Eric Oldfield
Born1948
London, England
CitizenshipBritish
EducationBristol University (B.Sc. 1969; D.Sc. 1982)
Sheffield University (Ph.D. 1972)
Indiana University (Post-Doc 1972–1974)
Massachusetts Institute of Technology (Visiting Scientist 1974–1975)
Known forNMR Spectroscopy and Drug Discovery
AwardsThe Meldola Medal, Royal Society of Chemistry
The Colworth Medal, Biochemical Society
Award in Pure Chemistry, American Chemical Society
Award in Spectroscopy, Royal Society of Chemistry
Award in Soft Matter and Biophysical Chemistry, Royal Society of Chemistry
Avanti Award in Lipids, Biophysical Society
Katz Basic Science Prize, American Heart Association
Scientific career
FieldsPhysical Chemistry, Chemical Biology, Microbiology, Parasitology
InstitutionsUniversity of Illinois at Urbana-Champaign
Thesis"Spectroscopic Studies of Lipids and Biological Membranes" (1972)
Doctoral advisorDennis Chapman
Other academic advisorsJake MacMillan
Geoffrey Eglinton
Adam Allerhand
John S. Waugh

Eric Oldfield (born 1948) is a British chemist, the Harriet A. Harlin Professor of Chemistry and a Professor of Biophysics at the University of Illinois at Urbana-Champaign.[1] He is known for his work in nuclear magnetic resonance spectroscopy of lipids, proteins, and membranes; of inorganic solids; in computational chemistry, and in microbiology and parasitology. He has received a number of recognitions for his work, including the American Chemical Society’s Award in Pure Chemistry, the Royal Society of Chemistry’s Meldola Medal and the Biochemical Society’s Colworth Medal, and he is a member of the American Association for the Advancement of Science, a Fellow of the Royal Society of Chemistry, and a Fellow of the American Physical Society.

Early life and education

Oldfield was born in London, England on May 23, 1948. He attended the University in Bristol doing research with Jake MacMillan on diterpenes and Geoffrey Eglinton on lipids and isoprenoids. He graduated with a Bachelor of Science degree in 1969. He obtained a PhD in Biophysical Chemistry from the University of Sheffield in 1972, with Dennis Chapman, developing NMR methods to study lipid and membrane structure. He worked as a Research Associate and EMBO Postdoctoral Fellow at Indiana University with Adam Allerhand, on the development of high-resolution NMR of proteins (1972–1974)[2] and was then a Visiting Scientist at MIT with John S. Waugh (1974-1975), working on solid-state NMR.[3]

Career

Oldfield joined the Department of Chemistry at the University of Illinois at Urbana-Champaign in 1975 as an assistant Professor of Chemistry. He was promoted to Associate Professor in 1980 and was a Professor from 1982 to 2002. He was then an Alumni Research Professor of Chemistry from 2003 to 2013 and since then has been the Harriet A. Harlin Professor of Chemistry. He has also been a Professor of Biophysics in the Center for Computational Biology and Biophysics since 1995 and was a Fellow in the Center for Advanced Study in 1979, a Richard G. and Carole J. Cline University Senior Scholar in 1995, and an Associate in the Center for Advanced Study in 2000. He has authored 450 publications and as of 2023, has an h-index of 104 with 35,000 citations, according to Google Scholar[4] and holds nine issued patents from the United States Patent and Trademark Office.[5]

Research

Oldfield is known for his research in nuclear magnetic resonance (NMR) spectroscopy, and drug discovery. His invention of deuterium and proton NMR methods led to new ways to study the structures of lipids and membranes; his carbon-13 NMR and quantum chemical developments led to new ways to investigate protein structures; his investigations of quadrupolar nuclei led to new research in materials science, geochemistry and catalysis, and his more recent research using NMR, computational and crystallographic methods has led to the development of new therapeutic approaches to treating both infectious diseases and cancer, targeting lipid biosynthesis.

