J. Mack

2.0k total citations
23 papers, 1.4k citations indexed

About

J. Mack is a scholar working on Molecular Biology, Materials Chemistry and Epidemiology. According to data from OpenAlex, J. Mack has authored 23 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 4 papers in Materials Chemistry and 3 papers in Epidemiology. Recurrent topics in J. Mack's work include Protein Structure and Dynamics (5 papers), Cell death mechanisms and regulation (4 papers) and Enzyme Structure and Function (4 papers). J. Mack is often cited by papers focused on Protein Structure and Dynamics (5 papers), Cell death mechanisms and regulation (4 papers) and Enzyme Structure and Function (4 papers). J. Mack collaborates with scholars based in United States, South Africa and Denmark. J. Mack's co-authors include Stephen W. Fesik, Philip J. Hajduk, Edward T. Olejniczak, Stephen F. Betz, Renaldo Mendoza, Haichao Zhang, Liping Yu, Robert Meadows, Edmund D. Matayoshi and Kerry M. Swift and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and PLoS ONE.

In The Last Decade

J. Mack

22 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J. Mack United States 19 1.1k 197 195 195 148 23 1.4k
Jun‐Goo Jee South Korea 23 1.2k 1.1× 135 0.7× 228 1.2× 180 0.9× 149 1.0× 65 1.9k
Kellon Belfon United States 5 1.1k 1.0× 191 1.0× 232 1.2× 242 1.2× 116 0.8× 6 1.5k
Karim M. ElSawy United Kingdom 11 1.2k 1.1× 174 0.9× 211 1.1× 236 1.2× 76 0.5× 26 1.7k
Lauren Raguette United States 5 1.1k 1.0× 191 1.0× 228 1.2× 243 1.2× 115 0.8× 7 1.6k
Lukáš Pravda Czechia 10 1.3k 1.2× 204 1.0× 255 1.3× 203 1.0× 82 0.6× 23 1.9k
Andras Boeszoermenyi United States 19 923 0.8× 97 0.5× 153 0.8× 254 1.3× 110 0.7× 28 1.5k
Jayashree Srinivasan United States 11 1.7k 1.6× 158 0.8× 310 1.6× 380 1.9× 147 1.0× 16 2.2k
David T. Barkan United States 12 1.4k 1.3× 139 0.7× 146 0.7× 175 0.9× 158 1.1× 16 1.9k
Irene Luque Spain 27 1.4k 1.3× 223 1.1× 406 2.1× 302 1.5× 82 0.6× 65 2.2k

Countries citing papers authored by J. Mack

Since Specialization
Citations

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

Fields of papers citing papers by J. Mack

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Mack

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

All Works

20 of 20 papers shown
1.
2.
Chang, Changsoo, Charles Brooke, Hailan Piao, et al.. (2019). A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315. Protein Science. 28(4). 794–799. 5 indexed citations
3.
Lohman, Jeremy R., Ming Ma, J. Osipiuk, et al.. (2015). Structural and evolutionary relationships of “AT-less” type I polyketide synthase ketosynthases. Proceedings of the National Academy of Sciences. 112(41). 12693–12698. 51 indexed citations
4.
Nocek, B., M. Makowska-Grzyska, R. Jedrzejczak, et al.. (2014). The Dimerization Domain in DapE Enzymes Is required for Catalysis. PLoS ONE. 9(5). e93593–e93593. 20 indexed citations
5.
Tan, Kemin, Changsoo Chang, M.E. Cuff, et al.. (2013). Structural and functional characterization of solute binding proteins for aromatic compounds derived from lignin:p-Coumaric acid and related aromatic acids. Proteins Structure Function and Bioinformatics. 81(10). 1709–1726. 19 indexed citations
6.
Pokkuluri, P. Raj, N.E.C. Duke, Rosemarie Wilton, et al.. (2013). Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2CP‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein. MicrobiologyOpen. 2(5). 766–777. 10 indexed citations
7.
Michalska, K., et al.. (2012). Characterization of Transport Proteins for Aromatic Compounds Derived from Lignin: Benzoate Derivative Binding Proteins. Journal of Molecular Biology. 423(4). 555–575. 26 indexed citations
8.
Makowska-Grzyska, M., Youngchang Kim, Ruiying Wu, et al.. (2012). Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes. Biochemistry. 51(31). 6148–6163. 29 indexed citations
9.
Petros, Andrew M., Jeffrey R. Huth, Thorsten Oost, et al.. (2010). Discovery of a potent and selective Bcl-2 inhibitor using SAR by NMR. Bioorganic & Medicinal Chemistry Letters. 20(22). 6587–6591. 51 indexed citations
10.
Yu, Liping, Philip J. Hajduk, J. Mack, & Edward T. Olejniczak. (2006). Structural Studies of Bcl-xL/ligand Complexes using 19F NMR. Journal of Biomolecular NMR. 34(4). 221–227. 22 indexed citations
11.
Huth, Jeffrey R., Liping Yu, Irene Collins, et al.. (2004). NMR-Driven Discovery of Benzoylanthranilic Acid Inhibitors of Far Upstream Element Binding Protein Binding to the Human Oncogene c-myc Promoter. Journal of Medicinal Chemistry. 47(20). 4851–4857. 32 indexed citations
12.
Zech, Stephan G., Edward T. Olejniczak, Philip J. Hajduk, J. Mack, & Ann E. McDermott. (2004). Characterization of Protein−Ligand Interactions by High-Resolution Solid-State NMR Spectroscopy. Journal of the American Chemical Society. 126(43). 13948–13953. 33 indexed citations
13.
Hajduk, Philip J., J. Mack, Edward T. Olejniczak, et al.. (2004). SOS-NMR:  A Saturation Transfer NMR-Based Method for Determining the Structures of Protein−Ligand Complexes. Journal of the American Chemical Society. 126(8). 2390–2398. 71 indexed citations
14.
Yu, Liping, J. Mack, Philip J. Hajduk, et al.. (2003). Solution structure and function of an essential CMP kinase of Streptococcus pneumoniae. Protein Science. 12(11). 2613–2621. 18 indexed citations
15.
Hajduk, Philip J., Stephen F. Betz, J. Mack, et al.. (2002). A Strategy for High-Throughput Assay Development Using Leads Derived from Nuclear Magnetic Resonance-Based Screening. SLAS DISCOVERY. 7(5). 429–432. 22 indexed citations
16.
Yu, Liping, Angelo Gunasekera, J. Mack, et al.. (2001). Solution structure and function of a conserved protein SP14.3 encoded by an essential Streptococcus pneumoniae gene 1 1Edited by M. F. Summers. Journal of Molecular Biology. 311(3). 593–604. 18 indexed citations
17.
Nettesheim, David G., Yi Wang, Edward T. Olejniczak, et al.. (2000). Rationale for Bcl‐XL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Science. 9(12). 2528–2534. 334 indexed citations
18.
Losonczi, Judit A., Edward T. Olejniczak, Stephen F. Betz, et al.. (2000). NMR Studies of the Anti-Apoptotic Protein Bcl-xL in Micelles. Biochemistry. 39(36). 11024–11033. 84 indexed citations
19.
Medek, A, Philip J. Hajduk, J. Mack, & Stephen W. Fesik. (2000). The Use of Differential Chemical Shifts for Determining the Binding Site Location and Orientation of Protein-Bound Ligands. Journal of the American Chemical Society. 122(6). 1241–1242. 83 indexed citations
20.
Colussi, Paul A., Christopher H. Taron, J. Mack, & Peter Orlean. (1997). Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe. Proceedings of the National Academy of Sciences. 94(15). 7873–7878. 66 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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