Raymond C. Stevens

Last updated
Raymond C. Stevens
Born1963
NationalityAmerican
Alma mater University of Southern Maine, University of Southern California
Awards Beckman Young Investigators Award, [1]
Scientific career
Fields Structural biology
Institutions ShanghaiTech University, University of Southern California

Raymond C. Stevens (born 1963) is an American chemist and structural biologist, Founder, CEO and Board Member of Structure Therapeutics; [2] Founding Director of the iHuman Institute at ShanghaiTech University; Professor Emeritus of Chemistry, and Founding Director of the Bridge Institute at the University of Southern California; Board Member, Danaher Corporation. [3]

Contents

Biography

Stevens was born into a military family. In 1969 his father died in the Air Force, and his mother took several part-time jobs to support the family. He was raised in Auburn, Maine.

In 1980, Stevens joined the Army under their split option training program and conducted basic training at Fort Dix, New Jersey and advanced individual training at Fort Sam Houston, Texas. While engaged in his military service, Stevens entered the University of Southern Maine in the Computer Science program in 1981. However, an enthusiastic professor (John Ricci) converted him to the study of Chemistry. He spent two summers working as an intern at the Brookhaven National Laboratory in Long Island with Professor Ricci, and Drs. Thomas Koetzle and Dick McMullan, where he first learned how to determine the molecular structure of compounds by X-ray and neutron diffraction. While there he also met a University of Southern California research team led by Dr. Robert Bau; after he obtained a Bachelor of Science degree in chemistry at USM, he entered the University of Southern California in pursuit of a Doctor of Philosophy degree in Chemistry working with Professor Robert Bau and Nobel Laureate Professor, George Olah. He completed his Ph.D. in 26 months, graduating in 1988. [4]

Although science is a major part of his life, Stevens climbs mountains with his wife and children and runs ultramarathons including the Vermont 100 Mile Endurance Run [5] and American River 50 Mile Endurance Run, [6] and in 2011 he successfully completed the 156 mile Marathon des Sables [7] across the Moroccan Sahara Desert. Currently working on climbing the 7 highest mountains on the 7 continents, he has climbed Mt. Kilimanjaro, Mt. Elbrus, Aconcagua, Vinson Massif and Mt. Kosciuszko. Next mountains are Mt. Everest and Denali.

Scientific career

After obtaining his Ph.D., Stevens accepted a postdoctoral position in 1988 in the lab of Nobel Laureate William N. Lipscomb, Jr. in the chemistry department at Harvard University where he focused on the large allosteric enzyme aspartate carbamoyltransferase. [8] [9] [10] [11] [12] [13] [14] [15] [16] In 1991, he accepted a tenure-track position at the University of California, Berkeley in the chemistry department with a joint appointment in neurobiology. His initial research as an assistant professor focused on structural neurobiology and immunology, combining chemistry, structural biology and protein chemistry with a specific biological interest in understanding how the G protein-coupled receptor (GPCR) superfamily works. A seminal collaboration for Stevens was with Professor Peter G. Schultz where they jointly published a series of Science and Nature papers describing the immunological evolution of antibodies through careful structural studies. [17] [18] [19] [20] In 1999, Stevens left Berkeley to take a tenured position at The Scripps Research Institute. While at The Scripps Research Institute, Stevens has helped to found and establish the Joint Center for Structural Genomics, [21] Joint Center for Innovative Membrane Protein Technologies, [22] and the GPCR Network, [23] all funded by the National Institutes of Health with direct guidance from NIGMS. In 2012, Stevens co-founded the iHuman Institute at ShanghaiTech University. [24] In 2014, Stevens moved his lab from The Scripps Research Institute to the University of Southern California, where he is currently the Provost Professor of Biological Sciences and Chemistry and he founded the Bridge Institute to converge the arts and sciences. [25]

Stevens is known for obtaining the structures of many biologically significant proteins and his technological innovations. He is considered a pioneer of high-throughput x-ray crystallography and structural genomics. [26] His laboratory has led to the contribution of over 500 protein structure entries in the Protein Data Bank www.pdb.org. Stevens has withdrawn two different structures of ligand-bound clostridial neurotoxins. [27] [28]

