Robert M. Breece

781 total citations
18 papers, 661 citations indexed

About

Robert M. Breece is a scholar working on Molecular Biology, Oncology and Molecular Medicine. According to data from OpenAlex, Robert M. Breece has authored 18 papers receiving a total of 661 indexed citations (citations by other indexed papers that have themselves been cited), including 6 papers in Molecular Biology, 4 papers in Oncology and 4 papers in Molecular Medicine. Recurrent topics in Robert M. Breece's work include Trace Elements in Health (4 papers), Antibiotic Resistance in Bacteria (4 papers) and Metal complexes synthesis and properties (3 papers). Robert M. Breece is often cited by papers focused on Trace Elements in Health (4 papers), Antibiotic Resistance in Bacteria (4 papers) and Metal complexes synthesis and properties (3 papers). Robert M. Breece collaborates with scholars based in United States, Poland and France. Robert M. Breece's co-authors include David L. Tierney, Michael W. Crowder, Brian Bennett, Amit R. Reddi, Brian R. Gibney, F.E. Jacobsen, Seth M. Cohen, George Georgiou, Brent L. Iverson and Everett Stone and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Robert M. Breece

18 papers receiving 656 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Robert M. Breece United States	14	267	141	123	120	92	18	661
Alison L. Costello United States	14	214 0.8×	85 0.6×	218 1.8×	37 0.3×	152 1.7×	18	589
Dheeraj Khare United States	11	710 2.7×	393 2.8×	159 1.3×	137 1.1×	95 1.0×	14	1.1k
Julia A. Cricco Argentina	13	333 1.2×	78 0.6×	215 1.7×	42 0.3×	38 0.4×	25	659
Kamila Stokowa‐Sołtys Poland	12	231 0.9×	116 0.8×	36 0.3×	49 0.4×	36 0.4×	38	501
Adriana Badarau United Kingdom	18	326 1.2×	100 0.7×	257 2.1×	181 1.5×	41 0.4×	28	808
Cecilia Pozzi Italy	18	536 2.0×	120 0.9×	303 2.5×	194 1.6×	145 1.6×	55	1.2k
C.G. Suresh India	19	742 2.8×	164 1.2×	34 0.3×	61 0.5×	279 3.0×	76	1.2k
E.M. Duguid United States	10	727 2.7×	75 0.5×	73 0.6×	27 0.2×	79 0.9×	13	906
P.T. Erskine United Kingdom	21	929 3.5×	77 0.5×	32 0.3×	94 0.8×	342 3.7×	49	1.3k
J.P. Bacik United States	17	615 2.3×	71 0.5×	38 0.3×	23 0.2×	98 1.1×	28	906

Countries citing papers authored by Robert M. Breece

Since Specialization

Citations

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

Fields of papers citing papers by Robert M. Breece

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert M. Breece. 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 Robert M. Breece. The network helps show where Robert M. Breece may publish in the future.

Co-authorship network of co-authors of Robert M. Breece

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

All Works

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18 of 18 papers shown

1.

Myers, William K., et al.. (2016). The Original CoII Heteroscorpionates Revisited: On the EPR of Pseudotetrahedral CoII. European Journal of Inorganic Chemistry. 2016(15-16). 2641–2647. 2 indexed citations

2.

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

3.

Gunasekera, Thusitha S., et al.. (2011). Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli. Journal of Inorganic Biochemistry. 111. 164–172. 35 indexed citations

4.

Marts, Amy R., Samuel M. Greer, Robert M. Breece, et al.. (2011). Dual Mode EPR Studies of a Kramers ion: High-Spin Co(II) in 4-, 5- and 6-Coordination. Applied Magnetic Resonance. 40(4). 501–511. 18 indexed citations

5.

Moller, Abraham, et al.. (2011). Structural and Kinetic Studies on Metallo-β-lactamase IMP-1. Biochemistry. 50(42). 9125–9134. 38 indexed citations

6.

Stone, Everett, Evan S. Glazer, Lynne Chantranupong, et al.. (2010). Replacing Mn²⁺ with Co²⁺ in Human Arginase I Enhances Cytotoxicity toward l-Arginine Auxotrophic Cancer Cell Lines. ACS Chemical Biology. 5(3). 333–342. 94 indexed citations

7.

Stone, Everett, Evan S. Glazer, Lynne Chantranupong, et al.. (2010). Replacing Mn²⁺ with Co²⁺ in Human Arginase I Enhances Cytotoxicity toward l-Arginine Auxotrophic Cancer Cell Lines. ACS Chemical Biology. 5(8). 797–797. 5 indexed citations

8.

Li, Zhimin, Zhengang Liu, Dae Won Cho, et al.. (2010). Rational design, synthesis and evaluation of first generation inhibitors of the Giardia lamblia fructose-1,6-biphosphate aldolase. Journal of Inorganic Biochemistry. 105(4). 509–517. 22 indexed citations

9.

Mukherjee, Madhumita, et al.. (2010). Nanometer to Millimeter Scale Peptide-Porphyrin Materials. Biomacromolecules. 11(10). 2602–2609. 22 indexed citations

10.

Breece, Robert M., et al.. (2009). Motion of the Zinc Ions in Catalysis by a Dizinc Metallo-β-Lactamase. Journal of the American Chemical Society. 131(33). 11642–11643. 27 indexed citations

11.

Breece, Robert M., Christine E. Hajdin, Alison L. Costello, et al.. (2009). Differential Binding of Co(II) and Zn(II) to Metallo-β-Lactamase Bla2 from Bacillus anthracis. Journal of the American Chemical Society. 131(30). 10753–10762. 40 indexed citations

12.

Yatsunyk, Liliya A., Brian Bennett, Robert M. Breece, et al.. (2007). Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. JBIC Journal of Biological Inorganic Chemistry. 13(2). 271–288. 92 indexed citations

13.

Reddi, Amit R., et al.. (2007). Deducing the Energetic Cost of Protein Folding in Zinc Finger Proteins Using Designed Metallopeptides. Journal of the American Chemical Society. 129(42). 12815–12827. 86 indexed citations

14.

Momb, Jessica, Pei W. Thomas, Robert M. Breece, David L. Tierney, & Walter Fast. (2006). The Quorum-Quenching Metallo-γ-lactonase from Bacillus thuringiensis Exhibits a Leaving Group Thio Effect. Biochemistry. 45(44). 13385–13393. 28 indexed citations

15.

Jacobsen, F.E., Robert M. Breece, William K. Myers, David L. Tierney, & Seth M. Cohen. (2006). Model Complexes of Cobalt-Substituted Matrix Metalloproteinases: Tools for Inhibitor Design. Inorganic Chemistry. 45(18). 7306–7315. 51 indexed citations

16.

Franzini, Raphael M., Richard M. Watson, Goutam Kumar Patra, et al.. (2006). Metal Binding to Bipyridine-Modified PNA. Inorganic Chemistry. 45(24). 9798–9811. 56 indexed citations

17.

Breece, Robert M., Alison L. Costello, Brian Bennett, et al.. (2005). A Five-coordinate Metal Center in Co(II)-substituted VanX. Journal of Biological Chemistry. 280(12). 11074–11081. 31 indexed citations

18.

Sigdel, Tara K., et al.. (2004). l-Alanine-p-nitroanilide is not a substrate for VanX. Analytical Biochemistry. 331(2). 398–400. 3 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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