George H. Lorimer

14.4k total citations · 4 hit papers
133 papers, 11.1k citations indexed

About

George H. Lorimer is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, George H. Lorimer has authored 133 papers receiving a total of 11.1k indexed citations (citations by other indexed papers that have themselves been cited), including 108 papers in Molecular Biology, 54 papers in Materials Chemistry and 24 papers in Cell Biology. Recurrent topics in George H. Lorimer's work include Enzyme Structure and Function (53 papers), Protein Structure and Dynamics (51 papers) and Heat shock proteins research (47 papers). George H. Lorimer is often cited by papers focused on Enzyme Structure and Function (53 papers), Protein Structure and Dynamics (51 papers) and Heat shock proteins research (47 papers). George H. Lorimer collaborates with scholars based in United States, Australia and Germany. George H. Lorimer's co-authors include Thomas S Andrews, Paul V. Viitanen, Anthony A. Gatenby, Pierre Goloubinoff, Henry M. Miziorko, Murray R. Badger, D. Thirumalai, Matthew J. Todd, John T. Christeller and N. E. Tolbert and has published in prestigious journals such as Nature, Science and Chemical Reviews.

In The Last Decade

George H. Lorimer

133 papers receiving 10.6k citations

Hit Papers

align trajectories

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.

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

1989 617 citations Pierre Goloubinoff, Anthony A. Gatenby et al. profile →
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

1989 589 citations Pierre Goloubinoff, Anthony A. Gatenby et al. profile →
RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE-OXYGENASE

1983 557 citations George H. Lorimer et al. profile →
The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications

1976 446 citations George H. Lorimer et al. Biochemistry profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
George H. Lorimer United States	55	9.4k	3.7k	1.6k	1.4k	826	133	11.1k
Ivan Rayment United States	65	10.7k 1.1×	2.5k 0.7×	1.1k 0.7×	2.9k 2.0×	543 0.7×	211	15.9k
Elizabeth D. Getzoff United States	62	7.6k 0.8×	1.5k 0.4×	2.8k 1.8×	1.1k 0.7×	792 1.0×	149	14.4k
Tomitake Tsukihara Japan	52	9.2k 1.0×	1.5k 0.4×	897 0.6×	1.2k 0.8×	858 1.0×	226	13.0k
W. W. Cleland United States	55	8.7k 0.9×	2.8k 0.8×	867 0.6×	1.8k 1.3×	343 0.4×	191	14.7k
Hartmut Michel Germany	67	17.9k 1.9×	3.7k 1.0×	1.3k 0.9×	1.4k 1.0×	2.1k 2.6×	259	21.6k
Kunio Miki Japan	44	7.1k 0.8×	3.1k 0.8×	932 0.6×	401 0.3×	1.5k 1.8×	328	10.9k
S.E. Ealick United States	52	6.7k 0.7×	2.0k 0.5×	442 0.3×	274 0.2×	558 0.7×	246	9.3k
Neil L. Kelleher United States	89	19.2k 2.0×	1.5k 0.4×	917 0.6×	996 0.7×	412 0.5×	440	29.1k
Matti Saraste Germany	55	9.5k 1.0×	1.4k 0.4×	579 0.4×	2.5k 1.7×	493 0.6×	99	12.4k
Werner Kühlbrandt Germany	74	14.8k 1.6×	1.6k 0.4×	2.2k 1.4×	690 0.5×	940 1.1×	226	17.7k

Countries citing papers authored by George H. Lorimer

Since Specialization

Citations

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

Fields of papers citing papers by George H. Lorimer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of George H. Lorimer

This figure shows the co-authorship network connecting the top 25 collaborators of George H. Lorimer. A scholar is included among the top collaborators of George H. Lorimer 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 H. Lorimer. George H. Lorimer 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

Shi, Ai, Huiwen Wu, Ying Deng, et al.. (2024). Serum binding folate receptor autoantibodies lower in autistic boys and positively-correlated with folate. Biomedicine & Pharmacotherapy. 172. 116191–116191. 4 indexed citations

Wang, Xiang, et al.. (2024). HemN2 Regulates the Virulence of Pseudomonas donghuensis HYS through 7-Hydroxytropolone Synthesis and Oxidative Stress. Biology. 13(6). 373–373. 1 indexed citations

