List of experimental and computational labs focusing on IDPs

List of experimental and computational labs focusing on IDPs. In the last ten years, a great number of laboratories have investigated protein disorders using both experimental (e.g. SAXS-NMR, single-molecule fluorescence) and computational (analysis of protein structure) techniques.

See also

References

  1. "About Us - Keith Dunker Lab - Center for Computational Biology and Bioinformatics". Compbio.iupui.edu. Retrieved 2014-03-11.
  2. Dunker, A. K.; Lawson, J. D.; Brown, C. J.; Williams, R. M.; Romero, P; Oh, J. S.; Oldfield, C. J.; Campen, A. M.; Ratliff, C. M.; Hipps, K. W.; Ausio, J; Nissen, M. S.; Reeves, R; Kang, C; Kissinger, C. R.; Bailey, R. W.; Griswold, M. D.; Chiu, W; Garner, E. C.; Obradovic, Z (2001). "Intrinsically disordered protein". Journal of molecular graphics & modelling. 19 (1): 26–59. doi:10.1016/s1093-3263(00)00138-8. PMID 11381529.
  3. "Peter Tompa Lab". Vib.be. 2011-05-11. Retrieved 2014-03-11.
  4. Tompa, P (2002). "Intrinsically unstructured proteins". Trends in Biochemical Sciences. 27 (10): 527–33. doi:10.1016/s0968-0004(02)02169-2. PMID 12368089.
  5. https://hsccf.hsc.usf.edu/facultyDirectory/researchDirectory/search_profile.cfm?person_id=2838234
  6. Uversky, V. N.; Gillespie, J. R.; Fink, A. L. (2000). "Why are "natively unfolded" proteins unstructured under physiologic conditions?". Proteins: Structure, Function, and Genetics. 41 (3): 415–27. doi:10.1002/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7. PMID 11025552.
  7. "Research | M. Madan Babu's Lab". Mbgroup.mrc-lmb.cam.ac.uk. Retrieved 2014-03-11.
  8. Gsponer, J; Futschik, M. E.; Teichmann, S. A.; Babu, M. M. (2008). "Tight regulation of unstructured proteins: From transcript synthesis to protein degradation". Science. 322 (5906): 1365–8. doi:10.1126/science.1163581. PMC 2803065Freely accessible. PMID 19039133.
  9. van der Lee, Robin; Lang, Benjamin; Kruse, Kai; Gsponer, Jörg; Sánchez de Groot, Natalia; Huynen, Martijn A.; Matouschek, Andreas; Fuxreiter, Monika; Babu, M. Madan. "Intrinsically Disordered Segments Affect Protein Half-Life in the Cell and during Evolution". Cell Reports. 8 (6): 1832–1844. doi:10.1016/j.celrep.2014.07.055. ISSN 2211-1247. PMC 4358326Freely accessible. PMID 25220455.
  10. "The Bardwell Lab the University of Michigan". Labs.mcdb.lsa.umich.edu. Retrieved 2014-03-11.
  11. Bardwell, J. C.; Jakob, U (2012). "Conditional disorder in chaperone action". Trends in Biochemical Sciences. 37 (12): 517–25. doi:10.1016/j.tibs.2012.08.006. PMC 3508372Freely accessible. PMID 23018052.
  12. "Ursula Jakob, Ph.D. | University of Michigan Department of Biological Chemistry". Biochem.med.umich.edu. Retrieved 2014-03-11.
  13. Bardwell, J. C.; Jakob, U (2012). "Conditional disorder in chaperone action". Trends in Biochemical Sciences. 37 (12): 517–25. doi:10.1016/j.tibs.2012.08.006. PMC 3508372Freely accessible. PMID 23018052.
  14. "Welcome to the Selenko Lab". In-cell NMR. Retrieved 2014-03-11.
  15. Binolfi, A.; Theillet, F. X.; Selenko, P. (2012). "Bacterial in-cell NMR of human α-synuclein: A disordered monomer by nature?". Biochemical Society Transactions. 40 (5): 950–4. doi:10.1042/BST20120096. PMID 22988846.
  16. "Woodside Lab". Ualberta.ca. 2012-08-22. Retrieved 2014-03-11.