NMR of lipids and membranes

In the 1970s and 1980s Oldfield developed ways to investigate lipid and membrane structure including the use of 2H nuclear magnetic resonance (NMR) spectroscopy of labelled compounds.[6][7] This method enabled the determination of the static and dynamic structures of lipids, and how they interact with proteins and sterol molecules such as cholesterol.[8] In addition, he developed 1H and 13C magic-angle sample-spinning methods to investigate lipid membranes without the need for isotopic labeling. The magic-angle technique was not thought to be applicable to 1H NMR (due to strong dipolar interactions), but he showed that due to fast axial diffusion, these interactions were scaled and that remarkably high-resolution spectra could be obtained.[9]

NMR of proteins

In the early 1970s, while working with Adam Allerhand, Oldfield reported the first high-resolution 13C NMR spectra of proteins—lysozyme, myoglobin and cytochrome c—in which numerous single carbon atom sites could be resolved and assigned.[10][11] The origins of the chemical shift non-equivalencies observed due to folding remained unexplained until 1993 when he showed that 13C and 15N chemical shifts in proteins could be well predicted by using quantum chemical methods. He reasoned that since the chemical shift is essentially a local phenomenon, it might be possible to compute chemical shifts just by using small peptide fragments and a “locally dense” basis set, and this turned out to be correct.[12] His early work also led to the demonstration that computed chemical shift tensors could be used in protein structure refinement.[13] Moreover, he showed that the chemical shifts of non-native species in proteins such as 19F nuclei, could be also be computed, and were due to electric field effects.[14]

Quantum chemistry

Followed by the observation that chemical shifts in proteins could be computed by using quantum chemical methods, Oldfield began a series of investigations of other spectroscopic properties[15] including Mössbauer isomer shifts[16] and quadrupole splittings,[17] hyperfine shifts in metalloproteins,[18] spin-spin couplings,[19] and electric field gradients, as well as the effects of hydrogen bonding on chemical shifts.[20]

NMR inorganic solids

Oldfield began to investigate structures of a variety of inorganic solids in the 1980s. He showed that high-resolution spectra of quadrupolar nuclei (such as 17O, 23Na) could be obtained by using variable-angle sample-spinning,[21] spin echo,[22] as well as spectral deconvolution methods.[23] In his collaborative research with R. James Kirkpatrick, he investigated the 29Si magic-angle sample-spinning NMR spectra of a wide range of natural and synthetic silicates,[24] showing that both Si-O bond length-chemical shift and bond strength-chemical shift relationships were useful tools for investigating the structures of crystalline silicates and, more importantly, silicate glasses, clays, and zeolites that cannot be examined by single crystal X-ray or neutron diffraction methods. He also worked on investigating Pt/Ru direct methanol oxidation fuel cell catalysts using 13C and 195Pt NMR, in collaboration with A. Wieckowksi, which clarified the mechanism of enhanced CO tolerance in Pt/Ru versus pure Pt catalysts.[25]

Antibiotics

In 1999, Oldfield shifted his research to more biomedical applications. Working in collaboration with Julio Urbina and Roberto Docampo, his group found, using 31P NMR spectroscopy, that the parasitic protozoan Trypanosoma cruzi, the causative agent of Chagas disease, contained very high levels of diphosphate, and that diphosphate analogs, bisphosphonates used clinically to treat bone resorption diseases, killed these parasites.[26] as well as others.[27] He also discovered that the bisphosphonate pamidronate cured mice of leishmaniasis[28] and proposed that farnesyl diphosphate synthase (FPPS) can be used as the target of bisphosphonate drugs[29]

Oldfield then discovered another compound that killed T. cruzi, the antiarrhythmic drug amiodarone, and that it acted synergistically with the azole drug posaconazole.[30] He then began to investigate antibacterial agents. The human pathogen Staphylococcus aureus contains a gold-colored virulence factor called staphyloxanthin that protects the bacterium from killing by reactive oxygen species.[31] Recognizing that the biosynthesis of the carotenoid pigment had similarities to the first steps in cholesterol biosynthesis, he synthesized a range of cholesterol biosynthesis inhibitors and tested them in S. aureus and in mice models of infection finding potent activity against the protein target dehydrosqualene synthase, the bacterium, and in a mice model of infection.[32] His group also showed that some drugs and drug leads that target tuberculosis bacteria function as protonophore uncouplers and in some cases they can also target isoprenoid biosynthesis, leading to potent multi-target inhibition.[33]

