HARTL, FRANZ ULRICH / Médecine / Chercheurs

Centre International de Recherche Scientifique

Chercheurs

Médecine / HARTL, FRANZ ULRICH

uhartlbiochem.mpg.de

Position

Managing Director of the Max Planck-Institut für Biochemie, Department of Cellular Biochemistry, Martinsreid, Germany.

Thèmes de recherche

Ongoing research focuses on the problem of protein folding in vivo. The main group of Ulrich Hartl is investigating the co- and post-translational events in folding in the cytosol and the involvement of molecular chaperones in that process.

Prix et récompenses

2004 International Gairdner Award Winner

Publications

Schaffar G, Breuer P, Boteva R, Behrends C, Tzvetkov N, Strippel N, Sakahira H, Siegers K, Hayer-Hartl M, Hartl FU.
Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation.
Mol Cell. 2004 Jul 2; in press

Etchells SA , Hartl FU.
The dynamic tunnel.
Nat Struct & Mol Biol. 2004; 11(5): 391-92

Agashe VR, Guha S, Chang H-C, Genevaux P, Hayer-Hartl M, Stemp M, Georgopoulos C, Hartl FU, Barral JM.
Function of trigger factor and DnaK in multi-domain protein folding: Increase in yield at the expense of folding speed.
Cell. 2004; 117: 199-209

Barral JM, Broadley SA, Schaffar G, Hartl FU.
Roles of molecular chaperones in protein folding diseases.
Semin Cell Dev Biol. 2004; 15(1): 17-29

Genevaux P, Keppel F, Schwager F, Langendijk-Genevaux PS, Hartl FU, Geogopoulos C.
In vivo analysis of the overlapping functions of DnaK and trigger factor.
EMBO reports. 2004; 5(2): 1-6

Figuereido L, Klunker D, Ang D, Naylor DJ, Kerner MJ, Georgopoulos C, Hartl FU, Hayer-Hartl M.
Functional characterization of an archeal GroEL/GroES chaperonin system: Significance of substrate encapsulation .
J Biol Chem. 2003; 279:1090-99

Young JC, Barral JM, Hartl FU.
More Than folding: Localized functions of cytosolic chaperones.
Trends in Biochem Sci. 2003; 28:541-547

Siegers K, Bölter B, Schwarz JP, Böttcher UMK, Guha S, Hartl FU.
TriC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes.
EMBO J. 2003; 22:5230-40

Brychzy A, Rein T, Winklhofer KF, Hartl FU, Young JC, Obermann WM.
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
EMBO J. 2003 Jul 15;22(14):3613-23

Young JC, Hartl FU.
A stress sensor for the bacterial periplasm.
Cell. 2003 Apr 4;113(1):1-2

Young JC, Hoogenraad NJ, Hartl FU.
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.
Cell 2003 Jan 10;112(1):41-50

Sondermann H, Ho AK, Listenberger LL, Siegers K, Moarefi I, Wente SR, Hartl FU, Young JC.
Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae.
J Biol Chem 2002 Sep 6;277(36):33220-7

Hartl FU, Hayer-Hartl M.
Molecular chaperones in the cytosol: from nascent chain to folded protein.
Science 2002 Mar 8;295(5561):1852-8

Brinker A, Scheufler C, von Der Mulbe F, Fleckenstein B, Herrmann C, Jung G, Moarefi I, Hartl FU.
Ligand discrimination by TPR domains: Relevance and selectivity of EEVD-peptide recognition in Hsp70-Hop-Hsp90 complexes.
J Biol Chem. 2002 May 31;277(22):19265-75

Barral JM, Hutagalung AH, Brinker A, Hartl FU, Epstein HF.
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin.
Science 2002 Jan 25;295(5555):669-71

Stöckel J, Hartl FU.
Chaperonin-mediated de novo generation of prion protein aggregates.
J Mol Biol 2001 Nov 2;313(4):861-72

Naylor DJ, Hartl FU.
Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells.
Biochem Soc Symp 2001;(68):45-68

Young JC, Moarefi I, Hartl FU.
Hsp90: a specialized but essential protein-folding tool.
J Cell Biol 2001 Jul 23;154(2):267-74

Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I.
Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors.
Science 2001 Feb 23;291(5508):1553-1557.

Sondermann H, Becker T, Mayhew M, Wieland F, Hartl FU.
Characterization of a receptor for heat shock protein 70 on macrophages and monocytes.
Biol Chem 2000 Dec;381(12):1165-74.

Leroux MR, Hartl FU.
Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.
Curr Biol 2000 Apr 6;10(7):R260-4. Review.

Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I.
Structure of the molecular chaperone prefoldin. Unique interaction of multiple coiled coil tentacles with unfolded proteins.
Cell 2000 Nov 10;103(4):621-32.

Fändrich M, Tito MA, Leroux MR, Rostom AA, Hartl FU, Dobson CM, Robinson CV.
Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.
Proc Natl Acad Sci U S A 2000 Dec 19;97(26):14151-5.

Young JC, Hartl FU.
Polypeptide release by hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.
EMBO J 2000 Nov 1;19(21):5930-40.

Muchowski, P.J., Schaffar, G., Sittler, A., Wanker, E.E., Hayer-Hartl, M.K. and Hartl, F.U.
Hsp70 and Hsp40 chaperones shift self-association of polyglutamine proteins from amyloidogenic to amorphous aggregation.
Proc Natl Acad Sci U S A 2000 Jul 5;97(14):7841-6.

Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I.
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
Cell 2000 Apr 14;101(2):199-210.

Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU.
Identification of in vivo substrates of the chaperonin GroEL.
Nature 1999 Nov 11;402(6758):147-54.

Leroux MR, Fandrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel E, Dobson CM, Hartl FU.
MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin.
EMBO J 1999 Dec 1;18(23):6730-43.

Tector M, Hartl FU.
An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator.
EMBO J 1999 Nov 15;18(22):6290-8.

Teter SA, Houry WA, Ang D, Tradler T, Rockabrand D, Fischer G, Blum P, Georgopoulos C, Hartl FU.
Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains.
Cell 1999 Jun 11;97(6):755-65.

Hartl FU.
Molecular chaperones in cellular protein folding.
Nature 1996 Jun 13;381(6583):571-9. Review.

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