Clark Ford

1.7k total citations
45 papers, 1.3k citations indexed

About

Clark Ford is a scholar working on Biotechnology, Molecular Biology and Oncology. According to data from OpenAlex, Clark Ford has authored 45 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Biotechnology, 21 papers in Molecular Biology and 17 papers in Oncology. Recurrent topics in Clark Ford's work include Enzyme Production and Characterization (33 papers), Peptidase Inhibition and Analysis (17 papers) and Microbial Metabolites in Food Biotechnology (11 papers). Clark Ford is often cited by papers focused on Enzyme Production and Characterization (33 papers), Peptidase Inhibition and Analysis (17 papers) and Microbial Metabolites in Food Biotechnology (11 papers). Clark Ford collaborates with scholars based in United States, Denmark and Finland. Clark Ford's co-authors include Peter J. Reilly, Charles E. Glatz, P. J. Reilly, Pedro M. Coutinho, Michael R. Sierks, Birte Svensson, Ilari Suominen, Wei-yeh Wang, C. R. Bronson and Z̆ivko L. Nikolov and has published in prestigious journals such as Applied and Environmental Microbiology, Biochemical Journal and Genetics.

In The Last Decade

Clark Ford

45 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Clark Ford United States 23 816 674 356 267 246 45 1.3k
Torben P. Frandsen Denmark 22 736 0.9× 776 1.2× 230 0.6× 334 1.3× 282 1.1× 33 1.2k
Takashi Tonozuka Japan 25 986 1.2× 1.0k 1.6× 406 1.1× 294 1.1× 536 2.2× 103 1.9k
Valerie Notenboom Canada 13 682 0.8× 382 0.6× 188 0.5× 309 1.2× 106 0.4× 13 1.1k
Karl Peter Rücknagel Germany 19 1.1k 1.4× 247 0.4× 113 0.3× 245 0.9× 110 0.4× 24 1.5k
Karin D. Breunig Germany 27 1.7k 2.0× 130 0.2× 377 1.1× 379 1.4× 165 0.7× 61 2.0k
D. J. Ballance United Kingdom 13 1.0k 1.2× 302 0.4× 501 1.4× 211 0.8× 70 0.3× 19 1.3k
Mário de Oliveira Neto Brazil 20 737 0.9× 316 0.5× 165 0.5× 459 1.7× 88 0.4× 52 1.4k
Sigrid Gåseidnes Norway 7 1.3k 1.6× 499 0.7× 285 0.8× 270 1.0× 53 0.2× 9 1.5k
Johanna Mansfeld Germany 18 736 0.9× 195 0.3× 123 0.3× 76 0.3× 71 0.3× 42 917
Paul V. Harris United States 19 1.2k 1.4× 576 0.9× 634 1.8× 972 3.6× 84 0.3× 28 1.8k

Countries citing papers authored by Clark Ford

Since Specialization
Citations

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

Fields of papers citing papers by Clark Ford

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Clark Ford

This figure shows the co-authorship network connecting the top 25 collaborators of Clark Ford. A scholar is included among the top collaborators of Clark Ford 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 Clark Ford. Clark Ford 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.
García‐Salinas, Carolina, et al.. (2010). Kinetic characterization of a glycoside hydrolase family 44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1. Enzyme and Microbial Technology. 48(1). 27–32. 15 indexed citations
2.
McDaniel, Allison L., et al.. (2008). Directed evolution of Aspergillus niger glucoamylase to increase thermostability. Microbial Biotechnology. 1(6). 523–531. 8 indexed citations
3.
Holding, David R., Brenda G. Hunter, Taijoon Chung, et al.. (2008). Genetic analysis of opaque2 modifier loci in quality protein maize. Theoretical and Applied Genetics. 117(2). 157–170. 68 indexed citations
4.
Liu, Hsuan‐Liang, Y. Doleyres, Pedro M. Coutinho, Clark Ford, & P. J. Reilly. (2000). Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability. Protein Engineering Design and Selection. 13(9). 655–659. 24 indexed citations
5.
Ford, Clark. (1999). Improving operating performance of glucoamylase by mutagenesis. Current Opinion in Biotechnology. 10(4). 353–357. 28 indexed citations
6.
Fang, Tsuei‐Yun, Pedro M. Coutinho, P. J. Reilly, & Clark Ford. (1998). Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48Phe49-->Trp, Tyr116-->Trp, Tyr175-->Phe, Arg241-->Lys, Ser411-- >Ala and Ser411-->Gly. Protein Engineering Design and Selection. 11(2). 119–126. 14 indexed citations
7.
Fang, Tsuei‐Yun & Clark Ford. (1998). Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum. Protein Engineering Design and Selection. 11(5). 383–388. 40 indexed citations
8.
9.
Li, Yuguo, Pedro M. Coutinho, & Clark Ford. (1998). Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase. Protein Engineering Design and Selection. 11(8). 661–667. 44 indexed citations
10.
Allen, Martin J., Pedro M. Coutinho, & Clark Ford. (1998). Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations. Protein Engineering Design and Selection. 11(9). 783–788. 44 indexed citations
11.
Reilly, P. J., et al.. (1997). Effect of introducing proline residues on the stability of Aspergillus awamori. Protein Engineering Design and Selection. 10(10). 1199–1204. 31 indexed citations
12.
Chen, Hsiu‐Mei, Clark Ford, & Peter J. Reilly. (1995). Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds in Aspergillus awamori glucoamylase. Protein Engineering Design and Selection. 8(6). 575–582. 23 indexed citations
13.
Reilly, P. J., et al.. (1994). Effect of amino acid deletions in the O-glycosylated region of Aspergillus awamori glucoamylase. Protein Engineering Design and Selection. 7(9). 1109–1114. 29 indexed citations
14.
Gorman, Maureen J., et al.. (1994). Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: inactivation kinetics and structural interpretation. Protein Engineering Design and Selection. 7(8). 1005–1012. 17 indexed citations
15.
Sierks, Michael R., Clark Ford, P. J. Reilly, & Birte Svensson. (1993). Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis. Protein Engineering Design and Selection. 6(1). 75–79. 20 indexed citations
16.
17.
Chen, Luojing, Clark Ford, Ann Kusnadi, & Z̆ivko L. Nikolov. (1991). Improved Adsorption to Starch of a β‐Galactosidase Fusion Protein Containing the Starch‐Binding Domain from Aspergillus Glucoamylase. Biotechnology Progress. 7(3). 225–229. 15 indexed citations
18.
Sierks, Michael R., Clark Ford, Peter J. Reilly, & Birte Svensson. (1990). Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori. Protein Engineering Design and Selection. 3(3). 193–198. 96 indexed citations
19.
Glatz, Charles E., et al.. (1990). Recovery of a charged‐fusion protein from cell extracts by polyelectrolyte precipitation. Biotechnology and Bioengineering. 36(5). 467–475. 28 indexed citations
20.
Sierks, Michael R., Clark Ford, Peter J. Reilly, & Birte Svensson. (1989). Site-directed mutagenesis at the active site Trpl20 of Aspergillus awamori glucoamylase. Protein Engineering Design and Selection. 2(8). 621–625. 52 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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