Anti-cancer drug leads

In 2012, Oldfield's group synthesized lipophilic analogs of the clinical bisphosphonate drugs zoledronate and risedronate, to prevent unwanted binding to bone mineral, and found they had potent anti-malarial activity.[34] Additionally, they had potent activity in a combination therapy with rapamycin in tumor cells and in mice, by targeting protein prenylation[35] with inhibition of protein prenylation also leading to activity as vaccine adjuvants.[36] Mechanistically, FPPS inhibition affects cell signaling, but it also leads to accumulation of isopentenyl diphosphate and dimethylallyl diphosphate, compounds that activate γδT cells by binding to butyrophilins in target cells[37] and this T cell activation led to tumor cell killing.[38] His group also showed that some clinically used bisphosphonate drugs are converted to analogs of adenosine triphosphate that function by inhibiting cell signaling pathways.[39]

Isoprenoid synthesis

Oldfield and his collaborators have reported the structures and mechanisms of action of many proteins involved in isoprenoid biosynthesis, focusing on the modular structures found.[40] They successfully predicted the αβγ tri-domain found in diterpene cyclases.[41] Furthermore, they used electron paramagnetic resonance and X-ray crystallography to develop the organometallic mechanism of action of the unusual 4Fe-4S proteins IspG and IspH involved in the early stages of isoprenoid biosynthesis,[42] and also used X-ray methods for providing mechanisms of action for the terpene cyclases.[43]

Awards

Selected articles

  • M. D. Meadows, K. A. Smith, R. A. Kinsey, T. M. Rothgeb, R. P. Skarjune and E. Oldfield, Proc. Natl. Acad. Sci. U.S.A., 79, 1351–1355 (1982), High-resolution solid state NMR of quadrupolar nuclei
  • J. Forbes, J. Bowers, L. Moran, X. Shan, E. Oldfield, and M. A. Moscarello, J. Chem. Soc., Faraday Transactions, 84, 3821–3849 (1988). Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems.
  • A. C. de Dios, J. G. Pearson and E. Oldfield, Science, 260, 1491–1496 (1993). Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach.
  • G. Benaim, J. M. Sanders, Y. Garcia-Marchán, C. Colina, R. Lira, A. R. Caldera, G. Payares, C. Sanoja, J. M. Burgos, A. Leon-Rossell, J. L. Concepcion, A. Schijman, M. Levin and E. Oldfield and J. A. Urbina, J. Med. Chem., 49, 892–899 (2006). Amiodarone has intrinsic anti-Trypanosoma cruzi activity and acts synergistically with posaconazole.
  • C.-I. Liu, G. Y. Liu, Y. Song, F. Yin, M. E. Hensler, W.-Y. Jeng, V. Nizet, A. H.-J. Wang and E. Oldfield, Science, 319, 1391–1394 (2008). A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence.
  • Y. Xia, N. Yeddula, M. Leblanc, E. Ke, Y. Zhang, E. Oldfield, R. J. Shaw and I. M. Verma, Nature Cell Biology, 14, 257–265 (2012). Reduced cell proliferation by IKK2/IKKb depletion in a mouse lung cancer model.
  • W. Wang and E. Oldfield, Angew. Chem. Int. Ed. Engl., 53, 4294–4310 (2014). Bioorganometallic chemistry with IspG and IspH: structure, function, and inhibition of the [Fe4S4] proteins involved in isoprenoid biosynthesis.
  • L. Yuan , X. Ma, Y. Yang, Y. Qu, X. Li, X. Zhu, W. Ma, J. Duan, J. Xue, H. Yang, J-W. Huang, S. Yi, M. Zhang, N. Cai, L. Zhang, Q. Ding, K. Lai, C. Liu, L. Zhang, X. Liu, Y. Yao, S. Zhou, X. Li, P. Shen, Q. Chang, S. R. Malwal, Y. He, W. Li, C. Chen, C-C. Chen, E. Oldfield, R-T. Guo, Y. Zhang. Nature. 2023 Sep; 621(7980): 840–848. Phosphoantigens glue butyrophilin 3A1 and 2A1 to activate Vγ9Vδ2 T cells.

