J.F. Cutfield

2.2k total citations · 1 hit paper
36 papers, 1.8k citations indexed

About

J.F. Cutfield is a scholar working on Molecular Biology, Nutrition and Dietetics and Biotechnology. According to data from OpenAlex, J.F. Cutfield has authored 36 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 9 papers in Nutrition and Dietetics and 9 papers in Biotechnology. Recurrent topics in J.F. Cutfield's work include Enzyme Production and Characterization (9 papers), Microbial Metabolites in Food Biotechnology (6 papers) and Enzyme Structure and Function (6 papers). J.F. Cutfield is often cited by papers focused on Enzyme Production and Characterization (9 papers), Microbial Metabolites in Food Biotechnology (6 papers) and Enzyme Structure and Function (6 papers). J.F. Cutfield collaborates with scholars based in New Zealand, United Kingdom and Australia. J.F. Cutfield's co-authors include E.J. Dodson, Susan M. Cutfield, Guy Dodson, D. C. Hodgkin, T.L. Blundell, Dan Mercola, S.M. Cutfield, Roderick E. Hubbard, Edward N. Baker and T.L. Blundell and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

J.F. Cutfield

36 papers receiving 1.7k citations

Hit Papers

The structure of 2Zn pig insulin crystals at 1.5 Å resolu... 1988 2026 2000 2013 1988 100 200 300 400 500
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. The structure of 2Zn pig insulin crystals at 1.5 Å resolution
    1988 558 citations Edward N. Baker, T.L. Blundell et al. Philosophical transactions of the Royal Society of London. Series B, Biological sciences profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.F. Cutfield New Zealand 22 1.2k 307 299 221 189 36 1.8k
Walter C. Mahoney United States 26 1.6k 1.3× 222 0.7× 165 0.6× 163 0.7× 162 0.9× 48 2.5k
Charles A. Collyer Australia 24 915 0.8× 176 0.6× 338 1.1× 242 1.1× 83 0.4× 57 1.8k
Hubertus M. Verheij Netherlands 35 2.6k 2.2× 253 0.8× 160 0.5× 85 0.4× 132 0.7× 79 3.3k
Yee‐Hsiung Chen Taiwan 19 1.9k 1.5× 105 0.3× 263 0.9× 132 0.6× 75 0.4× 33 2.7k
Frederick H. Carpenter United States 31 1.9k 1.6× 225 0.7× 218 0.7× 146 0.7× 114 0.6× 69 2.8k
T.L. Blundell United Kingdom 21 1.3k 1.1× 194 0.6× 305 1.0× 307 1.4× 92 0.5× 30 1.8k
S. P. Wood United Kingdom 17 1.1k 0.9× 147 0.5× 235 0.8× 139 0.6× 116 0.6× 45 1.4k
Gregory D. Reinhart United States 25 1.6k 1.3× 254 0.8× 463 1.5× 161 0.7× 52 0.3× 75 2.0k
Jui‐Yoa Chang United States 29 1.8k 1.5× 163 0.5× 261 0.9× 37 0.2× 141 0.7× 93 2.8k
B S Hartley United Kingdom 20 2.4k 2.0× 122 0.4× 449 1.5× 127 0.6× 226 1.2× 28 3.5k

Countries citing papers authored by J.F. Cutfield

Since Specialization
Citations

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

Fields of papers citing papers by J.F. Cutfield

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J.F. Cutfield

This figure shows the co-authorship network connecting the top 25 collaborators of J.F. Cutfield. A scholar is included among the top collaborators of J.F. Cutfield 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 J.F. Cutfield. J.F. Cutfield 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.
Nakatani, Yoshio, David S. Larsen, S.M. Cutfield, & J.F. Cutfield. (2014). Major Change in Regiospecificity for the Exo-1,3-β-glucanase from Candida albicans following Its Conversion to a Glycosynthase. Biochemistry. 53(20). 3318–3326. 8 indexed citations
2.
Nakatani, Yoshio, Susan M. Cutfield, Nathan Cowieson, & J.F. Cutfield. (2011). Structure and activity of exo‐1,3/1,4‐β‐glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C‐terminal domain. FEBS Journal. 279(3). 464–478. 28 indexed citations
3.
4.
Mace, Peter D., et al.. (2006). Bacterial expression and purification of the ovine type II bone morphogenetic protein receptor ectodomain. Protein Expression and Purification. 52(1). 40–49. 4 indexed citations
5.
Mace, Peter D., et al.. (2006). High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: Implications for ligand binding. Biochemical and Biophysical Research Communications. 351(4). 831–838. 43 indexed citations
6.
Cutfield, J.F., et al.. (2004). Biophysical Characterization of ERp29. Journal of Biological Chemistry. 280(14). 13529–13537. 22 indexed citations
7.
8.
Cutfield, J.F., et al.. (2001). New BEL-like LTR-retrotransposons in Fugu rubripes , Caenorhabditis elegans , and Drosophila melanogaster. Gene. 263(1-2). 219–230. 39 indexed citations
9.
Cutfield, J.F., P. A. Sullivan, & S.M. Cutfield. (2000). Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase. Protein Engineering Design and Selection. 13(10). 735–738. 22 indexed citations
10.
Davies, G.J., Garib N. Murshudov, Bryan F. Anderson, et al.. (1999). The structure of the exo-β-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases 1 1Edited by I. A. Wilson. Journal of Molecular Biology. 294(3). 771–783. 92 indexed citations
11.
Abad‐Zapatero, Cele, Robert C. Goldman, Steven W. Muchmore, et al.. (1998). Structure of Secreted Aspartic Proteinases from Candida. Advances in experimental medicine and biology. 436. 297–313. 13 indexed citations
12.
Mackenzie, Lloyd, et al.. (1997). Identification of Glu-330 as the Catalytic Nucleophile of Candida albicans Exo-β-(1,3)-glucanase. Journal of Biological Chemistry. 272(6). 3161–3167. 50 indexed citations
13.
Chambers, Ross, et al.. (1993). Identification of a putative active site residue in the exo‐β‐(1,3)‐glucanase of Candida albicans. FEBS Letters. 327(3). 366–369. 24 indexed citations
14.
Marshall, C. J., et al.. (1993). Crystallization of Inhibited Aspartic Proteinase from Candida albicans. Journal of Molecular Biology. 234(4). 1266–1269. 13 indexed citations
15.
Sullivan, Patrick S., et al.. (1992). Crystallization of the exo(1,3)-β-glucanase from Candida albicans. Journal of Molecular Biology. 225(1). 217–218. 8 indexed citations
16.
Baker, Edward N., et al.. (1988). The structure of 2Zn pig insulin crystals at 1.5 Å resolution. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 319(1195). 369–456. 558 indexed citations breakdown →
17.
Galloway, Susan & J.F. Cutfield. (1988). Insulin-like meterial from the digestive tract of the tunicate Pyura pachydermatina (sea tulip). General and Comparative Endocrinology. 69(1). 106–113. 9 indexed citations
18.
Sullivan, P. A., et al.. (1977). The structure of L-lactate oxidase from Mycobacterium smegmatis. Biochemical Journal. 165(2). 375–383. 42 indexed citations
19.
20.
Cutfield, J.F., David R. Hall, & T. N. Waters. (1967). The crystal structure of copper(II) pyridoxylidene (±)-valine complex. Chemical Communications (London). 0(15). 785–786. 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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