James C. Sacchettini

30.7k total citations · 3 hit papers
292 papers, 23.4k citations indexed

About

James C. Sacchettini is a scholar working on Molecular Biology, Infectious Diseases and Materials Chemistry. According to data from OpenAlex, James C. Sacchettini has authored 292 papers receiving a total of 23.4k indexed citations (citations by other indexed papers that have themselves been cited), including 204 papers in Molecular Biology, 113 papers in Infectious Diseases and 76 papers in Materials Chemistry. Recurrent topics in James C. Sacchettini's work include Tuberculosis Research and Epidemiology (103 papers), Enzyme Structure and Function (72 papers) and Biochemical and Molecular Research (65 papers). James C. Sacchettini is often cited by papers focused on Tuberculosis Research and Epidemiology (103 papers), Enzyme Structure and Function (72 papers) and Biochemical and Molecular Research (65 papers). James C. Sacchettini collaborates with scholars based in United States, United Kingdom and Germany. James C. Sacchettini's co-authors include Thomas R. Ioerger, Jeffrey I. Gordon, Li‐Wei Hung, Thomas C. Terwilliger, Ralf W. Grosse‐Kunstleve, Paul D. Adams, Airlie J. McCoy, Randy J. Read, Nigel W. Moriarty and Nicholas K. Sauter and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

James C. Sacchettini

288 papers receiving 23.1k citations

Hit Papers

PHENIX: building new soft... 1998 2026 2007 2016 2002 1998 2013 1000 2.0k 3.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James C. Sacchettini United States 81 14.9k 5.5k 4.1k 2.9k 2.4k 292 23.4k
Li‐Wei Hung United States 30 21.2k 1.4× 2.5k 0.5× 1.9k 0.5× 5.5k 1.9× 2.5k 1.1× 68 29.4k
Ian Davis United States 23 20.8k 1.4× 2.4k 0.4× 1.9k 0.5× 5.3k 1.9× 2.2k 0.9× 56 28.9k
Gary J. Kapral United States 11 25.5k 1.7× 3.0k 0.5× 2.3k 0.6× 6.3k 2.2× 2.7k 1.1× 12 35.1k
Vincent B. Chen United States 16 25.3k 1.7× 3.0k 0.6× 2.3k 0.6× 6.3k 2.2× 2.7k 1.2× 22 35.1k
Wim G. J. Hol United States 82 15.6k 1.1× 1.6k 0.3× 2.4k 0.6× 3.9k 1.4× 1.7k 0.7× 316 23.2k
Nathaniel Echols United States 30 20.1k 1.4× 2.3k 0.4× 1.7k 0.4× 5.8k 2.0× 2.1k 0.9× 43 27.5k
Peter H. Zwart United States 31 20.6k 1.4× 2.3k 0.4× 1.8k 0.4× 6.0k 2.1× 2.2k 0.9× 60 28.6k
Lorenza Bordoli Switzerland 20 15.3k 1.0× 2.0k 0.4× 1.6k 0.4× 1.7k 0.6× 1.3k 0.5× 23 24.1k
Nigel W. Moriarty United States 35 26.8k 1.8× 3.2k 0.6× 2.4k 0.6× 7.8k 2.7× 2.9k 1.2× 77 37.9k
Jeffrey J. Headd United States 17 28.2k 1.9× 3.3k 0.6× 2.5k 0.6× 7.4k 2.6× 3.1k 1.3× 20 39.1k

Countries citing papers authored by James C. Sacchettini

Since Specialization
Citations

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

Fields of papers citing papers by James C. Sacchettini

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James C. Sacchettini. 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 James C. Sacchettini. The network helps show where James C. Sacchettini may publish in the future.

