Laura J. Lemieux

1.6k total citations
21 papers, 1.4k citations indexed

About

Laura J. Lemieux is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Cell Biology. According to data from OpenAlex, Laura J. Lemieux has authored 21 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 8 papers in Cellular and Molecular Neuroscience and 8 papers in Cell Biology. Recurrent topics in Laura J. Lemieux's work include Photosynthetic Processes and Mechanisms (14 papers), Photoreceptor and optogenetics research (8 papers) and Hemoglobin structure and function (7 papers). Laura J. Lemieux is often cited by papers focused on Photosynthetic Processes and Mechanisms (14 papers), Photoreceptor and optogenetics research (8 papers) and Hemoglobin structure and function (7 papers). Laura J. Lemieux collaborates with scholars based in United States, Canada and Germany. Laura J. Lemieux's co-authors include Robert B. Gennis, Jeffrey W. Thomas, Melissa W. Calhoun, D C Au, Philip G. Hultin, Xianqi Kong, Paul E. Fraser, Walter A. Szarek, Robert Kisilevsky and James O. Alben and has published in prestigious journals such as Journal of Biological Chemistry, Nature Medicine and The EMBO Journal.

In The Last Decade

Laura J. Lemieux

20 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Laura J. Lemieux United States	16	1.2k	359	318	179	138	21	1.4k
Hideo Shimada Japan	21	1.1k 0.9×	332 0.9×	275 0.9×	93 0.5×	286 2.1×	43	1.6k
Motonari Tsubaki Japan	25	1.2k 1.0×	758 2.1×	174 0.5×	241 1.3×	212 1.5×	85	1.9k
M.T. Wilson United Kingdom	18	707 0.6×	354 1.0×	221 0.7×	349 1.9×	70 0.5×	39	1.3k
Yasuhiro Isogai Japan	21	838 0.7×	193 0.5×	183 0.6×	105 0.6×	107 0.8×	64	1.2k
J. Guy Guillemette Canada	24	643 0.5×	174 0.5×	155 0.5×	553 3.1×	83 0.6×	55	1.3k
Tsunehisa Araiso Japan	19	500 0.4×	146 0.4×	207 0.7×	104 0.6×	160 1.2×	62	1.0k
Johannes P. M. Schelvis United States	21	683 0.6×	241 0.7×	279 0.9×	322 1.8×	126 0.9×	41	1.3k
Clare Peters Libeu United States	6	801 0.7×	182 0.5×	261 0.8×	80 0.4×	197 1.4×	6	1.0k
J.C. Salerno United States	21	820 0.7×	203 0.6×	119 0.4×	78 0.4×	151 1.1×	37	1.1k
John Fetter United States	15	1.0k 0.9×	134 0.4×	323 1.0×	39 0.2×	61 0.4×	21	1.3k

Countries citing papers authored by Laura J. Lemieux

Since Specialization

Citations

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

Fields of papers citing papers by Laura J. Lemieux

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Laura J. Lemieux. 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 Laura J. Lemieux. The network helps show where Laura J. Lemieux may publish in the future.

Co-authorship network of co-authors of Laura J. Lemieux

This figure shows the co-authorship network connecting the top 25 collaborators of Laura J. Lemieux. A scholar is included among the top collaborators of Laura J. Lemieux 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 Laura J. Lemieux. Laura J. Lemieux 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

Schaller, Rebecca, et al.. (2024). Observations of Atmospheric Corrosion Testing on Heated Austenitic Stainless Steel Surfaces: Exploring the Role of Inert Dust Particulates and Seawater. Nuclear Technology. 210(9). 1658–1671. 2 indexed citations

Boyle, Timothy J., Alexander L. Brown, Joshua L. Santarpia, et al.. (2021). Determination of Airborne Release Fractions from Solid Surrogate Nuclear Waste Fires. Nuclear Technology. 208(1). 137–153. 1 indexed citations