  17. Yu, H; Liu, X; Neupane, K; Gupta, A. N.; Brigley, A. M.; Solanki, A; Sosova, I; Woodside, M. T. (2012). "Direct observation of multiple misfolding pathways in a single prion protein molecule". Proceedings of the National Academy of Sciences. 109 (14): 5283–8. doi:10.1073/pnas.1107736109. PMC 3325692Freely accessible. PMID 22421432.
  18. UK (2013-11-21). "Alan Fersht | MRC Laboratory of Molecular Biology". .mrc-lmb.cam.ac.uk. Retrieved 2014-03-11.
  19. Binolfi, A.; Theillet, F. X.; Selenko, P. (2012). "Bacterial in-cell NMR of human α-synuclein: A disordered monomer by nature?". Biochemical Society Transactions. 40 (5): 950–4. doi:10.1042/BST20120096. PMID 22988846.
  20. "dr. S.G.D. (Stefan) Rüdiger - Betawetenschappen - Universiteit Utrecht". Uu.nl. Retrieved 2014-03-11.
  21. Karagöz, G. E.; Duarte, A. M.; Akoury, E; Ippel, H; Biernat, J; Morán Luengo, T; Radli, M; Didenko, T; Nordhues, B. A.; Veprintsev, D. B.; Dickey, C. A.; Mandelkow, E; Zweckstetter, M; Boelens, R; Madl, T; Rüdiger, S. G. (2014). "Hsp90-tau complex reveals molecular basis for specificity in chaperone action". Cell. 156 (5): 963–74. doi:10.1016/j.cell.2014.01.037. PMID 24581495.
  22. "Emmy-Noether Nachwuchsgruppe: Startseite". Madllab.ch.tum.de. Retrieved 2014-03-11.
  23. MacKereth, C. D.; Madl, T; Bonnal, S; Simon, B; Zanier, K; Gasch, A; Rybin, V; Valcárcel, J; Sattler, M (2011). "Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF". Nature. 475 (7356): 408–11. doi:10.1038/nature10171. PMID 21753750.
  24. "Yongli Zhang, PhD > Biological & Biomedical Sciences | Yale University". Bbs.yale.edu. 2012-12-12. Retrieved 2014-03-11.
  25. Gao, Y; Zorman, S; Gundersen, G; Xi, Z; Ma, L; Sirinakis, G; Rothman, J. E.; Zhang, Y (2012). "Single reconstituted neuronal SNARE complexes zipper in three distinct stages". Science. 337 (6100): 1340–3. doi:10.1126/science.1224492. PMC 3677750Freely accessible. PMID 22903523.
  26. "Peter Wright". Scripps.edu. Retrieved 2014-03-11.
  27. Demarest, S. J.; Martinez-Yamout, M.; Chung, J.; Chen, H.; Xu, W.; Dyson, H. J.; Evans, R. M.; Wright, P. E. (2002). "Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators". Nature. 415 (6871): 549–553. doi:10.1038/415549a. PMID 11823864.
  28. "Jane Dyson". Scripps.edu. Retrieved 2014-03-11.
  29. Dyson, H. J. (2011). "Expanding the proteome: Disordered and alternatively folded proteins". Quarterly Reviews of Biophysics. 44 (4): 467–518. doi:10.1017/S0033583511000060. PMC 3189428Freely accessible. PMID 21729349.
  30. Alex Holehouse (2014-02-11). "Pappu Lab". Pappulab.wustl.edu. Retrieved 2014-03-11.
  31. Das, R. K.; Pappu, R. V. (2013). "Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues". Proceedings of the National Academy of Sciences. 110 (33): 13392–7. doi:10.1073/pnas.1304749110. PMC 3746876Freely accessible. PMID 23901099.
  32. Das, R. K.; Pappu, R. V. (2013). "Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues". Proceedings of the National Academy of Sciences. 110 (33): 13392–7. doi:10.1073/pnas.1304749110. PMC 3746876Freely accessible. PMID 23901099.
  33. "Inke Nathke |". Lifesci.dundee.ac.uk. Retrieved 2014-03-11.
  34. Nelson, S; Näthke, I. S. (2013). "Interactions and functions of the adenomatous polyposis coli (APC) protein at a glance". Journal of Cell Science. 126 (Pt 4): 873–7. doi:10.1242/jcs.100479. PMID 23589686.
  35. "Maurice - Cell Biology UMC Utrecht". Cellbiology-utrecht.nl. Retrieved 2014-03-11.
