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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Protein Conformation

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Disease relevance of Protein Conformation

  • Our studies indicate that HSP70 or related molecular chaperones may provide a means of treating these and other neurodegenerative diseases associated with abnormal protein conformation and toxicity [1].
  • These findings suggest the possibility that the conversion of the cellular isoform of PrP to the scrapie isoform of PrP involves the transition of one or more putative PrP alpha-helices into beta-sheets and that prion diseases are disorders of protein conformation [2].
  • However, introduction of individual substitution mutations in this region did not impair Vpr nuclear localization and virion incorporation, suggesting that this region is necessary for the stability and/or optimal protein conformation relevant to these Vpr functions [3].
  • The naturally occurring mutation L141R (also associated with coronary heart disease) that is located in this segment does not change the protein conformation but leads to a reduced stability and a decreased rate of association with DMPC liposomes that may relate to the observed altered functions of this mutant [4].
  • On the contrary, studies with plasma or albumin have highlighted the importance of protein conformation in dethiolation processes and have clarified the reason why homocysteine (thiol with potential toxicity) is preferentially bound to albumin as protein-thiol mixed disulfide with respect to other NPSH [5].

High impact information on Protein Conformation

  • These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face [6].
  • Optical properties of single elastin fibres indicate random protein conformation [7].
  • The coupling between protein conformation and nucleotide hydrolysis in Fe-protein exhibits general similarities to the H-Ras p21 and recA proteins that have been recently characterized structurally [8].
  • This model predicts that C/EBP must undertake significant changes in protein conformation as it binds and releases DNA [9].
  • The data agree with the concept that water retention in cells is due to multilayer adsorption on proteins and that the maintenance of the normal state of water relies on the presence of adenosine triphosphate as a cardinal adsorbent, controlling the protein conformations [10].

