K. Ishikawa

1.5k total citations
41 papers, 1.2k citations indexed

About

K. Ishikawa is a scholar working on Molecular Biology, Organic Chemistry and Materials Chemistry. According to data from OpenAlex, K. Ishikawa has authored 41 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 11 papers in Organic Chemistry and 9 papers in Materials Chemistry. Recurrent topics in K. Ishikawa's work include Protein Structure and Dynamics (8 papers), RNA and protein synthesis mechanisms (8 papers) and Enzyme Structure and Function (8 papers). K. Ishikawa is often cited by papers focused on Protein Structure and Dynamics (8 papers), RNA and protein synthesis mechanisms (8 papers) and Enzyme Structure and Function (8 papers). K. Ishikawa collaborates with scholars based in Japan, United States and India. K. Ishikawa's co-authors include Eiichiro Suzuki, Tatsuki Kashiwagi, Vadim A. Soloshonok, Tamio Hayashi, Nobuya Nagashima, Daisuke Ejima, Haruki Nakamura, Hiroshi Matsui, K. Yokoyama and Gary W. Griffin and has published in prestigious journals such as Journal of Biological Chemistry, The EMBO Journal and Journal of Molecular Biology.

In The Last Decade

K. Ishikawa

40 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
K. Ishikawa Japan 18 655 212 209 202 125 41 1.2k
Claudia Muhle‐Goll Germany 25 1.2k 1.8× 213 1.0× 43 0.2× 73 0.4× 52 0.4× 68 1.7k
Nicholas C. Price United Kingdom 16 667 1.0× 89 0.4× 24 0.1× 179 0.9× 93 0.7× 24 1.2k
Congyi Zheng China 24 746 1.1× 181 0.9× 32 0.2× 68 0.3× 96 0.8× 82 1.6k
Teresa Dı́az-Mauriño Spain 14 674 1.0× 183 0.9× 50 0.2× 46 0.2× 68 0.5× 34 882
Stephen T. Isaacs United States 10 983 1.5× 294 1.4× 72 0.3× 75 0.4× 13 0.1× 13 1.5k
H.A. McKenzie Australia 24 769 1.2× 98 0.5× 26 0.1× 113 0.6× 198 1.6× 47 1.5k
Michael L. Oldham United States 19 1.4k 2.1× 74 0.3× 69 0.3× 183 0.9× 58 0.5× 26 2.6k
James A. Magnuson United States 21 474 0.7× 98 0.5× 18 0.1× 73 0.4× 161 1.3× 67 1.3k
Goran Kragol Croatia 19 706 1.1× 320 1.5× 18 0.1× 72 0.4× 27 0.2× 43 1.3k
Shio Makino Japan 20 1.0k 1.6× 253 1.2× 46 0.2× 108 0.5× 75 0.6× 51 1.7k

Countries citing papers authored by K. Ishikawa

Since Specialization
Citations

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

Fields of papers citing papers by K. Ishikawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K. Ishikawa

This figure shows the co-authorship network connecting the top 25 collaborators of K. Ishikawa. A scholar is included among the top collaborators of K. Ishikawa 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. Ishikawa. K. Ishikawa 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.
Nagata, Koji, Nobuko Hongo, Akihiro Yamamura, et al.. (2013). The structure of brazzein, a sweet-tasting protein from the wild African plantPentadiplandra brazzeana. Acta Crystallographica Section D Biological Crystallography. 69(4). 642–647. 15 indexed citations
2.
Takahashi, Kazutoshi, Uno Tagami, Nobuhisa Shimba, et al.. (2010). Crystal structure of Bifidobacterium Longum phosphoketolase; key enzyme for glucose metabolism in Bifidobacterium. FEBS Letters. 584(18). 3855–3861. 18 indexed citations
3.
Ishikawa, K., et al.. (2006). Engineering of Escherichia colil-serine O-acetyltransferase on the basis of crystal structure: desensitization to feedback inhibition by l-cysteine. Protein Engineering Design and Selection. 19(4). 163–167. 24 indexed citations
4.
Nakamura, T., Tamotsu Yamamoto, Takafumi Inoue, et al.. (2005). Crystal structure of hyperthermostable thioredoxin peroxidase fromAeropyrum pernixK1. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c262–c262. 1 indexed citations
5.
Mihara, Yasuhiro, K. Ishikawa, Eiichiro Suzuki, & Yasuhisa Asano. (2004). Improving the Pyrophosphate-inosine Phosphotransferase Activity ofEscherichia blattaeAcid Phosphatase by Sequential Site-directed Mutagenesis. Bioscience Biotechnology and Biochemistry. 68(5). 1046–1050. 15 indexed citations
6.
7.
Shimba, Nobuhisa, et al.. (2002). Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Letters. 517(1-3). 175–179. 26 indexed citations
8.
Kashiwagi, Tatsuki, K. Yokoyama, K. Ishikawa, et al.. (2002). Crystal Structure of Microbial Transglutaminase fromStreptoverticillium mobaraense. Journal of Biological Chemistry. 277(46). 44252–44260. 218 indexed citations
9.
Ishikawa, K., Yasuhiro Mihara, Nobuhisa Shimba, et al.. (2002). Enhancement of nucleoside phosphorylation activity in an acid phosphatase. Protein Engineering Design and Selection. 15(7). 539–543. 23 indexed citations
10.
Sugiura, Katsuaki, Hideo Ogura, Kazuya Ito, et al.. (2001). Eradication of foot and mouth disease in Japan. Revue Scientifique et Technique de l OIE. 20(3). 701–713. 26 indexed citations
11.
Ishikawa, K., et al.. (2001). Crystal Structure of Red Sea Bream Transglutaminase. Journal of Biological Chemistry. 276(15). 12055–12059. 75 indexed citations
12.
13.
Ishikawa, K., Kaizhi Yue, & Ken A. Dill. (1999). Predicting the structures of 18 peptides using Geocore. Protein Science. 8(4). 716–721. 19 indexed citations
14.
Ishikawa, K., et al.. (1996). Crystallization and preliminary X-ray analysis of brazzein, a new sweet protein. Acta Crystallographica Section D Biological Crystallography. 52(3). 577–578. 6 indexed citations
15.
Ishikawa, K., Eiichiro Suzuki, Masaru Tanokura, & Kenji Takahashi. (1996). Crystal Structure of Ribonuclease T1 Carboxymethylated at Glu58 in Complex with 2‘-GMP. Biochemistry. 35(25). 8329–8334. 8 indexed citations
16.
Ishikawa, K., Kazuhiko Katayama, Kiyoshi Tanabayashi, et al.. (1995). Comparison of the entire nucleotide and deduced amino acid sequences of the attenuated hog cholera vaccine strain GPE? and the wild-type parental strain ALD. Archives of Virology. 140(8). 1385–1391. 46 indexed citations
17.
Ishikawa, K., et al.. (1993). Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability. Protein Engineering Design and Selection. 6(1). 85–91. 53 indexed citations
18.
Ishikawa, K., et al.. (1993). Crystallization and preliminary crystallographic analysis of ribonuclease H from Thermus thermophilus HB8. Proteins Structure Function and Bioinformatics. 15(1). 108–111.
19.
Ishikawa, K., et al.. (1993). Crystal Structure of Ribonuclease H from Thermus thermophilus HB8 Refined at 2·8 Å Resolution. Journal of Molecular Biology. 230(2). 529–542. 105 indexed citations
20.
Ishikawa, K., et al.. (1993). Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77 .fwdarw. Ala substitution. Biochemistry. 32(28). 7136–7142. 22 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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