Teresa B. Fitzpatrick

5.6k total citations
80 papers, 3.1k citations indexed

About

Teresa B. Fitzpatrick is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, Teresa B. Fitzpatrick has authored 80 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 33 papers in Materials Chemistry and 19 papers in Plant Science. Recurrent topics in Teresa B. Fitzpatrick's work include Enzyme Structure and Function (33 papers), Photosynthetic Processes and Mechanisms (21 papers) and Biochemical and Molecular Research (15 papers). Teresa B. Fitzpatrick is often cited by papers focused on Enzyme Structure and Function (33 papers), Photosynthetic Processes and Mechanisms (21 papers) and Biochemical and Molecular Research (15 papers). Teresa B. Fitzpatrick collaborates with scholars based in Switzerland, Germany and Ireland. Teresa B. Fitzpatrick's co-authors include Nikolaus Amrhein, Peter Macheroux, Thomas Raschle, Svetlana Boycheva, Alisdair R. Fernie, Ivo Tews, Barbara Kappes, Maite Colinas, Michaël Moulin and Karina Kitzing and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Teresa B. Fitzpatrick

77 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Teresa B. Fitzpatrick Switzerland 33 1.8k 1.1k 593 346 272 80 3.1k
Margaret E. Daub United States 33 1.7k 0.9× 2.2k 2.0× 384 0.6× 88 0.3× 151 0.6× 82 3.6k
Gilles J. Basset United States 27 1.4k 0.8× 1.0k 0.9× 57 0.1× 217 0.6× 299 1.1× 54 2.4k
Carlos Gancedo Spain 38 4.1k 2.2× 1.1k 1.0× 454 0.8× 423 1.2× 35 0.1× 105 5.1k
S. Mahadevan India 33 1.9k 1.0× 417 0.4× 202 0.3× 225 0.7× 39 0.1× 119 3.1k
Renaud Dumas France 33 2.2k 1.2× 1.5k 1.4× 410 0.7× 189 0.5× 319 1.2× 73 2.9k
Alberto Á. Iglesias Argentina 33 2.5k 1.4× 1.4k 1.3× 628 1.1× 354 1.0× 40 0.1× 169 4.0k
Guy Branlant France 36 3.0k 1.6× 150 0.1× 886 1.5× 710 2.1× 48 0.2× 121 3.7k
Jean‐Charles Portais France 39 3.8k 2.1× 2.4k 2.2× 264 0.4× 356 1.0× 17 0.1× 124 6.5k
Lars I. Leichert Germany 25 1.7k 1.0× 363 0.3× 217 0.4× 313 0.9× 20 0.1× 59 2.7k
M.W. Vetting United States 32 2.5k 1.4× 232 0.2× 693 1.2× 202 0.6× 47 0.2× 59 3.4k