Biological context of Protein Conformation


Anatomical context of Protein Conformation


Associations of Protein Conformation with chemical compounds


Gene context of Protein Conformation


Analytical, diagnostic and therapeutic context of Protein Conformation


  1. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Warrick, J.M., Chan, H.Y., Gray-Board, G.L., Chai, Y., Paulson, H.L., Bonini, N.M. Nat. Genet. (1999) [Pubmed]
  2. Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. Gasset, M., Baldwin, M.A., Lloyd, D.H., Gabriel, J.M., Holtzman, D.M., Cohen, F., Fletterick, R., Prusiner, S.B. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  3. Mutagenic analysis of human immunodeficiency virus type 1 Vpr: role of a predicted N-terminal alpha-helical structure in Vpr nuclear localization and virion incorporation. Yao, X.J., Subbramanian, R.A., Rougeau, N., Boisvert, F., Bergeron, D., Cohen, E.A. J. Virol. (1995) [Pubmed]
  4. Lipid-free structure and stability of apolipoprotein A-I: probing the central region by mutation. Gorshkova, I.N., Liu, T., Zannis, V.I., Atkinson, D. Biochemistry (2002) [Pubmed]
  5. Biochemical and biological aspects of protein thiolation in cells and plasma. Di Simplicio, P., Frosali, S., Priora, R., Summa, D., Cherubini Di Simplicio, F., Di Giuseppe, D., Di Stefano, A. Antioxid. Redox Signal. (2005) [Pubmed]
  6. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Locher, K.P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J.P., Moras, D. Cell (1998) [Pubmed]
  7. Optical properties of single elastin fibres indicate random protein conformation. Aaron, B.B., Gosline, J.M. Nature (1980) [Pubmed]
  8. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Georgiadis, M.M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J.J., Rees, D.C. Science (1992) [Pubmed]
  9. Evidence of changes in protease sensitivity and subunit exchange rate on DNA binding by C/EBP. Shuman, J.D., Vinson, C.R., McKnight, S.L. Science (1990) [Pubmed]
  10. What retains water in living cells? Ling, G.N., Walton, C.L. Science (1976) [Pubmed]
  11. A mechanism of nonphotochemical energy dissipation, independent from PsbS, revealed by a conformational change in the antenna protein CP26. Dall'Osto, L., Caffarri, S., Bassi, R. Plant Cell (2005) [Pubmed]
  12. Identification of three related human GRO genes encoding cytokine functions. Haskill, S., Peace, A., Morris, J., Sporn, S.A., Anisowicz, A., Lee, S.W., Smith, T., Martin, G., Ralph, P., Sager, R. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  13. The murine C'-terminally alternatively spliced form of p53 induces attenuated apoptosis in myeloid cells. Almog, N., Li, R., Peled, A., Schwartz, D., Wolkowicz, R., Goldfinger, N., Pei, H., Rotter, V. Mol. Cell. Biol. (1997) [Pubmed]
  14. The H1 histones and their interphase phosphorylated states in differentiated and undifferentiated cell lines derived from murine teratocarcinomas. Lennox, R.W., Oshima, R.G., Cohen, L.H. J. Biol. Chem. (1982) [Pubmed]
  15. Some properties of the reaction site for the esterase activity of hemoglobin. Elbaum, D., Wiedenmann, B., Nagel, R.L. J. Biol. Chem. (1982) [Pubmed]
  16. Plasmodesmatal function is probed using transgenic tobacco plants that express a virus movement protein. Wolf, S., Deom, C.M., Beachy, R., Lucas, W.J. Plant Cell (1991) [Pubmed]
  17. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation. Kirschner, D.A., Abraham, C., Selkoe, D.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  18. Protein kinase C-mediated phosphorylation of HIV-I nef in human cell lines. Coates, K., Cooke, S.J., Mann, D.A., Harris, M.P. J. Biol. Chem. (1997) [Pubmed]
  19. Regions controlling hyperphosphorylation and conformation of the retinoblastoma gene product are independent of domains required for transcriptional repression. Hamel, P.A., Gill, R.M., Phillips, R.A., Gallie, B.L. Oncogene (1992) [Pubmed]
  20. Mutational analysis of Saccharomyces cerevisiae Smf1p, a member of the Nramp family of metal transporters. Liu, X.F., Culotta, V.C. J. Mol. Biol. (1999) [Pubmed]
  21. Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation. Biondi, R.M. Trends Biochem. Sci. (2004) [Pubmed]
  22. Growth retardation and early death of beta-1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. Asano, M., Furukawa, K., Kido, M., Matsumoto, S., Umesaki, Y., Kochibe, N., Iwakura, Y. EMBO J. (1997) [Pubmed]
  23. Characterization of a birch pollen allergen, Bet v III, representing a novel class of Ca2+ binding proteins: specific expression in mature pollen and dependence of patients' IgE binding on protein-bound Ca2+. Seiberler, S., Scheiner, O., Kraft, D., Lonsdale, D., Valenta, R. EMBO J. (1994) [Pubmed]
  24. HAMLET kills tumor cells by an apoptosis-like mechanism--cellular, molecular, and therapeutic aspects. Svanborg, C., Agerstam, H., Aronson, A., Bjerkvig, R., Düringer, C., Fischer, W., Gustafsson, L., Hallgren, O., Leijonhuvud, I., Linse, S., Mossberg, A.K., Nilsson, H., Pettersson, J., Svensson, M. Adv. Cancer Res. (2003) [Pubmed]
  25. Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations. Jang, D.J., el-Sayed, M.A. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  26. Hsp90 is essential for restoring cellular functions of temperature-sensitive p53 mutant protein but not for stabilization and activation of wild-type p53: implications for cancer therapy. Müller, P., Ceskova, P., Vojtesek, B. J. Biol. Chem. (2005) [Pubmed]
  27. Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Steinacher, R., Schär, P. Curr. Biol. (2005) [Pubmed]
  28. Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure. Lewis, H.A., Zhao, X., Wang, C., Sauder, J.M., Rooney, I., Noland, B.W., Lorimer, D., Kearins, M.C., Conners, K., Condon, B., Maloney, P.C., Guggino, W.B., Hunt, J.F., Emtage, S. J. Biol. Chem. (2005) [Pubmed]
  29. Distinct conformations of vitamin D receptor/retinoid X receptor-alpha heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes. Staal, A., van Wijnen, A.J., Birkenhäger, J.C., Pols, H.A., Prahl, J., DeLuca, H., Gaub, M.P., Lian, J.B., Stein, G.S., van Leeuwen, J.P., Stein, J.L. Mol. Endocrinol. (1996) [Pubmed]
  30. Protection of the membrane calcium adenosine triphosphatase by cholesterol from thermal inactivation. Cheng, K.H., Hui, S.W., Lepock, J.R. Cancer Res. (1987) [Pubmed]
  31. Direct enthalpy measurements of factor X and prothrombin association with small and large unilamellar vesicles. Plager, D.A., Nelsestuen, G.L. Biochemistry (1994) [Pubmed]
  32. Apolipoprotein D is a component of compact but not diffuse amyloid-beta plaques in Alzheimer's disease temporal cortex. Desai, P.P., Ikonomovic, M.D., Abrahamson, E.E., Hamilton, R.L., Isanski, B.A., Hope, C.E., Klunk, W.E., DeKosky, S.T., Kamboh, M.I. Neurobiol. Dis. (2005) [Pubmed]
  33. FTIR/ATR study of protein adsorption and brushite transformation to hydroxyapatite. Xie, J., Riley, C., Kumar, M., Chittur, K. Biomaterials (2002) [Pubmed]
  34. Changes in the protein conformation of human spermatozoal membranes after treatment with cyclic adenosine 3':5'-monophosphate and human follicular fluid. Delgado, N.M., Huacuja, L., Pancardo, R.M., Merchant, H., Rosado, A. Fertil. Steril. (1976) [Pubmed]
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