In October 2007, Stevens and colleagues published the first high-resolution structure of a human GPCR. [29] [30] The β2-adrenergic receptor work was quickly followed up 9 months later by the determination of the structure of the human A2A adenosine receptor structure, [31] also known as the caffeine receptor. In 2010, the structures of the human chemokine CXCR4 receptor (HIV co-receptor), [32] the human dopamine D3 receptor [33] and the human Histamine H1 receptor [34] were published. In addition to these inactive-state structures, Stevens and colleagues solved the structure of an agonist-bound A2A adenosine receptor. [35]

Subsequent novel human receptor structures include:

2012: The first structure of a lipid-activated GPCR, the sphingolipid, [36] the human kappa-opioid receptor [37] and the human nociceptin/orphanin FQ peptide receptor. [38]

2013: Serotonin receptors 5-HT1B and 5-HT2B, [39] [40] the second HIV co-receptor, C-C chemokine receptor type 5 (CCR5) [41] and the first structure of a non-class A GPCR, the transmembrane domain of the human Metabotropic glutamate receptor 1 (mGluR1) [42] and the first structures of non-rhodopsin family GPCRs, the transmembrane domain of the human Smoothened receptor from the Frizzled/Taste2 family [40] and the transmembrane domain of the human glucagon receptor (GCGR) from the adhesion (class B) family.

2014: The human P2Y receptor 12 (P2Y12) bound to antagonist or agonist; [43] [44] the human Delta opioid receptor at 1.8A [45] and the first structure of a class C GPCR, the transmembrane domain of the human Metabotropic glutamate receptor 1 (mGluR1). [42]

2015: The human Lysophosphatidic acid receptor 1 (LPAR1), [46] the human angiotensin II receptor type 1 (AT1R), [47] human P2Y receptor 1 (P2Y1); [48] and the human Rhodopsin-Arrestin complex. [49]

2016: The marijuana receptor—human Cannabinoid receptor type 1 (CB1) [50] and the human C-C chemokine receptor type 2 (CCR2) [51]

2017:The human apelin receptor [52] and the human angiotensin II receptor 2 (AT2R) [53] as well as the full length human glucagon receptor (GPCR) [54] and trans membrane domain of the human glucagon like peptide receptor 1 (GLP1R) [55]

2018: The human seratonin receptor 5HT2C [56] human neuropeptide Y Y1 receptor [57] platelet activating factor receptor [58] and the trans membrane domain of the human frizzled 4 receptor [59]

2019: The human prostaglandin E2 receptor3 (EP3), [60] the human cannabinoid receptor CB2, [61] the human neurokinin 1 receptor, [62] and the melatonin receptors MT1 [63] and MT2 [64]

2020:The human melanocortin 4 receptor (MC4), [65] [66] [67]

In combination with the structural studies, working with the computational biology community to conduct GPCR Dock 2008 [68] and GPCR Dock 2010 [69] has helped to evaluate where the field is at, and functional studies using HDX [70] and NMR are conducted by Stevens and collaborators to understand how the receptors work at the molecular level, and what fundamental and basic insights can be gained towards developing therapeutic drugs.

Structure based drug discovery

In 1992, Stevens worked with researchers at Gilead on the structural studies of neuraminidase inhibitors that eventually became Tamiflu, [71] [72] [73] and later partnered with Roche. After the initial experience with structure based drug discovery from 1992 to 1997 with Gilead and Tamiflu, Stevens focused on understanding the basic mechanism of how Botox (botulinum toxin) works, and on ways to use this scaffold for next generation protein therapeutics. In parallel to the work on botulinum toxin, he worked on the enzymes involved in the catecholamine biosynthetic pathway, specifically the three aromatic amino acid hydroxylases including phenylalanine hydroxylase. From 1999 to 2004, Stevens was involved in the startup of Syrrx that developed the marketed drug Nesina for type II diabetes. From 2000 to 2010, Stevens has worked with BioMarin Pharmaceutical to develop Kuvan (tetrahydrobiopterin) and assisted in the design and development of PEG-PAL (pegylated Phenylalanine ammonia-lyase) as treatments for mild and classical phenylketonuria (PKU). [74] [75] [76] In 2008, Stevens started Receptos that developed an S1P1 agonist for multiple sclerosis and inflammatory bowel disease, now on the market called Zeposia and sold by BMS. [77]

