H. Nicholson

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

About

H. Nicholson is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, H. Nicholson has authored 14 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 12 papers in Materials Chemistry and 4 papers in Ecology. Recurrent topics in H. Nicholson's work include Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (12 papers) and RNA and protein synthesis mechanisms (5 papers). H. Nicholson is often cited by papers focused on Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (12 papers) and RNA and protein synthesis mechanisms (5 papers). H. Nicholson collaborates with scholars based in United States and New Zealand. H. Nicholson's co-authors include Brian W. Matthews, Wayne J. Becktel, Brian W. Matthews, Uwe H. Sauer, David E. Anderson, S. Daopin, Walter A. Baase, Jeffrey A. Bell, Dale E. Tronrud and Anthony R. Poteete and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

H. Nicholson

14 papers receiving 1.8k citations

Hit Papers

align trajectories

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.

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.

1987 647 citations Brian W. Matthews, H. Nicholson et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
H. Nicholson United States	13	1.6k	932	215	163	140	14	1.8k
Kyoko Ogasahara Japan	33	2.4k 1.5×	1.4k 1.5×	224 1.0×	158 1.0×	81 0.6×	91	2.8k
Nand K. Vyas United States	21	1.5k 1.0×	586 0.6×	161 0.7×	193 1.2×	84 0.6×	27	2.1k
Munehito Arai Japan	27	2.6k 1.6×	1.2k 1.3×	128 0.6×	214 1.3×	92 0.7×	81	3.0k
H. Klump South Africa	25	1.8k 1.2×	354 0.4×	69 0.3×	111 0.7×	147 1.1×	91	2.2k
Kyriacos Petratos Greece	19	1.7k 1.1×	445 0.5×	156 0.7×	97 0.6×	117 0.8×	47	2.0k
Eric de La Fortelle United Kingdom	11	2.2k 1.4×	898 1.0×	102 0.5×	119 0.7×	96 0.7×	14	2.8k
Masamichi Ikeguchi Japan	20	1.4k 0.9×	746 0.8×	107 0.5×	142 0.9×	46 0.3×	66	1.8k
Dimitri Gilis Belgium	22	2.1k 1.3×	565 0.6×	114 0.5×	90 0.6×	80 0.6×	41	2.5k
R. Bott United States	21	1.6k 1.0×	575 0.6×	484 2.3×	126 0.8×	99 0.7×	43	2.0k
Beatriz Ibarra‐Molero Spain	22	1.6k 1.0×	745 0.8×	63 0.3×	187 1.1×	60 0.4×	44	1.9k

Countries citing papers authored by H. Nicholson

Since Specialization

Citations

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

Fields of papers citing papers by H. Nicholson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by H. Nicholson. 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 H. Nicholson. The network helps show where H. Nicholson may publish in the future.

Co-authorship network of co-authors of H. Nicholson

This figure shows the co-authorship network connecting the top 25 collaborators of H. Nicholson. A scholar is included among the top collaborators of H. Nicholson 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 H. Nicholson. H. Nicholson is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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14 of 14 papers shown

Daopin, S., et al.. (2007). Structural and Genetic Analysis of Electrostatic and Other Interactions in Bacteriophage T4 Lysozyme. Novartis Foundation symposium. 161. 52–62. 1 indexed citations

Nicholson, H., et al.. (1997). Mutagenesis of the Histidine Ligand in Human Lactoferrin: Iron Binding Properties and Crystal Structure of the Histidine-253 → Methionine Mutant^,. Biochemistry. 36(2). 341–346. 30 indexed citations

Anderson, David E., James H. Hurley, H. Nicholson, Walter A. Baase, & Brian W. Matthews. (1993). Hydrophobic core repacking and aromatic–aromatic interaction in the thermostable mutant of T4 lysozyme ser 117 → phe. Protein Science. 2(8). 1285–1290. 68 indexed citations

Baase, Walter A., et al.. (1992). Folding kinetics of T4 lysozyme and nine mutants at 12 .degree.C. Biochemistry. 31(5). 1464–1476. 69 indexed citations

Dixon, M.M., H. Nicholson, Lisa M. Shewchuk, W.A. Baase, & Brian W. Matthews. (1992). Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3 → Pro. Journal of Molecular Biology. 227(3). 917–933. 69 indexed citations

Nicholson, H., Dale E. Tronrud, Wayne J. Becktel, & Brian W. Matthews. (1992). Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. Biopolymers. 32(11). 1431–1441. 50 indexed citations

Bell, Jeffrey A., et al.. (1991). Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins Structure Function and Bioinformatics. 10(1). 10–21. 49 indexed citations

Sauer, Uwe H., et al.. (1991). Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry. 30(29). 7142–7153. 211 indexed citations

Poteete, Anthony R., et al.. (1991). Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. Biochemistry. 30(5). 1425–1432. 91 indexed citations

10.

Nicholson, H., David E. Anderson, S. Daopin, & Brian W. Matthews. (1991). Analysis of the interaction between charged side chains and the .alpha.-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry. 30(41). 9816–9828. 145 indexed citations

11.

Nicholson, H., Eskil Söderlind, Dale E. Tronrud, & Brian W. Matthews. (1989). Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. Journal of Molecular Biology. 210(1). 181–193. 44 indexed citations

12.

Nicholson, H., Wayne J. Becktel, & Brian W. Matthews. (1988). Enhanced protein thermostability from designed mutations that interact with α-helix dipoles. Nature. 336(6200). 651–656. 244 indexed citations

13.

Alber, Tom, Jeffrey A. Bell, Sun Daopin, et al.. (1988). Replacements of Pro ⁸⁶ in Phage T4 Lysozyme Extend an α-Helix But Do Not Alter Protein Stability. Science. 239(4840). 631–635. 119 indexed citations

14.

Matthews, Brian W., H. Nicholson, & Wayne J. Becktel. (1987). Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.. Proceedings of the National Academy of Sciences. 84(19). 6663–6667. 647 indexed citations breakdown →

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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