Deng, Wenwen, Xuan Tian, Bo Sun, et al.. (2022). Extraction of weak hydrophobic sulforaphane from broccoli by salting-out assisted hydrophobic deep eutectic solvent extraction. Food Chemistry. 405(Pt A). 134817–134817. 20 indexed citations

Bathellier, Camille, Li‐Juan Yu, Graham D. Farquhar, et al.. (2020). Ribulose 1,5-bisphosphate carboxylase/oxygenase activates O ₂ by electron transfer. Proceedings of the National Academy of Sciences. 117(39). 24234–24242. 30 indexed citations

Bathellier, Camille, Guillaume Tcherkez, George H. Lorimer, & Graham D. Farquhar. (2018). Rubisco is not really so bad. Plant Cell & Environment. 41(4). 705–716. 72 indexed citations

Chakrabarti, Shaon, Changbong Hyeon, Xiang Ye, George H. Lorimer, & D. Thirumalai. (2017). Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium. Proceedings of the National Academy of Sciences. 114(51). E10919–E10927. 32 indexed citations

Roh, Soung‐Hun, Corey F. Hryc, Hyun-Hwan Jeong, et al.. (2017). Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. Proceedings of the National Academy of Sciences. 114(31). 8259–8264. 70 indexed citations

Nonomura, Arthur M., et al.. (2017). The paths of Andrew A. Benson: a radio-autobiography. Photosynthesis Research. 134(1). 93–105. 8 indexed citations

Nonomura, Arthur M., et al.. (2015). Andrew A. Benson: personal recollections. Photosynthesis Research. 127(3). 369–378. 7 indexed citations

10.

X, Fei, et al.. (2014). Formation and structures of GroEL:GroES ₂ chaperonin footballs, the protein-folding functional form. Proceedings of the National Academy of Sciences. 111(35). 12775–12780. 63 indexed citations

11.

Stan, George, Bernard R. Brooks, George H. Lorimer, & D. Thirumalai. (2006). Residues in substrate proteins that interact with GroEL in the capture process are buried in the native state. Proceedings of the National Academy of Sciences. 103(12). 4433–4438. 30 indexed citations

12.

Stan, George, Bernard R. Brooks, George H. Lorimer, & D. Thirumalai. (2004). Identifying natural substrates for chaperonins using a sequence‐based approach. Protein Science. 14(1). 193–201. 20 indexed citations

13.

Viitanen, Paul V., George H. Lorimer, Wolfgang Bergmeier, et al.. (1998). [18] Purification of mammalian mitochondrial chaperonin 60 through in Vitro reconstitution of active oligomers. Methods in enzymology on CD-ROM/Methods in enzymology. 290. 203–217. 46 indexed citations

14.

Todd, Matthew J. & George H. Lorimer. (1995). Stability of the Asymmetric Escherichia coli Chaperonin Complex. Journal of Biological Chemistry. 270(10). 5388–5394. 29 indexed citations

15.

Todd, Matthew J., Stefan Walke, George H. Lorimer, Kaye N. Truscott, & Robert K. Scopes. (1995). The Single-Ring Thermoanaerobacter brockii Chaperonin 60 (Tbr-EL7) Dimerizes to Tbr-EL14.cntdot.Tbr-ES7 under Protein Folding Conditions. Biochemistry. 34(45). 14932–14941. 23 indexed citations

16.

Viitanen, Paul V., Marion Schmidt, Johannes Büchner, et al.. (1995). Functional Characterization of the Higher Plant Chloroplast Chaperonins. Journal of Biological Chemistry. 270(30). 18158–18164. 77 indexed citations

17.

Gibson, Katharine J., George H. Lorimer, Alan R. Rendina, et al.. (1995). Dethiobiotin Synthetase: The Carbonylation of 7,8-Diaminononanoic Acid Proceeds Regiospecifically via the N7-Carbamate. Biochemistry. 34(35). 10976–10984. 30 indexed citations

18.

Viitanen, Paul V., Gail K. Donaldson, George H. Lorimer, Thomas Lübben, & Anthony A. Gatenby. (1991). Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry. 30(40). 9716–9723. 171 indexed citations

19.

Gatenby, A.A., Paul V. Viitanen, & George H. Lorimer. (1990). Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria. Trends in biotechnology. 8(12). 354–358. 34 indexed citations

20.

Berry, Joseph A., C. B. Osmond, & George H. Lorimer. (1978). Fixation of ¹⁸O₂ during Photorespiration. PLANT PHYSIOLOGY. 62(6). 954–967. 66 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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