Ko Suzuki

2.9k total citations · 1 hit paper
25 papers, 2.4k citations indexed

About

Ko Suzuki is a scholar working on Cancer Research, Molecular Biology and Oncology. According to data from OpenAlex, Ko Suzuki has authored 25 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Cancer Research, 16 papers in Molecular Biology and 9 papers in Oncology. Recurrent topics in Ko Suzuki's work include Protease and Inhibitor Mechanisms (17 papers), Peptidase Inhibition and Analysis (9 papers) and Signaling Pathways in Disease (6 papers). Ko Suzuki is often cited by papers focused on Protease and Inhibitor Mechanisms (17 papers), Peptidase Inhibition and Analysis (9 papers) and Signaling Pathways in Disease (6 papers). Ko Suzuki collaborates with scholars based in United States, Japan and Denmark. Ko Suzuki's co-authors include Hideaki Nagase, Jan J. Enghild, Guy S. Salvesen, John L. Fowlkes, T. Morodomi, Keith Brew, Kathryn M. Thrailkill, Michael Betz, Andreas Bergner and K. Maskos and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Ko Suzuki

24 papers receiving 2.3k 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.

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

1997 501 citations K. Maskos, Michael Betz et al. Nature profile →

Peers

Countries citing papers authored by Ko Suzuki

Since Specialization

Citations

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

Fields of papers citing papers by Ko Suzuki

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ko Suzuki

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

All Works

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20 of 20 papers shown

#	Work	Indexed citations
1	CLPX regulates mitochondrial fatty acid β-oxidation in liver cells 2023 ·Journal of Biological Chemistry ·Ko Suzuki, Yoshiko Kubota, Kiriko Kaneko, (unknown), Kazumichi Furuyama	0
2	The promoting role of lysosome-localized c-Src in autophagosome-lysosome fusion 2020 ·Cellular Signalling ·Ko Suzuki, Takuya Honda, (unknown), Noritaka Yamaguchi, Naoto Yamaguchi	5
3	Large-Scale Phosphoproteomic Study of Arabidopsis Membrane Proteins Reveals Early Signaling Events in Response to Cold 2020 ·International Journal of Molecular Sciences ·(unknown), Shin-nosuke Ishikawa, Fuminori Takahashi, Ko Suzuki, Masaharu Kamo, Taishi Umezawa, Kazuo Shinozaki, Yukio Kawamura, Matsuo Uemura	23
4	v-Src-driven transformation is due to chromosome abnormalities but not Src-mediated growth signaling 2018 ·Scientific Reports ·Takuya Honda, (unknown), Yuji Nakayama, Ko Suzuki, Noritaka Yamaguchi, Naoto Yamaguchi	11
5	Expression of Human Pro-Matrix Metalloproteinase 3 that Lacks the N-terminal 34 Residues in Escherichia coli: Autoactivation and Interaction with Tissue Inhibitor of Metalloproteinase 1 (TIMP-1) 1998 ·Biological Chemistry ·Ko Suzuki, Chen‐Chen Kan, (unknown), Michael R. Gehring, Keith Brew, Hideaki Nagase	43
6	Hydroxyapatite Induces Autolytic Degradation and Inactivation of Matrix Metalloproteinase-1 and -3 1998 ·Journal of Bone and Mineral Research ·(unknown), (unknown), Ko Suzuki, Hideaki Nagase, Jeffrey Gorski	43
7	Mutational Study of the Amino-terminal Domain of Human Tissue Inhibitor of Metalloproteinases 1 (TIMP-1) Locates an Inhibitory Region for Matrix Metalloproteinases 1997 ·Journal of Biological Chemistry ·Wen Huang, Qi Meng, Ko Suzuki, Hideaki Nagase, Keith Brew	86
8	Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1 breakdown → 1997 ·Nature ·(unknown), K. Maskos, Michael Betz, Andreas Bergner, Robert Huber, Ko Suzuki, Naoki Yoshida, Hideaki Nagase, Keith Brew, Gleb Bourenkov, H.D. Bartunik, Wolfram Bode	501
9	Involvement of Tissue Inhibitors of Metalloproteinases (TIMPS) During Matrix Metalloproteinase Activation 1996 ·Advances in experimental medicine and biology ·Hideaki Nagase, Ko Suzuki, Yoshifumi Itoh, C. Kan, Chris Gehring, Wen Huang, Keith Brew	30
10	Folding and characterization of the amino‐terminal domain of human tissue inhibitor of metalloproteinases‐1 (TIMP‐1) expressed at high yield in E. coli 1996 ·FEBS Letters ·Wen Huang, Ko Suzuki, Hideaki Nagase, (unknown), Steven R. Van Doren, Keith Brew	93
11	Matrix metalloproteinases as insulin-like growth factor binding protein-degrading proteinases 1995 ·PubMed ·John L. Fowlkes, Kathryn M. Thrailkill, Delila Serra, Ko Suzuki, Hideaki Nagase	112
12	Characterization of insulin-like growth factor-binding protein 5-degrading proteases produced throughout murine osteoblast differentiation. 1995 ·Endocrinology ·Kathryn M. Thrailkill, L. Darryl Quarles, Hideaki Nagase, Ko Suzuki, (unknown), John L. Fowlkes	125
13	Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures. 1994 ·Journal of Biological Chemistry ·John L. Fowlkes, Jan J. Enghild, Ko Suzuki, Hideaki Nagase	275
14	Activation mechanisms of the precursors of matrix metalloproteinases 1, 2 and 3. 1992 ·PubMed ·Hisamitsu Nagase, Ko Suzuki, T. Morodomi, Jan J. Enghild, Guy S. Salvesen	86
15	Comparative studies of a 92-kDa gelatinolytic metalloproteinase from U937 cells and matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. 1992 ·PubMed ·T. Morodomi, Ko Suzuki, Yasuyuki Sasaguri, (unknown), Hisamitsu Nagase	3
16	Identification of rabbit uterine cervical procollagenase activator as rabbit matrix metalloproteinase 3 (stromelysin) 1991 ·Comparative Biochemistry and Physiology Part B Comparative Biochemistry ·Akira Itô, Yoshifumi Itoh, Takashi Sato, Yo Mori, Ko Suzuki, Hideaki Nagase	5
17	Substrate specificities and activation mechanisms of matrix metalloproteinases 1991 ·Biochemical Society Transactions ·Hideaki Nagase, Yutaka Ogata, Ko Suzuki, Jan J. Enghild, Guy S. Salvesen	142
18	Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate 1990 ·Biochemistry ·(unknown), Jan J. Enghild, Ko Suzuki, Guy S. Salvesen	328
19	Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin) 1990 ·Biochemistry ·Ko Suzuki, Jan J. Enghild, T. Morodomi, Guy S. Salvesen, Hideaki Nagase	359
20	Chemotactic Response of Human Neutrophils to N‐Acetyl Chitohexaose in vitro 1988 ·Microbiology and Immunology ·Akio Tokoro, Ko Suzuki, Tatsuji Matsumoto, Takeshi Mikami, Shigeo Suzuki, Masuko Suzuki	28

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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