K.C. Ingham

2.4k total citations · 1 hit paper
42 papers, 2.1k citations indexed

About

K.C. Ingham is a scholar working on Molecular Biology, Immunology and Allergy and Cancer Research. According to data from OpenAlex, K.C. Ingham has authored 42 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 12 papers in Immunology and Allergy and 11 papers in Cancer Research. Recurrent topics in K.C. Ingham's work include Cell Adhesion Molecules Research (12 papers), Protease and Inhibitor Mechanisms (11 papers) and Monoclonal and Polyclonal Antibodies Research (7 papers). K.C. Ingham is often cited by papers focused on Cell Adhesion Molecules Research (12 papers), Protease and Inhibitor Mechanisms (11 papers) and Monoclonal and Polyclonal Antibodies Research (7 papers). K.C. Ingham collaborates with scholars based in United States, United Kingdom and Russia. K.C. Ingham's co-authors include Donald H. Atha, Shelesa A. Brew, D Ménaché, Shirley I. Miekka, Thomas F. Busby, Harold Edelhoch, Leonid Medved, Mary Migliorini, Salvatore M. Aloj and Valery Novokhatny and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

K.C. Ingham

42 papers receiving 2.0k citations

Hit Papers

Mechanism of precipitation of proteins by polyethylene gl... 1981 2026 1996 2011 1981 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
K.C. Ingham United States 23 1.0k 547 380 340 233 42 2.1k
Kenneth C. Ingham United States 29 944 0.9× 539 1.0× 386 1.0× 423 1.2× 274 1.2× 69 2.5k
Milton E. Noelken United States 26 936 0.9× 969 1.8× 239 0.6× 253 0.7× 249 1.1× 49 2.2k
Gerd Bendas Germany 32 1.8k 1.8× 441 0.8× 359 0.9× 440 1.3× 240 1.0× 118 3.3k
Michael Etzerodt Denmark 30 1.6k 1.6× 242 0.4× 703 1.9× 294 0.9× 364 1.6× 69 2.8k
Suet‐Mien Tan Singapore 23 806 0.8× 721 1.3× 245 0.6× 326 1.0× 196 0.8× 66 2.1k
Toshihiko Takeuchi Japan 21 684 0.7× 159 0.3× 275 0.7× 107 0.3× 256 1.1× 97 2.1k
Helmut Hörmann Germany 22 644 0.6× 756 1.4× 423 1.1× 446 1.3× 120 0.5× 96 1.8k
Jay E. Valinsky United States 27 905 0.9× 250 0.5× 204 0.5× 148 0.4× 488 2.1× 43 2.9k
Steven Rosenberg United States 27 1.8k 1.8× 1.0k 1.9× 1.9k 4.9× 356 1.0× 1.0k 4.5× 49 4.1k
M. Laurie Phillips United States 21 1.7k 1.6× 1.3k 2.4× 188 0.5× 299 0.9× 366 1.6× 47 3.3k

Countries citing papers authored by K.C. Ingham

Since Specialization
Citations

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

Fields of papers citing papers by K.C. Ingham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K.C. Ingham

