Keith Brew

16.2k total citations · 5 hit papers
170 papers, 13.3k citations indexed

About

Keith Brew is a scholar working on Molecular Biology, Cancer Research and Genetics. According to data from OpenAlex, Keith Brew has authored 170 papers receiving a total of 13.3k indexed citations (citations by other indexed papers that have themselves been cited), including 99 papers in Molecular Biology, 44 papers in Cancer Research and 39 papers in Genetics. Recurrent topics in Keith Brew's work include Protease and Inhibitor Mechanisms (43 papers), Enzyme Structure and Function (32 papers) and Glycosylation and Glycoproteins Research (31 papers). Keith Brew is often cited by papers focused on Protease and Inhibitor Mechanisms (43 papers), Enzyme Structure and Function (32 papers) and Glycosylation and Glycoproteins Research (31 papers). Keith Brew collaborates with scholars based in United States, United Kingdom and Germany. Keith Brew's co-authors include Hideaki Nagase, Deendayal Dinakarpandian, Thomas Vanaman, Robert L. Hill, K. Ravi Acharya, Robert L. Hill, Sudhir K. Sinha, Janet T. Powell, Masahide Kashiwagi and Micky D. Tortorella and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Keith Brew

169 papers receiving 12.7k citations

Hit Papers

Tissue inhibitors of meta... 1968 2026 1987 2006 2000 2010 1997 1969 1968 500 1000 1.5k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Keith Brew 7.0k 3.5k 2.4k 1.7k 1.6k 170 13.3k
Vito Türk 12.8k 1.8× 7.1k 2.0× 4.3k 1.8× 826 0.5× 1.6k 1.0× 424 25.3k
Jan J. Enghild 8.4k 1.2× 4.3k 1.2× 2.3k 1.0× 591 0.3× 1.4k 0.9× 358 19.8k
Francis Castellino 6.3k 0.9× 4.1k 1.2× 1.0k 0.4× 803 0.5× 935 0.6× 418 15.0k
Stuart Linn 13.3k 1.9× 2.4k 0.7× 2.1k 0.9× 707 0.4× 2.6k 1.7× 163 17.4k
Robin W. Carrell 8.1k 1.2× 7.8k 2.2× 2.5k 1.1× 880 0.5× 1.3k 0.8× 214 19.8k
Darryl Pappin 17.0k 2.4× 1.8k 0.5× 2.0k 0.8× 720 0.4× 1.5k 0.9× 137 24.1k
Dominique Belin 8.0k 1.1× 4.2k 1.2× 1.3k 0.5× 278 0.2× 4.3k 2.7× 114 15.0k
Robert Schimke 13.4k 1.9× 1.9k 0.5× 2.7k 1.1× 637 0.4× 3.3k 2.1× 215 20.5k
Torben E. Petersen 4.5k 0.6× 1.1k 0.3× 578 0.2× 1.1k 0.6× 946 0.6× 158 8.8k
Joël Vandekerckhove 13.6k 2.0× 1.8k 0.5× 2.8k 1.1× 691 0.4× 1.2k 0.7× 307 21.5k

Countries citing papers authored by Keith Brew

Since Specialization
Citations

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

Fields of papers citing papers by Keith Brew

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Keith Brew

This figure shows the co-authorship network connecting the top 25 collaborators of Keith Brew. A scholar is included among the top collaborators of Keith Brew 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 Keith Brew. Keith Brew 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.
Brew, Keith & Hideaki Nagase. (2010). The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803(1). 55–71. 1036 indexed citations breakdown →
2.
Tremblay, Évelyne, Oualid Sbai, Lotfi Ferhat, et al.. (2009). A New Role for TIMP-1 in Modulating Neurite Outgrowth and Morphology of Cortical Neurons. PLoS ONE. 4(12). e8289–e8289. 52 indexed citations
3.
Lauer‐Fields, Janelle L., et al.. (2008). Selective Modulation of Matrix Metalloproteinase 9 (MMP-9) Functions via Exosite Inhibition. Journal of Biological Chemistry. 283(29). 20087–20095. 73 indexed citations
4.
Kopitz, Charlotte, Michael Gerg, Obul Reddy Bandapalli, et al.. (2007). Tissue Inhibitor of Metalloproteinases-1 Promotes Liver Metastasis by Induction of Hepatocyte Growth Factor Signaling. Cancer Research. 67(18). 8615–8623. 128 indexed citations
5.
Wei, Shuo, et al.. (2007). Constraining specificity in the N‐domain of tissue inhibitor of metalloproteinases‐1; gelatinase‐selective inhibitors. Protein Science. 16(9). 1905–1913. 56 indexed citations
6.
Wei, Shuo, Masahide Kashiwagi, Smitha Kota, et al.. (2005). Reactive Site Mutations in Tissue Inhibitor of Metalloproteinase-3 Disrupt Inhibition of Matrix Metalloproteinases but Not Tumor Necrosis Factor-α-converting Enzyme. Journal of Biological Chemistry. 280(38). 32877–32882. 45 indexed citations
7.
Azzarolo, Ana Maria, et al.. (2004). Presence of tear lipocalin and other major proteins in lacrimal fluid of rabbits. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 138(2). 111–117. 33 indexed citations
8.
Arumugam, Sengodagounder, et al.. (2003). Increased Backbone Mobility in β-Barrel Enhances Entropy Gain Driving Binding of N-TIMP-1 to MMP-3. Journal of Molecular Biology. 327(3). 719–734. 68 indexed citations
9.
Greene, Lesley H., Daizo Hamada, Stephen J. Eyles, & Keith Brew. (2003). Conserved signature proposed for folding in the lipocalin superfamily. FEBS Letters. 553(1-2). 39–44. 23 indexed citations
10.
Nagase, Hideaki & Keith Brew. (2002). Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics.. Arthritis Research. 4(Suppl 3). S51–S51. 48 indexed citations
11.
Yu, Wei‐Hsuan, et al.. (2000). TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix. Journal of Biological Chemistry. 275(40). 31226–31232. 276 indexed citations
12.
Wu, Bin, Sengodagounder Arumugam, Guanghua Gao, et al.. (2000). NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases. Journal of Molecular Biology. 295(2). 257–268. 33 indexed citations
13.
Brew, Keith, Deendayal Dinakarpandian, & Hideaki Nagase. (2000). Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1477(1-2). 267–283. 1564 indexed citations breakdown →
15.
Nagase, Hideaki, Ko Suzuki, Yoshifumi Itoh, et al.. (1996). Involvement of Tissue Inhibitors of Metalloproteinases (TIMPS) During Matrix Metalloproteinase Activation. Advances in experimental medicine and biology. 389. 23–31. 30 indexed citations
18.
Kasahara, Masanori, Jutta Gutknecht, Keith Brew, Nigel K. Spurr, & Peter N. Goodfellow. (1989). Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Genomics. 5(3). 527–534. 142 indexed citations
19.
Brew, Keith, et al.. (1989). Calcium regulates folding and disulfide-bond formation in α-lactalbumin. Biochemical and Biophysical Research Communications. 163(3). 1390–1396. 47 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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