M. Badasso

1.3k total citations
24 papers, 1.1k citations indexed

About

M. Badasso is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, M. Badasso has authored 24 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 15 papers in Materials Chemistry and 7 papers in Biotechnology. Recurrent topics in M. Badasso's work include Enzyme Structure and Function (15 papers), Biochemical and Structural Characterization (7 papers) and RNA and protein synthesis mechanisms (7 papers). M. Badasso is often cited by papers focused on Enzyme Structure and Function (15 papers), Biochemical and Structural Characterization (7 papers) and RNA and protein synthesis mechanisms (7 papers). M. Badasso collaborates with scholars based in United Kingdom, United States and Denmark. M. Badasso's co-authors include Dwight L. Anderson, Michael G. Rossmann, Marc C. Morais, P.G. Leiman, Yizhi Jane Tao, A.A. Simpson, Paul J. Jardine, Yongning He, Norman H. Olson and Shelley Grimes and has published in prestigious journals such as Nature, Journal of Molecular Biology and FEBS Letters.

In The Last Decade

M. Badasso

24 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M. Badasso United Kingdom	13	755	502	173	142	102	24	1.1k
L. Jeanne Perry United States	21	1.2k 1.6×	149 0.3×	118 0.7×	382 2.7×	68 0.7×	28	1.7k
Gavin C. Fox France	19	637 0.8×	198 0.4×	292 1.7×	225 1.6×	171 1.7×	33	1.0k
Gerrit G. Langer Germany	5	1.1k 1.4×	100 0.2×	196 1.1×	451 3.2×	97 1.0×	8	1.5k
Katsuo Katayanagi Japan	19	1.4k 1.9×	199 0.4×	387 2.2×	326 2.3×	205 2.0×	33	1.7k
Neil G. Paterson United Kingdom	19	837 1.1×	96 0.2×	319 1.8×	191 1.3×	100 1.0×	38	1.4k
N. Vasisht United Kingdom	11	920 1.2×	115 0.2×	147 0.8×	60 0.4×	177 1.7×	11	1.4k
B.G. Guimarães Brazil	21	864 1.1×	65 0.1×	122 0.7×	143 1.0×	75 0.7×	65	1.3k
I. Li de la Sierra-Gallay France	24	1.4k 1.8×	219 0.4×	430 2.5×	218 1.5×	200 2.0×	71	1.8k
Mark J. Fogg United Kingdom	20	862 1.1×	206 0.4×	374 2.2×	193 1.4×	86 0.8×	28	1.1k
B. K. Chernov Russia	25	993 1.3×	206 0.4×	179 1.0×	52 0.4×	101 1.0×	62	1.5k

Countries citing papers authored by M. Badasso

Since Specialization

Citations

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

Fields of papers citing papers by M. Badasso

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Badasso

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Bailey, David, Elisabeth P. Carpenter, Alun R. Coker, et al.. (2012). An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases. Acta Crystallographica Section D Biological Crystallography. 68(5). 541–552. 5 indexed citations

Badasso, M., V. Dhanaraj, S. P. Wood, J.B. Cooper, & Tom L. Blundell. (2004). Crystallization and X-ray analysis of the Y75N mutant ofMucor pusilluspepsin complexed with inhibitor. Acta Crystallographica Section D Biological Crystallography. 60(4). 770–772. 1 indexed citations

Morais, Marc C., Shuji Kanamaru, M. Badasso, et al.. (2003). Bacteriophage φ29 scaffolding protein gp7 before and after prohead assembly. Nature Structural & Molecular Biology. 10(7). 572–576. 105 indexed citations

Guasch, Alı́cia, Joan Pous, Borja Ibarra, et al.. (2002). Note to the Paper by Guasch et al. (2002) Detailed Architecture of a DNA Translocating Machine: The High-resolution Structure of the Bacteriophage φ29 Connector Particle. Journal of Molecular Biology. 321(2). 379–380. 1 indexed citations

Simpson, A.A., P.G. Leiman, Yizhi Jane Tao, et al.. (2001). Structure determination of the head–tail connector of bacteriophage ϕ29. Acta Crystallographica Section D Biological Crystallography. 57(9). 1260–1269. 80 indexed citations