This figure shows the co-authorship network connecting the top 25 collaborators of K.C. Ingham. A scholar is included among the top collaborators of K.C. Ingham 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 K.C. Ingham. K.C. Ingham 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.
Raju, Suneil A, K.C. Ingham, Calvin M. Johnson, et al.. (2024). What is the Role of Measuring Urinary Gluten Immunogenic Peptides in Clinical Practice in Patients with Coeliac Disease?. Journal of Gastrointestinal and Liver Diseases. 33(4). 482–487. 1 indexed citations
2.
Shiha, Mohamed G., K.C. Ingham, Suneil A Raju, et al.. (2024). Role of capsule endoscopy and double-balloon enteroscopy in the management of adult patients with coeliac disease and persisting symptoms. Endoscopy. 56(S 02). S64–S64. 1 indexed citations
3.
Ingham, K.C., Shelesa A. Brew, & Mary Migliorini. (2002). Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity. Archives of Biochemistry and Biophysics. 407(2). 217–223. 28 indexed citations
4.
Ingham, K.C., Shelesa A. Brew, & Valery Novokhatny. (1995). Influence of Carbohydrate on Structure, Stability, and Function of Gelatin-Binding Fragments of Fibronectin. Archives of Biochemistry and Biophysics. 316(1). 235–240. 21 indexed citations
5.
Ingham, K.C., Shelesa A. Brew, & Mary Migliorini. (1994). An Unusual Heparin-Binding Peptide from the Carboxy-Terminal hep-2 Region of Fibronectin. Archives of Biochemistry and Biophysics. 314(1). 242–246. 18 indexed citations
6.
Rivas, Germán, K.C. Ingham, & Allen P. Minton. (1994). Ca2+-Linked Association of Human Complement C1s.hivin. and C1r.hivin.. Biochemistry. 33(8). 2341–2348. 18 indexed citations
7.
Matsuka, Yury V., Leonid Medved, Shelesa A. Brew, & K.C. Ingham. (1994). The NH2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coli. Journal of Biological Chemistry. 269(13). 9539–9546. 39 indexed citations
8.
Ingham, K.C., Shelesa A. Brew, Mary Migliorini, & Thomas F. Busby. (1993). Binding of heparin by type III domains and peptides from the carboxy terminal Hep-2 region of fibronectin. Biochemistry. 32(46). 12548–12553. 45 indexed citations
9.
Radek, James T., Jae Min Jeong, S. N. Prasanna Murthy, K.C. Ingham, & L. Lóránd. (1993). Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin.. Proceedings of the National Academy of Sciences. 90(8). 3152–3156. 69 indexed citations
10.
Rivas, Germán, K.C. Ingham, & Allen P. Minton. (1992). Calcium ion induced self-association of human complement C1.lovin.s. Biochemistry. 31(47). 11707–11712. 17 indexed citations
11.
Ingham, K.C. & Shelesa A. Brew. (1992). Integrity of refolded and reoxidized gelatin‐binding fragments of fibronectin. Proteins Structure Function and Bioinformatics. 12(2). 180–187. 7 indexed citations
12.
Novokhatny, Valery, K.C. Ingham, & Leonid Medved. (1991). Domain structure and domain-domain interactions of recombinant tissue plasminogen activator. Journal of Biological Chemistry. 266(20). 12994–13002. 44 indexed citations
13.
Busby, Thomas F. & K.C. Ingham. (1990). Amino-terminal calcium-binding domain of human complement C1.hivin.s mediates the interaction of C1.hivin.r with C1q. Biochemistry. 29(19). 4613–4618. 53 indexed citations
14.
Filimonov, Vladimir V., Peter L. Privalov, Madis Metsis, et al.. (1990). Co-operative domains in fibronectin. Journal of Molecular Biology. 211(1). 161–169. 16 indexed citations
15.
Busby, Thomas F. & K.C. Ingham. (1988). Domain structure, stability, and interactions of human complement C1.lovin.s: characterization of a derivative lacking most of the B chain. Biochemistry. 27(16). 6127–6135. 24 indexed citations
16.
Busby, Thomas F. & K.C. Ingham. (1987). Calcium-sensitive thermal transitions and domain structure of human complement subcomponent C1.hivin.r. Biochemistry. 26(17). 5564–5571. 20 indexed citations
17.
Ingham, K.C., Shelesa A. Brew, T J Broekelmann, & J.A. McDonald. (1984). Thermal stability of human plasma fibronectin and its constituent domains.. Journal of Biological Chemistry. 259(19). 11901–11907. 43 indexed citations
18.
Miekka, Shirley I., K.C. Ingham, & D Ménaché. (1982). Rapid methods for isolation of human plasma fibronectin. Thrombosis Research. 27(1). 1–14. 304 indexed citations
19.
Ingham, K.C., Salvatore M. Aloj, & Harold Edelhoch. (1973). The rates of dissociation and recombination of the subunits of human luteinizing hormone. Archives of Biochemistry and Biophysics. 159(2). 596–605. 21 indexed citations
20.
Aloj, Salvatore M., Harold Edelhoch, K.C. Ingham, et al.. (1973). The rates of dissociation and reassociation of the subunits of human chorionic gonadotropin. Archives of Biochemistry and Biophysics. 159(1). 497–504. 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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