References

  1. ↑ "Eric Oldfield | Chemistry at Illinois". chemistry.illinois.edu.
  2. ↑ Allerhand, Adam; Childers, RayF; Oldfield, Eric (August 1, 1973). "Carbon-13 fourier transform nmr at 14.2 kg in a 20 mm probe". Journal of Magnetic Resonance. 11 (2): 272–278. Bibcode:1973JMagR..11..272A. doi:10.1016/0022-2364(73)90013-9 – via ScienceDirect.
  3. ↑ "Chemistry Tree - John S. Waugh". academictree.org.
  4. ↑ "Eric Oldfield". scholar.google.com.
  5. ↑ "Eric Oldfield Inventions, Patents and Patent Applications – Justia Patents Search". patents.justia.com.
  6. ↑ "deuteron resonance:A novel approach to the study of hydrocarbon chain mobility in membrane systems" (PDF).
  7. ↑ Oldfield, Eric; Meadows, Michael; Rice, David; Jacobs, Russell (July 11, 1978). "Spectroscopic studies of specifically deuterium labeled membrane systems. Nuclear magnetic resonance investigation of the effects of cholesterol in model systems". Biochemistry. 17 (14): 2727–2740. doi:10.1021/bi00607a006. PMID 687560.
  8. ↑ Seelig, Joachim (1977). "Deuterium magnetic resonance: theory and application to lipid membranes". Quarterly Reviews of Biophysics. 10 (3): 353–418. doi:10.1017/S0033583500002948. PMID 335428. S2CID 33372264.
  9. ↑ Forbes, Jeffrey; Bowers, John; Shan, Xi; Moran, Liam; Oldfield, Eric; Moscarello, Mario A. (1988). "Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems". Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 84 (11): 3821. doi:10.1039/F19888403821.
  10. ↑ Allerhand, Adam; Childres, Ray F.; Oldfield, Eric (1973). "Natural-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Numerous single-carbon resonances of hen egg-white lysozyme". Biochemistry. 12 (7): 1335–1341. doi:10.1021/bi00731a013. PMID 4735301.
  11. ↑ Oldfield, Eric; Allerhand, Adam (1973). "Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy". Proceedings of the National Academy of Sciences. 70 (12): 3531–3535. doi:10.1073/pnas.70.12.3531. PMC 427274. PMID 4357878.
  12. ↑ De Dios, Angel C.; Pearson, John G.; Oldfield, Eric (1993). "Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach". Science. 260 (5113): 1491–1496. Bibcode:1993Sci...260.1491D. doi:10.1126/science.8502992. PMID 8502992.
  13. ↑ Wylie, Benjamin J.; Schwieters, Charles D.; Oldfield, Eric; Rienstra, Chad M. (January 28, 2009). "Protein Structure Refinement Using 13 Cα Chemical Shift Tensors". Journal of the American Chemical Society. 131 (3): 985–992. doi:10.1021/ja804041p. PMC 2751586. PMID 19123862.
  14. ↑ Pearson, John G.; Oldfield, Eric; Lee, Frederick S.; Warshel, Arieh (1993). "Chemical shifts in proteins: a shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach". Journal of the American Chemical Society. 115 (15): 6851–6862. doi:10.1021/ja00068a049.
  15. ↑ Oldfield, Eric (2005). "Quantum chemical studies of protein structure". Philosophical Transactions of the Royal Society B: Biological Sciences. 360 (1458): 1347–1361. doi:10.1098/rstb.2003.1421. PMC 1569496. PMID 16147526.
  16. ↑ Zhang, Yong; Mao, Junhong; Oldfield, Eric (2002). "57Fe Mössbauer Isomer Shifts of Heme Protein Model Systems: Electronic Structure Calculations". Journal of the American Chemical Society. 124 (26): 7829–7839. doi:10.1021/ja011583v. PMID 12083937.