Biotechnology Startups

Stevens has started four biotechnology companies (Syrrx (1999), MemRx (2002), Receptos (2009), and RuiYi (2011)), all focused on structure based drug discovery and each company started with one of his former Ph.D. students.

Awards

Philanthropy

The John S. Ricci Lecture Hall

Stevens honored his University of Southern Maine professor and mentor, John Ricci, by facilitating the renovation of the lecture hall inside the University science building and renaming it The John S. Ricci Lecture Hall. [93]

The Professor Emeritus John Ricci Undergraduate Fellowships

Established by Stevens to honor USM Professor Emeritus John Ricci and his innovative educational program at Brookhaven National Laboratory, these summer fellowships offer a unique opportunity for USM undergraduates to pursue research at The University of Southern California in Los Angeles, California, one of the oldest private research universities. [94] In 2018, Stevens and his wife supported the building of the John S. Ricci Lecture Hall in honor of his undergraduate teacher and mentor. [95] [96]

The Robert Bau Endowed Graduate Fellowship

Established by Stevens and Charles McKenna in 2010 to honor USC distinguished professor Robert Bau after his death in December 2008, the fellowship proposes to help celebrate Professor Bau's life and honor his extraordinary mentorship by linking him to new generations of young chemists at USC. [97]

Related Research Articles

Histamine H<sub>4</sub> receptor Mammalian protein found in Homo sapiens

The histamine H4 receptor, like the other three histamine receptors, is a member of the G protein-coupled receptor superfamily that in humans is encoded by the HRH4 gene.

GABAB receptors (GABABR) are G-protein coupled receptors for gamma-aminobutyric acid (GABA), therefore making them metabotropic receptors, that are linked via G-proteins to potassium channels. The changing potassium concentrations hyperpolarize the cell at the end of an action potential. The reversal potential of the GABAB-mediated IPSP is –100 mV, which is much more hyperpolarized than the GABAA IPSP. GABAB receptors are found in the central nervous system and the autonomic division of the peripheral nervous system.

Neuropeptide Y receptors are a family of receptors belonging to class A G-protein coupled receptors and they are activated by the closely related peptide hormones neuropeptide Y, peptide YY and pancreatic polypeptide. These receptors are involved in the control of a diverse set of behavioral processes including appetite, circadian rhythm, and anxiety.

<span class="mw-page-title-main">Glucagon receptor</span> Protein-coding gene in the species Homo sapiens

The glucagon receptor is a 62 kDa protein that is activated by glucagon and is a member of the class B G-protein coupled family of receptors, coupled to G alpha i, Gs and to a lesser extent G alpha q. Stimulation of the receptor results in the activation of adenylate cyclase and phospholipase C and in increased levels of the secondary messengers intracellular cAMP and calcium. In humans, the glucagon receptor is encoded by the GCGR gene.

<span class="mw-page-title-main">P2Y receptor</span> Subclass of purinergic P2 receptors

P2Y receptors are a family of purinergic G protein-coupled receptors, stimulated by nucleotides such as adenosine triphosphate, adenosine diphosphate, uridine triphosphate, uridine diphosphate and UDP-glucose.To date, 8 P2Y receptors have been cloned in humans: P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13 and P2Y14.

<span class="mw-page-title-main">GDF2</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 2 (GDF2) also known as bone morphogenetic protein (BMP)-9 is a protein that in humans is encoded by the GDF2 gene. GDF2 belongs to the transforming growth factor beta superfamily.

