P.F. Zagalsky

1.9k total citations
57 papers, 1.5k citations indexed

About

P.F. Zagalsky is a scholar working on Molecular Biology, Aquatic Science and Cellular and Molecular Neuroscience. According to data from OpenAlex, P.F. Zagalsky has authored 57 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 18 papers in Aquatic Science and 17 papers in Cellular and Molecular Neuroscience. Recurrent topics in P.F. Zagalsky's work include Antioxidant Activity and Oxidative Stress (17 papers), Neurobiology and Insect Physiology Research (16 papers) and Aquaculture Nutrition and Growth (16 papers). P.F. Zagalsky is often cited by papers focused on Antioxidant Activity and Oxidative Stress (17 papers), Neurobiology and Insect Physiology Research (16 papers) and Aquaculture Nutrition and Growth (16 papers). P.F. Zagalsky collaborates with scholars based in United Kingdom, France and United States. P.F. Zagalsky's co-authors include D. F. Cheesman, Hubert J. Ceccaldi, Naomi E. Chayen, John R. Helliwell, Elias Eliopoulos, James Raftery, P.J. Rizkallah, Michele Cianci, Andrzej Ołczak and R. Daumas and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

P.F. Zagalsky

57 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
P.F. Zagalsky United Kingdom	21	504	490	485	414	361	57	1.5k
Roman Ulm Switzerland	39	286 0.6×	72 0.1×	4.6k 9.5×	472 1.1×	159 0.4×	69	6.8k
N. Murata Japan	35	127 0.3×	79 0.2×	3.2k 6.5×	332 0.8×	365 1.0×	66	4.9k
Elisabeth Gantt United States	33	958 1.9×	111 0.2×	2.9k 6.0×	210 0.5×	257 0.7×	82	3.6k
F. T. Haxo United States	23	58 0.1×	74 0.2×	763 1.6×	113 0.3×	541 1.5×	45	1.9k
D. F. Cheesman United Kingdom	11	127 0.3×	184 0.4×	160 0.3×	106 0.3×	125 0.3×	20	629
Riccardo Stradi Italy	22	384 0.8×	61 0.1×	256 0.5×	114 0.3×	536 1.5×	108	2.0k
Michèle C. Loewen Canada	23	77 0.2×	70 0.1×	940 1.9×	406 1.0×	351 1.0×	68	1.9k
Alfred Batschauer Germany	41	327 0.6×	45 0.1×	3.6k 7.4×	1.4k 3.4×	153 0.4×	81	5.9k
Robert MacColl United States	27	73 0.1×	61 0.1×	1.9k 4.0×	276 0.7×	145 0.4×	92	2.7k
Kirk E. Apt United States	20	47 0.1×	173 0.4×	1.7k 3.6×	62 0.1×	661 1.8×	36	2.6k

Countries citing papers authored by P.F. Zagalsky

Since Specialization

Citations

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

Fields of papers citing papers by P.F. Zagalsky

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by P.F. Zagalsky. 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 P.F. Zagalsky. The network helps show where P.F. Zagalsky may publish in the future.

Co-authorship network of co-authors of P.F. Zagalsky

This figure shows the co-authorship network connecting the top 25 collaborators of P.F. Zagalsky. A scholar is included among the top collaborators of P.F. Zagalsky 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 P.F. Zagalsky. P.F. Zagalsky 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

Habash, J., John R. Helliwell, James Raftery, et al.. (2004). The structure and refinement of apocrustacyanin C₂to 1.3 Å resolution and the search for differences between this protein and the homologous apoproteins A₁and C₁. Acta Crystallographica Section D Biological Crystallography. 60(3). 493–498. 9 indexed citations

Chayen, Naomi E., Michele Cianci, J. Günter Grossmann, et al.. (2003). Unravelling the structural chemistry of the colouration mechanism in lobster shell. Acta Crystallographica Section D Biological Crystallography. 59(12). 2072–2082. 77 indexed citations

Habash, J., Titus J. Boggon, James Raftery, et al.. (2003). Apocrustacyanin C₁crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons. Acta Crystallographica Section D Biological Crystallography. 59(7). 1117–1123. 9 indexed citations

Dellisanti, Cosma, Silvia Spinelli, Christian Cambillau, et al.. (2003). Quaternary structure of alpha‐crustacyanin from lobster as seen by small‐angle X‐ray scattering. FEBS Letters. 544(1-3). 189–193. 17 indexed citations

