Márta Tóth

5.1k total citations
83 papers, 4.3k citations indexed

About

Márta Tóth is a scholar working on Molecular Medicine, Molecular Biology and Oncology. According to data from OpenAlex, Márta Tóth has authored 83 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Medicine, 30 papers in Molecular Biology and 30 papers in Oncology. Recurrent topics in Márta Tóth's work include Antibiotic Resistance in Bacteria (39 papers), Protease and Inhibitor Mechanisms (29 papers) and Peptidase Inhibition and Analysis (26 papers). Márta Tóth is often cited by papers focused on Antibiotic Resistance in Bacteria (39 papers), Protease and Inhibitor Mechanisms (29 papers) and Peptidase Inhibition and Analysis (26 papers). Márta Tóth collaborates with scholars based in United States, Hungary and Japan. Márta Tóth's co-authors include Rafael Fridman, Shahriar Mobashery, Sergei B. Vakulenko, Rafael Fridman, Clyde A. Smith, M. Margarida Bernardo, David C. Gervasi, Sonia Hernandez‐Barrantes, Anjum Sohail and Hilary Frase and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Blood.

In The Last Decade

Márta Tóth

82 papers receiving 4.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Márta Tóth United States 36 2.0k 1.6k 1.4k 931 608 83 4.3k
Susheela Tridandapani United States 49 742 0.4× 3.1k 1.9× 1.1k 0.7× 164 0.2× 343 0.6× 115 6.4k
Jørgen Rygaard Denmark 38 755 0.4× 2.1k 1.3× 988 0.7× 247 0.3× 228 0.4× 108 5.0k
Anders Sundan Norway 51 821 0.4× 3.5k 2.1× 1.8k 1.3× 74 0.1× 2.0k 3.3× 160 8.2k
K. Maskos Germany 38 1.5k 0.8× 2.1k 1.3× 1.6k 1.1× 55 0.1× 471 0.8× 59 4.0k
Richard A. Williamson United Kingdom 30 752 0.4× 1.4k 0.9× 612 0.4× 118 0.1× 305 0.5× 73 3.0k
Norman M. Schechter United States 49 895 0.5× 2.8k 1.7× 546 0.4× 79 0.1× 935 1.5× 93 8.1k
Brian Wong United States 45 1.6k 0.8× 4.6k 2.8× 3.3k 2.3× 45 0.0× 427 0.7× 92 8.6k
Chunhong Ma China 45 930 0.5× 2.7k 1.7× 1.4k 1.0× 79 0.1× 269 0.4× 193 6.7k
Marco Tripodi Italy 42 1.5k 0.8× 3.3k 2.1× 766 0.5× 79 0.1× 137 0.2× 132 5.9k
Paul Schwarzenberger United States 34 333 0.2× 1.4k 0.9× 1.7k 1.2× 59 0.1× 472 0.8× 112 7.2k