<span class="mw-page-title-main">S1PR1</span> Protein and coding gene in humans

Sphingosine-1-phosphate receptor 1, also known as endothelial differentiation gene 1 (EDG1) is a protein that in humans is encoded by the S1PR1 gene. S1PR1 is a G-protein-coupled receptor which binds the bioactive signaling molecule sphingosine 1-phosphate (S1P). S1PR1 belongs to a sphingosine-1-phosphate receptor subfamily comprising five members (S1PR1-5). S1PR1 was originally identified as an abundant transcript in endothelial cells and it has an important role in regulating endothelial cell cytoskeletal structure, migration, capillary-like network formation and vascular maturation. In addition, S1PR1 signaling is important in the regulation of lymphocyte maturation, migration and trafficking.

<span class="mw-page-title-main">Adiponectin receptor 1</span> Protein-coding gene in the species Homo sapiens

Adiponectin receptor 1 (AdipoR1) is a protein which in humans is encoded by the ADIPOR1 gene. It is a member of the progestin and adipoQ receptor (PAQR) family, and is also known as PAQR1.

<span class="mw-page-title-main">Neuropeptide Y receptor Y1</span> Protein-coding gene in the species Homo sapiens

Neuropeptide Y receptor type 1 is a protein that in humans is encoded by the NPY1R gene.

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<span class="mw-page-title-main">TAS2R10</span> Protein-coding gene in the species Homo sapiens

Taste receptor type 2 member 10 is a protein that in humans is encoded by the TAS2R10 gene. The protein is responsible for bitter taste recognition in mammals. It serves as a defense mechanism to prevent consumption of toxic substances which often have a characteristic bitter taste.

<span class="mw-page-title-main">TAS2R46</span> Protein-coding gene in the species Homo sapiens

Taste receptors for bitter substances (T2Rs/TAS2Rs) belong to the family of G-protein coupled receptors and are related to class A-like GPCRs. There are 25 known T2Rs in humans responsible for bitter taste perception.

<span class="mw-page-title-main">GFER</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">MED4</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">OR51E2</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Tropoflavin</span> Chemical compound

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<span class="mw-page-title-main">AlkB homolog 5, RNA demethylase</span> Protein-coding gene in the species Homo sapiens

