Ulrich Hartl Selected Publications
Olzscha, H., Schermann, S.M., Woerner, A.C., Pinkert, S., Hecht, M.H., Tartaglia, G.G., Vendruscolo, M., Hayer-Hartl, M., Hartl, F.U., and Vabulas, R.M. (2011). Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144, 67-78.
Chakraborty, K., Chatila, M., Sinha, J., Shi, Q., Poschner, B.C., Sikor, M., Jiang, G., Lamb, D.C., Hartl, F.U., and Hayer-Hartl, M. (2010). Chaperonin-catalyzed rescue of entropically trapped states in protein folding. Cell 142, 112-122.
Liu, C., Young, A.L, Starling-Windhof, A., Bracher, A., Saschenbrecker, S., Vasudeva Rao, B., Vasudeva Rao, K., Berninghausen, O., Mielke, T., Hartl, F.U. Beckmann, R. and Hayer-Hartl, M. (2010). Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature 463, 197-202.
Hirtreiter, A.M., Calloni, G., Forner, F., Scheibe, B., Puype, M., Vandekerckhove, J., Mann, M., Hartl, F.U. and Hayer-hartl, M. (2009). Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei. Mol. Microbiol. 74,1152-1168.
Broadley, S.A. and Hartl, F.U. (2009). the role of molecular chaperones in human misfolding diseases. FEBS Lett. 583, 2647-2653.
Hartl, F.U. and Hayer-Hartl, M. (2009): Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 16, 574-581.
Gamerdinger, M.,Hajieva, P., Kaya, A.M., Hartl, F.U. and Behl, C. (2009). Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J. 28,889-901.
Brandt, F., Elcock, A.H., Etchells, S.A., Ortiz, J.O., Hartl, F.U. and Baumeister, W. (2009). The native 3D topology of bacterial polysomes. Cell 136, 261-271.
Saschenbrecker, S., Bracher, A., Vasudeva Rao, K., Vasudeva Rao, B., Hartl, F.U., and Hayer-Hartl, M. (2007). Structure and function of RbcX, a specific assembly chaperone for hexadecameric Rubisco. Cell 129, 1189-1200.
Dragovic, Z., Shomura, Y., Tzvetkov, N., Hartl, F.U. and Bracher, A. (2006). Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p. Biol Chem. 387, 1593-1600.
Fonseca, R., Vabulas, R.M., Hartl, F.U., Bonhoeffer, T. and Naegerl, U.V. (2006). A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron 52, 239-245.
Roeben, A., Kofler, C., Nagy, I., Nickell, S., Hartl, F.U. and Bracher, A. (2006). Crystal structure of an archaeal actin homolog. J Mol Biol. 358, 145-156.
Tomic, Sl, Johnson, A.E., Hartl, F.U. and Etchells, S. (2006). Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. FEBS Lett. 580, 72-76.
Chang, H.-C., Kaiser, C.M., Hartl, F.U. and Barral, J.M. (2005). De novo folding of GFP fusion proteins: High efficiency in eukaryotes but not in bacteria. J Mol Biol. 353, 397-409.
Stemp, M.J., Guha, S., Hartl, F.U. and Barral, J.M. (2005). Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC. Biol Chem. 386, 753-757.
Shomura, Y., Dragovic, Z., Chang, H.-C., Tzvetkov, N., Young, J.C., Brodsky, J.L., Guerriero, V., Hartl, F.U. and Bracher, A. (2005). Regulation of Hsp70 function by HspBP1: Structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol Cell 17, 367-379.
Figueiredo, L., Klunker, D., Ang, D., Naylor, D.J., Kerner, M.J., Georgopoulos, C., Hartl, F.U., and Hayer-Hartl, M. (2004). Functional characterization of an archeal GroEL/GroES chaperonin system: Significance of substrate encapsulation. J Biol Chem. 279, 1090-1099.
Brychzy, A., Rein, T., Winklhofer, K.F., Hartl, F.U., Young, J.C. and Obermann, W. (2003). The cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22, 3613-3623.
Brinker, A., Pfeifer, G., Kerner, M.J., Naylor D.J., Hartl, F.U. and Hayer-Hartl, M. (2001). Dual function of protein confinement in chaperone-assisted protein folding. Cell 107, 223-233.
Young, J.C., Moarefi, I. and Hartl, F.U. (2001). Hsp90: a specialized but essential protein-folding tool. J Cell Biol. 154, 267-273.
Sondermann, H., Scheufler, C., Schneider, C., Höhfeld, J., Hartl, F.U. and Moarefi, I. (2001). Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557.
Siegert, R., Leroux, M.R. , Scheufler, C., Hartl, F.U. and Moarefi, I. (2000). Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632.
Young, J.C. and Hartl, F.U. (2000). Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperones p23. EMBO J. 19, 5930-5940.
Scheufler, C., Brinker, A, Hartl, F.U. and Moarefi, I. (2000). Structure of a TPR domain-peptide complex: A critical element in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210.