  36. Minde, D. P.; Anvarian, Z.; Rüdiger, S. G.; Maurice, M. M. (2011). "Messing up disorder: How do missense mutations in the tumor suppressor protein APC lead to cancer?". Molecular Cancer. 10: 101. doi:10.1186/1476-4598-10-101. PMC 3170638Freely accessible. PMID 21859464.
  37. Li, V. S.; Ng, S. S.; Boersema, P. J.; Low, T. Y.; Karthaus, W. R.; Gerlach, J. P.; Mohammed, S; Heck, A. J.; Maurice, M. M.; Mahmoudi, T; Clevers, H (2012). "Wnt signaling through inhibition of β-catenin degradation in an intact Axin1 complex". Cell. 149 (6): 1245–56. doi:10.1016/j.cell.2012.05.002. PMID 22682247.
  38. Koo, B. K.; Spit, M; Jordens, I; Low, T. Y.; Stange, D. E.; Van De Wetering, M; Van Es, J. H.; Mohammed, S; Heck, A. J.; Maurice, M. M.; Clevers, H (2012). "Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis of Wnt receptors". Nature. 488 (7413): 665–9. doi:10.1038/nature11308. PMID 22895187.
  39. "Kriwacki laboratory". St. Jude Research. Retrieved 2014-03-11.
  40. Wang, Y; Fisher, J. C.; Mathew, R; Ou, L; Otieno, S; Sublet, J; Xiao, L; Chen, J; Roussel, M. F.; Kriwacki, R. W. (2011). "Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21". Nature Chemical Biology. 7 (4): 214–21. doi:10.1038/nchembio.536. PMC 3124363Freely accessible. PMID 21358637.
  41. "Ben Schuler research group". Bioc.uzh.ch. 2013-10-31. Retrieved 2014-03-11.
  42. Brucale, M; Schuler, B; Samorì, B (2014). "Single-Molecule Studies of Intrinsically Disordered Proteins". Chemical Reviews. 114 (6): 140117081415006. doi:10.1021/cr400297g. PMID 24432838.
  43. "The Deniz Lab". Scripps.edu. 2014-01-23. Retrieved 2014-03-11.
  44. Ferreon, A. C.; Ferreon, J. C.; Wright, P. E.; Deniz, A. A. (2013). "Modulation of allostery by protein intrinsic disorder". Nature. 498 (7454): 390–4. doi:10.1038/nature12294. PMC 3718496Freely accessible. PMID 23783631.
  45. "Klenerman | Department of Chemistry". Ch.cam.ac.uk. Retrieved 2014-03-11.
  46. Cremades, N; Cohen, S. I.; Deas, E; Abramov, A. Y.; Chen, A. Y.; Orte, A; Sandal, M; Clarke, R. W.; Dunne, P; Aprile, F. A.; Bertoncini, C. W.; Wood, N. W.; Knowles, T. P.; Dobson, C. M.; Klenerman, D (2012). "Direct observation of the interconversion of normal and toxic forms of α-synuclein". Cell. 149 (5): 1048–59. doi:10.1016/j.cell.2012.03.037. PMC 3383996Freely accessible. PMID 22632969.
  47. Hilser, V. J.; Thompson, E. B. (2007). "Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins". Proceedings of the National Academy of Sciences. 104 (20): 8311–5. doi:10.1073/pnas.0700329104. PMC 1895946Freely accessible. PMID 17494761.
  48. Tsvetkov, P.; Myers, N.; Moscovitz, O.; Sharon, M.; Prilusky, J.; Shaul, Y. (2012). "Thermo-resistant intrinsically disordered proteins are efficient 20S proteasome substrates". Molecular BioSystems. Royal Society of Chemistry. 8 (1): 368–373. doi:10.1039/c1mb05283g. PMID 22027891.
  49. Eliezer, D; Kutluay, E; Bussell Jr, R; Browne, G (2001). "Conformational properties of alpha-synuclein in its free and lipid-associated states". Journal of Molecular Biology. 307 (4): 1061–73. doi:10.1006/jmbi.2001.4538. PMID 11286556.
  50. Eliezer, D; Barré, P; Kobaslija, M; Chan, D; Li, X; Heend, L (2005). "Residual structure in the repeat domain of tau: Echoes of microtubule binding and paired helical filament formation". Biochemistry. 44 (3): 1026–36. doi:10.1021/bi048953n. PMID 15654759.
This article is issued from Wikipedia - version of the 1/31/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.