M.L. Speranza

573 total citations
18 papers, 473 citations indexed

About

M.L. Speranza is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, M.L. Speranza has authored 18 papers receiving a total of 473 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 8 papers in Materials Chemistry and 5 papers in Biochemistry. Recurrent topics in M.L. Speranza's work include Enzyme Structure and Function (8 papers), Amino Acid Enzymes and Metabolism (5 papers) and Protein Structure and Dynamics (5 papers). M.L. Speranza is often cited by papers focused on Enzyme Structure and Function (8 papers), Amino Acid Enzymes and Metabolism (5 papers) and Protein Structure and Dynamics (5 papers). M.L. Speranza collaborates with scholars based in Italy, Qatar and United Kingdom. M.L. Speranza's co-authors include Giovanna Valentini, Andrea Mattevi, Alessandro Galizzi, Laurent R. Chiarelli, R. Fortin, Alessandro Coda, Martino Bolognesi, Menico Rizzi, Giuseppina Ferri and Alessandra M. Albertini and has published in prestigious journals such as Journal of Biological Chemistry, Biochemical Pharmacology and Structure.

In The Last Decade

M.L. Speranza

17 papers receiving 457 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.L. Speranza Italy 9 340 122 78 70 70 18 473
H. M. Kalckar United States 16 377 1.1× 120 1.0× 132 1.7× 79 1.1× 62 0.9× 34 584
Melissa Sondej United States 12 335 1.0× 101 0.8× 36 0.5× 77 1.1× 140 2.0× 13 494
E. Inagaki Japan 12 379 1.1× 105 0.9× 60 0.8× 25 0.4× 60 0.9× 21 562
S Kovacevic United States 11 365 1.1× 48 0.4× 31 0.4× 23 0.3× 75 1.1× 13 641
David P. Richey United States 7 449 1.3× 36 0.3× 92 1.2× 50 0.7× 74 1.1× 8 624
R. Toro United States 15 393 1.2× 93 0.8× 49 0.6× 44 0.6× 56 0.8× 22 578
Gisèle Le Bras France 12 403 1.2× 222 1.8× 128 1.6× 16 0.2× 54 0.8× 20 587
Dominique Liger France 18 587 1.7× 145 1.2× 37 0.5× 29 0.4× 117 1.7× 29 750
Peter A. Chalk United Kingdom 15 348 1.0× 82 0.7× 33 0.4× 35 0.5× 39 0.6× 21 672
Thomas G. Warner United States 16 542 1.6× 60 0.5× 29 0.4× 139 2.0× 68 1.0× 29 749

Countries citing papers authored by M.L. Speranza

Since Specialization
Citations

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

Fields of papers citing papers by M.L. Speranza

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M.L. Speranza

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

All Works

18 of 18 papers shown
1.
2.
Valentini, Giovanna, Laurent R. Chiarelli, R. Fortin, et al.. (2000). The Allosteric Regulation of Pyruvate Kinase. Journal of Biological Chemistry. 275(24). 18145–18152. 155 indexed citations
3.
Valentini, Giovanna, Andrea Mattevi, Daniela Barillà, Alessandro Galizzi, & M.L. Speranza. (1997). Recombinant pyruvate kinase type I from Escherichia coli: overproduction and revised C-terminus of the polypeptide.. PubMed. 378(7). 719–21. 7 indexed citations
4.
Valentini, Giovanna, Paolo Iadarola, Giuseppina Ferri, & M.L. Speranza. (1995). Affinity Labelling of the Catalytic and Allosteric ATP Binding Sites on Pyruvate KinaseType I fromEscherichia coli. Biological Chemistry Hoppe-Seyler. 376(4). 231–236. 4 indexed citations
5.
Albertini, Alessandra M., et al.. (1995). The outB Gene of Bacillus subtilis Codes for NAD Synthetase. Journal of Biological Chemistry. 270(11). 6181–6185. 43 indexed citations
6.
Mattevi, Andrea, et al.. (1995). Crystallization and preliminary X-ray analysis of pyruvate kinase type I fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 51(6). 1089–1091. 2 indexed citations
7.
Mattevi, Andrea, Giovanna Valentini, Menico Rizzi, et al.. (1995). Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure. 3(7). 729–741. 115 indexed citations
8.
Valentini, Giovanna, Monica Stoppini, Paolo Iadarola, et al.. (1993). Divergent Binding Sites in Pyruvate Kinases I and II fromEscherichia coli. Biological Chemistry Hoppe-Seyler. 374(1-6). 69–74. 4 indexed citations
9.
Valentini, Giovanna, Monica Stoppini, M.L. Speranza, Massimo Malcovati, & Giuseppina Ferri. (1991). Bacterial Pyruvate Kinases Have a Shorter N-Terminal Domain. Biological Chemistry Hoppe-Seyler. 372(1). 91–94. 9 indexed citations
10.
Speranza, M.L., Giovanna Valentini, Paolo Iadarola, et al.. (1989). Primary Structure of Three Peptides at the Catalytic and Allosteric Sites of the Fructose-1,6-bisphosphate-Activated Pyruvate Kinase fromEscherichia coli. Biological Chemistry Hoppe-Seyler. 370(1). 211–216. 25 indexed citations
11.
Valentini, Giovanna, M.L. Speranza, Paolo Iadarola, Giuseppina Ferri, & Massimo Malcovati. (1988). Reactivity of the Fructose 1,6-bisphosphate-Activated Pyruvate Kinase fromEscherichia coliwith Pyridoxal 5´ -phosphate. Biological Chemistry Hoppe-Seyler. 369(2). 1219–1226. 10 indexed citations
12.
Speranza, M.L., Giovanna Valentini, & Alberto Calligaro. (1987). Influence of Fibronectin on the Fibrillogenesis of Type I and Type III Collagen. Collagen and Related Research. 7(2). 115–123. 25 indexed citations
13.
Speranza, M.L., et al.. (1978). Purification and properties of NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from spinach leaves. Biochimica et Biophysica Acta (BBA) - Enzymology. 522(1). 32–42. 7 indexed citations
14.
Ferri, Giuseppina, et al.. (1978). Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts. Biochimica et Biophysica Acta (BBA) - Enzymology. 522(1). 19–31. 46 indexed citations
15.
Speranza, M.L., Silvia Ronchi, & Lorenzo Minchiotti. (1973). Purification and characterization of yeast thioredoxin reductase. Biochimica et Biophysica Acta (BBA) - Enzymology. 327(2). 274–281. 12 indexed citations
16.
Speranza, M.L., et al.. (1971). The mode of action of β-benzal butyric acid, an hypocholesterolemic drug, in affecting mitochondrial respiration. Biochemical Pharmacology. 20(9). 2477–2484. 1 indexed citations
17.
Speranza, M.L., et al.. (1970). The inhibition of mitochondrial respiration by β-benzal butyric acid and the possible relationship to cholesterol biosynthesis. Biochemical Pharmacology. 19(10). 2737–2743. 4 indexed citations
18.
Gaetani, Massimiliano, et al.. (1967). The identification and determination of phosphagen in insects and their eggs. Comparative Biochemistry and Physiology. 20(2). 607–618. 4 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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