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Groves, M.R.1
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When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
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Kobe B., Kajava A.V. When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem Sci. 25:2000;509-515.
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Kobe, B.1
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Classification and properties of solenoid proteins on World Wide Web URL:
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Classification and properties of solenoid proteins on World Wide Web URL: http://cmm.info.nih.gov/kajava/solenoidtable.html.
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0037147328
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What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
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An interesting study of the factors that contribute to the twist and curvature of repeat proteins.
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Kajava A.V. What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J Biol Chem. 277:2002;49791-49798 An interesting study of the factors that contribute to the twist and curvature of repeat proteins.
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Kajava, A.V.1
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PFAM - top twenty families on World Wide Web URL:
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PFAM - top twenty families on World Wide Web URL: http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00400.
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Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat Struct Biol. 7:2000;1091-1095.
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A minimum folding unit in the ankyrin repeat protein p16(INK4)
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The first study to show that it is possible to remove various numbers of repeats from a repeat protein and still produce stable, folded fragments.
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Zhang B., Peng Z. A minimum folding unit in the ankyrin repeat protein p16(INK4). J Mol Biol. 299:2000;1121-1132 The first study to show that it is possible to remove various numbers of repeats from a repeat protein and still produce stable, folded fragments.
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Zhang, B.1
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Sequential unfolding of ankyrin repeats in tumor suppressor p16
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The first study to characterize the folding transition state of a repeat protein using Φ-value analysis.
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Tang K.S., Fersht A.R., Itzhaki L.S. Sequential unfolding of ankyrin repeats in tumor suppressor p16. Structure. 11:2003;67-73 The first study to characterize the folding transition state of a repeat protein using Φ-value analysis.
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Tang, K.S.1
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Stability and folding of the tumour suppressor protein p16
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Tang K.S., Guralnick B.J., Wang W.K., Fersht A.R., Itzhaki L.S. Stability and folding of the tumour suppressor protein p16. J Mol Biol. 285:1999;1869-1886.
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Design and characterization of a hyperstable p16(INK4a) that restores Cdk4 binding activity when combined with oncogenic mutations
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Cammett T.J., Luo L., Peng Z. Design and characterization of a hyperstable p16(INK4a) that restores Cdk4 binding activity when combined with oncogenic mutations. J Mol Biol. 327:2003;285-297.
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Equilibrium folding and stability of myotrophin: A model ankyrin repeat protein
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Mosavi L.K., Williams S., Peng Z.-y. Equilibrium folding and stability of myotrophin: a model ankyrin repeat protein. J Mol Biol. 320:2002;165-170.
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Mosavi, L.K.1
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0036304525
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Protein folding and stability of human CDK inhibitor p19(INK4d)
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Zeeb M., Rosner H., Zeslawski W., Canet D., Holak T.A., Balbach J. Protein folding and stability of human CDK inhibitor p19(INK4d). J Mol Biol. 315:2002;447-457.
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Balbach, J.6
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18
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0036438808
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Limits of cooperativity in a structurally modular protein: Response of the Notch ankyrin domain to analogous alanine substitutions in each repeat
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A study that characterises the cooperative nature of the equilibrium unfolding of a larger ank repeat protein in response to specific point mutations.
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Bradley C.M., Barrick D. Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat. J Mol Biol. 324:2002;373-386 A study that characterises the cooperative nature of the equilibrium unfolding of a larger ank repeat protein in response to specific point mutations.
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J Mol Biol
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Bradley, C.M.1
Barrick, D.2
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0035807867
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Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties
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•] showing the initial biophysical characterisation of a larger ank-containing protein.
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•] showing the initial biophysical characterisation of a larger ank-containing protein.
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Biochemistry
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Zweifel, M.E.1
Barrick, D.2
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20
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0035807936
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Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding
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•] showing the initial biophysical characterisation of a larger ank-containing protein.
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•] showing the initial biophysical characterisation of a larger ank-containing protein.
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Biochemistry
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Zweifel, M.E.1
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0034719144
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The stability, structural organization, and denaturation of pectate lyase C, a parallel beta-helix protein
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Kamen D.E., Griko Y., Woody R.W. The stability, structural organization, and denaturation of pectate lyase C, a parallel beta-helix protein. Biochemistry. 39:2000;15932-15943.
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Biochemistry
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Kamen, D.E.1
Griko, Y.2
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0037046153
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Identification of proline residues responsible for the slow folding kinetics in pectate lyase C by mutagenesis
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Kamen D.E., Woody R.W. Identification of proline residues responsible for the slow folding kinetics in pectate lyase C by mutagenesis. Biochemistry. 41:2002;4724-4732.
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0037046158
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Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization
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Kamen D.E., Woody R.W. Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization. Biochemistry. 41:2002;4713-4723.
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Biochemistry
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Kamen, D.E.1
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24
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0034808018
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A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS)
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Kamen D.E., Woody R.W. A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS). Protein Sci. 10:2001;2123-2130.
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Protein Sci
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25
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0034141471
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Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
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Nikolova P.V., Wong K.B., DeDecker B., Henckel J., Fersht A.R. Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. EMBO J. 19:2000;370-378.
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26
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0037221599
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Is there a unifying mechanism for protein folding?
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Daggett V., Fersht A.R. Is there a unifying mechanism for protein folding? Trends Biochem Sci. 28:2003;18-25.
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Trends Biochem Sci
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Daggett, V.1
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30
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0036271498
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The consensus concept for thermostability engineering of proteins: Further proof of concept
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Lehmann M., Loch C., Middendorf A., Studer D., Lassen S.F., Pasamontes L., van Loon A.P., Wyss M. The consensus concept for thermostability engineering of proteins: further proof of concept. Protein Eng. 15:2002;403-411.
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Protein Eng
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Lehmann, M.1
Loch, C.2
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Studer, D.4
Lassen, S.F.5
Pasamontes, L.6
Van Loon, A.P.7
Wyss, M.8
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31
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0034635335
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Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
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Knappik A., Ge L., Honegger A., Pack P., Fischer M., Wellnhofer G., Hoess A., Wolle J., Pluckthun A., Virnekas B. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J Mol Biol. 296:2000;57-86.
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Knappik, A.1
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Hoess, A.7
Wolle, J.8
Pluckthun, A.9
Virnekas, B.10
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32
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0029881007
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MOLMOL: A program for display and analysis of macromolecular structures
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Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 14:1996;51-55.
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MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
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SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
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36
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85031069090
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POV-Ray and the Persistence of Vision Raytracer on World Wide Web URL:
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POV-Ray and the Persistence of Vision Raytracer on World Wide Web URL: http://www.povray.org/.
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