Countries citing papers authored by Teresa B. Fitzpatrick

Since Specialization
Citations

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

Fields of papers citing papers by Teresa B. Fitzpatrick

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Teresa B. Fitzpatrick

This figure shows the co-authorship network connecting the top 25 collaborators of Teresa B. Fitzpatrick. A scholar is included among the top collaborators of Teresa B. Fitzpatrick 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 Teresa B. Fitzpatrick. Teresa B. Fitzpatrick 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.
Fitzpatrick, Teresa B., et al.. (2025). Paraquat resistance mutations have differential effects on plant fitness in two rice cultivars. Biochemical Journal. 482(8). 401–412.
2.
Fitzpatrick, Teresa B., et al.. (2024). Two pyridoxal phosphate homeostasis proteins are essential for management of the coenzyme pyridoxal 5′-phosphate in Arabidopsis. The Plant Cell. 36(9). 3689–3708. 1 indexed citations
3.
Steensma, Priscille, Marion Eisenhut, Maite Colinas, et al.. (2023). PYRIDOX(AM)INE 5′-PHOSPHATE OXIDASE3 ofArabidopsis thalianamaintains carbon/nitrogen balance in distinct environmental conditions. PLANT PHYSIOLOGY. 193(2). 1433–1455. 4 indexed citations
4.
Liu, Ying, Ricardo Fabiano Hettwer Giehl, Michael Melzer, et al.. (2022). PDX1.1-dependent biosynthesis of vitamin B6 protects roots from ammonium-induced oxidative stress. Molecular Plant. 15(5). 820–839. 50 indexed citations
5.
Chew, Yin Hoon, Daniel D. Seaton, Virginie Mengin, et al.. (2022). The Arabidopsis Framework Model version 2 predicts the organism-level effects of circadian clock gene mis-regulation. Edinburgh Research Explorer (University of Edinburgh). 4(2). 7 indexed citations
6.
Haferkamp, Ilka, Priscille Steensma, Teresa B. Fitzpatrick, et al.. (2022). Loss of a pyridoxal-phosphate phosphatase rescues Arabidopsis lacking an endoplasmic reticulum ATP carrier. PLANT PHYSIOLOGY. 189(1). 49–65. 5 indexed citations
7.
Strobbe, Simon, Teresa B. Fitzpatrick, Tiago Lourenço, et al.. (2022). A novel panel of yeast assays for the assessment of thiamin and its biosynthetic intermediates in plant tissues. New Phytologist. 234(2). 748–763. 6 indexed citations
8.
Rosado-Souza, Laíse, Sebastian Proost, Michaël Moulin, et al.. (2019). Appropriate Thiamin Pyrophosphate Levels Are Required for Acclimation to Changes in Photoperiod. PLANT PHYSIOLOGY. 180(1). 185–197. 22 indexed citations
9.
Wu, Ting‐Ying, Takayuki Tohge, Alisdair R. Fernie, et al.. (2019). Enhancement of vitamin B6 levels in rice expressing Arabidopsis vitamin B6 biosynthesis de novo genes. The Plant Journal. 99(6). 1047–1065. 34 indexed citations
10.
Robinson, Graham, et al.. (2019). Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3: a total eclipse. Acta Crystallographica Section D Structural Biology. 75(4). 400–415. 12 indexed citations
11.
Loubéry, Sylvain, et al.. (2019). Clarification of the dispensability of PDX1.2 for Arabidopsis viability using CRISPR/Cas9. BMC Plant Biology. 19(1). 2 indexed citations
12.
Colinas, Maite, et al.. (2014). A Pathway for Repair of NAD(P)H in Plants. Journal of Biological Chemistry. 289(21). 14692–14706. 21 indexed citations
13.
Vanderschuren, Hervé, et al.. (2013). Strategies for vitamin B6 biofortification of plants: a dual role as a micronutrient and a stress protectant. Frontiers in Plant Science. 4. 143–143. 64 indexed citations
14.
Moulin, Michaël, et al.. (2013). Analysis of Chlamydomonas thiamin metabolism in vivo reveals riboswitch plasticity. Proceedings of the National Academy of Sciences. 110(36). 14622–14627. 37 indexed citations
15.
Raschle, Thomas, Jacek Mazurkiewicz, Karsten Rippe, et al.. (2006). Structure of a bacterial pyridoxal 5′-phosphate synthase complex. Proceedings of the National Academy of Sciences. 103(51). 19284–19289. 103 indexed citations
16.
Raschle, Thomas, et al.. (2006). Reaction Mechanism of Pyridoxal 5′-Phosphate Synthase. Journal of Biological Chemistry. 282(9). 6098–6105. 41 indexed citations
17.
Warzych, Ewelina, et al.. (2006). PDX1 is essential for vitamin B6 biosynthesis, development and stress tolerance in Arabidopsis. The Plant Journal. 48(6). 933–946. 134 indexed citations
18.
Raschle, Thomas, et al.. (2005). Vitamin B6 biosynthesis in higher plants. Proceedings of the National Academy of Sciences. 102(38). 13687–13692. 194 indexed citations
19.
20.
Fitzpatrick, Teresa B. & J. Paul G. Malthouse. (1996). Proof that serine hydroxymethyltransferase retains its specificity for the pro-2S proton of glycine in the absence of tetrahydrofolate. Biochemical Society Transactions. 24(1). 132S–132S. 4 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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