F U Hartl

Summary

Country: Germany

Publications

  1. ncbi request reprint Molecular chaperones in the cytosol: from nascent chain to folded protein
    F Ulrich Hartl
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Science 295:1852-8. 2002
  2. ncbi request reprint Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation
    Luis Figueiredo
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 279:1090-9. 2004
  3. pmc Hsp90: a specialized but essential protein-folding tool
    J C Young
    Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D 82152, Germany
    J Cell Biol 154:267-73. 2001
  4. doi request reprint Molecular chaperone functions in protein folding and proteostasis
    Yujin E Kim
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Annu Rev Biochem 82:323-55. 2013
  5. pmc Protein abundance profiling of the Escherichia coli cytosol
    Yasushi Ishihama
    Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997 0017, Japan
    BMC Genomics 9:102. 2008
  6. doi request reprint Converging concepts of protein folding in vitro and in vivo
    F Ulrich Hartl
    Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany
    Nat Struct Mol Biol 16:574-81. 2009
  7. doi request reprint Molecular chaperones in protein folding and proteostasis
    F Ulrich Hartl
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 475:324-32. 2011
  8. pmc Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    J C Young
    Cellular Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    EMBO J 19:5930-40. 2000
  9. ncbi request reprint Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors
    H Sondermann
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Science 291:1553-7. 2001
  10. pmc In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
    W M Obermann
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    J Cell Biol 143:901-10. 1998

Collaborators

Detail Information

Publications76

  1. ncbi request reprint Molecular chaperones in the cytosol: from nascent chain to folded protein
    F Ulrich Hartl
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Science 295:1852-8. 2002
    ..Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine...
  2. ncbi request reprint Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation
    Luis Figueiredo
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 279:1090-9. 2004
    ..Additionally, the release of only the folded protein from the GroEL/GroES cage may prevent adverse interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment...
  3. pmc Hsp90: a specialized but essential protein-folding tool
    J C Young
    Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D 82152, Germany
    J Cell Biol 154:267-73. 2001
    ..Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy...
  4. doi request reprint Molecular chaperone functions in protein folding and proteostasis
    Yujin E Kim
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Annu Rev Biochem 82:323-55. 2013
    ..This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation...
  5. pmc Protein abundance profiling of the Escherichia coli cytosol
    Yasushi Ishihama
    Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997 0017, Japan
    BMC Genomics 9:102. 2008
    ..Thus far, protein concentrations have been difficult to measure on a large scale, but proteomic technologies have now advanced to a stage where this information becomes readily accessible...
  6. doi request reprint Converging concepts of protein folding in vitro and in vivo
    F Ulrich Hartl
    Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany
    Nat Struct Mol Biol 16:574-81. 2009
    ....
  7. doi request reprint Molecular chaperones in protein folding and proteostasis
    F Ulrich Hartl
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 475:324-32. 2011
    ..Interventions in these and numerous other pathological states may spring from a detailed understanding of the pathways underlying proteome maintenance...
  8. pmc Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    J C Young
    Cellular Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    EMBO J 19:5930-40. 2000
    ..p23 couples the ATPase activity to polypeptide dissociation and thus can function as a substrate release factor for Hsp90...
  9. ncbi request reprint Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors
    H Sondermann
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Science 291:1553-7. 2001
    ..Thus, functional convergence has allowed proteins with different architectures to trigger a conserved conformational shift in Hsp70 that leads to nucleotide exchange...
  10. pmc In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
    W M Obermann
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    J Cell Biol 143:901-10. 1998
    ..Our results establish Hsp90 as an ATP-dependent chaperone...
  11. ncbi request reprint Chaperonin-mediated de novo generation of prion protein aggregates
    J Stockel
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, D 82152, Germany
    J Mol Biol 313:861-72. 2001
    ..These results show that chaperonins of the Hsp60 class can, in principle, mediate PrP aggregation de novo, i.e. independently of a pre-existent PrP(Sc) template...
  12. ncbi request reprint Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins
    R Siegert
    Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D82152 Martinsried, Germany
    Cell 103:621-32. 2000
    ..The distal regions of the coiled coils expose hydrophobic patches and are required for multivalent binding of nonnative proteins...
