Joseph T. Jarrett

7.2k total citations · 2 hit papers
47 papers, 5.9k citations indexed

About

Joseph T. Jarrett is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Cell Biology. According to data from OpenAlex, Joseph T. Jarrett has authored 47 papers receiving a total of 5.9k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 23 papers in Renewable Energy, Sustainability and the Environment and 13 papers in Cell Biology. Recurrent topics in Joseph T. Jarrett's work include Metalloenzymes and iron-sulfur proteins (23 papers), Biotin and Related Studies (13 papers) and CO2 Reduction Techniques and Catalysts (12 papers). Joseph T. Jarrett is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (23 papers), Biotin and Related Studies (13 papers) and CO2 Reduction Techniques and Catalysts (12 papers). Joseph T. Jarrett collaborates with scholars based in United States and Canada. Joseph T. Jarrett's co-authors include Peter T. Lansbury, Natalia B. Ugulava, Jason Wan, Rowena G. Matthews, Catherine L. Drennan, Yvain Nicolet, Brian R. Gibney, Corey J. Fugate, Christine Farrar and Martha Ludwig and has published in prestigious journals such as Science, Cell and Journal of the American Chemical Society.

In The Last Decade

Joseph T. Jarrett

47 papers receiving 5.8k citations

Hit Papers

Seeding “one-dimensional crystallization” of amyloid: A p... 1993 2026 2004 2015 1993 1993 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph T. Jarrett United States 29 3.6k 3.0k 955 591 556 47 5.9k
Lin Jiang United States 30 4.0k 1.1× 1.5k 0.5× 90 0.1× 388 0.7× 278 0.5× 52 5.6k
Claudio O. Fernández Argentina 39 1.9k 0.5× 2.4k 0.8× 77 0.1× 100 0.2× 176 0.3× 86 5.3k
Kazuhiro Irie Japan 39 2.9k 0.8× 2.1k 0.7× 50 0.1× 568 1.0× 1.4k 2.5× 250 5.5k
Peep Palumaa Estonia 30 1.2k 0.3× 1.0k 0.3× 134 0.1× 201 0.3× 199 0.4× 70 3.1k
W. Rodney Mathews United States 32 2.4k 0.7× 1.8k 0.6× 83 0.1× 343 0.6× 609 1.1× 63 4.7k
Daniela Valensin Italy 35 2.4k 0.7× 1.5k 0.5× 30 0.0× 264 0.4× 286 0.5× 122 5.3k
Jean‐Christophe Rochet United States 37 4.0k 1.1× 4.0k 1.3× 47 0.0× 154 0.3× 315 0.6× 108 10.3k
Monica Bucciantini Italy 31 3.7k 1.0× 2.5k 0.8× 48 0.1× 232 0.4× 292 0.5× 87 5.6k
Claudia Binda Italy 45 4.1k 1.1× 424 0.1× 68 0.1× 622 1.1× 1.4k 2.5× 81 7.1k
John H. Viles United Kingdom 36 3.6k 1.0× 2.3k 0.8× 20 0.0× 409 0.7× 303 0.5× 66 5.5k

Countries citing papers authored by Joseph T. Jarrett

Since Specialization
Citations

This map shows the geographic impact of Joseph T. Jarrett'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 Joseph T. Jarrett with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Joseph T. Jarrett more than expected).

Fields of papers citing papers by Joseph T. Jarrett

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph T. Jarrett. 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 Joseph T. Jarrett. The network helps show where Joseph T. Jarrett may publish in the future.