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References

  1. 1 2 "Raymond C. Stevens". Arnold and Mabel Beckman Foundation. Retrieved 1 August 2018.
  2. 1 2 https://structuretx.com/
  3. ↑ "Danaher Announces Appointment of Raymond C. Stevens, Ph.D. To Danaher Board".
  4. ↑ Emerson, Eva (1 October 2007). "Fast-Tracking Lifesaving Discoveries". USC Dornsife. Retrieved 2 August 2018.
  5. ↑ Vermont100 race results 2006
  6. ↑ American River 50 Miler race results
  7. ↑ "26th SULTAN MARATHON DES SABLES". www.darbaroud.com. Archived from the original on 2011-09-03.
  8. ↑ Stevens, R. C., & Lipscomb, W. N., "Allosteric Enzymes" Eds., R. Diamond, T. F. Koetzle, K. Prout, & J. Richardson, Molecular Structures in Biology (Oxford, UK: Oxford University Press, 1993) pp. 223–259.
  9. ↑ Stebbins, J. W., Robertson, D. E., Roberts, M. F., Stevens, R. C., Lipscomb, W. N., & Kantrowitz, E. R., "Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic study," Prot. Sci. 1, 1435–1446 (1992).
  10. ↑ Stevens, R. C., & Lipscomb, W. N., "A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamylase," Proc. Natl. Acad. Sci. USA 89, 5281–5285 (1992).
  11. ↑ Stevens, R. C., Reinisch, K. M., & Lipscomb, W. N., "Molecular Structure of Bacillus subtilis Aspartate transcarbamoylase at 3.0 A Resolution," Proc. Natl. Acad. Sci. USA 88, 6087–6091 (1991).
  12. ↑ Stevens, R. C., Chook, Y. M., Cho, C. Y., Lipscomb, W. N., & Kantrowitz, E. R., "Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis," Protein Engineering 4, 391–408 (1991).
  13. ↑ Gouaux, J. E., Stevens, R. C., & Lipscomb, W. N., "Crystal Structures of Aspartate Carbamoyltransferase Li gated with Phosphonoacetamide, Malonate and CTP or ATP at 2.8-A Resolution and Neutral pH," Biochemistry 29, 7702–7715 (1990).
  14. ↑ Stevens, R. C., J.E. Gouaux, & Lipscomb, W. N., "Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase Crystal Structures of the Unligated and ATP- and CTP-Complexed Enzymes at 2.6-A Resolution," Biochemistry 29, 7691–7701 (1990).
  15. ↑ Stevens, R. C., & Lipscomb, W. N., "Allosteric control of quaternary states in E. coli aspartate transcarbamylase," Biochemistry and Biophysics Research Communications 171, 1312–1318 (1990).
  16. ↑ Gouaux, J. E., Stevens, R. C., Ke, H., & Lipscomb, W. N., "Crystal structure of the Glu-239 to Gln mutant of aspartate carbamoyltransferase at 3.1 A resolution: An intermediate quaternary structure," Proc. Natl. Acad. Sci. USA 86, 8212–8216 (1989).
  17. ↑ H. D. Ulrich, E. Mundorff, B. D. Santarsiero, E. M. Driggers, R. C. Stevens and P. G. Schultz (1997) The interplay between binding energy and catalysis in the evolution of a catalytic antibody Nature 389: 271–5
  18. ↑ G. J. Wedemayer, P. A. Patten, L. H. Wang, P. G. Schultz and R. C. Stevens (1997) Structural insights into the evolution of an antibody combining site Science 276: 1665–9
  19. ↑ F. E. Romesberg, B. Spiller, P. G. Schultz and R. C. Stevens (1998) Immunological origins of binding and catalysis in a Diels-Alderase antibody Science 279: 1929–33
  20. ↑ A. Simeonov, M. Matsushita, E. A. Juban, E. H. Thompson, T. Z. Hoffman, A. E. t. Beuscher, M. J. Taylor, P. Wirsching, W. Rettig, J. K. McCusker, R. C. Stevens, D. P. Millar, P. G. Schultz, R. A. Lerner and K. D. Janda (2000) Blue-fluorescent antibodies Science 290: 307–13
  21. ↑ www.jcsg.org
  22. ↑ jcimpt.scripps.edu
  23. ↑ cmpd.scripps.edu
  24. ↑ ihuman.shanghaitech.edu.cn
  25. ↑ "The San Diego Union-Tribune - San Diego, California & National News".