  17. ↑ Zhang, Yong; Mao, Junhong; Godbout, Nathalie; Oldfield, Eric (2002). "Mössbauer Quadrupole Splittings and Electronic Structure in Heme Proteins and Model Systems: A Density Functional Theory Investigation". Journal of the American Chemical Society. 124 (46): 13921–13930. doi:10.1021/ja020298o. PMID 12431124.
  18. ↑ Mao, Junhong; Zhang, Yong; Oldfield, Eric (2002). "Nuclear Magnetic Resonance Shifts in Paramagnetic Metalloporphyrins and Metalloproteins". Journal of the American Chemical Society. 124 (46): 13911–13920. doi:10.1021/ja020297w. PMID 12431123.
  19. ↑ Arnold, William D.; Mao, Junhong; Sun, Haihong; Oldfield, Eric (2000). "Computation of Through-Space 19F−19F Scalar Couplings via Density Functional Theory". Journal of the American Chemical Society. 122 (49): 12164–12168. doi:10.1021/ja002361k.
  20. ↑ Arnold, William D.; Oldfield, Eric (2000). "The Chemical Nature of Hydrogen Bonding in Proteins via NMR: J-Couplings, Chemical Shifts, and AIM Theory". Journal of the American Chemical Society. 122 (51): 12835–12841. doi:10.1021/ja0025705.
  21. ↑ Ganapathy, Subramanian; Schramm, Suzanne; Oldfield, Eric (1982). "Variable-angle sample-spinning high resolution NMR of solids". The Journal of Chemical Physics. 77 (9): 4360–4365. doi:10.1063/1.444436.
  22. ↑ Kunwar, A.C; Turner, Gary L.; Oldfield, Eric (1986). "Solid-state spin-echo Fourier transform NMR of 39K and 67Zn salts at high field". Journal of Magnetic Resonance (1969). 69: 124–127. doi:10.1016/0022-2364(86)90224-6.
  23. ↑ Oldfield, Eric; Timken, Hye Kyung C.; Montez, Ben; Ramachandran, R. (1985). "High-resolution solid-state NMR of quadrupolar nuclei". Nature. 318 (6042): 163–165. Bibcode:1985Natur.318..163O. doi:10.1038/318163a0. S2CID 4329616.
  24. ↑ "High-resolution silicon-29 nuclear magnetic resonance spectroscopic study of rock-forming silicates".
  25. ↑ Babu, P. K.; Oldfield, E.; Wieckowski, A. (March 17, 2003). Vayenas, C. G.; Conway, B. E.; White, Ralph E.; Gamboa-Adelco, Maria E. (eds.). Modern Aspects of Electrochemistry No. 36. Springer US. pp. 1–50. doi:10.1007/0-306-47927-3_1 – via Springer Link.
  26. ↑ Urbina, Julio A.; Moreno, Benjamin; Vierkotter, Stephanie; Oldfield, Eric; Payares, Gilberto; Sanoja, Cristina; Bailey, Brian N.; Yan, Wen; Scott, David A.; Moreno, Silvia N. J.; Docampo, Roberto (November 19, 1999). "Trypanosoma cruzi Contains Major Pyrophosphate Stores, and Its Growth in Vitro and in Vivo Is Blocked by Pyrophosphate Analogs *". Journal of Biological Chemistry. 274 (47): 33609–33615. doi:10.1074/jbc.274.47.33609. PMID 10559249 – via www.jbc.org.
  27. ↑ Martin, Michael B.; Grimley, Joshua S.; Lewis, Jared C.; Heath, Huel T.; Bailey, Brian N.; Kendrick, Howard; Yardley, Vanessa; Caldera, Aura; Lira, Renee; Urbina, Julio A.; Moreno, Silvia N. J.; Docampo, Roberto; Croft, Simon L.; Oldfield, Eric (March 1, 2001). "Bisphosphonates Inhibit the Growth of Trypanosoma brucei, Trypanosoma cruzi, Leishmania d onovani, Toxoplasma g ondii, and Plasmodium f alciparum : A Potential Route to Chemotherapy". Journal of Medicinal Chemistry. 44 (6): 909–916. doi:10.1021/jm0002578. PMID 11300872.
