George McLendon

9.2k total citations
179 papers, 7.7k citations indexed

About

George McLendon is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, George McLendon has authored 179 papers receiving a total of 7.7k indexed citations (citations by other indexed papers that have themselves been cited), including 94 papers in Molecular Biology, 58 papers in Materials Chemistry and 34 papers in Cell Biology. Recurrent topics in George McLendon's work include Photosynthetic Processes and Mechanisms (51 papers), Hemoglobin structure and function (31 papers) and Porphyrin and Phthalocyanine Chemistry (29 papers). George McLendon is often cited by papers focused on Photosynthetic Processes and Mechanisms (51 papers), Hemoglobin structure and function (31 papers) and Porphyrin and Phthalocyanine Chemistry (29 papers). George McLendon collaborates with scholars based in United States, Canada and United Kingdom. George McLendon's co-authors include Arthur E. Martell, David Heiler, John A. Marohn, Anna M. Helms, Martin A. Case, Fred Sherman, Michael O’Neil, Deborah S. Miller, Julie M. Rehm and Thomas F. Guarr and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

George McLendon

175 papers receiving 7.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
George McLendon United States 47 3.4k 2.9k 1.9k 1.3k 1.0k 179 7.7k
Harry B. Gray United States 41 1.7k 0.5× 1.6k 0.6× 1.8k 0.9× 853 0.6× 794 0.8× 81 5.7k
Gerard W. Canters Netherlands 52 5.0k 1.5× 2.3k 0.8× 1.8k 1.0× 498 0.4× 918 0.9× 264 8.8k
Christopher C. Moser United States 41 5.8k 1.7× 1.8k 0.6× 1.8k 0.9× 1.0k 0.8× 1.4k 1.4× 95 9.2k
John A. Shelnutt United States 56 3.8k 1.1× 7.5k 2.6× 1.4k 0.7× 941 0.7× 765 0.7× 177 10.7k
John H. Richards United States 44 3.7k 1.1× 1.1k 0.4× 858 0.4× 623 0.5× 486 0.5× 174 7.4k
Chi K. Chang United States 51 3.1k 0.9× 5.3k 1.8× 905 0.5× 714 0.5× 286 0.3× 239 8.5k
Craig J. Medforth United States 48 2.6k 0.8× 6.6k 2.2× 930 0.5× 1.1k 0.8× 360 0.4× 111 8.0k
David F. Bocian United States 65 4.7k 1.4× 10.0k 3.4× 3.7k 1.9× 2.4k 1.8× 1.8k 1.8× 324 15.3k
R. Brian Dyer United States 49 3.9k 1.1× 2.4k 0.8× 550 0.3× 524 0.4× 1.3k 1.3× 162 6.8k
Abhik Ghosh Norway 55 2.0k 0.6× 7.3k 2.5× 959 0.5× 1.1k 0.8× 841 0.8× 325 10.1k

