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Randy Read

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Randy Read
Randy Read in 2014, portrait via the Royal Society
Born
Randy John Read

(1957-06-09) June 9, 1957 (age 67)[3]
Alma materUniversity of Alberta (BSc, PhD)
Known for
Awards
Scientific career
Fields
InstitutionsUniversity of Cambridge
ThesisX-ray crystallographic studies on serine proteinases and their protein inhibitors (1986)
Websitewww-structmed.cimr.cam.ac.uk/Personal/randy/

Randy John Read (born 9 June 1957)[3] FRS[1] is a Wellcome Trust Principal Research Fellow and Professor of Protein Crystallography, in the Cambridge Institute for Medical Research (CIMR) at the University of Cambridge.[2][8][9][10]

Education

Read was educated at the University of Alberta, Edmonton where he was awarded a Bachelor of Science degree in 1979 and a PhD in 1986 for X-ray crystallographic studies on Serine proteases and their protein inhibitors.[3][11]

Career

Following his PhD, Read was appointed Assistant Professor from 1988 to 1993 and Associate Professor from 1993 to 1998 at the University of Alberta.[3]

Research

Read's research interests are in protein crystallography and maximum likelihood.[2] His research has been published in leading peer reviewed scientific journals including Nature,[12][13][14] Science,[15] the Journal of Applied Crystallography[4] Acta Crystallographica,[7][16][17] Structure,[18][19] PNAS,[20] the Journal of Molecular Biology[21][22] and the Journal of Clinical Endocrinology and Metabolism[23]

Awards and honours

Read was elected Fellow of the Royal Society (FRS) in 2014. His nomination reads:

Professor Read is known internationally for his outstanding and fundamental contributions to the development of macromolecular crystallographic software. His application of maximum likelihood based algorithms to the solution of macromolecular crystal structures by molecular replacement (a technique that uses a known structure of a homologue to solve an unknown structure) has resulted in software (Phaser) that is foremost in the field. He also devised and demonstrated an improved likelihood target function for model refinement that has been adopted by all major refinement programs. In addition, Professor Read has led structural work that has made significant contributions to understanding the mechanisms of proteins relevant to disease (bacterial toxins and serpins).[1]

