S. Colette Daubner

2.5k total citations · 1 hit paper
38 papers, 2.0k citations indexed

About

S. Colette Daubner is a scholar working on Molecular Biology, Clinical Biochemistry and Biochemistry. According to data from OpenAlex, S. Colette Daubner has authored 38 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 20 papers in Clinical Biochemistry and 16 papers in Biochemistry. Recurrent topics in S. Colette Daubner's work include Metabolism and Genetic Disorders (19 papers), Enzyme Structure and Function (15 papers) and Amino Acid Enzymes and Metabolism (12 papers). S. Colette Daubner is often cited by papers focused on Metabolism and Genetic Disorders (19 papers), Enzyme Structure and Function (15 papers) and Amino Acid Enzymes and Metabolism (12 papers). S. Colette Daubner collaborates with scholars based in United States, China and Japan. S. Colette Daubner's co-authors include Shanzhi Wang, Paul F. Fitzpatrick, Rowena G. Matthews, John W. Haycock, Crystal M. Lauriano, Patrick J. Hillas, Graham R. Moran, Thomas Baldwin, Stephen J. Benkovic and Daniel L. Lohse and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

S. Colette Daubner

38 papers receiving 2.0k citations

Hit Papers

Tyrosine hydroxylase and regulation of dopamine synthesis 2010 2026 2015 2020 2010 250 500 750
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.

  1. Tyrosine hydroxylase and regulation of dopamine synthesis
    2010 760 citations S. Colette Daubner, Shanzhi Wang et al. Archives of Biochemistry and Biophysics profile →

Peers

S. Colette Daubner
Anant B. Patel India
In‐Young Choi South Korea
Toshiharu Nagatsu Japan
Igor Rebrin United States
Antonio Cortés Spain
Samuel T. Henderson United States
N. Weiner United States
Moo Ho Won South Korea
Motomasa Tanaka Japan
Margaret M. Sedensky United States
Anant B. Patel India
S. Colette Daubner
Citations per year, relative to S. Colette Daubner S. Colette Daubner (= 1×) peers Anant B. Patel

Countries citing papers authored by S. Colette Daubner

Since Specialization
Citations

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

Fields of papers citing papers by S. Colette Daubner

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by S. Colette Daubner. 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 S. Colette Daubner. The network helps show where S. Colette Daubner may publish in the future.

Co-authorship network of co-authors of S. Colette Daubner

This figure shows the co-authorship network connecting the top 25 collaborators of S. Colette Daubner. A scholar is included among the top collaborators of S. Colette Daubner 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 S. Colette Daubner. S. Colette Daubner 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
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Lou, Haiyan, Jian Wang, Jian Wu, et al.. (2010). Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo. Journal of Biological Chemistry. 285(23). 17648–17661. 96 indexed citations
3.
Daubner, S. Colette, et al.. (2010). Tyrosine hydroxylase and regulation of dopamine synthesis. Archives of Biochemistry and Biophysics. 508(1). 1–12. 760 indexed citations breakdown →
4.
Daubner, S. Colette, et al.. (2006). A Flexible Loop in Tyrosine Hydroxylase Controls Coupling of Amino Acid Hydroxylation to Tetrahydropterin Oxidation. Journal of Molecular Biology. 359(2). 299–307. 16 indexed citations
5.
Daubner, S. Colette, et al.. (2006). Kinetics of regulatory serine variants of tyrosine hydroxylase with cyclic AMP-dependent protein kinase and extracellular signal-regulated protein kinase 2. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(4). 786–792. 4 indexed citations
6.
Daubner, S. Colette, et al.. (2004). Effects of phosphorylation by protein kinase A on binding of catecholamines to the human tyrosine hydroxylase isoforms. Journal of Neurochemistry. 90(4). 970–978. 31 indexed citations
7.
Kansy, Janice W., S. Colette Daubner, Akinori Nishi, et al.. (2004). Identification of tyrosine hydroxylase as a physiological substrate for Cdk5. Journal of Neurochemistry. 91(2). 374–384. 41 indexed citations
8.
Daubner, S. Colette, et al.. (2004). Specificity of the MAP kinase ERK2 for phosphorylation of tyrosine hydroxylase. Archives of Biochemistry and Biophysics. 423(2). 247–252. 6 indexed citations
9.
Fitzpatrick, Paul F., et al.. (2004). Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: effects on enzyme stability and activity. Archives of Biochemistry and Biophysics. 434(2). 266–274. 25 indexed citations
10.
Daubner, S. Colette, et al.. (2004). Effects of mutations in tyrosine hydroxylase associated with progressive dystonia on the activity and stability of the protein. Proteins Structure Function and Bioinformatics. 58(1). 14–21. 26 indexed citations
11.
Daubner, S. Colette, Graham R. Moran, & Paul F. Fitzpatrick. (2002). Role of Tryptophan Hydroxylase Phe313 in Determining Substrate Specificity. Biochemical and Biophysical Research Communications. 292(3). 639–641. 14 indexed citations
12.
Daubner, S. Colette, et al.. (2001). Effects of Substitution at Serine 40 of Tyrosine Hydroxylase on Catecholamine Binding. Biochemistry. 40(24). 7273–7278. 33 indexed citations
13.
Moran, Graham R., S. Colette Daubner, & Paul F. Fitzpatrick. (1998). Expression and Characterization of the Catalytic Core of Tryptophan Hydroxylase. Journal of Biological Chemistry. 273(20). 12259–12266. 55 indexed citations
14.
Daubner, S. Colette, et al.. (1995). Deletion mutants of tyrosine hydroxylase identify a region critical for heparin binding. Protein Science. 4(3). 538–541. 16 indexed citations
15.
Daubner, S. Colette, et al.. (1995). Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues. Protein Science. 4(10). 2082–2086. 30 indexed citations
16.
Daubner, S. Colette, et al.. (1993). Lysine241 of Tyrosine Hydroxylase Is Not Required for Binding of Tetrahydrobiopterin Substrate. Archives of Biochemistry and Biophysics. 302(2). 455–460. 4 indexed citations
17.
Daubner, S. Colette, Daniel L. Lohse, & Paul F. Fitzpatrick. (1993). Expression and characterization of catalytic and regulatory domains of rat tyrosine hydroxylase. Protein Science. 2(9). 1452–1460. 55 indexed citations
18.
Daubner, S. Colette & Paul F. Fitzpatrick. (1993). Alleviation of Catecholamine Inhibition of Tyrosine Hydroxylase by Phosphorylation at Serine40. Advances in experimental medicine and biology. 338. 87–92. 7 indexed citations
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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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