Leonard C. Packman

3.0k total citations
62 papers, 2.5k citations indexed

About

Leonard C. Packman is a scholar working on Molecular Biology, Biochemistry and Clinical Biochemistry. According to data from OpenAlex, Leonard C. Packman has authored 62 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 29 papers in Biochemistry and 21 papers in Clinical Biochemistry. Recurrent topics in Leonard C. Packman's work include Biochemical Acid Research Studies (22 papers), Metabolism and Genetic Disorders (21 papers) and Enzyme Structure and Function (12 papers). Leonard C. Packman is often cited by papers focused on Biochemical Acid Research Studies (22 papers), Metabolism and Genetic Disorders (21 papers) and Enzyme Structure and Function (12 papers). Leonard C. Packman collaborates with scholars based in United Kingdom, United States and South Sudan. Leonard C. Packman's co-authors include Richard N. Perham, Dudley H. Williams, Mark S. Searle, Sandra Robb, Peter D. Evans, Nigel S. Scrutton, John C. Gray, Lloyd D. Graham, William V. Shaw and F. Scott Mathews and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Leonard C. Packman

62 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Leonard C. Packman United Kingdom	30	1.6k	775	548	400	304	62	2.5k
E.S. Canellakis United States	38	3.7k 2.3×	1.5k 1.9×	358 0.7×	143 0.4×	337 1.1×	102	4.4k
Hideyuki Hayashi Japan	32	1.9k 1.2×	672 0.9×	118 0.2×	822 2.1×	142 0.5×	93	2.9k
R. BRIAN BEECHEY United Kingdom	26	1.9k 1.2×	215 0.3×	228 0.4×	114 0.3×	197 0.6×	114	2.9k
Guy Branlant France	36	3.0k 1.8×	710 0.9×	350 0.6×	886 2.2×	150 0.5×	121	3.7k
C W Tabor United States	28	3.5k 2.2×	1.7k 2.1×	181 0.3×	170 0.4×	615 2.0×	35	4.1k
Hans Ulrich Schairer Germany	28	2.3k 1.4×	222 0.3×	147 0.3×	205 0.5×	211 0.7×	67	2.9k
Riccardo Percudani Italy	25	1.7k 1.1×	264 0.3×	163 0.3×	353 0.9×	453 1.5×	67	2.5k
Alexander J. Kastaniotis Finland	29	1.8k 1.1×	509 0.7×	348 0.6×	173 0.4×	403 1.3×	50	2.5k
T. Hastings Wilson United States	30	1.5k 0.9×	424 0.5×	122 0.2×	280 0.7×	180 0.6×	68	2.3k
A.E. Senior United States	43	4.6k 2.9×	167 0.2×	455 0.8×	358 0.9×	100 0.3×	90	5.6k

Countries citing papers authored by Leonard C. Packman

Since Specialization

Citations

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

Fields of papers citing papers by Leonard C. Packman

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leonard C. Packman. 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 Leonard C. Packman. The network helps show where Leonard C. Packman may publish in the future.

Co-authorship network of co-authors of Leonard C. Packman

This figure shows the co-authorship network connecting the top 25 collaborators of Leonard C. Packman. A scholar is included among the top collaborators of Leonard C. Packman 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 Leonard C. Packman. Leonard C. Packman 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

Webster, Carl I., Leonard C. Packman, & John C. Gray. (2001). HMG‐1 enhances HMG‐I/Y binding to an A/T‐rich enhancer element from the pea plastocyanin gene. European Journal of Biochemistry. 268(11). 3154–3162. 22 indexed citations

Webster, Carl I., Leonard C. Packman, Keng‐Hock Pwee, & John C. Gray. (1997). High mobility group proteins HMG‐1 and HMG‐I/Y bind to a positive regulatory region of the pea plastocyanin gene promoter. The Plant Journal. 11(4). 703–715. 73 indexed citations

Mewies, Martin, Leonard C. Packman, F. Scott Mathews, & Nigel S. Scrutton. (1996). Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine. Biochemical Journal. 317(1). 267–272. 19 indexed citations

Searle, Mark S., et al.. (1996). Native-like β-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues. Protein Engineering Design and Selection. 9(7). 559–565. 63 indexed citations

