E M Bailyes

1.5k total citations
33 papers, 1.3k citations indexed

About

E M Bailyes is a scholar working on Surgery, Endocrinology, Diabetes and Metabolism and Molecular Biology. According to data from OpenAlex, E M Bailyes has authored 33 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Surgery, 16 papers in Endocrinology, Diabetes and Metabolism and 12 papers in Molecular Biology. Recurrent topics in E M Bailyes's work include Pancreatic function and diabetes (15 papers), Adenosine and Purinergic Signaling (8 papers) and Alkaline Phosphatase Research Studies (6 papers). E M Bailyes is often cited by papers focused on Pancreatic function and diabetes (15 papers), Adenosine and Purinergic Signaling (8 papers) and Alkaline Phosphatase Research Studies (6 papers). E M Bailyes collaborates with scholars based in United Kingdom, United States and Netherlands. E M Bailyes's co-authors include John C. Hutton, J. Paul Luzio, Kenneth Siddle, Paul C. Guest, Maria A. Soos, Susan D. Arden, N.G. Rutherford, B. Nave, Amanda C. Hayward and Susan J. Brown and has published in prestigious journals such as Nature, The Lancet and Journal of Biological Chemistry.

In The Last Decade

E M Bailyes

33 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E M Bailyes United Kingdom 18 668 464 430 274 272 33 1.3k
J C Hutton United Kingdom 15 667 1.0× 885 1.9× 426 1.0× 359 1.3× 219 0.8× 21 1.2k
Joan‐Marc Servitja Spain 22 1.0k 1.6× 644 1.4× 205 0.5× 389 1.4× 258 0.9× 42 1.9k
Satsuki Matsushima Japan 19 536 0.8× 410 0.9× 89 0.2× 134 0.5× 279 1.0× 38 1.0k
Gwenn M. Hansen United States 25 1.0k 1.5× 133 0.3× 130 0.3× 337 1.2× 247 0.9× 48 1.7k
Emily Foulstone United Kingdom 18 1.2k 1.9× 223 0.5× 306 0.7× 129 0.5× 212 0.8× 30 1.7k
Pamela Itkin‐Ansari United States 21 548 0.8× 957 2.1× 419 1.0× 549 2.0× 282 1.0× 36 1.4k
Yi‐Fen Lee United States 26 1.0k 1.6× 187 0.4× 127 0.3× 410 1.5× 70 0.3× 48 1.7k
Michael Trus Israel 20 889 1.3× 244 0.5× 60 0.1× 98 0.4× 334 1.2× 44 1.2k
Benjamin Kefas United States 18 2.1k 3.1× 250 0.5× 176 0.4× 105 0.4× 100 0.4× 21 2.6k
Jean‐Michel Culouscou France 17 1.1k 1.6× 100 0.2× 219 0.5× 122 0.4× 95 0.3× 22 1.9k

