David L. Tierney

4.7k total citations
114 papers, 3.5k citations indexed

About

David L. Tierney is a scholar working on Molecular Medicine, Molecular Biology and Oncology. According to data from OpenAlex, David L. Tierney has authored 114 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Medicine, 25 papers in Molecular Biology and 23 papers in Oncology. Recurrent topics in David L. Tierney's work include Antibiotic Resistance in Bacteria (31 papers), Metal complexes synthesis and properties (19 papers) and Magnetism in coordination complexes (15 papers). David L. Tierney is often cited by papers focused on Antibiotic Resistance in Bacteria (31 papers), Metal complexes synthesis and properties (19 papers) and Magnetism in coordination complexes (15 papers). David L. Tierney collaborates with scholars based in United States, Argentina and China. David L. Tierney's co-authors include Michael W. Crowder, Robert M. Breece, Alison L. Costello, James E. Penner‐Hahn, Walter Fast, Brian Bennett, Brian M. Hoffman, Mahesh Aitha, Pei W. Thomas and Everett Stone 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

David L. Tierney

110 papers receiving 3.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David L. Tierney United States 35 1.1k 1.0k 644 586 574 114 3.5k
Stefano Mangani Italy 41 2.6k 2.5× 955 0.9× 631 1.0× 1.2k 2.0× 1.0k 1.7× 165 5.9k
Michael W. Crowder United States 40 1.6k 1.5× 2.4k 2.3× 284 0.4× 592 1.0× 394 0.7× 134 4.6k
Nataša Mitić Australia 29 978 0.9× 342 0.3× 644 1.0× 858 1.5× 336 0.6× 52 2.4k
Winfried Hinrichs Germany 33 2.1k 2.0× 359 0.4× 292 0.5× 333 0.6× 734 1.3× 113 3.5k
Caroline Kisker Germany 52 5.7k 5.4× 483 0.5× 931 1.4× 727 1.2× 979 1.7× 139 8.7k
Grant K. Walkup United States 16 1.9k 1.8× 1.0k 1.0× 110 0.2× 408 0.7× 762 1.3× 25 4.3k
Dingguo Xu China 28 1.0k 1.0× 353 0.3× 480 0.7× 172 0.3× 899 1.6× 158 3.3k
Elizabeth M. Nolan United States 45 4.3k 4.1× 630 0.6× 321 0.5× 423 0.7× 3.1k 5.4× 116 9.0k
Richard S. Magliozzo United States 32 1.2k 1.1× 358 0.4× 353 0.5× 319 0.5× 308 0.5× 71 3.4k
Małgorzata Jeżowska‐Bojczuk Poland 28 1.0k 1.0× 170 0.2× 348 0.5× 908 1.5× 253 0.4× 106 2.4k

Countries citing papers authored by David L. Tierney

Since Specialization
Citations

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

Fields of papers citing papers by David L. Tierney

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David L. Tierney. 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 David L. Tierney. The network helps show where David L. Tierney may publish in the future.

