Crossref journal-article
Elsevier BV
Journal of Molecular Biology (78)
Bibliography

Masino, L., Nicastro, G., Menon, R. P., Piaz, F. D., Calder, L., & Pastore, A. (2004). Characterization of the Structure and the Amyloidogenic Properties of the Josephin Domain of the Polyglutamine-containing Protein Ataxin-3. Journal of Molecular Biology, 344(4), 1021–1035.

Authors 6
  1. Laura Masino (first)
  2. Giuseppe Nicastro (additional)
  3. Rajesh P. Menon (additional)
  4. Fabrizio Dal Piaz (additional)
  5. Lesley Calder (additional)
  6. Annalisa Pastore (additional)
References 47 Referenced 107
  1. 10.1038/ng1194-221 / Nature Genet. / CAG expansions in a novel gene for Machado–Joseph disease at chromosome 14q32.1 by Kawaguchi (1994)
  2. 10.1146/annurev.neuro.23.1.217 / Annu. Rev. Neurosci. / Glutamine repeats and neurodegeneration by Zoghbi (2000)
  3. 10.1016/S0896-6273(02)00872-3 / Neuron / Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders by Ross (2002)
  4. 10.1016/S0140-6736(03)13304-1 / Lancet / Huntingtin aggregation and toxicity in Huntington's disease by Bates (2003)
  5. 10.1038/nrn1007 / Nature Rev. Neurosci. / Unfolding the role of protein misfolding in neurodegenerative diseases by Soto (2003)
  6. 10.1073/pnas.182426899 / Proc. Natl Acad. Sci. USA / Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity by Sakahira (2002)
  7. 10.1006/jmbi.2001.4850 / J. Mol. Biol. / Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity by Chen (2001)
  8. 10.1021/bi00869a011 / Biochemistry / Synthetic polypeptides containing side-chain amide groups. Water-soluble polymers by Krull (1966)
  9. 10.1016/S0092-8674(00)80514-0 / Cell / Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo by Scherzinger (1997)
  10. 10.1073/pnas.96.8.4604 / Proc. Natl Acad. Sci. USA / Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology by Scherzinger (1999)
  11. 10.1016/j.jmb.2003.08.064 / J. Mol. Biol. / Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease by Chow (2004)
  12. 10.1016/S0896-6273(03)00328-3 / Neuron / Polyglutamines placed into context by La Spada (2003)
  13. 10.1074/jbc.M304205200 / J. Biol. Chem. / Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature by Marchal (2003)
  14. 10.1016/S0014-5793(02)02335-9 / FEBS Letters / Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins by Masino (2002)
  15. 10.1097/00001756-200110290-00042 / Neuroreport / Amino acid sequences flanking polyglutamine stretches influence their potential for aggregate formation by Nozaki (2001)
  16. 10.1093/hmg/9.6.909 / Hum. Mol. Genet. / Fourteen and counting: unraveling trinucleotide repeat diseases by Cummings (2000)
  17. 10.1073/pnas.211305198 / Proc. Natl Acad. Sci. USA / An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils by Bevivino (2001)
  18. 10.1002/prot.10280 / Proteins: Struct. Funct. Genet. / Structural modeling of ataxin-3 reveals distant homology to adaptins by Albrecht (2003)
  19. 10.1093/hmg/ddg297 / Hum. Mol. Genet. / Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics by Scheel (2003)
  20. 10.1016/S0014-5793(03)00748-8 / FEBS Letters / Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail by Masino (2003)
  21. 10.1021/bi0352825 / Biochemistry / Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36) by Shehi (2003)
  22. 10.1074/jbc.M200650200 / J. Biol. Chem. / Structural characterization of the M* partly folded intermediate of wild type and P138A aspartate aminotransferase from Escherichia coli by Birolo (2002)
  23. 10.1126/science.8235611 / Science / Detection of transient protein folding populations by mass spectrometry by Miranker (1993)
  24. 10.1002/pro.5560020404 / Protein Sci. / Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation by Zhang (1993)
  25. 10.1002/prot.340170110 / Proteins: Struct. Funct. Genet. / Primary structure effects on peptide group hydrogen exchange by Bai (1993)