  26. ↑ R. C. Stevens and I. A. Wilson (2001) Tech.Sight. Industrializing structural biology. Science 293: 519-20
  27. ↑ M. A. Hanson, R. C. Stevens (2009) Retraction: Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution Nat Struct Mol Biol. 16(7):795.
  28. ↑ M. A. Hanson, T. K. Oost, C. Sukonpan, D. H. Rich, R. C. Stevens (2002) Structural Basis for BABIM Inhibition of Botulinum Neurotoxin Type B Protease [J. Am. Chem. Soc. 2000, 122, 11268−11269] J. Am. Chem. Soc. 124(34):10248–10248
  29. ↑ USC College : News : October 2007 : Raymond Stevens
  30. ↑ V. Cherezov, D. M. Rosenbaum, M. A. Hanson, S. G. Rasmussen, F. S. Thian, T. S. Kobilka, H. J. Choi, P. Kuhn, W. I. Weis, B. K. Kobilka and R. C. Stevens (2007) High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor Science 318: 1258–65.
  31. ↑ V. P. Jaakola, M. T. Griffith, M. A. Hanson, V. Cherezov, E. Y. Chien, J. R. Lane, A. P. Ijzerman and R. C. Stevens (2008) The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist, Science 322: 1211–7
  32. ↑ B. Wu, E.Y.T. Chien, C.D. Mol, G. Fenalti, W. Liu, V. Katritch, R. Abagyan, A. Brooun, P. Wells, F.C. Bi, D.J. Hamel, P. Kuhn, T.M. Handel, V. Cherezov, R.C. Stevens "Structures of the CXCR4 chemokine GPCR with small molecule and cyclic peptide antagonists" Science 330, 1066-1071 (2010).
  33. ↑ E.Y.T. Chien, W. Liu, Q. Zhao, V. Katritch, G.W. Han, M.A. Hanson, L. Shi, A.H. Newman, J.A. Javitch, V. Cherezov, R.C. Stevens "Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist" Science 330, 1091-1095 (2010).
  34. ↑ T. Shimamura, M. Shiroishi, S. Weyand, H. Tsujimoto, G. Winter, V. Katritch, R. Abagyan, V. Cherezov, W. Liu, G.W. Han, T. Kobayashi, R.C. Stevens, S. Iwata. "Structure of the human histamine H1 receptor in complex with doxepin" Nature 475, 65-70 (2011).
  35. ↑ F. Xu, H. Wu, V. Katritch, G.W. Han, K.A. Jacobson, Z.-G. Gao, V. Cherezov, R.C. Stevens "Structure of an agonist-bound human A2A adenosine receptor" Science 332, 322-327 (2011).
  36. ↑ M. A. Hanson, C. B. Roth, E. Jo, M. T. Griffith, F. L. Scott, G. Reinhart, H. Desale, B. Clemons, S. M. Cahalan, S. C. Schuerer, M. G. Sanna, G. W. Han, P. Kuhn, H. Rosen and R. C. Stevens (2012) Crystal structure of a lipid G protein-coupled receptor Science 335: 851-5
  37. ↑ H. Wu, D. Wacker, M. Mileni, V. Katritch, G. W. Han, E. Vardy, W. Liu, A. A. Thompson, X. P. Huang, F. I. Carroll, S. W. Mascarella, R. B. Westkaemper, P. D. Mosier, B. L. Roth, V. Cherezov and R. C. Stevens (2012) Structure of the human kappa-opioid receptor in complex with JDTic Nature 485: 327-332
  38. ↑ A. A. Thompson, W. Liu, E. Chun, V. Katritch, H. Wu, E. Vardy, X. P. Huang, C. Trapella, R. Guerrini, G. Calo, B. L. Roth, V. Cherezov and R. C. Stevens (2012) Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic Nature 485: 395-9
  39. ↑ C. Wang, Y. Jiang, J. Ma, H. Wu, D. Wacker, V. Katritch, G. W. Han, W. Liu, X. P. Huang, E. Vardy, J. D. McCorvy, X. Gao, X. E. Zhou, K. Melcher, C. Zhang, F. Bai, H. Yang, L. Yang, H. Jiang, B. L. Roth, V. Cherezov, R. C. Stevens and H. E. Xu (2013) Structural basis for molecular recognition at serotonin receptors Science 340: 610-4
  40. 1 2 C. Wang, H. Wu, V. Katritch, G. W. Han, X. P. Huang, W. Liu, F. Y. Siu, B. L. Roth, V. Cherezov and R. C. Stevens (2013) Structure of the human smoothened receptor bound to an antitumour agent Nature 497: 338-43
  41. ↑ Q. Tan, Y. Zhu, J. Li, Z. Chen, G. W. Han, I. Kufareva, T. Li, L. Ma, G. Fenalti, J. Li, W. Zhang, X. Xie, H. Yang, H. Jiang, V. Cherezov, H. Liu, R. C. Stevens, Q. Zhao and B. Wu (2013) Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex Science 341: 1387-90
