Mark Mabanglo

1.1k total citations
19 papers, 558 citations indexed

About

Mark Mabanglo is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Mark Mabanglo has authored 19 papers receiving a total of 558 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 6 papers in Materials Chemistry and 4 papers in Pharmacology. Recurrent topics in Mark Mabanglo's work include Enzyme Structure and Function (6 papers), RNA and protein synthesis mechanisms (5 papers) and Biochemical and Structural Characterization (4 papers). Mark Mabanglo is often cited by papers focused on Enzyme Structure and Function (6 papers), RNA and protein synthesis mechanisms (5 papers) and Biochemical and Structural Characterization (4 papers). Mark Mabanglo collaborates with scholars based in Canada, United States and Brazil. Mark Mabanglo's co-authors include Walid A. Houry, Vaibhav Bhandari, Keith S. Wong, Robert A. Batey, Frank M. Raushel, Jin Zhou, Andrew N. Bigley, Steven P. Harvey, C. Dale Poulter and Kamran Rizzolo and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Mark Mabanglo

19 papers receiving 556 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark Mabanglo Canada 13 399 81 71 59 59 19 558
Cammy K.-M. Chen Taiwan 8 473 1.2× 125 1.5× 89 1.3× 49 0.8× 69 1.2× 9 640
Melody Holmquist United States 4 396 1.0× 47 0.6× 93 1.3× 57 1.0× 37 0.6× 7 544
María‐Natalia Lisa France 11 276 0.7× 40 0.5× 51 0.7× 94 1.6× 60 1.0× 25 556
Heinrich Delbrück Germany 12 280 0.7× 28 0.3× 90 1.3× 57 1.0× 51 0.9× 14 508
Jacob Lesniak United States 7 353 0.9× 37 0.5× 60 0.8× 75 1.3× 48 0.8× 8 555
S. Parès France 7 360 0.9× 64 0.8× 115 1.6× 123 2.1× 78 1.3× 8 747
Christopher T. Walsh United States 13 575 1.4× 95 1.2× 61 0.9× 77 1.3× 67 1.1× 14 726
Felix Kaspar Germany 13 368 0.9× 45 0.6× 21 0.3× 46 0.8× 29 0.5× 29 552
Heather E. Upton United States 14 677 1.7× 51 0.6× 66 0.9× 19 0.3× 55 0.9× 19 888
Karthik Veeravalli United States 9 391 1.0× 23 0.3× 77 1.1× 25 0.4× 63 1.1× 12 599

Countries citing papers authored by Mark Mabanglo

Since Specialization
Citations

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

Fields of papers citing papers by Mark Mabanglo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark Mabanglo

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

All Works

19 of 19 papers shown
1.
Mabanglo, Mark, Keith S. Wong, Jingping Shen, et al.. (2025). Small molecule dysregulation of ClpP activity via bidirectional allosteric pathways. Structure. 33(10). 1700–1716.e6. 1 indexed citations
2.
Ahmad, Shabbir, Mark Mabanglo, Levon Halabelian, et al.. (2024). Development of Peptide Displacement Assays to Screen for Antagonists of DDB1 Interactions. Biochemistry. 63(10). 1297–1306. 2 indexed citations
3.
Mabanglo, Mark, Jin Zhou, Keith S. Wong, et al.. (2024). Structure-Based Design and Development of Phosphine Oxides as a Novel Chemotype for Antibiotics that Dysregulate Bacterial ClpP Proteases. Journal of Medicinal Chemistry. 67(17). 15131–15147. 8 indexed citations
4.
Mabanglo, Mark & Walid A. Houry. (2022). Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules. Journal of Biological Chemistry. 298(5). 101781–101781. 38 indexed citations
5.
Mabanglo, Mark, Keith S. Wong, Elisa Leung, et al.. (2022). Potent ClpP agonists with anticancer properties bind with improved structural complementarity and alter the mitochondrial N-terminome. Structure. 31(2). 185–200.e10. 31 indexed citations
6.
Mabanglo, Mark, Vaibhav Bhandari, & Walid A. Houry. (2021). Substrates and interactors of the ClpP protease in the mitochondria. Current Opinion in Chemical Biology. 66. 102078–102078. 36 indexed citations
7.
Mabanglo, Mark, Jordan D. Goodreid, Elisa Leung, et al.. (2020). Development of Antibiotics That Dysregulate the Neisserial ClpP Protease. ACS Infectious Diseases. 6(12). 3224–3236. 23 indexed citations
8.
9.
Mabanglo, Mark, Elisa Leung, Siavash Vahidi, et al.. (2019). ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. Communications Biology. 2(1). 410–410. 29 indexed citations
10.
Wong, Keith S., Mark Mabanglo, Thiago Vargas Seraphim, et al.. (2018). Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death. Cell chemical biology. 25(8). 1017–1030.e9. 77 indexed citations
11.
12.
Bhandari, Vaibhav, Keith S. Wong, Jin Zhou, et al.. (2018). The Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases. ACS Chemical Biology. 13(6). 1413–1425. 114 indexed citations
13.
Vahidi, Siavash, Zev A. Ripstein, Massimiliano Bonomi, et al.. (2018). Reversible inhibition of the ClpP protease via an N-terminal conformational switch. Proceedings of the National Academy of Sciences. 115(28). E6447–E6456. 44 indexed citations
14.
Mabanglo, Mark, Dao Feng Xiang, Andrew N. Bigley, & Frank M. Raushel. (2016). Structure of a Novel Phosphotriesterase from Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed β-Propeller Protein Fold. Biochemistry. 55(28). 3963–3974. 18 indexed citations
15.
Bigley, Andrew N., Mark Mabanglo, Steven P. Harvey, & Frank M. Raushel. (2015). Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR. Biochemistry. 54(35). 5502–5512. 59 indexed citations
16.
Mabanglo, Mark, Michael A. Hast, Nathan B. Lubock, Homme W. Hellinga, & L.S. Beese. (2013). Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design. Protein Science. 23(3). 289–301. 19 indexed citations
17.
Mabanglo, Mark, et al.. (2012). Mutagenesis of Isopentenyl Phosphate Kinase To Enhance Geranyl Phosphate Kinase Activity. ACS Chemical Biology. 7(7). 1241–1246. 12 indexed citations
18.
Mabanglo, Mark, Adrian W.R. Serohijos, & C. Dale Poulter. (2011). The Streptomyces-Produced Antibiotic Fosfomycin Is a Promiscuous Substrate for Archaeal Isopentenyl Phosphate Kinase. Biochemistry. 51(4). 917–925. 8 indexed citations
19.
Mabanglo, Mark, Heidi Schubert, Mo Chen, Christopher P. Hill, & C. Dale Poulter. (2010). X-ray Structures of Isopentenyl Phosphate Kinase. ACS Chemical Biology. 5(5). 517–527. 28 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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