Countries citing papers authored by George McLendon

Since Specialization
Citations

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

Fields of papers citing papers by George McLendon

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of George McLendon

This figure shows the co-authorship network connecting the top 25 collaborators of George McLendon. A scholar is included among the top collaborators of George McLendon 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 George McLendon. George McLendon 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.
Allen, John E. & George McLendon. (2006). Tryptophan and tyrosine to terbium fluorescence resonance energy transfer as a method to “map” aromatic residues and monitor docking. Biochemical and Biophysical Research Communications. 349(4). 1264–1268. 7 indexed citations
2.
Webber, Andrew N., et al.. (2005). Endonuclease-like activity of heme proteins. JBIC Journal of Biological Inorganic Chemistry. 10(7). 790–799. 28 indexed citations
3.
Balakrishnan, Gurusamy, Qiang Wu, Martin A. Case, et al.. (2004). Hemoglobin Site-mutants Reveal Dynamical Role of Interhelical H-bonds in the Allosteric Pathway: Time-resolved UV Resonance Raman Evidence for Intra-dimer Coupling. Journal of Molecular Biology. 340(4). 857–868. 32 indexed citations
4.
Balakrishnan, Gurusamy, et al.. (2004). Time-resolved Absorption and UV Resonance Raman Spectra Reveal Stepwise Formation of T Quaternary Contacts in the Allosteric Pathway of Hemoglobin. Journal of Molecular Biology. 340(4). 843–856. 58 indexed citations
5.
Springs, Stacy L., et al.. (2002). The Kinetics of Translocation of Smac/DIABLO from the Mitochondria to the Cytosol in HeLa Cells. Journal of Biological Chemistry. 277(48). 45715–45718. 30 indexed citations
6.
Wei, Yen, George McLendon, Martin A. Case, et al.. (2001). Disruption of protein–protein interactions: design of a synthetic receptor that blocks the binding of cytochrome c to cytochrome c peroxidase. Chemical Communications. 1580–1581. 47 indexed citations
7.
Frederick, Ronnie O., Ananya Majumdar, Weijun Xu, et al.. (1999). RNA architecture dictates the conformations of a bound peptide. Chemistry & Biology. 6(9). 657–669. 63 indexed citations
8.
Sherman, Fred, et al.. (1995). Stabilizing Amino Acid Replacements at Position 52 in Yeast Iso-1-cytochrome c: In Vivo and in Vitro Effects. Biochemistry. 34(21). 7094–7102. 18 indexed citations
9.
Karpishin, Timothy B., et al.. (1994). Electron transfer in cytochrome c depends upon the structure of the intervening medium. Structure. 2(5). 415–422. 33 indexed citations
10.
Jeng, Mei‐Fen, et al.. (1994). Structural dynamics in an electron–transfer complex. Nature Structural & Molecular Biology. 1(4). 234–238. 26 indexed citations
11.
McLendon, George, et al.. (1994). [7] Electron-transfer reactions of hemoglobin with small molecules: A potential probe of conformational dynamics. Methods in enzymology on CD-ROM/Methods in enzymology. 232. 86–94. 4 indexed citations
12.
Weis, David D., et al.. (1994). Thermodynamics of the Equilibrium Unfolding of Oxidized and Reduced Saccharomyces cerevisiae Iso-1-cytochromes c. Biochemistry. 33(34). 10556–10560. 14 indexed citations
13.
McLendon, George, et al.. (1992). Interprotein electron transfer. Chemical Reviews. 92(3). 481–490. 252 indexed citations
14.
Langen, Ralf, G.D. Brayer, Albert M. Berghuis, et al.. (1992). Effect of the Asn52 → Ile mutation on the redox potential of yeast cytochrome c. Journal of Molecular Biology. 224(3). 589–600. 76 indexed citations
15.
McLendon, George, et al.. (1991). Migration of small molecules through the structure of hemoglobin: evidence for gating in a protein electron-transfer reaction. Biochemistry. 30(20). 5051–5055. 41 indexed citations
16.
Guo, Liang‐Hong, et al.. (1991). Direct electrochemistry of proteins. European Journal of Biochemistry. 202(2). 543–549. 40 indexed citations
17.
Whitford, David, Yuan Gao, Gary J. Pielak, et al.. (1991). The role of the internal hydrogen bond network in first‐order protein electron transfer between Saccharomyces cerevisiae iso‐1‐cytochrome c and bovine microsomal cytochrome b5. European Journal of Biochemistry. 200(2). 359–367. 16 indexed citations
18.
McLendon, George, et al.. (1991). Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c. Biochemistry. 30(49). 11585–11595. 36 indexed citations
19.
Magner, Edmond & George McLendon. (1989). Photochemical generation and reactions of heme cation radicals in heme proteins. Biochemical and Biophysical Research Communications. 159(2). 472–476. 2 indexed citations
20.

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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Harry B. Gray Breakdown of academic impact, for papers by Gerard W. Canters Breakdown of academic impact, for papers by Christopher C. Moser Breakdown of academic impact, for papers by John A. Shelnutt Breakdown of academic impact, for papers by John H. Richards Breakdown of academic impact, for papers by Chi K. Chang Breakdown of academic impact, for papers by Craig J. Medforth Breakdown of academic impact, for papers by David F. Bocian Breakdown of academic impact, for papers by R. Brian Dyer Breakdown of academic impact, for papers by Abhik Ghosh
Rankless by CCL
2026