  13. ncbi request reprint Dual function of protein confinement in chaperonin-assisted protein folding
    A Brinker
    Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany
    Cell 107:223-33. 2001
    ....
  14. ncbi request reprint Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    C Scheufler
    Max Planck Institute for Biochemistry, Martinsried, Germany
    Cell 101:199-210. 2000
    ..The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes...
  15. ncbi request reprint Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC
    Markus J Stemp
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Biol Chem 386:753-7. 2005
    ..In addition, it provides a robust alternative for the production of substantial amounts of eukaryotic proteins that otherwise misfold or lead to cellular toxicity upon expression in heterologous hosts...
  16. ncbi request reprint Roles of molecular chaperones in protein misfolding diseases
    Jose M Barral
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Semin Cell Dev Biol 15:17-29. 2004
    ..Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies...
  17. doi request reprint Monitoring protein conformation along the pathway of chaperonin-assisted folding
    Shruti Sharma
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 133:142-53. 2008
    ..Segmental chain release and compaction may be important in avoiding misfolding by proteins that fail to fold efficiently through spontaneous hydrophobic collapse...
  18. ncbi request reprint Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation
    Gregor Schaffar
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Mol Cell 15:95-105. 2004
    ..These results outline a molecular mechanism of cellular toxicity in polyQ disease and can explain the beneficial effects of molecular chaperones...
  19. pmc Essential role of the chaperonin folding compartment in vivo
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    EMBO J 27:1458-68. 2008
    ..Altering the net-negative charge of the GroEL cage wall also strongly affected chaperonin function. Based on these findings, the GroEL/GroES compartment is essential for protein folding in vivo...
  20. ncbi request reprint Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    Holger Sondermann
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    J Biol Chem 277:33220-7. 2002
    ..Thus, Snl1p is the first Bag domain protein identified in S. cerevisiae, and its interaction with Hsp70 is essential for biological activity...
  21. ncbi request reprint De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria
    Hung chun Chang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 353:397-409. 2005
    ..By following the accumulation of enzymatic activity, we found that the rate of appearance of correctly folded fusion protein per ribosome is indeed considerably higher in yeast than in bacteria...
  22. pmc MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
    M R Leroux
    Max Planck Institut fur Biochemie, Department of Cellular Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    EMBO J 18:6730-43. 1999
    ..In light of the absence of Hsp70 chaperones in many archaea, GimC may fulfil an ATP-independent, Hsp70-like function in archaeal de novo protein folding...
  23. ncbi request reprint Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    S A Teter
    Max Planck Institut fur Biochemie, Department of Cellular Biochemistry, Martinsried, Germany
    Cell 97:755-65. 1999
    ..These findings indicate important, partially overlapping functions of DnaK and trigger factor in de novo protein folding and explain why the loss of either chaperone can be tolerated by E. coli...
  24. ncbi request reprint Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    Michael J Kerner
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 122:209-20. 2005
    ..We suggest that the chaperonin system may have facilitated the evolution of this fold into a versatile platform for the implementation of numerous enzymatic functions...
  25. ncbi request reprint Protein synthesis upon acute nutrient restriction relies on proteasome function
    Ramunas M Vabulas
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Science 310:1960-3. 2005
    ..Proteasome inhibition during nutrient deprivation caused rapid amino acid depletion and marked impairment of translation. Thus, the proteasome plays a crucial role in cell survival after acute disruption of amino acid supply...
  26. ncbi request reprint Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    Christian Behrends
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried
    Mol Cell 23:887-97. 2006
    ..We suggest that TRiC cooperates with the Hsp70 system as a key component in the cellular defense against amyloid-like protein misfolding...
  27. ncbi request reprint Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed
    Vishwas R Agashe
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 117:199-209. 2004
    ..These findings suggest important differences in the coupling of translation and folding between bacterial and eukaryotic cells...
  28. doi request reprint Coupled chaperone action in folding and assembly of hexadecameric Rubisco
    Cuimin Liu
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 463:197-202. 2010
    ..Finally, addition of RbcS results in RbcX(2) release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly...
