Converging concepts of protein folding in vitro and in vivo
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[1] Peter J McCormick,et al. Nascent Membrane and Secretory Proteins Differ in FRET-Detected Folding Far inside the Ribosome and in Their Exposure to Ribosomal Proteins , 2004, Cell.
[2] Richard I. Morimoto,et al. Adapting Proteostasis for Disease Intervention , 2008, Science.
[3] S. Lindquist,et al. Hsp90 as a capacitor for morphological evolution , 1998, Nature.
[4] Shawn Y. Stevens,et al. Structural insights into substrate binding by the molecular chaperone DnaK , 2000, Nature Structural Biology.
[5] H. Saibil,et al. Chaperonin complex with a newly folded protein encapsulated in the folding chamber , 2009, Nature.
[6] Thomas Nyström,et al. Genomic buffering mitigates the effects of deleterious mutations in bacteria , 2005, Nature Genetics.
[7] K. Wüthrich,et al. Folding trajectories of human dihydrofolate reductase inside the GroEL–GroES chaperonin cavity and free in solution , 2007, Proceedings of the National Academy of Sciences.
[8] Jason C. Young,et al. More than folding: localized functions of cytosolic chaperones. , 2003, Trends in biochemical sciences.
[9] G. Farr,et al. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated , 2001, Cell.
[10] C. Bruce,et al. Chaperone Suppression of a-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease , 2002 .
[11] D. J. Naylor,et al. Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding , 2001, Cell.
[12] M. Oliveberg,et al. Malleability of protein folding pathways: a simple reason for complex behaviour. , 2007, Current opinion in structural biology.
[13] E. Orlova,et al. Topologies of a Substrate Protein Bound to the Chaperonin GroEL , 2007, Molecular cell.
[14] S. Lindquist,et al. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+] , 2009, Nature Structural &Molecular Biology.
[15] F. Hartl,et al. SnapShot: Molecular Chaperones, Part II , 2007, Cell.
[16] Sheena E Radford,et al. Intermediates: ubiquitous species on folding energy landscapes? , 2007, Current opinion in structural biology.
[17] F. Hartl,et al. Real-time observation of trigger factor function on translating ribosomes , 2006, Nature.
[18] Luis Moroder,et al. Structure of TPR Domain–Peptide Complexes Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine , 2000, Cell.
[19] Wayne A. Hendrickson,et al. Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 , 2007, Cell.
[20] Borries Demeler,et al. Structure of the Hsp110:Hsc70 nucleotide exchange machine. , 2008, Molecular cell.
[21] A. Horwich,et al. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation , 2008, Proceedings of the National Academy of Sciences.
[22] Hiroshi Kimura,et al. Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state , 2006, Nature Cell Biology.
[23] P. Jenö,et al. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[24] E. Wanker,et al. Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[25] F. Hartl,et al. Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein , 2007 .
[26] A. Bashan,et al. Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[27] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[28] Judith Frydman,et al. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones , 1994, Nature.
[29] D. Boehringer,et al. Molecular mechanism and structure of Trigger Factor bound to the translating ribosome , 2008, The EMBO journal.
[30] S. Rüdiger,et al. Interaction of Hsp70 chaperones with substrates , 1997, Nature Structural Biology.
[31] S. Teichmann,et al. The importance of sequence diversity in the aggregation and evolution of proteins , 2005, Nature.
[32] R. Ellis,et al. Molecular chaperones: assisting assembly in addition to folding. , 2006, Trends in biochemical sciences.
[33] J. Shea,et al. Effects of confinement in chaperonin assisted protein folding: rate enhancement by decreasing the roughness of the folding energy landscape. , 2003, Journal of molecular biology.
[34] H. Rye,et al. Expansion and compression of a protein folding intermediate by GroEL. , 2004, Molecular cell.
[35] W. Skach. Cellular mechanisms of membrane protein folding , 2009, Nature Structural &Molecular Biology.
[36] A. Horwich,et al. CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7 , 1997 .
[37] J. Frydman,et al. Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells , 2006, Cell.
[38] Sheena E Radford,et al. An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms , 2009, Nature Structural &Molecular Biology.
[39] E. Craig,et al. Human Mpp11 J Protein: Ribosome-Tethered Molecular Chaperones Are Ubiquitous , 2005, Science.
[40] M. Mayer,et al. Molecular Basis for Interactions of the DnaK Chaperone with Substrates , 2000, Biological chemistry.
[41] A. Minton,et al. A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding. , 2006, Biochemistry.
[42] P. Muchowski,et al. Modulation of neurodegeneration by molecular chaperones , 2005, Nature Reviews Neuroscience.
[43] F. Hartl,et al. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. , 2006, Molecular cell.
[44] H. Taguchi,et al. Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant*♦ , 2008, Journal of Biological Chemistry.
[45] F. Schmid,et al. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase , 2002, Nature Structural Biology.
[46] F. Hartl,et al. Molecular chaperones in cellular protein folding. , 1995, BioEssays : news and reviews in molecular, cellular and developmental biology.
[47] Vijay S. Pande,et al. A Role for Confined Water in Chaperonin Function , 2008, Journal of the American Chemical Society.
[48] J. Buchner,et al. The Hsp90 Chaperone Machinery* , 2008, Journal of Biological Chemistry.
[49] Walid A Houry,et al. In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System , 1997, Cell.
[50] B. Bukau,et al. The C-terminal Domain of Escherichia coli Trigger Factor Represents the Central Module of Its Chaperone Activity* , 2006, Journal of Biological Chemistry.
[51] Judith Frydman,et al. In vivo newly translated polypeptides are sequestered in a protected folding environment , 1999, The EMBO journal.
[52] Arturo Muga,et al. The structure of CCT–Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin , 2008, Nature Structural &Molecular Biology.