Leroux, M.R., Fändrich, M., Klunker, D., Siegers, J., Lupas, A.N., Brown, J.R., Schiebel, E., Dobson, C.M. and Hartl, F.U. (1999). MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin. EMBO J. 18, 6730-6743.
Houry, W.A., Frishman, D., Eckerskorn, C, Lottspeich, F. and Hartl, F.U. (1999). Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147-154.
Teter, S.A., Houry, W.A., Ang, D.A., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C. and Hartl, F.U. (1999). Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97, 755-765.
Weber, F., Keppel, F. Georgopoulos, C., Hayer-Hart, M.K. and Hartl, F. U. (1998) The oligomeric cage of GroEL-GroES is required for biologically significant cheperonin function in protein folding. Nat Struct Biol. 11, 977-985.
Ewalt, K.L., Hendrick, J.P., Houry, W.A. and Hartl, F.U. (1997). In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 491-500.
Netzer, B. and Hartl, F.U. (1997). Recombination of protein domains facilitated by sequential folding in eukaryotes. Nature 388, 343-349.
Stebbins, C.E., Russo, A.A., Schneider, C., Rosen, N., Hartl, F.U. and Pavletich, N.P. (1997). Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250.
Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F.U. and Kuriyan, J. (1997). Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK Science 276,431-435.
Martin, J. and Hartl, F.-U. (1997). The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc Natl Acad Sci U.S.A 94, 1107-1112.
Frydman, J. and Hartl, F. U. (1996). Principles of chaperone-assisted folding: Differences between in vitro and in vivo mechanisms. Science 272, 1497-1502.
Mayhew, M., da Silva, A.C.R., Martin, J., Erdjument-Bromage, H., Tempst, P. and Hartl, F.U. (1996). Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379, 420-426.
Höhfeld, J., Minami, Y., and Hartl, F.U. (1995). Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598.
Hayer-Hartl, M.K., Martin, J., and Hartl, F.U. (1995). The Asymmetrical Interaction of GroEL and GroES in the Chaperonin ATPase Cycle of Assisted Protein Folding. Science 269, 836-841.
Engel, A. , Hayer-Hartl, M.K., Goldie, K.N., Pfeifer, G., Hegerl, R., and Hartl, F.U. (1995) Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science 269, 832-836.
Robinson, C.V., Groß, M., Eyles, S.J., Ewbank, J.J., Mayhew, M., Hartl, F.U., Dobson, C.M. and Radford, S. (1994). Conformation of GroEL-bound a-lactalbumin probed by mass spectrometry. Nature 372, 646-651.
Höhfeld, J. and Hartl, F.U. (1994). Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J Cell Biol. 126, 305-315.
Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hartl, F.U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
Martin, J., Mayhew, M., Langer, T., and Hartl, F.U. (1993). The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366, 228-233.
Schröder, H., Langer, T., Hartl, F.U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
Langer, T., Pfeifer, G., Martin, J., Baumeister, W. and Hartl, F.U. (1992). Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765.
Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P. and Hartl, F.U. (1992). Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 11, 4767-4778.
Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K. and Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
Trent, J.D., Nimmesgern, E., Wall, J.S., Hartl, F.U., and Horwich, A.L. (1991). A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354, 490-493.
Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L. and Hartl, F.U. (1991). Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate. Nature 352, 36-42.
Cheng, M.Y., Hartl, F.U. and Horwich, A.L. (1990). The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348, 455-458.
Ostermann. J., Horwich, A., Neupert, W. and Hartl, F.U. (1989). Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341, 125-130
Cheng, M.Y., Hartl, F.U., Martin, J., Pollock, R.A., Kalousek, F., Neupert, W., Hallberg, E.M., Hallberg, R.L. and Horwich, A.L. (1989). Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620-625.
Vollständige Publikationsliste
Wickner, W., Driessen, A.J.M., and Hartl, F.U. (1991). The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu Rev Biochem. 60, 101-124
Hendrick, J. and Hartl, F.U. (1993). Molecular chaperone functions of heat shock proteins. Annu Rev Biochem. 62, 349-384
Martin, J. and Hartl, F.U. (1993). Protein folding in the cell: molecular chaperones pave the way. Structure 1, 161-164.
Hartl, F.U., Hlodan, R., and Langer, T. (1994). Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci. 19, 20-25.
Hartl, F.U., and Martin, J. (1995). Molecular chaperones in cellular protein folding. Curr Opin Struct Biol. 5, 92-102.
Hartl, F.U. (1996). Molecular Chaperones in Cellular Protein Folding. Nature 381, 571- 580.
Martin, J. and Hartl, F.U. Chaperone-assisted protein folding (1997). Curr Opin Struct Biol. 7, 41-52
Netzer, W.J. and Hartl, F.U. (1998) Protein folding in the cytosol: Chaperonin-dependent and independent mechanisms. Trends Biochem Sci. 23, 68-73.
Ellis, R.J. and Hartl, F.U. (1999). Principles of protein folding in the cellular environment. Curr Opin Struct Biol. 9, 102-110.
Hartl, F.U. and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295, 1852-1858.
rss
Top
Print