  42. 1 2 H. Wu, C. Wang, K. J. Gregory, G. W. Han, H. P. Cho, Y. Xia, C. M. Niswender, V. Katritch, J. Meiler, V. Cherezov, P. J. Conn and R. C. Stevens (2014) Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator Science 344: 58-64
  43. ↑ J. Zhang, K. Zhang, Z. G. Gao, S. Paoletta, D. Zhang, G. W. Han, T. Li, L. Ma, W. Zhang, C. Müller, H. Yang, H. Jiang, V. Cherezov, V. Katritch, K. A. Jacobson, R. C. Stevens, B. Wu and Q. Zhao (2014) Agonist-bound structure of the human P2Y12 receptor Nature 509: 119-122
  44. ↑ K. Zhang, J. Zhang, Z. G. Gao, D. Zhang, L. Zhu, G. W. Han, S. M. Moss, S. Paoletta, E. Kiselev, W. Lu, G. Fenalti, W. Zhang, C. Müller, H. Yang, H. Jiang, V. Cherezov, V. Katritch, K. A. Jacobson, R. C. Stevens, B. Wu and Q. Zhao (2014) Structure of the human P2Y12 receptor in complex with an antithrombotic drug Nature 509: 115-118
  45. ↑ G. Fenalti, P. M. Giguere, V. Katritch, X. P. Huang, A. A. Thompson, V. Cherezov, B. L. Roth and R. C. Stevens (2014) Molecular control of delta-opioid receptor signalling Nature 506: 191-6
  46. ↑ J.E. Chrencik, C.B. Roth, M. Terakado, H. Kurata, R. Omi, Y. Kihara, D.T. Warshaviak, S. Nakade, G. Asmar-Rovira, M. Mileni, H. Mizuno, M.T. Griffith, C. Rodgers, G.W. Han, J. Velasquez, J. Chun, R.C. Stevens, M.A. Hanson (2015) Crystal structure of human lysophosphatidic acid receptor 1 Cell 161: 1633-1643
  47. ↑ H. Zhang, H. Unal, C. Gati, G.W. Han, W. Liu, N.A. Zatsepin, D. James, D. Wang, G. Nelson, U. Weierstall, M.R. Sawaya, Q. Xu, M. Messerschmidt, G.J. Williams, S. Boutet, O.M. Yefanov, T.A. White, C. Wang, A. Ishchenko, K.C. Tirupula, R. Desnoyer, J. Coe, C.E. Conrad, P. Fromme, R.C. Stevens, V. Katritch, S.S. Karnik, V. Cherezov (2015) Structure of the angiotensin receptor revealed by serial femtosecond crystallography Cell 161: 833-844
  48. ↑ D. Zhang, Z.G. Gao, K. Zhang, E. Kiselev, S. Crane, J. Wang, S. Paoletta, C. Yi, L. Ma, W. Zhang, G.W. Han, H. Liu, V. Cherezov, V. Katritch, H. Jiang, R.C. Stevens, K.A. Jacobson, Q. Zhao, B. Wu (2015) Two disparate ligand binding sites in the human P2Y1 receptor Nature 520: 317-321
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  83. ↑ "Structure Therapeutics Extends Financing, Advances Diabetes and Obesity Clinical Program and Changes Name from ShouTi" (Press release). August 2022.
  84. ↑ "Legacy Leaders: Raymond Stevens".
  85. ↑ "Exceptional Mentoring is Key to Building a Supportive Academic Environment". 17 April 2019.
  86. ↑ "Raymond Stevens to Receive 2019 BPS Anatrace Membrane Protein Award".
  87. ↑ "Home". Npkua.org. Retrieved 2022-06-21.
  88. ↑ "The Protein Society : Protein Society Awards".
  89. ↑ "ShanghaiTech University".
  90. ↑ "50 foreigners receive Magnolia Silver Award in Shanghai". Chinadaily.com.cn. Retrieved 2022-06-21.
  91. ↑ "Norwegian Academy of Science and Letters".§
  92. ↑ "Thomson Reuters Highly Cited Researchers".§
  93. ↑ "World-renowned scientist and USM alumnus recognizes professor & mentor | Office of Public Affairs | University of Southern Maine".
  94. ↑ TSRI Stevens Lab: John Ricci Undergraduate Fellowship
  95. ↑ "Bill Nemitz: Maine professor, struggling student had a chemistry". Press Herald. April 2018.
  96. ↑ "World-renowned scientist and USM alumnus recognizes professor & mentor | Office of Public Affairs | University of Southern Maine".
  97. ↑ USC Department of Chemistry: In Memoriaum-Robert Bau
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