  28. ↑ "Radical Cure of Experimental Cutaneous Leishmaniasis by the Bisphosphonate Pamidronate".
  29. ↑ Martin, Michael B.; Arnold, William; Heath, Huel T.; Urbina, Julio A.; Oldfield, Eric (1999). "Nitrogen-Containing Bisphosphonates as Carbocation Transition State Analogs for Isoprenoid Biosynthesis". Biochemical and Biophysical Research Communications. 263 (3): 754–758. doi:10.1006/bbrc.1999.1404. PMID 10512752.
  30. ↑ Benaim, Gustavo; Sanders, John M.; Garcia-Marchán, Yael; Colina, Claudia; Lira, Renee; Caldera, Aura R.; Payares, Gilberto; Sanoja, Cristina; Burgos, Juan Miguel; Leon-Rossell, Annette; Concepcion, Juan Luis; Schijman, Alejandro G.; Levin, Mariano; Oldfield, Eric; Urbina, Julio A. (2006). "Amiodarone Has Intrinsic Anti-Trypanosoma cruzi Activity and Acts Synergistically with posaconazole†". Journal of Medicinal Chemistry. 49 (3): 892–899. doi:10.1021/jm050691f. hdl:11336/79898. PMID 16451055.
  31. ↑ "Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity".
  32. ↑ Liu, Chia-I; Liu, George Y.; Song, Yongcheng; Yin, Fenglin; Hensler, Mary E.; Jeng, Wen-Yih; Nizet, Victor; Wang, Andrew H.-J.; Oldfield, Eric (2008). "A Cholesterol Biosynthesis Inhibitor Blocks Staphylococcus aureus Virulence". Science. 319 (5868): 1391–1394. Bibcode:2008Sci...319.1391L. doi:10.1126/science.1153018. PMC 2747771. PMID 18276850.
  33. ↑ Li, Kai; Schurig-Briccio, Lici A.; Feng, Xinxin; Upadhyay, Ashutosh; Pujari, Venugopal; Lechartier, Benoit; Fontes, Fabio L.; Yang, Hongliang; Rao, Guodong; Zhu, Wei; Gulati, Anmol; No, Joo Hwan; Cintra, Giovana; Bogue, Shannon; Liu, Yi-Liang; Molohon, Katie; Orlean, Peter; Mitchell, Douglas A.; Freitas-Junior, Lucio; Ren, Feifei; Sun, Hong; Jiang, Tong; Li, Yujie; Guo, Rey-Ting; Cole, Stewart T.; Gennis, Robert B.; Crick, Dean C.; Oldfield, Eric (April 10, 2014). "Multitarget Drug Discovery for Tuberculosis and Other Infectious Diseases". Journal of Medicinal Chemistry. 57 (7): 3126–3139. doi:10.1021/jm500131s. PMC 4084622. PMID 24568559.
  34. ↑ No, Joo Hwan; De Macedo Dossin, Fernando; Zhang, Yonghui; Liu, Yi-Liang; Zhu, Wei; Feng, Xinxin; Yoo, Jinyoung Anny; Lee, Eunhae; Wang, Ke; Hui, Raymond; Freitas-Junior, Lucio H.; Oldfield, Eric (2012). "Lipophilic analogs of zoledronate and risedronate inhibit Plasmodium geranylgeranyl diphosphate synthase (GGPPS) and exhibit potent antimalarial activity". Proceedings of the National Academy of Sciences. 109 (11): 4058–4063. Bibcode:2012PNAS..109.4058N. doi:10.1073/pnas.1118215109. PMC 3306666. PMID 22392982. S2CID 10108911.
  35. ↑ Xia, Yifeng; Liu, Yi-Liang; Xie, Yonghua; Zhu, Wei; Guerra, Francisco; Shen, Shen; Yeddula, Narayana; Fischer, Wolfgang; Low, William; Zhou, Xiaoying; Zhang, Yonghui; Oldfield, Eric; Verma, Inder M. (2014). "A combination therapy for KRAS-driven lung adenocarcinomas using lipophilic bisphosphonates and rapamycin". Science Translational Medicine. 6 (263): 263ra161. doi:10.1126/scitranslmed.3010382. PMC 4326221. PMID 25411474.
  36. ↑ Xia, Yun; Xie, Yonghua; Yu, Zhengsen; Xiao, Hongying; Jiang, Guimei; Zhou, Xiaoying; Yang, Yunyun; Li, Xin; Zhao, Meng; Li, Liping; Zheng, Mingke; Han, Shuai; Zong, Zhaoyun; Meng, Xianbin; Deng, Haiteng; Ye, Huahu; Fa, Yunzhi; Wu, Haitao; Oldfield, Eric; Hu, Xiaoyu; Liu, Wanli; Shi, Yan; Zhang, Yonghui (2018). "The Mevalonate Pathway Is a Druggable Target for Vaccine Adjuvant Discovery". Cell. 175 (4): 1059–1073.e21. doi:10.1016/j.cell.2018.08.070. PMID 30270039.