[53] Jimena Weibezahn,et al. Novel insights into the mechanism of chaperone-assisted protein disaggregation , 2005, Biological chemistry.
[54] Renée L. Brost,et al. The interaction network of the chaperonin CCT , 2008, The EMBO journal.
[55] M. Gerstein,et al. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly-made proteins with complex topologies , 2008, Nature Structural &Molecular Biology.
[56] J. Frydman,et al. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions , 2006, Nature Cell Biology.
[57] J. Frydman,et al. The Interaction of the Chaperonin Tailless Complex Polypeptide 1 (Tcp1) Ring Complex (Tric) with Ribosome-Bound Nascent Chains Examined Using Photo-Cross-Linking , 2000, The Journal of cell biology.
[58] F. Hartl,et al. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.
[59] F. Hartl,et al. Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding , 2008, Cell.
[60] Yun-chi Tang,et al. Essential role of the chaperonin folding compartment in vivo , 2008, The EMBO journal.
[61] Kurt Wüthrich,et al. Direct NMR observation of a substrate protein bound to the chaperonin GroEL. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[62] Jianli Lu,et al. Folding zones inside the ribosomal exit tunnel , 2005, Nature Structural &Molecular Biology.
[63] A. Minton,et al. Protein aggregation in crowded environments , 2006, Biological chemistry.
[64] Andreas Bracher,et al. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s , 2006, The EMBO journal.
[65] F. Hartl,et al. Roles of molecular chaperones in protein misfolding diseases. , 2004, Seminars in cell & developmental biology.
[66] J. Vandekerckhove,et al. Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin , 1998, Cell.
[67] H. Lehrach,et al. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. , 2001, Human molecular genetics.
[68] Andreas Bracher,et al. Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding , 2008, Cell.
[69] H. Rye,et al. GroEL stimulates protein folding through forced unfolding , 2008, Nature Structural &Molecular Biology.
[70] F. Hartl,et al. Recombination of protein domains facilitated by co-translational folding in eukaryotes , 1997, Nature.
[71] A. Shevchenko,et al. Compartmentation of protein folding in vivo: sequestration of non‐native polypeptide by the chaperonin–GimC system , 1999, The EMBO journal.
[72] S Walter Englander,et al. Protein folding and misfolding: mechanism and principles , 2007, Quarterly Reviews of Biophysics.
[73] Daniel N. Wilson,et al. The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction , 2005, Structure.
[74] F. Hartl,et al. Structure and Function of RbcX, an Assembly Chaperone for Hexadecameric Rubisco , 2007, Cell.
[75] R. Vabulas,et al. Protein Synthesis upon Acute Nutrient Restriction Relies on Proteasome Function , 2005, Science.
[76] J. Onuchic,et al. Theory of Protein Folding This Review Comes from a Themed Issue on Folding and Binding Edited Basic Concepts Perfect Funnel Landscapes and Common Features of Folding Mechanisms , 2022 .
[77] F. Hartl,et al. SnapShot: Molecular Chaperones, Part I , 2007, Cell.
[78] F. Hartl,et al. Function of Trigger Factor and DnaK in Multidomain Protein Folding Increase in Yield at the Expense of Folding Speed , 2004, Cell.
[79] Zoya Ignatova,et al. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[80] T. Steitz,et al. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. , 2000, Science.
[81] Julio O. Ortiz,et al. The Native 3D Organization of Bacterial Polysomes , 2009, Cell.
[82] Jonathan S. Weissman,et al. Directed Evolution of Substrate-Optimized GroEL/S Chaperonins , 2002, Cell.
[83] M. Textor,et al. Probing protein-chaperone interactions with single-molecule fluorescence spectroscopy. , 2008, Angewandte Chemie.
[84] F. Hartl,et al. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding , 1992, Nature.
[85] Holger Patzelt,et al. Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins , 2005 .
[86] Bernd Bukau,et al. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins , 2009, Nature Structural &Molecular Biology.
[87] M Michael Gromiha,et al. Inter-residue interactions in protein folding and stability. , 2004, Progress in biophysics and molecular biology.
[88] Bernd Bukau,et al. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor , 2006, The EMBO journal.
[89] W. Houry,et al. Molecular interaction network of the Hsp90 chaperone system. , 2007, Advances in experimental medicine and biology.
[90] B. Bukau,et al. Trigger factor and DnaK cooperate in folding of newly synthesized proteins , 1999, Nature.
[91] F. Hartl,et al. Polypeptide Flux through Bacterial Hsp70 DnaK Cooperates with Trigger Factor in Chaperoning Nascent Chains , 1999, Cell.
[92] G. Farr,et al. Two families of chaperonin: physiology and mechanism. , 2007, Annual review of cell and developmental biology.
[93] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[94] D. Thirumalai,et al. Chaperonin-mediated protein folding. , 2001, Annual review of biophysics and biomolecular structure.
[95] Sheena E Radford,et al. The Yin and Yang of protein folding , 2005, The FEBS journal.
[96] Craig M. Ogata,et al. Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK , 1996, Science.
[97] D. J. Naylor,et al. Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli , 2005, Cell.
[98] J Kuriyan,et al. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. , 1997, Science.
[99] R. Morimoto,et al. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. , 2003, Molecular biology of the cell.
[100] F. Hartl,et al. Identification of Nascent Chain Interaction Sites on Trigger Factor* , 2007, Journal of Biological Chemistry.
[101] C. Dobson. Protein folding and misfolding , 2003, Nature.
[102] J. Frydman. Folding of newly translated proteins in vivo: the role of molecular chaperones. , 2001, Annual review of biochemistry.
[103] I. Braakman,et al. Protein folding and quality control in the endoplasmic reticulum. , 2004, Current opinion in cell biology.