack J. Skalicky has authored 54 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 15 papers in Cell Biology and 7 papers in Organic Chemistry. Recurrent topics in Jack J. Skalicky's work include Protein Structure and Dynamics (11 papers), Nicotinic Acetylcholine Receptors Study (9 papers) and Chemical Synthesis and Analysis (8 papers). Jack J. Skalicky is often cited by papers focused on Protein Structure and Dynamics (11 papers), Nicotinic Acetylcholine Receptors Study (9 papers) and Chemical Synthesis and Analysis (8 papers). Jack J. Skalicky collaborates with scholars based in United States, Poland and Canada. Jack J. Skalicky's co-authors include Wesley I. Sundquist, Daryl A. Bosco, Dmitry M. Korzhnev, Dorothee Kern, Wladimir Labeikovsky, Óscar Millet, Elan Eisenmesser, Lewis E. Kay, Magnus Wolf‐Watz and P. Leslie Dutton and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Jack J. Skalicky

54 papers receiving 3.4k 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.

Intrinsic dynamics of an enzyme underlies catalysis

2005 883 citations Elan Eisenmesser, Óscar Millet et al. Nature profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jack J. Skalicky United States	31	2.6k	880	554	324	263	54	3.4k
Karyn T. O’Neil United States	27	3.6k 1.4×	361 0.4×	726 1.3×	275 0.8×	142 0.5×	53	4.4k
Perttu Permi Finland	35	2.0k 0.8×	585 0.7×	488 0.9×	564 1.7×	150 0.6×	147	3.6k
Alemayehu A. Gorfe United States	41	4.4k 1.7×	996 1.1×	738 1.3×	202 0.6×	375 1.4×	113	5.0k
Robert Fairman United States	38	3.5k 1.3×	497 0.6×	976 1.8×	259 0.8×	97 0.4×	102	4.4k
John H. Bushweller United States	44	4.9k 1.9×	657 0.7×	453 0.8×	503 1.6×	107 0.4×	113	6.1k
Ulf Diederichsen Germany	28	3.0k 1.1×	713 0.8×	275 0.5×	211 0.7×	200 0.8×	150	3.7k
Hidekazu Hiroaki Japan	30	2.5k 1.0×	473 0.5×	444 0.8×	271 0.8×	259 1.0×	98	3.3k
Igor Barsukov United Kingdom	38	2.4k 0.9×	1.9k 2.1×	222 0.4×	286 0.9×	206 0.8×	84	4.2k
Xiao Zhu United States	5	2.9k 1.1×	241 0.3×	635 1.1×	287 0.9×	144 0.5×	5	4.0k
Jay R. Knutson United States	32	2.5k 1.0×	422 0.5×	485 0.9×	390 1.2×	132 0.5×	123	4.2k

Countries citing papers authored by Jack J. Skalicky

Since Specialization

Citations

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

Fields of papers citing papers by Jack J. Skalicky

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jack J. Skalicky

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

Skalicky, Jack J., Frank G. Whitby, Douglas R. Mackay, et al.. (2023). The Calpain-7 protease functions together with the ESCRT-III protein IST1 within the midbody to regulate the timing and completion of abscission. eLife. 12. 5 indexed citations

Wenzel, Dawn M., et al.. (2022). Comprehensive analysis of the human ESCRT-III-MIT domain interactome reveals new cofactors for cytokinetic abscission. eLife. 11. 19 indexed citations

Sinha, Dhiraj, et al.. (2022). Mutations of Rad6 E2 ubiquitin-conjugating enzymes at alanine-126 in helix-3 affect ubiquitination activity and decrease enzyme stability. Journal of Biological Chemistry. 298(11). 102524–102524. 12 indexed citations

Zheng, Nan, Sean Christensen, Cheryl Dowell, et al.. (2021). Discovery of Methylene Thioacetal-Incorporated α-RgIA Analogues as Potent and Stable Antagonists of the Human α9α10 Nicotinic Acetylcholine Receptor for the Treatment of Neuropathic Pain. Journal of Medicinal Chemistry. 64(13). 9513–9524. 23 indexed citations