Packman, Leonard C. & Alan Berry. (1995). A Reactive, Surface Cysteine Residue of the Class‐II Fructose‐1,6‐Bisphosphate Aldolase of Escherichia coli Revealed by Electrospray Ionisation Mass Spectrometry. European Journal of Biochemistry. 227(1-2). 510–515. 19 indexed citations

Yang, Chien‐Chih, Leonard C. Packman, & Nigel S. Scrutton. (1995). The Primary Structure of Hyphomicrobium X Dimethylamine Dehydrogenase. European Journal of Biochemistry. 232(1). 264–271. 34 indexed citations

Packman, Leonard C., Martin Mewies, & Nigel S. Scrutton. (1995). The Flavinylation Reaction of Trimethylamine Dehydrogenase.. Journal of Biological Chemistry. 270(22). 13186–13191. 20 indexed citations

Mathews, F. Scott, et al.. (1995). Electron Tunneling in Substrate-Reduced Trimethylamine Dehydrogenase: Kinetics of Electron Transfer and Analysis of the Tunneling Pathway. Biochemistry. 34(8). 2584–2591. 17 indexed citations

Gray, John C., et al.. (1994). Proteolytic removal of the C‐terminal transmembrane region of cytochrome f during extraction from turnip and charlock leaves generates a water‐soluble monomeric form of the protein. European Journal of Biochemistry. 223(2). 481–488. 11 indexed citations

10.

Cox, J. P., Philip A. Evans, Leonard C. Packman, Dudley H. Williams, & Derek N. Woolfson. (1993). Dissecting the Structure of a Partially Folded Protein. Journal of Molecular Biology. 234(2). 483–492. 108 indexed citations

11.

Mathews, F. Scott, et al.. (1992). Trimethylamine dehydrogenase of bacterium W₃A₁ Molecular cloning, sequence determination and over‐expression of the gene. FEBS Letters. 308(3). 271–276. 46 indexed citations

12.

Caffrey, Patrick, et al.. (1991). An acyl‐carrier‐protein – thioesterase domain from the 6‐deoxyerythronolide B synthase of Saccharopolyspora erythraea. European Journal of Biochemistry. 195(3). 823–830. 54 indexed citations

13.

Gay, Nicholas J., et al.. (1991). A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a β‐sheet structure. FEBS Letters. 291(1). 87–91. 58 indexed citations

14.

Borges, Adolfo, Christopher F. Hawkins, Leonard C. Packman, & Richard N. Perham. (1990). Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. European Journal of Biochemistry. 194(1). 95–102. 51 indexed citations

15.

Dardel, Frédéric, Leonard C. Packman, & Richard N. Perham. (1990). Expression in Escherichia coli of a sub‐gene encoding the lipoyl domain of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. FEBS Letters. 264(2). 206–210. 35 indexed citations

16.

Perham, Richard N. & Leonard C. Packman. (1989). 2‐Oxo Acid Dehydrogenase Multienzyme Complexes: Domains, Dynamics, and Design^a. Annals of the New York Academy of Sciences. 573(1). 1–20. 77 indexed citations

17.

Graham, Lloyd D., Leonard C. Packman, & Richard N. Perham. (1989). Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes. Biochemistry. 28(4). 1574–1581. 59 indexed citations

18.

Webber, Andrew N., Leonard C. Packman, & John C. Gray. (1989). A 10 kDa polypeptide associated with the oxygen‐evolving complex of photosystem II has a putative C‐terminal non‐cleavable thylakoid transfer domain. FEBS Letters. 242(2). 435–438. 26 indexed citations

19.

Graham, Lloyd D., John R. Guest, Hilary Lewis, et al.. (1986). The pyruvate dehydrogenase multi-enzyme complex of Escherichia coli : genetic reconstruction and functional analysis of the lipoyl domains. Philosophical Transactions of the Royal Society of London Series A Mathematical and Physical Sciences. 317(1540). 391–404. 15 indexed citations

20.

Packman, Leonard C., Richard N. Perham, & Gordon C. K. Roberts. (1984). Domain structure and1H-n.m.r. spectroscopy of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. Biochemical Journal. 217(1). 219–227. 45 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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