Order within disorder: Aggrecan chondroitin sulphate-attachment region provides new structural insights into protein sequences classified as disordered
暂无分享,去创建一个
T. Jowitt | T. Hardingham | A. Murdoch | C. Baldock | J. Day | R. Berry
[1] Jianmin Gao,et al. Localized Thermodynamic Coupling between Hydrogen Bonding and Microenvironment Polarity Substantially Stabilizes Proteins , 2009, Nature Structural &Molecular Biology.
[2] T. Creamer,et al. A survey of left‐handed polyproline II helices , 2008, Protein science : a publication of the Protein Society.
[3] M. Bolognesi,et al. Function and Structure of Inherently Disordered Proteins This Review Comes from a Themed Issue on Proteins Edited Prediction of Non-folding Proteins and Regions Frequency of Disordered Regions Protein Evolution Partitioning Unstructured Proteins and Regions into Groups Involvement of Inherently Diso , 2022 .
[4] Christopher J. Oldfield,et al. The unfoldomics decade: an update on intrinsically disordered proteins , 2008, BMC Genomics.
[5] Christopher J. Oldfield,et al. Intrinsically disordered proteins in human diseases: introducing the D2 concept. , 2008, Annual review of biophysics.
[6] J. Ladias,et al. Structural basis for polyproline recognition by the FE65 WW domain. , 2007, Journal of molecular biology.
[7] Dmitri I. Svergun,et al. Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg , 2007 .
[8] Ronald T. Raines,et al. Stereoelectronic effects on polyproline conformation , 2006, Protein science : a publication of the Protein Society.
[9] Olwyn Byron,et al. SOMO (SOlution MOdeler) differences between X-Ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics. , 2005, Structure.
[10] T. Creamer,et al. Urea promotes polyproline II helix formation: implications for protein denatured states. , 2005, Biochemistry.
[11] H. Dyson,et al. Intrinsically unstructured proteins and their functions , 2005, Nature Reviews Molecular Cell Biology.
[12] G. Rose,et al. Reassessing random-coil statistics in unfolded proteins. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[13] D. Logan,et al. Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins. , 2004, Structure.
[14] P Lukacik,et al. Complement regulation at the molecular level: the structure of decay-accelerating factor. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[15] P. Patwari,et al. Individual cartilage aggrecan macromolecules and their constituent glycosaminoglycans visualized via atomic force microscopy. , 2003, Journal of structural biology.
[16] Manuel C. Peitsch,et al. SWISS-MODEL: an automated protein homology-modeling server , 2003, Nucleic Acids Res..
[17] Gajendra P. S. Raghava,et al. An evaluation of ß-turn prediction methods , 2002, Bioinform..
[18] George D Rose,et al. Polyproline II structure in a sequence of seven alanine residues , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[19] T. Creamer,et al. Polyproline II helical structure in protein unfolded states: Lysine peptides revisited , 2002, Protein science : a publication of the Protein Society.
[20] K. Ma,et al. Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. , 2001, Biochemistry.
[21] P. Schuck,et al. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. , 2000, Biophysical journal.
[22] T. Hardingham,et al. The Folded Protein Modules of the C-terminal G3 Domain of Aggrecan Can Each Facilitate the Translocation and Secretion of the Extended Chondroitin Sulfate Attachment Sequence* , 1999, The Journal of Biological Chemistry.
[23] D T Jones,et al. Protein secondary structure prediction based on position-specific scoring matrices. , 1999, Journal of molecular biology.
[24] S Doniach,et al. Association-induced folding of globular proteins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[25] N. Brissett,et al. Conserved basic residues in the C-type lectin and short complement repeat domains of the G3 region of proteoglycans. , 1998, The Biochemical journal.
[26] H. Orland,et al. Partially folded states of proteins: characterization by X-ray scattering. , 1995, Journal of molecular biology.
[27] M. Sternberg,et al. Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building , 1994, Protein science : a publication of the Protein Society.
[28] P. Shewry,et al. Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare). , 1992, The Biochemical journal.
[29] T. Hardingham,et al. Proteoglycans: many forms and many functions , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[30] A. V. Semenyuk,et al. GNOM – a program package for small-angle scattering data processing , 1991 .
[31] W. Burchard,et al. Determination of chain stiffness and polydispersity from static light‐scattering , 1991 .
[32] P. Shewry,et al. Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein. , 1989, The Biochemical journal.
[33] R. Timpl,et al. Extended and globular protein domains in cartilage proteoglycans. , 1987, The Biochemical journal.
[34] Manfred Schmidt,et al. Remarks on the determination of chain stiffness from static scattering experiments , 1985 .
[35] G. Rose,et al. Hydrophobicity of amino acid residues in globular proteins. , 1985, Science.
[36] J. Janin,et al. Surface and inside volumes in globular proteins , 1979, Nature.
[37] M. Levitt. Conformational preferences of amino acids in globular proteins. , 1978, Biochemistry.
[38] A. Holtzer. Interpretation of the angular distribution of the light scattered by a polydisperse system of rods , 1955 .
[39] G. Porod,et al. Diffuse small-angle scattering of X-rays in colloid systems. , 1949, Journal of colloid science.
[40] S. Subramaniam,et al. Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex. , 2008, Structure.
[41] Hector H. Huang,et al. Contour length and refolding rate of a small protein controlled by engineered disulfide bonds. , 2007, Biophysical journal.
[42] R D Appel,et al. Protein identification and analysis tools in the ExPASy server. , 1999, Methods in molecular biology.
[43] C. Tanford. Protein denaturation. , 1968, Advances in protein chemistry.