Countries citing papers authored by Márta Tóth

Since Specialization
Citations

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

Fields of papers citing papers by Márta Tóth

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Márta Tóth

This figure shows the co-authorship network connecting the top 25 collaborators of Márta Tóth. A scholar is included among the top collaborators of Márta Tóth 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 Márta Tóth. Márta Tóth 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.
Stewart, Nichole K., et al.. (2025). Evolution of carbapenemase activity in the class C β-lactamase ADC-1. mBio. 16(6). e0018525–e0018525. 1 indexed citations
2.
Tóth, Márta, Nichole K. Stewart, Jonathan A. G. Cox, et al.. (2025). Dual mechanism of the OXA-23 carbapenemase inhibition by the carbapenem NA-1-157. Antimicrobial Agents and Chemotherapy. 69(10). e0091825–e0091825.
3.
Tóth, Márta, Nichole K. Stewart, Ailiena O. Maggiolo, et al.. (2024). Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the OXA-58 Carbapenemase. ACS Infectious Diseases. 10(12). 4347–4359. 3 indexed citations
4.
Stewart, Nichole K., et al.. (2024). Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES-5 Carbapenemase. ACS Infectious Diseases. 10(4). 1232–1249. 4 indexed citations
5.
Smith, Clyde A., et al.. (2023). The C5α-Methyl-Substituted Carbapenem NA-1-157 Exhibits Potent Activity against Klebsiella spp. Isolates Producing OXA-48-Type Carbapenemases. ACS Infectious Diseases. 9(5). 1123–1136. 4 indexed citations
6.
Stewart, Nichole K., et al.. (2019). The crystal structures of CDD-1, the intrinsic class D β-lactamase from the pathogenic Gram-positive bacterium Clostridioides difficile, and its complex with cefotaxime. Journal of Structural Biology. 208(3). 107391–107391. 9 indexed citations
7.
Tóth, Márta, et al.. (2017). The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D β-lactamases. Acta Crystallographica Section D Structural Biology. 73(8). 692–701. 26 indexed citations
8.
Tóth, Márta, Nuno T. Antunes, Nichole K. Stewart, et al.. (2015). Class D β-lactamases do exist in Gram-positive bacteria. Nature Chemical Biology. 12(1). 9–14. 50 indexed citations
9.
Smith, Clyde A., Nuno T. Antunes, Nichole K. Stewart, et al.. (2013). Structural Basis for Carbapenemase Activity of the OXA-23 β-Lactamase from Acinetobacter baumannii. Chemistry & Biology. 20(9). 1107–1115. 103 indexed citations
10.
Tóth, Márta, Joseph W. Chow, Shahriar Mobashery, & Sergei B. Vakulenko. (2009). Source of Phosphate in the Enzymic Reaction as a Point of Distinction among Aminoglycoside 2″-Phosphotransferases. Journal of Biological Chemistry. 284(11). 6690–6696. 37 indexed citations
11.
Tóth, Márta, Sergei B. Vakulenko, & Clyde A. Smith. (2009). Purification, crystallization and preliminary X-ray analysis ofEnterococcus casseliflavusaminoglycoside-2′′-phosphotransferase-IVa. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(1). 81–84. 4 indexed citations
12.
Lee, Mijoon, Giuseppe Celenza, Bill Boggess, et al.. (2009). A Potent Gelatinase Inhibitor with Anti‐Tumor‐Invasive Activity and its Metabolic Disposition. Chemical Biology & Drug Design. 73(2). 189–202. 32 indexed citations
13.
Osenkowski, Pamela, Huiren Zhao, Márta Tóth, et al.. (2008). The Inactive 44-kDa Processed Form of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Enhances Proteolytic Activity via Regulation of Endocytosis of Active MT1-MMP. Journal of Biological Chemistry. 283(25). 17391–17405. 29 indexed citations
14.
Thomas, Stacey L., Pamela Osenkowski, Márta Tóth, et al.. (2007). SPARC upregulates MT1-MMP expression, MMP-2 activation, and the secretion and cleavage of galectin-3 in U87MG glioma cells. Neuroscience Letters. 419(2). 172–177. 79 indexed citations
15.
Hesek, Dušan, Márta Tóth, Samy O. Meroueh, et al.. (2006). Design and Characterization of a Metalloproteinase Inhibitor-Tethered Resin for the Detection of Active MMPs in Biological Samples. Chemistry & Biology. 13(4). 379–386. 22 indexed citations
16.
Tóth, Márta, et al.. (2003). Pro-MMP-9 activation by the MT1-MMP/MMP-2 axis and MMP-3: role of TIMP-2 and plasma membranes. Biochemical and Biophysical Research Communications. 308(2). 386–395. 164 indexed citations
17.
Tóth, Márta, Sonia Hernandez‐Barrantes, Pamela Osenkowski, et al.. (2002). Complex Pattern of Membrane Type 1 Matrix Metalloproteinase Shedding. Journal of Biological Chemistry. 277(29). 26340–26350. 106 indexed citations
18.
Tóth, Márta, M. Margarida Bernardo, David C. Gervasi, et al.. (2000). Tissue Inhibitor of Metalloproteinase (TIMP)-2 Acts Synergistically with Synthetic Matrix Metalloproteinase (MMP) Inhibitors but Not with TIMP-4 to Enhance the (Membrane Type 1)-MMP-dependent Activation of Pro-MMP-2. Journal of Biological Chemistry. 275(52). 41415–41423. 121 indexed citations
19.
Vakulenko, Sergei B., et al.. (1999). Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coli. Journal of Biological Chemistry. 274(33). 23052–23060. 60 indexed citations
20.
Olson, Matthew W., Márta Tóth, David C. Gervasi, et al.. (1998). High Affinity Binding of Latent Matrix Metalloproteinase-9 to the α2(IV) Chain of Collagen IV. Journal of Biological Chemistry. 273(17). 10672–10681. 121 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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