C.B. Caputo

1.9k total citations
33 papers, 1.7k citations indexed

About

C.B. Caputo is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, C.B. Caputo has authored 33 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 16 papers in Physiology and 14 papers in Cell Biology. Recurrent topics in C.B. Caputo's work include Alzheimer's disease research and treatments (16 papers), Prion Diseases and Protein Misfolding (9 papers) and Proteoglycans and glycosaminoglycans research (9 papers). C.B. Caputo is often cited by papers focused on Alzheimer's disease research and treatments (16 papers), Prion Diseases and Protein Misfolding (9 papers) and Proteoglycans and glycosaminoglycans research (9 papers). C.B. Caputo collaborates with scholars based in United States, United Kingdom and Canada. C.B. Caputo's co-authors include Clay W. Scott, Vincent Hascall, James H. Kimura, Xi Chen, J Brett, Mark A. Smith, Ann Marie Schmidt, Thierry Frappier, Gabriel C. Godman and Shi Du Yan and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Analytical Biochemistry.

In The Last Decade

C.B. Caputo

33 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
C.B. Caputo United States 19 880 750 656 201 200 33 1.7k
Kunihiko Suzuki United States 30 2.1k 2.4× 1.6k 2.1× 669 1.0× 109 0.5× 222 1.1× 56 3.1k
Midori OGAWARA Japan 13 1.0k 1.2× 1.2k 1.5× 405 0.6× 30 0.1× 295 1.5× 30 1.9k
Ángeles Martín‐Requero Spain 26 780 0.9× 561 0.7× 146 0.2× 47 0.2× 165 0.8× 82 1.6k
Noriaki Kinoshita Japan 21 476 0.5× 518 0.7× 117 0.2× 70 0.3× 95 0.5× 36 1.3k
D. Kirk Ways United States 24 1.6k 1.8× 196 0.3× 221 0.3× 22 0.1× 209 1.0× 44 2.3k
J.L. Nussbaum France 25 1.0k 1.2× 273 0.4× 141 0.2× 88 0.4× 287 1.4× 47 1.6k
Silva Hečimović Croatia 20 818 0.9× 852 1.1× 199 0.3× 43 0.2× 226 1.1× 44 1.6k
Mary F. Knauer United States 13 798 0.9× 1.2k 1.6× 195 0.3× 16 0.1× 222 1.1× 16 1.6k
Shinya Tokuhiro Japan 13 556 0.6× 466 0.6× 127 0.2× 99 0.5× 194 1.0× 21 1.3k
Jayne Marasa United States 18 881 1.0× 529 0.7× 291 0.4× 11 0.1× 331 1.7× 26 1.7k

Countries citing papers authored by C.B. Caputo

Since Specialization
Citations

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

Fields of papers citing papers by C.B. Caputo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C.B. Caputo

This figure shows the co-authorship network connecting the top 25 collaborators of C.B. Caputo. A scholar is included among the top collaborators of C.B. Caputo 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 C.B. Caputo. C.B. Caputo 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.
Greenwood, Jeffrey A., Clay W. Scott, Russell C. Spreen, C.B. Caputo, & G. V. Johnson. (1994). Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor.. Journal of Biological Chemistry. 269(6). 4373–4380. 69 indexed citations
2.
Scott, Clay W., et al.. (1993). Aggregation of tau protein by aluminum. Brain Research. 628(1-2). 77–84. 47 indexed citations
3.
Scott, Clay W., Philip R Vulliet, & C.B. Caputo. (1993). Phosphorylation of tau by proline-directed protein kinase (p34cdc2/p58cyclin A) decreases tau-induced microtubule assembly and antibody SMI33 reactivity. Brain Research. 611(2). 237–242. 34 indexed citations
4.
Sygowski, Linda A., et al.. (1993). Phosphorylation of tau protein in tau-transfected 3T3 cells. Molecular Brain Research. 20(3). 221–228. 15 indexed citations
5.
Caputo, C.B., et al.. (1993). The Influence of Amino Acid Sequence on the Fibrillogenicity and Amyloidogenicity of the Carboxy-Terminus of β-Amyloid Precursor Protein. Archives of Biochemistry and Biophysics. 306(2). 321–330. 6 indexed citations
6.
Caputo, C.B., et al.. (1992). THERAPEUTIC APPROACHES TARGETED AT THE AMYLOID PROTEINS IN ALZHEIMERʼS DISEASE. Clinical Neuropharmacology. 15. 414A–415A. 1 indexed citations
7.
Caputo, C.B., et al.. (1992). Association of the carboxy-terminus of β-amyloid protein precursor with Alzheimer paired helical filaments. Biochemical and Biophysical Research Communications. 185(3). 1034–1040. 19 indexed citations
8.
Caputo, C.B., et al.. (1992). Role of tau in the polymerization of peptides from β-amyloid precursor protein. Brain Research. 597(2). 227–232. 23 indexed citations
9.
Scott, Clay W., et al.. (1992). Tau protein induces bundling of microtubules in vitro: Comparison of different tau isoforms and a tau protein fragment. Journal of Neuroscience Research. 33(1). 19–29. 54 indexed citations
10.
Caputo, C.B., et al.. (1992). Immunoreactivity of an Antibody to a β/A4 Sequence with Alzheimer Paired Helical Filaments and τ Protein. Alzheimer Disease & Associated Disorders. 6(4). 225–235. 2 indexed citations
11.
Caputo, C.B., et al.. (1992). Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of β-amyloid protein precursor. Archives of Biochemistry and Biophysics. 292(1). 199–205. 28 indexed citations
12.
Caputo, C.B., Claude M. Wischik, Michael Novák, et al.. (1992). Immunological characterization of the region of tau protein that is bound to Alzheimer paired helical filaments. Neurobiology of Aging. 13(2). 267–274. 23 indexed citations
13.
Scott, Clay W., David P. Blowers, P T Barth, et al.. (1991). Differences in the abilities of human tau isoforms to promote microtubule assembly. Journal of Neuroscience Research. 30(1). 154–162. 39 indexed citations
14.
Caputo, C.B., et al.. (1989). Properties of several protein kinases that copurify with rat spinal cord neurofilaments. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1012(3). 299–307. 27 indexed citations
15.
Caputo, C.B. & Andre I. Salama. (1989). The amyloid proteins of Alzheimer's disease as potential targets for drug therapy. Neurobiology of Aging. 10(5). 451–461. 30 indexed citations
16.
Caputo, C.B., et al.. (1988). Degradation of rat chondrosarcoma proteoglycans by a neutral metalloprotease from rabbit chondrocytes. Connective Tissue Research. 18(3). 191–203. 3 indexed citations
17.
Caputo, C.B., et al.. (1988). Protease inhibitors decrease rabbit cartilage degradation after meniscectomy. Journal of Orthopaedic Research®. 6(1). 103–108. 11 indexed citations
18.
Poole, A. Robin, A Reiner, John S. Mort, et al.. (1984). Cartilage link proteins. Biochemical and immunochemical studies of isolation and heterogeneity.. Journal of Biological Chemistry. 259(23). 14849–14856. 17 indexed citations
19.
Kimura, James H., C.B. Caputo, & Vincent Hascall. (1981). The effect of cycloheximide on synthesis of proteoglycans by cultured chondrocytes from the Swarm rat chondrosarcoma.. Journal of Biological Chemistry. 256(9). 4368–4376. 111 indexed citations
20.

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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