R.E. Monro

2.6k total citations
22 papers, 2.1k citations indexed

About

R.E. Monro is a scholar working on Molecular Biology, Oncology and Materials Chemistry. According to data from OpenAlex, R.E. Monro has authored 22 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 6 papers in Oncology and 4 papers in Materials Chemistry. Recurrent topics in R.E. Monro's work include RNA and protein synthesis mechanisms (14 papers), RNA modifications and cancer (8 papers) and Peptidase Inhibition and Analysis (6 papers). R.E. Monro is often cited by papers focused on RNA and protein synthesis mechanisms (14 papers), RNA modifications and cancer (8 papers) and Peptidase Inhibition and Analysis (6 papers). R.E. Monro collaborates with scholars based in United Kingdom, Spain and Germany. R.E. Monro's co-authors include D. Vázquez, Robert R. Traut, Kjeld A. Marcker, B.E.H. Maden, M. L. Celma, T. Staehelin, John W.B. Hershey, J. Černá, Donna Maglott and Kenneth C. Holmes and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Cell Biology and Journal of Molecular Biology.

In The Last Decade

R.E. Monro

22 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
R.E. Monro United Kingdom 19 1.9k 437 259 181 145 22 2.1k
Albert J. Wahba United States 26 1.9k 1.0× 118 0.3× 396 1.5× 110 0.6× 250 1.7× 44 2.2k
Gary R. Craven United States 19 1.8k 0.9× 120 0.3× 365 1.4× 79 0.4× 213 1.5× 49 2.1k
Frédéric Dardel France 34 2.0k 1.0× 379 0.9× 411 1.6× 117 0.6× 201 1.4× 76 2.4k
James Ofengand United States 42 4.8k 2.5× 219 0.5× 585 2.3× 130 0.7× 266 1.8× 123 5.0k
Eiko Otaka Japan 25 1.5k 0.8× 119 0.3× 353 1.4× 33 0.2× 191 1.3× 60 1.7k
Ross I. Brinkworth Australia 23 988 0.5× 142 0.3× 132 0.5× 183 1.0× 89 0.6× 41 1.6k
Hans Sternbach Germany 24 1.5k 0.8× 109 0.2× 203 0.8× 125 0.7× 61 0.4× 69 1.6k
Reiji Okazaki Japan 24 1.6k 0.8× 136 0.3× 484 1.9× 169 0.9× 258 1.8× 38 1.9k
Robert J. Peanasky United States 24 867 0.5× 172 0.4× 75 0.3× 33 0.2× 161 1.1× 38 1.5k
S. James Remington United States 28 1.6k 0.8× 199 0.5× 240 0.9× 105 0.6× 143 1.0× 42 2.1k

Countries citing papers authored by R.E. Monro

Since Specialization
Citations

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

Fields of papers citing papers by R.E. Monro

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by R.E. Monro. 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 R.E. Monro. The network helps show where R.E. Monro may publish in the future.

Co-authorship network of co-authors of R.E. Monro

This figure shows the co-authorship network connecting the top 25 collaborators of R.E. Monro. A scholar is included among the top collaborators of R.E. Monro 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 R.E. Monro. R.E. Monro 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.
Celma, M. L., R.E. Monro, & D. Vázquez. (1971). Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes: Binding of UACCA‐Leu to 50 S subunits. FEBS Letters. 13(4). 247–251. 72 indexed citations
2.
3.
Celma, M. L., R.E. Monro, & D. Vázquez. (1970). Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes. FEBS Letters. 6(3). 273–277. 107 indexed citations
4.
Neth, R., R.E. Monro, G Heller, E. Battaner, & D. Vázquez. (1970). Catalysis of peptidyl transfer by human tonsil ribosomes and effects of some antibiotics. FEBS Letters. 6(3). 198–202. 41 indexed citations
5.
Jimènez, A., R.E. Monro, & D. Vázquez. (1970). Interaction of Ac‐Phe‐tRNA with E. coli ribosomal subunits. 2. Resistance of the sparsomycin‐induced complex to hydroxylamine action. FEBS Letters. 7(2). 109–111. 4 indexed citations
6.
Vázquez, D., et al.. (1969). The Function of 80 S Ribosomal Subunits and Effects of Some Antibiotics. Cold Spring Harbor Symposia on Quantitative Biology. 34(0). 369–375. 50 indexed citations
7.
Staehelin, T., Donna Maglott, & R.E. Monro. (1969). On The Catalytic Center of Peptidyl Transfer: A Part of the 50 S Ribosome Structure. Cold Spring Harbor Symposia on Quantitative Biology. 34(0). 39–48. 97 indexed citations
8.
Monro, R.E., J. Černá, & Kjeld A. Marcker. (1968). Ribosome-catalyzed peptidyl transfer: substrate specificity at the P-site.. Proceedings of the National Academy of Sciences. 61(3). 1042–1049. 119 indexed citations
9.
Maden, B.E.H. & R.E. Monro. (1968). Ribosome‐Catalyzed Peptidyl Transfer. European Journal of Biochemistry. 6(2). 309–316. 122 indexed citations
10.
Maden, B.E.H., Robert R. Traut, & R.E. Monro. (1968). Ribosome-catalysed peptidyl transfer: the polyphenylalanine system. Journal of Molecular Biology. 35(2). 333–345. 104 indexed citations
11.
Monro, R.E.. (1967). Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coli. Journal of Molecular Biology. 26(1). 147–151. 224 indexed citations
12.
Vázquez, D. & R.E. Monro. (1967). Effects of some inhibitors of protein synthesis on the binding of aminoacyl tRNA to ribosomal subunits. Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis. 142(1). 155–173. 95 indexed citations
13.
Monro, R.E. & Kjeld A. Marcker. (1967). Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. Journal of Molecular Biology. 25(2). 347–350. 227 indexed citations
14.
Monro, R.E. & D. Vázquez. (1967). Ribosome-catalysed peptidyl transfer: Effects of some inhibitors of protein synthesis. Journal of Molecular Biology. 28(1). 161–165. 157 indexed citations
15.
Hershey, John W.B. & R.E. Monro. (1966). A competitive inhibitor of the GTP reaction in protein synthesis. Journal of Molecular Biology. 18(1). 68–76. 80 indexed citations
16.
Holmes, Kenneth C. & R.E. Monro. (1965). Studies on the structure of parasporal inclusions from Bacillus thuringiensis. Journal of Molecular Biology. 14(2). 572–IN25. 55 indexed citations
17.
Smith, Johan, et al.. (1965). Action of puromycin in polyadenylic acid-directed polylysine synthesis. Journal of Molecular Biology. 13(3). 617–628. 73 indexed citations
18.
Traut, Robert R. & R.E. Monro. (1964). The puromycin reaction and its relation to protein synthesis. Journal of Molecular Biology. 10(1). 63–72. 285 indexed citations
19.
Monro, R.E.. (1961). SEROLOGICAL STUDIES ON THE FORMATION OF PROTEIN PARASPORAL INCLUSIONS IN BACILLUS THURINGIENSIS . The Journal of Cell Biology. 11(2). 321–331. 18 indexed citations
20.
Monro, R.E.. (1961). Protein turnover and the formation of protein inclusions during sporulation of Bacillus thuringiensis. Biochemical Journal. 81(2). 225–232. 69 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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