Co-authorship network of co-authors of Joseph T. Jarrett

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph T. Jarrett. A scholar is included among the top collaborators of Joseph T. Jarrett 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 Joseph T. Jarrett. Joseph T. Jarrett 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.
Bockman, Matthew R., Curtis A. Engelhart, Neeraj K. Mishra, et al.. (2019). Investigation of (S)-(−)-Acidomycin: A Selective Antimycobacterial Natural Product That Inhibits Biotin Synthase. ACS Infectious Diseases. 5(4). 598–617. 26 indexed citations
2.
Jarrett, Joseph T., et al.. (2018). Purification, Characterization, and Biochemical Assays of Biotin Synthase From Escherichia coli. Methods in enzymology on CD-ROM/Methods in enzymology. 606. 363–388. 7 indexed citations
3.
Taylor, Andrew M., Christine Farrar, & Joseph T. Jarrett. (2008). 9-Mercaptodethiobiotin Is Formed as a Competent Catalytic Intermediate by Escherichia coli Biotin Synthase. Biochemistry. 47(35). 9309–9317. 38 indexed citations
4.
Jarrett, Joseph T., et al.. (2007). Loss of iron–sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation. Archives of Biochemistry and Biophysics. 471(1). 32–41. 19 indexed citations
5.
Nicolet, Yvain, et al.. (2004). Crystal Structure of Biotin Synthase, an S -Adenosylmethionine-Dependent Radical Enzyme. Science. 303(5654). 76–79. 350 indexed citations
6.
Jarrett, Joseph T.. (2004). The novel structure and chemistry of iron–sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase. Archives of Biochemistry and Biophysics. 433(1). 312–321. 58 indexed citations
7.
Jarrett, Joseph T.. (2003). The generation of 5′-deoxyadenosyl radicals by adenosylmethionine-dependent radical enzymes. Current Opinion in Chemical Biology. 7(2). 174–182. 70 indexed citations
8.
Jarrett, Joseph T. & Jason Wan. (2002). Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli. FEBS Letters. 529(2-3). 237–242. 6 indexed citations
9.
Wan, Jason & Joseph T. Jarrett. (2002). Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli. Archives of Biochemistry and Biophysics. 406(1). 116–126. 52 indexed citations
10.
Ugulava, Natalia B., Brian R. Gibney, & Joseph T. Jarrett. (2000). Iron−Sulfur Cluster Interconversions in Biotin Synthase:  Dissociation and Reassociation of Iron during Conversion of [2Fe-2S] to [4Fe-4S] Clusters. Biochemistry. 39(17). 5206–5214. 75 indexed citations
11.
Jarrett, Joseph T., et al.. (1997). Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli. Methods in enzymology on CD-ROM/Methods in enzymology. 281. 196–213. 36 indexed citations
13.
Jarrett, Joseph T., Catherine L. Drennan, Mohan Amaratunga, et al.. (1996). A protein radical cage slows photolysis of methylcobalamin in methionine synthase from Escherichia coli. Bioorganic & Medicinal Chemistry. 4(8). 1237–1246. 24 indexed citations
14.
Bailey, Steven, et al.. (1995). Stereospecificity of folate binding to DNA photolyase from Escherichia coli. Biochemistry. 34(35). 11217–11220. 1 indexed citations
15.
Drummond, James T., Joseph T. Jarrett, J.C. González, Sha Huang, & Rowena G. Matthews. (1995). Characterization of Nonradioactive Assays for Cobalamin-Dependent and Cobalamin-Independent Methionine Synthase Enzymes. Analytical Biochemistry. 228(2). 323–329. 65 indexed citations
16.
Weinreb, Paul H., Joseph T. Jarrett, & Peter T. Lansbury. (1994). Peptide Models of a Hydrophobic Cluster at the C-Terminus of the .beta.-Amyloid Protein. Journal of the American Chemical Society. 116(23). 10835–10836. 20 indexed citations
17.
Jarrett, Joseph T., et al.. (1993). The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry. 32(18). 4693–4697. 1630 indexed citations breakdown →
18.
Jarrett, Joseph T., et al.. (1993). The C‐Terminus of the β Protein is Critical in Amyloidogenesisa. Annals of the New York Academy of Sciences. 695(1). 144–148. 215 indexed citations
19.
Jarrett, Joseph T. & Peter T. Lansbury. (1992). Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry. 31(49). 12345–12352. 267 indexed citations
20.
Jarrett, Joseph T., et al.. (1992). Studies related to a convergent fragment-coupling approach to peptide synthesis using the Kaiser oxime resin. The Journal of Organic Chemistry. 57(12). 3414–3420. 15 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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