Co-authorship network of co-authors of David L. Tierney

This figure shows the co-authorship network connecting the top 25 collaborators of David L. Tierney. A scholar is included among the top collaborators of David L. Tierney 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 David L. Tierney. David L. Tierney 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.
Marts, Amy R., et al.. (2023). Field- and Temperature-Dependent Paramagnetic Relaxation Enhancements in Co(II) Trispyrazolylmethanes. Inorganic Chemistry. 62(39). 15952–15962.
2.
Tierney, David L., et al.. (2023). Beyond the individual: Sexual minority help-seeking and the consequences of structural barriers.. Journal of Counseling Psychology. 70(2). 133–145. 10 indexed citations
3.
Zhang, Huan, Kundi Yang, Zishuo Cheng, et al.. (2021). Spectroscopic and biochemical characterization of metallo-β-lactamase IMP-1 with dicarboxylic, sulfonyl, and thiol inhibitors. Bioorganic & Medicinal Chemistry. 40. 116183–116183. 5 indexed citations
4.
5.
Cheng, Zishuo, Kundi Yang, Stacey Lowery Bretz, et al.. (2020). An integrated biophysical approach to discovering mechanisms of NDM-1 inhibition for several thiol-containing drugs. JBIC Journal of Biological Inorganic Chemistry. 25(5). 717–727. 8 indexed citations
6.
Cheng, Zishuo, Christopher R. Bethel, Huan Zhang, et al.. (2018). A Noncanonical Metal Center Drives the Activity of the Sediminispirochaeta smaragdinae Metallo-β-lactamase SPS-1. Biochemistry. 57(35). 5218–5229. 11 indexed citations
7.
McCarrick, Robert M., et al.. (2017). Trispyrazolylborate Complexes: An Advanced Synthesis Experiment Using Paramagnetic NMR, Variable-Temperature NMR, and EPR Spectroscopies. Journal of Chemical Education. 94(12). 1960–1964. 4 indexed citations
8.
Bethel, Christopher R., Zishuo Cheng, Cameron Williams, et al.. (2017). Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity. ACS Infectious Diseases. 3(12). 927–940. 54 indexed citations
9.
Pedroso, Marcelo Monteiro, Jeffrey R. Harmer, Nataša Mitić, et al.. (2017). Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community. Metallomics. 9(8). 1157–1168. 15 indexed citations
10.
Neves, Ademir, Rosely A. Peralta, Elene C. Pereira‐Maia, et al.. (2017). Second-Sphere Effects in Dinuclear FeIIIZnII Hydrolase Biomimetics: Tuning Binding and Reactivity Properties. Inorganic Chemistry. 57(1). 187–203. 32 indexed citations
11.
Chen, Allie Y., Pei W. Thomas, Zishuo Cheng, et al.. (2017). Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1. Journal of Medicinal Chemistry. 60(17). 7267–7283. 128 indexed citations
12.
Cheng, Zishuo, Hao Yang, Mahesh Aitha, et al.. (2017). Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7. ACS Infectious Diseases. 4(2). 135–145. 47 indexed citations
13.
Pedroso, Marcelo Monteiro, Jeffrey R. Harmer, Lawrence R. Gahan, et al.. (2017). Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents. Dalton Transactions. 46(39). 13194–13201. 6 indexed citations
14.
Marts, Amy R., David P. Martin, Robert M. McCarrick, et al.. (2017). Substituent Effects on the Coordination Chemistry of Metal-Binding Pharmacophores. Inorganic Chemistry. 56(19). 11721–11728. 2 indexed citations
15.
Lisa, María‐Natalia, Mahesh Aitha, Mariano M. González, et al.. (2017). A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases. Nature Communications. 8(1). 538–538. 105 indexed citations
16.
Marts, Amy R., Robert M. McCarrick, Abed Hasheminasab, et al.. (2016). Paramagnetic Resonance of Cobalt(II) Trispyrazolylmethanes and Counterion Association. Inorganic Chemistry. 56(1). 618–626. 6 indexed citations
17.
Tierney, David L. & Gerhard Schenk. (2014). X-Ray Absorption Spectroscopy of Dinuclear Metallohydrolases. Biophysical Journal. 107(6). 1263–1272. 13 indexed citations
18.
Byrne, David, et al.. (2013). A Statistical Dead-Time Deconvolution Method for Fermi/GBM TGF Observations. EGUGA. 1 indexed citations
19.
Breece, Robert M., et al.. (2012). X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus. Journal of Inorganic Biochemistry. 111. 182–186. 11 indexed citations
20.
Thomas, Pei W., et al.. (2005). THE QUORUM-QUENCHING LACTONASE FROM BACILLUS THURINGIENSIS IS A METALLOPROTEIN. Macromolecules. 38. 1 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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