Countries citing papers authored by E M Bailyes

Since Specialization
Citations

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

Fields of papers citing papers by E M Bailyes

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of E M Bailyes

This figure shows the co-authorship network connecting the top 25 collaborators of E M Bailyes. A scholar is included among the top collaborators of E M Bailyes 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 E M Bailyes. E M Bailyes 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.
Luzio, J. Paul & E M Bailyes. (2003). Isolation of a Membrane-Bound Enzyme, 5'-Nucleotidase. Humana Press eBooks. 19. 229–242. 2 indexed citations
2.
Guest, Paul C., E M Bailyes, & John C. Hutton. (1997). Endoplasmic reticulum Ca2+ is important for the proteolytic processing and intracellular transport of proinsulin in the pancreatic β-cell. Biochemical Journal. 323(2). 445–450. 50 indexed citations
3.
Hurk, Helma van den, et al.. (1995). Identification of the Region within the Neuroendocrine Polypeptide 7B2 Responsible for the Inhibition of Prohormone Convertase PC2. Journal of Biological Chemistry. 270(24). 14292–14296. 59 indexed citations
4.
Bailyes, E M, et al.. (1995). Monoclonal antibodies recognize 2300 years aged alkaline phosphatase. Immunology Letters. 48(3). 187–191. 7 indexed citations
5.
Roep, Bart O., Wouter L. W. Hazenbos, Jan Bruining, et al.. (1994). T-cell reactivity to 38 kD insulin-secretory granule protein in patients with recent onset type 1 diabetes. Journal of Endocrinological Investigation. 17(7). 559–563. 3 indexed citations
6.
Bieg, Sabine, E M Bailyes, Josef Amann, et al.. (1993). A multiplicity of protein antigens in subcellular fractions of rat insulinoma tissue are able to stimulate T cells obtained from non-obese diabetic mice. Diabetologia. 36(5). 385–390. 18 indexed citations
7.
Bennett, D.L., E M Bailyes, Eva-Maria D. Nielsen, et al.. (1992). Identification of the type 2 proinsulin processing endopeptidase as PC2, a member of the eukaryote subtilisin family.. Journal of Biological Chemistry. 267(21). 15229–15236. 132 indexed citations
8.
Mullock, Barbara M., et al.. (1991). The presence and measurement of secretory component in human bile and blood. Clinica Chimica Acta. 197(3). 171–187. 6 indexed citations
9.
Roep, Bart O., Wouter L. W. Hazenbos, RenéR.P. de Vries, et al.. (1991). T-cell reactivity to 38 kD insulin-secretory-granule protein in patients with recent-onset type 1 diabetes. The Lancet. 337(8755). 1439–1441. 94 indexed citations
10.
Bailyes, E M, Michael A. J. Ferguson, Camilo Colaço, & J. Paul Luzio. (1990). Inositol is a constituent of detergent-solubilized immunoaffinity-purified rat liver 5′-nucleotidase. Biochemical Journal. 265(3). 907–909. 22 indexed citations
11.
Miura, Masakazu, et al.. (1989). Differences between human liver- and bone-type alkaline phosphatases. Clinica Chimica Acta. 180(2). 177–187. 32 indexed citations
12.
Rhodes, Christopher J., et al.. (1989). The inhibition of proinsulin-processing endopeptidase activities by active-site-directed peptides. Biochemical Journal. 258(1). 305–308. 31 indexed citations
13.
Bailyes, E M, et al.. (1988). A monoclonal antibody capture assay for intestinal alkaline phosphatase and the measurement of this isoenzyme in pregnancy. Clinica Chimica Acta. 172(2-3). 267–274. 7 indexed citations
14.
Bailyes, E M, et al.. (1988). The distinction of bone and liver isoenzymes of alkaline phosphatase in serum using a monoclonal antibody. Clinica Chimica Acta. 172(2-3). 261–266. 25 indexed citations
15.
Bailyes, E M, J Calvin, Gerald A. Maguire, et al.. (1987). The preparation of monoclonal antibodies to human bone and liver alkaline phosphatase and their use in immunoaffinity purification and in studying these enzymes when present in serum. Biochemical Journal. 244(3). 725–733. 29 indexed citations
16.
Bailyes, E M, Kenneth Siddle, & J. Paul Luzio. (1985). Monoclonal antibodies against human alkaline phosphatases. Biochemical Society Transactions. 13(1). 107–107. 2 indexed citations
17.
Bailyes, E M, Maria A. Soos, Peter Jackson, et al.. (1984). The existence and properties of two dimers of rat liver ecto-5′-nucleotidase. Biochemical Journal. 221(2). 369–377. 40 indexed citations
18.
Bailyes, E M, Andrew C. Newby, Kenneth Siddle, & J. Paul Luzio. (1982). Solubilization and purification of rat liver 5′-nucleotidase by use of a zwitterionic detergent and a monoclonal-antibody immunoadsorbent. Biochemical Journal. 203(1). 245–251. 61 indexed citations
19.
Siddle, Kenneth, E M Bailyes, & J. Paul Luzio. (1981). A monoclonal antibody inhibiting rat liver 5′‐nucleotidase. FEBS Letters. 128(1). 103–107. 27 indexed citations
20.
Bailyes, E M, J. Paul Luzio, & Andrew C. Newby. (1981). The use of a zwitterionic detergent in the solubilization and purification of the intrinsic membrane protein 5′-nucleotidase. Biochemical Society Transactions. 9(1). 140–141. 9 indexed citations

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