  29. ncbi request reprint Real-time observation of trigger factor function on translating ribosomes
    Christian M Kaiser
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Nature 444:455-60. 2006
    ..These findings can explain how TF prevents misfolding events during translation and may provide a paradigm for the regulation of nucleotide-independent chaperones...
  30. ncbi request reprint Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p
    Zdravko Dragovic
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Biol Chem 387:1593-600. 2006
    ..Interestingly, Fes1p inhibits the stimulation of Ssb1p ATPase by RAC, suggesting a complex regulatory role of Fes1p in modulating the function of Ssb Hsp70s in co-translational protein folding...
  31. pmc TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
    Katja Siegers
    Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, D 82152 Martinsried, Germany
    EMBO J 22:5230-40. 2003
    ..These findings expand the substrate range of the eukaryotic chaperonin by a structurally defined class of proteins and demonstrate an essential role for upstream chaperones in TRiC-assisted folding...
  32. ncbi request reprint Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei
    Daniel Klunker
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    J Biol Chem 278:33256-67. 2003
    ....
  33. ncbi request reprint Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90
    J C Young
    Department of Cellular Biochemistry, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 273:18007-10. 1998
    ..In reticulocyte lysate, the C90 fusion protein recognized the TPR proteins p60, FKBP52, and Cyp40. Thus, our results identify the C90 domain as the specific binding site for a set of hsp90 cofactors having TPR domains...
  34. ncbi request reprint Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Cell 125:903-14. 2006
    ..We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways...
  35. doi request reprint Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein
    Sigrun Polier
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Mol Biol 401:696-707. 2010
    ..Under extreme stress conditions, Sse2p appears to take over the nucleotide exchange factor function of Sse1p and might promote the controlled aggregation of stress-denatured proteins...
  36. ncbi request reprint SnapShot: molecular chaperones, Part II
    Yun Chi Tang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    Cell 128:412. 2007
  37. ncbi request reprint Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains
    Sladjana Tomic
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    FEBS Lett 580:72-6. 2006
    ..Thus, TF is not a general shield for nascent chains. Protease protection appears to depend on a hydrophobic interaction of TF with nascent polypeptides...
  38. pmc Versatility of trigger factor interactions with ribosome-nascent chain complexes
    Sathish Kumar Lakshmipathy
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried 82152, Germany
    J Biol Chem 285:27911-23. 2010
    ..Thus, unlike other chaperones, TF appears to employ multiple mechanisms to interact with a wide range of substrate proteins...
  39. pmc Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    Zdravko Dragovic
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    EMBO J 25:2519-28. 2006
    ..Similarly, deletion of SSE1 causes a firefly luciferase folding defect in yeast cells under heat stress in vivo. Our data indicate that Hsp110 proteins are important components of the eukaryotic Hsp70 machinery of protein folding...
  40. doi request reprint Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei
    Angela M Hirtreiter
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Mol Microbiol 74:1152-68. 2009
    ..Thus, the group II chaperonins may have facilitated the evolution of the highly complex proteomes characteristic of eukaryotic cells...
  41. pmc Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    Hideki Sakahira
    Max Planck Institut fur Biochemie, Department of Cellular Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 99:16412-8. 2002
    ..These recent findings suggest that an imbalance between the neuronal chaperone capacity and the production of potentially dangerous polyQ proteins may trigger the onset of polyQ disease...
  42. ncbi request reprint Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    Jason C Young
    Cellular Biochemistry, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Cell 112:41-50. 2003
    ..We outline a novel mechanism in which chaperones are recruited for a specific targeting event by a membrane-bound receptor...
  43. pmc Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
    Alexander Brychzy
    Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    EMBO J 22:3613-23. 2003
    ..We propose a novel mechanism in which Tpr2 mediates the retrograde transfer of substrates from Hsp90 onto Hsp70. At normal levels substoichiometric to Hsp90 and Hsp70, this activity optimizes the function of the multichaperone machinery...
  44. ncbi request reprint Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    Yasuhito Shomura
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 17:367-79. 2005
    ..In contrast, BAG-1 and GrpE trigger a conserved conformational change in lobe II of the ATPase domain. Thus, nucleotide exchange on eukaryotic Hsp70 occurs through two distinct mechanisms...