Cronin, Nora, M. Badasso, Ian J. Tickle, et al.. (2000). X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity 1 1Edited by R. Huber. Journal of Molecular Biology. 303(5). 745–760. 7 indexed citations

Badasso, M., P.G. Leiman, Yizhi Jane Tao, et al.. (2000). Purification, crystallization and initial X-ray analysis of the head–tail connector of bacteriophage ϕ29. Acta Crystallographica Section D Biological Crystallography. 56(9). 1187–1190. 19 indexed citations

Badasso, M., Jon Read, V. Dhanaraj, et al.. (2000). Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor I^A3 complexed with saccharopepsin fromSaccharomyces cerevisiae. Acta Crystallographica Section D Biological Crystallography. 56(7). 915–917. 1 indexed citations

Simpson, A.A., Yizhi Jane Tao, P.G. Leiman, et al.. (2000). Structure of the bacteriophage φ29 DNA packaging motor. Nature. 408(6813). 745–750. 443 indexed citations

10.

Bunting, Karen, Jon Cooper, M. Badasso, et al.. (1998). Engineering a change in metal‐ion specificity of the iron‐dependent superoxide dismutase from Mycobacterium tuberculosis. European Journal of Biochemistry. 251(3). 795–803. 30 indexed citations

11.

Groves, Matthew R., V. Dhanaraj, M. Badasso, et al.. (1998). A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure. Protein Engineering Design and Selection. 11(10). 833–840. 19 indexed citations

12.

Aguilar, C. F., Nora Cronin, M. Badasso, et al.. (1997). The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae. Journal of Molecular Biology. 267(4). 899–915. 29 indexed citations

13.

Aguilar, C. F., V. Dhanaraj, Kunchur Guruprasad, et al.. (1995). Comparisons of the Three-Dimensional Structures, Specificities and Glycosylation of Renins, Yeast Proteinase A and Cathepsin D. Advances in experimental medicine and biology. 362. 155–166. 6 indexed citations

14.

Cooper, J.B., Kim W. McIntyre, M. Badasso, et al.. (1995). X-ray Structure Analysis of the Iron-dependent Superoxide Dismutase fromMycobacterium tuberculosisat 2.0 Ångstroms Resolution Reveals Novel Dimer–Dimer Interactions. Journal of Molecular Biology. 246(4). 531–544. 83 indexed citations

15.

Dealwis, Chris, Carlos Frazão, M. Badasso, et al.. (1994). X-ray Analysis at 2·0 Å Resolution of Mouse Submaxillary Renin Complexed with a Decapeptide Inhibitor CH-66, Based on the 4-16 Fragment of Rat Angiotensinogen. Journal of Molecular Biology. 236(1). 342–360. 34 indexed citations

16.

Badasso, M., S. P. Wood, C. F. Aguilar, et al.. (1993). Crystallization and Preliminary Crystallographic Characterization of Aspartic Proteinase-A from Baker's Yeast and Its Complexes with Inhibitors. Journal of Molecular Biology. 232(2). 701–703. 7 indexed citations

17.

Lunney, Elizabeth A., John C. Hodges, James S. Kaltenbronn, et al.. (1993). Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors. Journal of Medicinal Chemistry. 36(24). 3809–3820. 13 indexed citations

18.

Dhanaraj, V., Chris Dealwis, Carlos Frazão, et al.. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature. 357(6378). 466–472. 102 indexed citations

19.

Badasso, M., Carlos Frazão, B. L. Sibanda, et al.. (1992). Crystallization and preliminary X-ray analysis of complexes of peptide inhibitors with human recombinant and mouse submandibular renins. Journal of Molecular Biology. 223(2). 447–453. 6 indexed citations

20.

Badasso, M., B. L. Sibanda, J.B. Cooper, Chris Dealwis, & S. P. Wood. (1992). Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin. Journal of Crystal Growth. 122(1-4). 393–399. 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.

Explore authors with similar magnitude of impact