Davulcu, Omar, et al.. (2016). The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase. Structure. 24(10). 1658–1667. 8 indexed citations

Davulcu, Omar, et al.. (2015). Parsimony in Protein Conformational Change. Structure. 23(7). 1190–1198. 7 indexed citations

Davulcu, Omar, Xiaogang Niu, Lei Bruschweiler‐Li, et al.. (2013). Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form. Biomolecular NMR Assignments. 8(2). 335–338. 3 indexed citations

Platt, Randall J., Tiffany Han, Brad R. Green, et al.. (2012). Stapling Mimics Noncovalent Interactions of γ-Carboxyglutamates in Conantokins, Peptidic Antagonists of N-Methyl-d-Aspartic Acid Receptors. Journal of Biological Chemistry. 287(24). 20727–20736. 19 indexed citations

Walewska, Aleksandra, Minmin Zhang, Jack J. Skalicky, et al.. (2009). Integrated Oxidative Folding of Cysteine/Selenocysteine Containing Peptides: Improving Chemical Synthesis of Conotoxins. Angewandte Chemie International Edition. 48(12). 2221–2224. 78 indexed citations

10.

Davulcu, Omar, Peter F. Flynn, Michael S. Chapman, & Jack J. Skalicky. (2009). Intrinsic Domain and Loop Dynamics Commensurate with Catalytic Turnover in an Induced-Fit Enzyme. Structure. 17(10). 1356–1367. 24 indexed citations

11.

Kieffer, Collin, Jack J. Skalicky, Eiji Morita, et al.. (2008). Two Distinct Modes of ESCRT-III Recognition Are Required for VPS4 Functions in Lysosomal Protein Targeting and HIV-1 Budding. Developmental Cell. 15(1). 62–73. 137 indexed citations

12.

Stuchell‐Brereton, Melissa D., et al.. (2007). ESCRT-III recognition by VPS4 ATPases. Nature. 449(7163). 740–744. 269 indexed citations

13.

Schroeder, Kersten T., Jack J. Skalicky, & Nancy L. Greenbaum. (2005). NMR spectroscopy of RNA duplexes containing pseudouridine in supercooled water. RNA. 11(7). 1012–1016. 18 indexed citations

14.

Eisenmesser, Elan, Óscar Millet, Wladimir Labeikovsky, et al.. (2005). Intrinsic dynamics of an enzyme underlies catalysis. Nature. 438(7064). 117–121. 883 indexed citations breakdown →

15.

Daujotyte, D., Giedrius Vilkaitis, Laura Manelytė, et al.. (2003). Solubility engineering of the HhaI methyltransferase. Protein Engineering Design and Selection. 16(4). 295–301. 19 indexed citations

16.

Liu, Gaohua, Jeffrey Mills, Seho Kim, et al.. (2003). Resonance assignments for the 21 kDa engineered fluorescein-binding lipocalin FluA. Journal of Biomolecular NMR. 27(2). 187–188. 2 indexed citations

17.

Donaldson, Logan W., Lawrence P. McIntosh, Jack J. Skalicky, Jeannine M. Petersen, & Barbara J. Graves. (1996). Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets‐1. Protein Science. 5(2). 296–309. 58 indexed citations

18.

Evans, R J, John D. Childs, Guy Vigers, et al.. (1995). Mapping Receptor Binding Sites in Interleukin (IL)-1 Receptor Antagonist and IL-1β by Site-directed Mutagenesis. Journal of Biological Chemistry. 270(19). 11477–11483. 83 indexed citations

19.

Skalicky, Jack J., et al.. (1993). Solution structure of the calcium channel antagonist ω‐conotoxin GVIA. Protein Science. 2(10). 1591–1603. 34 indexed citations

20.

Pardi, Arthur, et al.. (1992). NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. Biochemistry. 31(46). 11357–11364. 97 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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