  45. ncbi request reprint A sensitive filter retention assay for the detection of PrP(Sc) and the screening of anti-prion compounds
    K F Winklhofer
    Department of Cellular Biochemistry, , D-82152, Martinsried, Germany
    FEBS Lett 503:41-5. 2001
    ..Laborious steps such as SDS-PAGE and Western blotting are avoided with concomitant gain in sensitivity and reliability. The new procedure also proved useful in a screen for anti-prion compounds in a scrapie-infected cell culture model...
  46. doi request reprint Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli
    Rashmi Gupta
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    FEBS Lett 584:3620-4. 2010
    ..By delaying folding relative to translation, the PPIase domain may increase the propensity of misfolding for certain eukaryotic proteins that rely on a mechanism of co-translational, domain-wise folding...
  47. doi request reprint Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
    Kausik Chakraborty
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 142:112-22. 2010
    ..The capacity to rescue proteins from such folding traps may explain the uniquely essential role of chaperonin cages within the cellular chaperone network...
  48. ncbi request reprint Identification of nascent chain interaction sites on trigger factor
    Sathish K Lakshmipathy
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Biol Chem 282:12186-93. 2007
    ..Our data indicate the existence of two regions on TF along which nascent chains can interact, the NC-domains as the main site and the PPIase domain as an auxiliary site...
  49. doi request reprint The role of molecular chaperones in human misfolding diseases
    Sarah A Broadley
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    FEBS Lett 583:2647-53. 2009
    ..Further understanding of the role of Hsp70, TRiC, and other chaperones in misfolding disease is likely to provide important insight into basic pathomechanistic principles that could potentially be exploited for therapeutic purposes...
  50. ncbi request reprint SnapShot: molecular chaperones, Part I
    Hung chun Chang
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    Cell 128:212. 2007
  51. ncbi request reprint Mitochondrial stress signaling: a pathway unfolds
    Sarah A Broadley
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Trends Cell Biol 18:1-4. 2008
    ..These findings suggest that molecular aspects of stress sensing might be conserved between bacteria and mitochondria...
  52. doi request reprint Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    Sigrun Polier
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 133:1068-79. 2008
    ....
  53. ncbi request reprint Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco
    Sandra Saschenbrecker
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 129:1189-200. 2007
    ..The strategies employed by RbcX in achieving substrate specificity and efficient product release may be generally relevant in assisted assembly reactions...
  54. ncbi request reprint Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model
    Niclas W Schiffer
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Biol Chem 282:9195-203. 2007
    ....
  55. pmc L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle
    Silke Grallath
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
    EMBO Rep 7:78-84. 2006
    ..These results identify L25 as a conserved interaction platform for specific cytosolic factors that guide nascent polypeptides to their proper cellular destination...
  56. pmc Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ
    Julio O Ortiz
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    J Cell Biol 190:613-21. 2010
    ..In situ studies with intact E. coli cells allowed us to demonstrate that 100S ribosomes do exist in vivo and represent an easily reversible state of quiescence; they readily vanish when the growth medium is replenished...
  57. doi request reprint The three-dimensional organization of polyribosomes in intact human cells
    Florian Brandt
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 39:560-9. 2010
    ..The distinct neighbor orientations found in situ resemble configurations of bacterial polysomes in vitro, indicating a conserved supramolecular organization with implications for nascent polypeptide folding...
  58. doi request reprint N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function
    Niclas W Schiffer
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Biol Chem 389:1455-66. 2008
    ....
  59. ncbi request reprint Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes
    Achim Brinker
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 277:19265-75. 2002
    ..Ile-4 in Hsp70 and Met-4 in Hsp90 are most important in determining the specific binding of TPR1 and TPR2A, respectively...
  60. ncbi request reprint Crystal structure of an archaeal actin homolog
    Annette Roeben
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Mol Biol 358:145-56. 2006
    ..Intriguingly, both genera are characterized by the lack of a cell wall, and therefore Ta0583 could have a function in cellular organization...