Co-authorship network of co-authors of James C. Sacchettini

This figure shows the co-authorship network connecting the top 25 collaborators of James C. Sacchettini. A scholar is included among the top collaborators of James C. Sacchettini 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 James C. Sacchettini. James C. Sacchettini 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.
Qu, Di, Peng Ge, Laure Botella, et al.. (2024). Mycobacterial biotin synthases require an auxiliary protein to convert dethiobiotin into biotin. Nature Communications. 15(1). 4161–4161. 3 indexed citations
2.
Zhu, Mingzhao, Kenneth G. Hull, Daniel Romo, et al.. (2021). Second-Shell Amino Acid R266 Helps Determine N-Succinylamino Acid Racemase Reaction Specificity in Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Enzymes. Biochemistry. 60(50). 3829–3840. 4 indexed citations
3.
Rifat, Dalin, Si-Yang Li, Thomas R. Ioerger, et al.. (2020). Mutations in fbiD ( Rv2983 ) as a Novel Determinant of Resistance to Pretomanid and Delamanid in Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy. 65(1). 56 indexed citations
4.
Jansen, Robert S., Shoko Wakabayashi, Jessica T. Pinkham, et al.. (2020). Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis. Nature Communications. 11(1). 1960–1960. 48 indexed citations
5.
Gülten, Gülçin, Anup Aggarwal, Inna V. Krieger, et al.. (2020). A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins. eLife. 9. 9 indexed citations
6.
Chen, Qingquan, Kush N. Shah, Fuwu Zhang, et al.. (2019). Minocycline and Silver Dual-Loaded Polyphosphoester-Based Nanoparticles for Treatment of Resistant Pseudomonas aeruginosa. Molecular Pharmaceutics. 16(4). 1606–1619. 22 indexed citations
7.
Krieger, Inna V., et al.. (2019). A DNA-Binding Protein Tunes Septum Placement during Bacillus subtilis Sporulation. Journal of Bacteriology. 201(16). 6 indexed citations
8.
Carey, Allison F., Jeremy M. Rock, Inna V. Krieger, et al.. (2018). TnSeq of Mycobacterium tuberculosis clinical isolates reveals strain-specific antibiotic liabilities. PLoS Pathogens. 14(3). e1006939–e1006939. 64 indexed citations
9.
Murkin, Andrew S., et al.. (2017). Mechanism-based inactivator of isocitrate lyases 1 and 2 from Mycobacterium tuberculosis. Proceedings of the National Academy of Sciences. 114(29). 7617–7622. 32 indexed citations
10.
Lehmann, Johannes, Tan‐Yun Cheng, Anup Aggarwal, et al.. (2017). Ein antibakterielles β‐Lacton bekämpft Mycobacterium tuberculosis durch Infiltration der Mykolsäurebiosynthese. Angewandte Chemie. 130(1). 354–359. 3 indexed citations
11.
Odingo, Joshua, Theresa O’Malley, Edward A. Kesicki, et al.. (2014). Synthesis and evaluation of the 2,4-diaminoquinazoline series as anti-tubercular agents. Bioorganic & Medicinal Chemistry. 22(24). 6965–6979. 26 indexed citations
12.
Nixon, Molly R, Kurt W. Saionz, Mi-Sun Koo, et al.. (2014). Folate Pathway Disruption Leads to Critical Disruption of Methionine Derivatives in Mycobacterium tuberculosis. Chemistry & Biology. 21(7). 819–830. 58 indexed citations
13.
Gülten, Gülçin & James C. Sacchettini. (2013). Structure of the Mtb CarD/RNAP β-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD. Structure. 21(10). 1859–1869. 31 indexed citations
14.
Kong, Ying, Hequan Yao, Hongjun Ren, et al.. (2010). Imaging tuberculosis with endogenous β-lactamase reporter enzyme fluorescence in live mice. Proceedings of the National Academy of Sciences. 107(27). 12239–12244. 157 indexed citations
15.
Barkan, Daniel, Zhen Liu, James C. Sacchettini, & Michael S. Glickman. (2009). Mycolic Acid Cyclopropanation is Essential for Viability, Drug Resistance, and Cell Wall Integrity of Mycobacterium tuberculosis. Chemistry & Biology. 16(5). 499–509. 93 indexed citations
16.
Gopal, Kreshna, Tod D. Romo, Erik McKee, et al.. (2005). TEXTAL™: automated crystallographic protein structure determination. Innovative Applications of Artificial Intelligence. 1483–1490. 1 indexed citations
17.
Xu, Min, et al.. (2005). Disulfide Isomerization After Membrane Release of Its SAR Domain Activates P1 Lysozyme. Science. 307(5706). 113–117. 116 indexed citations
18.
Ronning, Donald R., Varalakshmi Vissa, Gurdyal S. Besra, John T. Belisle, & James C. Sacchettini. (2004). Mycobacterium tuberculosis Antigen 85A and 85C Structures Confirm Binding Orientation and Conserved Substrate Specificity. Journal of Biological Chemistry. 279(35). 36771–36777. 73 indexed citations
19.
Baier, Leslie J., James C. Sacchettini, William C. Knowler, et al.. (1995). An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance.. Journal of Clinical Investigation. 95(3). 1281–1287. 307 indexed citations
20.
Scapin, Giovanna, Aideen C. M. Young, Arno Kromminga, et al.. (1993). High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid: protein interactions. Molecular and Cellular Biochemistry. 123(1-2). 3–13. 32 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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