Cianci, Michele, P.J. Rizkallah, Andrzej Ołczak, et al.. (2001). Structure of lobster apocrustacyanin A₁using softer X-rays. Acta Crystallographica Section D Biological Crystallography. 57(9). 1219–1229. 34 indexed citations

Gordon, E., Gordon A. Leonard, Seán McSweeney, & P.F. Zagalsky. (2001). The C₁subunit of α-crustacyanin: thede novophasing of the crystal structure of a 40 kDa homodimeric protein using the anomalous scattering from S atoms combined with direct methods. Acta Crystallographica Section D Biological Crystallography. 57(9). 1230–1237. 22 indexed citations

Chayen, Naomi E., Michele Cianci, Andrzej Ołczak, et al.. (2000). Apocrustacyanin A1 from the lobster carotenoprotein α-crustacyanin: crystallization and initial X-ray analysis involving softer X-rays. Acta Crystallographica Section D Biological Crystallography. 56(8). 1064–1066. 5 indexed citations

Chayen, Naomi E., Titus J. Boggon, James Raftery, John R. Helliwell, & P.F. Zagalsky. (1999). Purification, crystallization and initial X-ray analysis of the C₁subunit of the astaxanthin protein, V_600,of the chondrophoreVelella velella. Acta Crystallographica Section D Biological Crystallography. 55(1). 266–268. 1 indexed citations

Snell, Edward H., Alberto Cassetta, John R. Helliwell, et al.. (1997). Partial Improvement of Crystal Quality for Microgravity-Grown Apocrustacyanin C₁. Acta Crystallographica Section D Biological Crystallography. 53(3). 231–239. 19 indexed citations

10.

Chayen, Naomi E., E. Gordon, Simon E. V. Phillips, Emmanuel Saridakis, & P.F. Zagalsky. (1996). Crystallization and initial X-ray analysis of β-crustacyanin, the dimer of apoproteins A2 and C1, each with a bound astaxanthin molecule. Acta Crystallographica Section D Biological Crystallography. 52(2). 409–410. 4 indexed citations

11.

Chayen, Naomi E., Emma Gordon, & P.F. Zagalsky. (1996). Crystallization of apocrustacyanin on the International Microgravity Laboratory (IML-2) mission. Acta Crystallographica Section D Biological Crystallography. 52(1). 156–159. 7 indexed citations

12.

Zagalsky, P.F., et al.. (1995). Crystallisation of α-crustacyanin, the lobster capapace astaxanthin-protein: Results from EURECA. Advances in Space Research. 16(8). 91–94. 11 indexed citations

13.

Wright, Charles E., John B. Rafferty, Darren R. Flower, et al.. (1992). Crystallization and initial X-ray analysis of the C2-subunit of crustacyanin. Journal of Molecular Biology. 224(1). 283–284. 11 indexed citations

14.

Keen, Jeffrey N., et al.. (1991). Complete sequence and model for the A₂ subunit of the carotenoid pigment complex, crustacyanin. European Journal of Biochemistry. 197(2). 407–417. 52 indexed citations

15.

Zagalsky, P.F., Elias Eliopoulos, & J. B. C. Findlay. (1991). The lobster carapace carotenoprotein, α-crustacyanin. A possible role for tryptophan in the bathochromic spectral shift of protein-bound astaxanthin. Biochemical Journal. 274(1). 79–83. 17 indexed citations

16.

Keen, Jeffrey N., et al.. (1991). Complete sequence and model for the C₁ subunit of the carotenoprotein crustacyanin, and model for the dimer, β‐crustacyanin, formed from the C₁ and A₂ subunits with astaxanthin. European Journal of Biochemistry. 202(1). 31–40. 37 indexed citations

17.

Zagalsky, P.F.. (1985). [9] Invertebrate carotenoproteins. Methods in enzymology on CD-ROM/Methods in enzymology. 111. 216–247. 59 indexed citations

18.

Clark, Robin J. H., et al.. (1980). Excitation profiles, absorption and resonance Raman spectra of the carotenoprotein ovorubin, and a resonance Raman study of some other astaxanthin proteins. Journal of the American Chemical Society. 102(22). 6693–6698. 27 indexed citations

19.

Zagalsky, P.F. & Peter J. Herring. (1977). Studies of the blue astaxanthin-proteins of velella velella (coelenterata: chondrophora). Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 279(964). 289–326. 29 indexed citations

20.

Zagalsky, P.F., D. F. Cheesman, & Hubert J. Ceccaldi. (1967). Studies on carotenoid-containing lipoproteins isolated from the eggs and ovaries of certain marine invertebrates. Comparative Biochemistry and Physiology. 22(3). 851–871. 76 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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