  26. 10.1006/abio.2000.4880 / Anal. Biochem. / Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set by Sreerama (2000)
  27. 10.1038/nsb0694-399 / Nature Struct. Biol. / Elucidating the folding problem of helical peptides using empirical parameters by Munoz (1994)
  28. 10.1021/bi00121a010 / Biochemistry / The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy by Wishart (1992)
  29. 10.1016/0076-6879(86)31045-0 / Methods Enzymol. / Determination and analysis of urea and guanidine hydrochloride denaturation curves by Pace (1986)
  30. 10.1016/j.bbrc.2004.07.131 / Biochem. Biophys. Res. Commun. / Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3 by Chow (2004)
  31. 10.1016/S0968-0004(01)01835-7 / Trends Biochem. Sci. / A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems by Hofmann (2001)
  32. 10.1093/emboj/cdg467 / EMBO J. / Structural determinants for the binding of ubiquitin-like domains to the proteasome by Mueller (2003)
  33. 10.1093/emboj/cdg471 / EMBO J. / Solution structure of Vps27 UIM–ubiquitin complex important for endosomal sorting and receptor downregulation by Swanson (2003)
  34. 10.1016/S0968-0004(99)01445-0 / Trends Biochem. Sci. / Protein misfolding, evolution and disease by Dobson (1999)
  35. {'key': '10.1016/j.jmb.2004.09.065_bib35', 'series-title': 'Protein Folding', 'author': 'Creighton', 'year': '1992'} / Protein Folding by Creighton (1992)
  36. 10.1038/35040584 / Nature / Identification of genes that modify ataxin-1-induced neurodegeneration by Fernandez-Funez (2000)
  37. 10.1017/S0033583500005217 / Quart. Rev. Biophys. / Hydrogen exchange and structural dynamics of proteins and nucleic acids by Englander (1983)
  38. 10.1016/0022-2836(91)90214-Q / J. Mol. Biol. / Relationship between nuclear magnetic resonance chemical shift and protein secondary structure by Wishart (1991)
  39. 10.1016/0014-5793(91)81155-2 / FEBS Letters / Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy by Wishart (1991)
  40. 10.1110/ps.9.8.1519 / Protein Sci. / Ligand binding and thermodynamic stability of a multidomain protein, calmodulin by Masino (2000)
  41. 10.1016/S0021-9258(20)79739-5 / J. Biol. Chem. / Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin by Greene (1974)
  42. 10.1007/BF02192855 / J. Biomol. NMR / Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions by Piotto (1992)
  43. 10.1007/BF00197809 / J. Biomol. NMR / NMRPipe – a multi dimensional spectral processing system based on UNIX pipes by Delaglio (1995)
  44. 10.1021/bi00449a003 / Biochemistry / Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease by Kay (1989)
  45. 10.1016/0009-2614(90)85567-V / Chem. Phys. Letters / Influence of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms upon longitudinal relaxation rates of 15N in macromolecules by Boyd (1990)
  46. 10.1021/ja00381a009 / J. Am. Chem. Soc. / A model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity by Lipari (1982)
  47. 10.1007/BF00197813 / J. Biomol. NMR / Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2 by Dingley (1995)
Dates
Type When
Created 20 years, 10 months ago (Oct. 12, 2004, 1:34 p.m.)
Deposited 4 years, 2 months ago (June 26, 2021, 9:39 a.m.)
Indexed 1 year ago (Aug. 12, 2024, 9:12 a.m.)
Issued 20 years, 8 months ago (Dec. 1, 2004)
Published 20 years, 8 months ago (Dec. 1, 2004)
Published Print 20 years, 8 months ago (Dec. 1, 2004)
Funders 0

None

@article{Masino_2004, title={Characterization of the Structure and the Amyloidogenic Properties of the Josephin Domain of the Polyglutamine-containing Protein Ataxin-3}, volume={344}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2004.09.065}, DOI={10.1016/j.jmb.2004.09.065}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Masino, Laura and Nicastro, Giuseppe and Menon, Rajesh P. and Piaz, Fabrizio Dal and Calder, Lesley and Pastore, Annalisa}, year={2004}, month=dec, pages={1021–1035} }