Boyle, Timothy J., Alexander L. Brown, Joshua L. Santarpia, et al.. (2020). Airborne Release Fractions from Surrogate Nuclear Waste Fires Containing Lanthanide Nitrates and Depleted Uranium Nitrate in 30% Tributyl Phosphate in Kerosene. Nuclear Technology. 207(1). 103–118. 4 indexed citations

Lemieux, Laura J., et al.. (2016). How Immersion in Nature Impacts the Human Spirit: A Phenomenological Study. SOPHIA (St. Catherine University). 1 indexed citations

Calhoun, Melissa W., Laura J. Lemieux, J. Arturo García‐Horsman, et al.. (1995). The highly conserved methionine of subunit I of the heme‐copper oxidases is not at the heme‐copper dinuclear center: Mutagenesis of M110 in subunit I of cytochrome bo₃‐type ubiquinol oxidase from Escherichia coli. FEBS Letters. 368(3). 523–525. 3 indexed citations

Kisilevsky, Robert, Laura J. Lemieux, Paul E. Fraser, et al.. (1995). Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nature Medicine. 1(2). 143–148. 280 indexed citations

Hallén, Stefan, et al.. (1995). Oxygen Reaction and Proton Uptake in Helix VIII Mutants of Cytochrome bo3. Biochemistry. 34(15). 5252–5258. 19 indexed citations

Thomas, Jeffrey W., Melissa W. Calhoun, Laura J. Lemieux, et al.. (1994). Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand. Biochemistry. 33(44). 13013–13021. 22 indexed citations

Hosler, Jonathan P., Shelagh Ferguson‐Miller, Melissa W. Calhoun, et al.. (1993). Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo. Journal of Bioenergetics and Biomembranes. 25(2). 121–136. 228 indexed citations

10.

Calhoun, Melissa W., John J. Hill, Laura J. Lemieux, et al.. (1993). Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: Amino acid substitutions for two histidines that are putative CuB ligands. Biochemistry. 32(43). 11524–11529. 28 indexed citations

11.

Thomas, Jeffrey W., Laura J. Lemieux, James O. Alben, & Robert B. Gennis. (1993). Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center. Biochemistry. 32(41). 11173–11180. 45 indexed citations

12.

Ma, Jixiang, Laura J. Lemieux, & Robert B. Gennis. (1993). Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme. Biochemistry. 32(30). 7692–7697. 17 indexed citations

13.

Calhoun, Melissa W., Laura J. Lemieux, Jeffrey W. Thomas, et al.. (1993). Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli. Biochemistry. 32(48). 13254–13261. 18 indexed citations

14.

Oost, John van der, Pekka Lappalainen, Tony Warne, et al.. (1992). Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.. The EMBO Journal. 11(9). 3209–3217. 133 indexed citations

15.

Hill, John J., Melissa W. Calhoun, J. Arturo García‐Horsman, et al.. (1992). Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product. Biochemistry. 31(46). 11435–11440. 50 indexed citations

16.

Lemieux, Laura J., Melissa W. Calhoun, Jeffrey W. Thomas, W. John Ingledew, & Robert B. Gennis. (1992). Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.. Journal of Biological Chemistry. 267(3). 2105–2113. 107 indexed citations

17.

Saraste, Matti, Liisa Holm, Laura J. Lemieux, Mathias Lübben, & John van der Oost. (1991). The happy family of cytochrome oxidases. Biochemical Society Transactions. 19(3). 608–612. 102 indexed citations

18.

Nakamura, Hiroshi, Ichiro Yamato, Yasutaka Anraku, Laura J. Lemieux, & Robert B. Gennis. (1990). Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the Escherichia coli cytochrome o complex is in subunit I.. Journal of Biological Chemistry. 265(19). 11193–11197. 38 indexed citations

19.

Lemieux, Laura J., et al.. (1990). Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1018(2-3). 124–127. 28 indexed citations

20.

Saraste, Matti, et al.. (1988). Cytochrome O from Escherichia coli Is Structurally Related to Cytochrome aa₃a. Annals of the New York Academy of Sciences. 550(1). 314–324. 26 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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