M Sajgó

407 total citations
25 papers, 331 citations indexed

About

M Sajgó is a scholar working on Molecular Biology, Cell Biology and Biochemistry. According to data from OpenAlex, M Sajgó has authored 25 papers receiving a total of 331 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 11 papers in Cell Biology and 6 papers in Biochemistry. Recurrent topics in M Sajgó's work include Amino Acid Enzymes and Metabolism (6 papers), Hemoglobin structure and function (6 papers) and Chemical Synthesis and Analysis (4 papers). M Sajgó is often cited by papers focused on Amino Acid Enzymes and Metabolism (6 papers), Hemoglobin structure and function (6 papers) and Chemical Synthesis and Analysis (4 papers). M Sajgó collaborates with scholars based in Hungary, Australia and Italy. M Sajgó's co-authors include J. Ieuan Harris, B E Davidson, Harry F. Noller, L. Gráf, G Cseh, Erzsébet Barát, Gy. Hajós, Péter Friedrich, B. Szajáni and Ágnes Kemény and has published in prestigious journals such as Nature, Journal of Molecular Biology and FEBS Letters.

In The Last Decade

M Sajgó

24 papers receiving 281 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M Sajgó Hungary	7	230	89	71	54	44	25	331
Standish Barry Ireland	9	352 1.5×	98 1.1×	54 0.8×	70 1.3×	15 0.3×	12	466
Kimio Oikawa Canada	14	423 1.8×	73 0.8×	66 0.9×	67 1.2×	40 0.9×	24	537
T Baranowski Poland	11	224 1.0×	98 1.1×	97 1.4×	31 0.6×	13 0.3×	54	418
Theodore O. Sippel United States	12	248 1.1×	39 0.4×	85 1.2×	56 1.0×	19 0.4×	23	420
Richard H. Palmieri United States	10	321 1.4×	97 1.1×	96 1.4×	106 2.0×	14 0.3×	14	572
Rosa Uy United States	7	295 1.3×	47 0.5×	66 0.9×	52 1.0×	26 0.6×	8	454
Marita M. King United States	12	308 1.3×	74 0.8×	56 0.8×	12 0.2×	63 1.4×	13	355
Sigrid M. Klein United States	9	290 1.3×	88 1.0×	58 0.8×	19 0.4×	39 0.9×	15	400
Walter F. Prouty United States	10	421 1.8×	77 0.9×	79 1.1×	26 0.5×	14 0.3×	11	526
S.M. Schuster United States	7	336 1.5×	30 0.3×	30 0.4×	23 0.4×	20 0.5×	9	393

Countries citing papers authored by M Sajgó

Since Specialization

Citations

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

Fields of papers citing papers by M Sajgó

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M Sajgó

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

All Works

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20 of 20 papers shown

Murvai, János, Péter Fábián, Miklós Hollósi, et al.. (1993). Is an amphiphilic region responsible for the haemolytic activity of Bacillus thuringiensis toxin?†. International journal of peptide & protein research. 42(6). 527–532. 9 indexed citations

Kisfaludy, L., et al.. (1986). A new solution synthesis of locust adipokinetic hormone. International journal of peptide & protein research. 27(4). 440–442. 3 indexed citations

Polgár, László & M Sajgó. (1981). Peptic peptide of thiolsubtilisin. Analytical evidence for the chemical transformation of the essential serine-221 to cysteine-221. Biochimica et Biophysica Acta (BBA) - Protein Structure. 667(2). 351–354. 3 indexed citations

Sajgó, M, et al.. (1981). Determination of tofisopam in serum by high-performance liquid chromatography. Journal of Chromatography B Biomedical Sciences and Applications. 222(2). 303–307. 10 indexed citations

Balázs, András, et al.. (1980). Purification of an endopeptide to homogenity and the verification of its selective inhibitory action on myeloid cell proliferation. Cell Biology International Reports. 4(4). 337–345. 11 indexed citations

Sajgó, M, et al.. (1980). Identification of an intramolecular cross-link in troponin C after cross-linking the troponin complex with 1,3-difluoro-4,6-dinitrobenzene. Biochimica et Biophysica Acta (BBA) - Protein Structure. 625(2). 304–309. 3 indexed citations

Sajgó, M. (1979). Untersuchungen über den enzymatischen Abbau von tert-Butyltryptophan-haltigen Peptiden. Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 360(1). 9–12. 5 indexed citations

Markovič, Oskar & M Sajgó. (1977). Terminal amino acids, peptide map and amino acid composition of one form of tomato pectinesterase (short communication).. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 12(1). 45–8.

Sajgó, M, et al.. (1975). Some structural features of rabbit muscle aldolase as derived from its limited proteolysis.. PubMed. 10(3). 185–99. 1 indexed citations

10.

Sajgó, M, et al.. (1974). Phosphopyridoxyl peptide from chicken heart aspartate aminotransferase.. PubMed. 9(3). 213–6. 1 indexed citations

11.

Sajgó, M & Gy. Hajós. (1974). The amino acid sequence of rabbit muscle aldolase.. PubMed. 9(3). 239–41. 5 indexed citations

12.

Sajgó, M & Gy. Hajós. (1974). Amino acid sequence of the N‐terminal 158 residues of rabbit muscle aldolase. FEBS Letters. 38(3). 341–344. 3 indexed citations

13.

Sajgó, M, et al.. (1973). On the Mechanism of Formation of a Partially Active Aldolase by Tryptic Digestion. European Journal of Biochemistry. 38(2). 283–292. 4 indexed citations

14.

Sajgó, M. (1971). Amino acid sequence of a fragment of rabbit muscle aldolase. FEBS Letters. 12(6). 349–351. 5 indexed citations

15.

Hajós, Gy., et al.. (1971). The N-terminal tryptic peptide of rabbit muscle aldolase.. PubMed. 6(1). 1–4. 2 indexed citations

16.

Szajáni, B., et al.. (1970). Identification of a Cysteinyl Residue Involved in the Activity of Rabbit Muscle Aldolase. European Journal of Biochemistry. 15(1). 171–178. 21 indexed citations

17.

Sajgó, M. (1969). Distribution of the sulfhydryl groups of rabbit muscle aldolase in the polypeptide chain (preliminary communication).. PubMed. 4(4). 385–9. 1 indexed citations

18.

Davidson, B E, M Sajgó, Harry F. Noller, & J. Ieuan Harris. (1967). Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle. Nature. 216(5121). 1181–1185. 171 indexed citations

19.

Sajgó, M. (1963). Photo-oxidation of myoglobin. Journal of Molecular Biology. 7(6). 752–755. 10 indexed citations

20.

Sajgó, M. (1961). The photooxidation of myoglobin.. PubMed. 18. 279–81. 2 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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