  37. ↑ Yuan, Linjie; Ma, Xianqiang; Yang, Yunyun; Li, Xin; Ma, Weiwei; Yang, Haoyu; Huang, Jian-Wen; Xue, Jing; Yi, Simin; Zhang, Mengting; Cai, Ningning; Ding, Qingyang; Li, Liping; Duan, Jianxin; Malwal, Satish; Chen, Chun-Chi; Oldfield, Eric; Guo, Rey-Ting; Zhang, Yonghui (2022). "Phosphoantigens are Molecular Glues that Promote Butyrophilin 3A1/2A1 Association Leading to Vγ9Vδ2 T Cell Activation". doi:10.1101/2022.01.02.474068. S2CID 245705122. {{cite journal}}: Cite journal requires |journal= (help)
  38. ↑ Zhou, Xiaoying; Gu, Yanzheng; Xiao, Hongying; Kang, Ning; Xie, Yonghua; Zhang, Guangbo; Shi, Yan; Hu, Xiaoyu; Oldfield, Eric; Zhang, Xueguang; Zhang, Yonghui (2017). "Combining Vγ9Vδ2 T Cells with a Lipophilic Bisphosphonate Efficiently Kills Activated Hepatic Stellate Cells". Frontiers in Immunology. 8: 1381. doi:10.3389/fimmu.2017.01381. PMC 5661056. PMID 29118758.
  39. ↑ Malwal, Satish R.; o'Dowd, Bing; Feng, Xinxin; Turhanen, Petri; Shin, Christopher; Yao, Jiaqi; Kim, Boo Kyung; Baig, Noman; Zhou, Tianhui; Bansal, Sandhya; Khade, Rahul L.; Zhang, Yong; Oldfield, Eric (2018). "Bisphosphonate-Generated ATP-Analogs Inhibit Cell Signaling Pathways". Journal of the American Chemical Society. 140 (24): 7568–7578. doi:10.1021/jacs.8b02363. PMC 6022752. PMID 29787268.
  40. ↑ Oldfield, Eric; Lin, Fu-Yang (2012). "Terpene Biosynthesis: Modularity Rules". Angewandte Chemie International Edition. 51 (5): 1124–1137. doi:10.1002/anie.201103110. PMC 3769779. PMID 22105807.
  41. ↑ Cao, Rong; Zhang, Yonghui; Mann, Francis M.; Huang, Cancan; Mukkamala, Dushyant; Hudock, Michael P.; Mead, Matthew E.; Prisic, Sladjana; Wang, Ke; Lin, Fu-Yang; Chang, Ting-Kai; Peters, Reuben J.; Oldfield, Eric (2010). "Diterpene cyclases and the nature of the isoprene fold". Proteins: Structure, Function, and Bioinformatics. 78 (11): 2417–2432. doi:10.1002/prot.22751. PMC 3805035. PMID 20602361.
  42. ↑ Wang, Weixue; Oldfield, Eric (2014). "Bioorganometallic Chemistry with IspG and IspH: Structure, Function, and Inhibition of the [Fe4S4] Proteins Involved in Isoprenoid Biosynthesis". Angewandte Chemie International Edition. 53 (17): 4294–4310. doi:10.1002/anie.201306712. PMC 3997630. PMID 24481599.
  43. ↑ Chen, Chun-Chi; Malwal, Satish R.; Han, Xu; Liu, Weidong; Ma, Lixin; Zhai, Chao; Dai, Longhai; Huang, Jian-Wen; Shillo, Alli; Desai, Janish; Ma, Xianqiang; Zhang, Yonghui; Guo, Rey-Ting; Oldfield, Eric (2021). "Terpene Cyclases and Prenyltransferases: Structures and Mechanisms of Action". ACS Catalysis. 11: 290–303. doi:10.1021/acscatal.0c04710. S2CID 230567887.
  44. ↑ "RSC Awards Archive – Meldola Medal and Prize". www.rsc.org.
  45. ↑ "The Colworth Medal". www.biochemistry.org.
  46. ↑ "Past Recipients". American Chemical Society.
  47. ↑ "Soft Matter and Biophysical Chemistry Award". Royal Society of Chemistry.
  48. ↑ "Society Awards – The Biophysical Society". www.biophysics.org.
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