References

  1. ^ a b c "Professor Randy Read FRS". London: The Royal Society. Archived from the original on 2014-08-05.
  2. ^ a b c Randy Read publications indexed by Google Scholar
  3. ^ a b c d READ. "READ, Prof. Randy John". Who's Who. Vol. 2014 (online Oxford University Press ed.). A & C Black. {{cite encyclopedia}}: Unknown parameter |othernames= ignored (help) (Subscription or UK public library membership required.) (subscription required)
  4. ^ a b McCoy, A. J.; Grosse-Kunstleve, R. W.; Adams, P. D.; Winn, M. D.; Storoni, L. C.; Read, R. J. (2007). "Phaser crystallographic software". Journal of Applied Crystallography. 40 (4): 658. doi:10.1107/S0021889807021206.
  5. ^ Phaser Crystallographic Software, University of Cambridge
  6. ^ Adams, P. D.; Grosse-Kunstleve, R. W.; Hung, L. W.; Ioerger, T. R.; McCoy, A. J.; Moriarty, N. W.; Read, R. J.; Sacchettini, J. C.; Sauter, N. K.; Terwilliger, T. C. (2002). "PHENIX: Building new software for automated crystallographic structure determination". Acta Crystallographica Section D Biological Crystallography. 58 (11): 1948. doi:10.1107/S0907444902016657.
  7. ^ a b Adams, P. D.; Afonine, P. V.; Bunkóczi, G. B.; Chen, V. B.; Davis, I. W.; Echols, N.; Headd, J. J.; Hung, L. W.; Kapral, G. J.; Grosse-Kunstleve, R. W.; McCoy, A. J.; Moriarty, N. W.; Oeffner, R.; Read, R. J.; Richardson, D. C.; Richardson, J. S.; Terwilliger, T. C.; Zwart, P. H. (2010). "PHENIX: A comprehensive Python-based system for macromolecular structure solution". Acta Crystallographica Section D Biological Crystallography. 66 (2): 213–21. doi:10.1107/S0907444909052925. PMC 2815670. PMID 20124702.
  8. ^ Randy Read publications indexed by Microsoft Academic
  9. ^ Randy Read's publications indexed by the Scopus bibliographic database. (subscription required)
  10. ^ "Randy Read's Homepage". University of Cambridge. Archived from the original on 2013-05-15.
  11. ^ Read, Randy John (1986). X-ray crystallographic studies on serine proteinases and their protein inhibitors (PhD thesis). University of Alberta.
  12. ^ Zhou, A.; Carrell, R. W.; Murphy, M. P.; Wei, Z.; Yan, Y.; Stanley, P. L. D.; Stein, P. E.; Pipkin, F. B.; Read, R. J. (2010). "A redox switch in angiotensinogen modulates angiotensin release". Nature. 468 (7320): 108–11. doi:10.1038/nature09505. PMC 3024006. PMID 20927107.
  13. ^ Dimaio, F.; Terwilliger, T. C.; Read, R. J.; Wlodawer, A.; Oberdorfer, G.; Wagner, U.; Valkov, E.; Alon, A.; Fass, D.; Axelrod, H. L.; Das, D.; Vorobiev, S. M.; Iwaï, H.; Pokkuluri, P. R.; Baker, D. (2011). "Improved molecular replacement by density- and energy-guided protein structure optimization". Nature. 473 (7348): 540. doi:10.1038/nature09964. PMID 21532589.
  14. ^ Qian, B.; Raman, S.; Das, R.; Bradley, P.; McCoy, A. J.; Read, R. J.; Baker, D. (2007). "High-resolution structure prediction and the crystallographic phase problem". Nature. 450 (7167): 259–64. doi:10.1038/nature06249. PMC 2504711. PMID 17934447.
  15. ^ Jackson, R. N.; Golden, S. M.; Van Erp, P. B.; Carter, J; Westra, E. R.; Brouns, S. J.; Van Der Oost, J; Terwilliger, T. C.; Read, R. J.; Wiedenheft, B (2014). "Structural biology. Crystal structure of the CRISPR RNA-guided surveillance complex from Escherichia coli". Science. 345 (6203): 1473–9. doi:10.1126/science.1256328. PMC 4188430. PMID 25103409.
  16. ^ Brünger, A. T.; Adams, P. D.; Clore, G. M.; Delano, W. L.; Gros, P.; Grosse-Kunstleve, R. W.; Jiang, J. S.; Kuszewski, J.; Nilges, M.; Pannu, N. S.; Read, R. J.; Rice, L. M.; Simonson, T.; Warren, G. L. (1998). "Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination". Acta Crystallographica Section D Biological Crystallography. 54 (5): 905. doi:10.1107/S0907444998003254.
  17. ^ Read, R. J.; Kleywegt, G. J. (2009). "Case-controlled structure validation". Acta Crystallographica Section D Biological Crystallography. 65 (Pt 2): 140–7. doi:10.1107/S0907444908041085. PMC 2631636. PMID 19171969.
  18. ^ Read, R. J.; Adams, P. D.; Arendall Wb, 3rd; Brunger, A. T.; Emsley, P; Joosten, R. P.; Kleywegt, G. J.; Krissinel, E. B.; Lütteke, T; Otwinowski, Z; Perrakis, A; Richardson, J. S.; Sheffler, W. H.; Smith, J. L.; Tickle, I. J.; Vriend, G; Zwart, P. H. (2011). "A new generation of crystallographic validation tools for the protein data bank". Structure. 19 (10): 1395–412. doi:10.1016/j.str.2011.08.006. PMC 3195755. PMID 22000512.{{cite journal}}: CS1 maint: numeric names: authors list (link)
  19. ^ Kleywegt, G. J.; Read, R. J. (1997). "Not your average density". Structure. 5 (12): 1557–69. doi:10.1016/s0969-2126(97)00305-5. PMID 9438862.
  20. ^ Deane, J. E.; Graham, S. C.; Kim, N. N.; Stein, P. E.; McNair, R; Cachón-González, M. B.; Cox, T. M.; Read, R. J. (2011). "Insights into Krabbe disease from structures of galactocerebrosidase". Proceedings of the National Academy of Sciences. 108 (37): 15169–73. doi:10.1073/pnas.1105639108. PMC 3174575. PMID 21876145.
  21. ^ Zhou, A; Wei, Z; Stanley, P. L.; Read, R. J.; Stein, P. E.; Carrell, R. W. (2008). "The S-to-R transition of corticosteroid-binding globulin and the mechanism of hormone release". Journal of Molecular Biology. 380 (1): 244–51. doi:10.1016/j.jmb.2008.05.012. PMID 18513745.
  22. ^ Stoop, A. A.; Eldering, E; Dafforn, T. R.; Read, R. J.; Pannekoek, H (2001). "Different structural requirements for plasminogen activator inhibitor 1 (PAI-1) during latency transition and proteinase inhibition as evidenced by phage-displayed hypermutated PAI-1 libraries". Journal of Molecular Biology. 305 (4): 773–83. doi:10.1006/jmbi.2000.4356. PMID 11162091.
  23. ^ Chan, W. L.; Carrell, R. W.; Zhou, A; Read, R. J. (2013). "How changes in affinity of corticosteroid-binding globulin modulate free cortisol concentration". The Journal of Clinical Endocrinology & Metabolism. 98 (8): 3315–22. doi:10.1210/jc.2012-4280. PMC 3813945. PMID 23783094.

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