  61. ncbi request reprint A stress sensor for the bacterial periplasm
    Jason C Young
    Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Cell 113:1-2. 2003
    ..This interaction relieves the inhibition of the neighboring protease domain of DegS, triggering a proteolysis cascade that leads to the sigma(E)-driven expression of periplasmic chaperones...
  62. ncbi request reprint Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3
    Annette Haacke
    Dept of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Hum Mol Genet 15:555-68. 2006
    ..These results establish the critical role of C-terminal, proteolytic fragments of AT3 in the molecular pathomechanism of SCA3, in strong support of the toxic fragment hypothesis...
  63. ncbi request reprint Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3
    Annette Haacke
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    J Biol Chem 282:18851-6. 2007
    ..These findings suggest a critical role of calpains in the pathogenesis of Spinocerebellar ataxia type 3...
  64. ncbi request reprint Pathways of chaperone-mediated protein folding in the cytosol
    Jason C Young
    Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada
    Nat Rev Mol Cell Biol 5:781-91. 2004
    ....
  65. ncbi request reprint A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP
    Rosalina Fonseca
    Department of Cellular and Systems Neurobiology, Max Planck Institute of Neurobiology, Am Klopferspitz 18, 82152 München Martinsried, Germany
    Neuron 52:239-45. 2006
    ..Instead, these findings point to a more facetted model, in which L-LTP is determined by the combined action of synthesis and degradation of plasticity proteins...
  66. pmc Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets
    Uwe Bertsch
    Zentrum für Neuropathologie und Prionforschung, Ludwig Maximilians Universitat, Feodor Lynen Str 23, D 81377 Munchen, Germany
    J Virol 79:7785-91. 2005
    ..Moreover, SIFT-based screening may facilitate the search for drugs against other diseases linked to protein aggregation...
  67. pmc In vivo analysis of the overlapping functions of DnaK and trigger factor
    Pierre Genevaux
    Departement de Biochimie Medicale, Centre Medical Universitaire, Geneve, Switzerland
    EMBO Rep 5:195-200. 2004
    ..coli is not totally dependent on an interaction with either TF and/or DnaK, and suggest that additional chaperones may be involved in this essential process...
  68. ncbi request reprint Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    Jose M Barral
    Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA
    Science 295:669-71. 2002
    ..Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans...
  69. pmc Chaperones increase association of tau protein with microtubules
    Fei Dou
    Fisher Center for Research on Alzheimer s Disease, Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Proc Natl Acad Sci U S A 100:721-6. 2003
    ..Our results suggest that up-regulation of molecular chaperones may suppress formation of neurofibrillary tangles by partitioning tau into a productive folding pathway and thereby preventing tau aggregation...
  70. ncbi request reprint Towards a complete structure of Hsp90
    Andreas Bracher
    Structure 13:501-2. 2005
  71. ncbi request reprint Hsp90 structure: when two ends meet
    Andreas Bracher
    Nat Struct Mol Biol 13:478-80. 2006
  72. ncbi request reprint The dynamic tunnel
    Stephanie A Etchells
    Nat Struct Mol Biol 11:391-2. 2004
  73. ncbi request reprint Paper of the Year 2002: Award to Cordelia Schiene-Fischer
    F Ulrich Hartl
    Biol Chem 384:1253-4. 2003
  74. ncbi request reprint Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptor
    Ulrike Schmidt
    Max Planck Institute of Psychiatry, Kraepelinstrasse 10, D 80804 Munich, Germany
    J Biol Chem 278:4926-31. 2003
    ..Thus, DNA binding and hsp70 interaction are required in cis. We propose that the nonsequence-specific DNA-binding protein BAG-1 acts at specific chromosomal loci by interacting with other proteins...
  75. ncbi request reprint Chaperones and transcriptional regulation by nuclear receptors
    Jason C Young
    Nat Struct Biol 9:640-2. 2002
  76. ncbi request reprint Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90
    Gabriela M Wochnik
    Max Planck Institute of Psychiatry, Kraepelinstrasse 10, D 80804 Munich, Germany
    FEBS Lett 560:35-8. 2004
    ..Importantly, similar results were obtained with a constitutively active GR. Thus, the action of p23 on the nuclear stage of GR regulation requires its Hsp90 co-chaperone function, but not its chaperone activity...