L. Powers

2.9k total citations
72 papers, 2.3k citations indexed

About

L. Powers is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, L. Powers has authored 72 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 17 papers in Cell Biology and 13 papers in Materials Chemistry. Recurrent topics in L. Powers's work include Hemoglobin structure and function (16 papers), Photosynthetic Processes and Mechanisms (13 papers) and Enzyme Structure and Function (10 papers). L. Powers is often cited by papers focused on Hemoglobin structure and function (16 papers), Photosynthetic Processes and Mechanisms (13 papers) and Enzyme Structure and Function (10 papers). L. Powers collaborates with scholars based in United States, Germany and Japan. L. Powers's co-authors include B. Chance, P. S. Pershan, Y. Ching, Paul J. Angiolillo, Thomas G. Spiro, Isao Yamazaki, Mark R. Chance, G. L. Woolery, B. M. Kincaid and C. Kumar and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

L. Powers

69 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L. Powers United States 28 1.3k 605 395 357 258 72 2.3k
Michael H. Klapper United States 24 1.1k 0.9× 292 0.5× 201 0.5× 313 0.9× 234 0.9× 66 2.1k
J.A. Fee United States 32 1.4k 1.1× 276 0.5× 782 2.0× 285 0.8× 139 0.5× 46 2.7k
Federico I. Rosell Canada 25 1.4k 1.0× 394 0.7× 217 0.5× 323 0.9× 177 0.7× 44 2.1k
Gaston Hui Bon Hoa France 31 1.7k 1.3× 530 0.9× 278 0.7× 334 0.9× 516 2.0× 101 2.9k
Shigetoshi Aono Japan 29 1.6k 1.2× 1.1k 1.9× 370 0.9× 604 1.7× 256 1.0× 129 2.7k
Marvin W. Makinen United States 27 1.1k 0.8× 518 0.9× 398 1.0× 532 1.5× 228 0.9× 80 2.2k
Pierre Douzou France 32 1.9k 1.4× 462 0.8× 144 0.4× 526 1.5× 510 2.0× 134 2.9k
Myles R. Cheesman United Kingdom 42 2.1k 1.6× 626 1.0× 866 2.2× 671 1.9× 175 0.7× 98 4.4k
Christiane Jung Germany 28 918 0.7× 362 0.6× 573 1.5× 396 1.1× 379 1.5× 84 2.3k
James E. Erman United States 32 2.3k 1.7× 1.1k 1.8× 424 1.1× 410 1.1× 318 1.2× 117 3.3k

Countries citing papers authored by L. Powers

Since Specialization
Citations

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

Fields of papers citing papers by L. Powers

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L. Powers

This figure shows the co-authorship network connecting the top 25 collaborators of L. Powers. A scholar is included among the top collaborators of L. Powers 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 L. Powers. L. Powers 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.
Alaiwa, Mahmoud H. Abou, Ankur Jain, Wenjie Yu, et al.. (2024). Disruption of the DNAI1 Gene in Pigs Produces a Model of Primary Ciliary Dyskinesia. A7263–A7263. 1 indexed citations
2.
Duncan, Andrew, et al.. (2004). Real-time detection of microbial contamination. IEEE Engineering in Medicine and Biology Magazine. 23(1). 122–129. 19 indexed citations
3.
Powers, L. & Mark A. Griep. (1997). Structure of the Escherichia coli Primase Zinc Site. The FASEB Journal. 11(9). 1367. 5 indexed citations
4.
Yue, Kan, et al.. (1997). X-ray absorption and resonance raman spectroscopy of human myeloperoxidase at neutral and acid pH. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1338(2). 282–294. 6 indexed citations
5.
Sinclair, Rodney, et al.. (1996). Active Site Structure in Cytochrome c Peroxidase and Myoglobin Mutants:  Effects of Altered Hydrogen Bonding to the Proximal Histidine. Biochemistry. 35(47). 15120–15128. 20 indexed citations
6.
Sinclair, Rodney, Bruce R. Copeland, Isao Yamazaki, & L. Powers. (1995). X-ray Absorption Spectroscopy Comparison of the Active Site Structures of Phanerochaete chrysosporium Lignin Peroxidase Isoenzymes H2, H3, H4, H5, H8, and H10. Biochemistry. 34(40). 13176–13182. 7 indexed citations
7.
Farhangrazi, Z. Shadi, Bruce R. Copeland, Tôru Nakayama, et al.. (1994). Oxidation-Reduction Properties of Compounds I and II of Arthromyces ramosus Peroxidase. Biochemistry. 33(18). 5647–5652. 53 indexed citations
8.
Yamazaki, Isao, et al.. (1993). pH dependence of the active site of horseradish peroxidase compound II. Biochemistry. 32(3). 923–928. 27 indexed citations
9.
Farhangrazi, Z. Shadi, Robert Sinclair, Isao Yamazaki, & L. Powers. (1992). Haloperoxidase activity of Phanerochaete chrysosporium lignin peroxidases H2 and H8. Biochemistry. 31(44). 10763–10768. 27 indexed citations
10.
Sinclair, Rodney, et al.. (1992). Structure of the active site of lignin peroxidase isozyme H2: native enzyme, compound III and reduced form. Biochemistry. 31(20). 4892–4900. 7 indexed citations
11.
Powers, L., et al.. (1989). EXAFS studies of the isolated bovine heart Rieske [2Fe-2S]1+(1+,2+) cluster. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 975(2). 293–298. 16 indexed citations
12.
Powers, L. & B. M. Kincaid. (1989). Comparison of the data, analysis, and results of x-ray absorption studies of cytochrome c oxidase. Biochemistry. 28(10). 4461–4468. 18 indexed citations
13.
Powers, L. & W. E. Blumberg. (1988). A comparison of various models for ligand recombination kinetics of myoglobin. Biophysical Journal. 54(1). 181–185. 7 indexed citations
14.
Powers, L., B. Chance, Mark R. Chance, et al.. (1987). Kinetic, structural, and spectroscopic indentification of geminate states of myoglobin: a ligand binding site on the reaction pathway. Biochemistry. 26(15). 4785–4796. 67 indexed citations
15.
Chance, Mark R., L. Powers, T.L. Poulos, & B. Chance. (1986). Cytochrome c peroxidase compound ES is identical with horseradish peroxidase compound I in iron-ligand distances. Biochemistry. 25(6). 1266–1270. 63 indexed citations
16.
Powers, L., et al.. (1984). X-ray absorption studies of the zinc(2+) site of glyoxalase I. Biochemistry. 23(4). 685–689. 28 indexed citations
17.
Eanes, E. D., L. Powers, & Jonathan L. Costa. (1981). Extended X-ray absorption fine structure (EXAFS) studies on calcium in crystalline and amorphous solids of biological interest. Cell Calcium. 2(3). 251–262. 19 indexed citations
18.
Brown, James M., L. Powers, B. M. Kincaid, James A. Larrabee, & Thomas G. Spiro. (1980). Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis. Journal of the American Chemical Society. 102(12). 4210–4216. 129 indexed citations
19.
Chance, Britton, et al.. (1980). Biological membranes. Physics Today. 33(10). 32–38. 7 indexed citations
20.
Stamatoff, J., et al.. (1979). Direct observation of the hydrocarbon chain tilt angle in phospholipid bilayers. Biophysical Journal. 25(2). 253–261. 42 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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