Search Results - (Author, Cooperation:F. Ulrich)
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1Articles: DFG German National LicensesGeorgellis, Dimitris ; Sohlberg, Björn ; Hartl, F. Ulrich ; Gabain, Alexander
Oxford, UK : Blackwell Publishing Ltd
Published 1995Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: An RNA-binding activity has been identified in Escherichia coli that provides physical protection of RNA against ribonucleases in an ATP- and Mg2+-dependent manner. This binding activity is stimulated under growth conditions known to cause a decrease in the rate of mRNA decay. RNA protection is mediated by a protein complex that contains a modified form of the chaperonin GroEL as an indispensable constituent. These results suggest a new role for GroEL as an RNA chaperone.Type of Medium: Electronic ResourceURL: -
2Articles: DFG German National LicensesHoury, Walid A. ; Frishman, Dmitrij ; Eckerskorn, Christoph ; Lottspeich, Friedrich ; Hartl, F. Ulrich
[s.l.] : Macmillian Magazines Ltd.
Published 1999Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300 newly translated polypeptides, including essential components of the transcription/translation ...Type of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesMayhew, Mark ; da Silva, Ana C. R. ; Martin, Jörg ; Erdjument-Bromage, Hediye ; Tempst, Paul ; Hartl, F. Ulrich
[s.l.] : Nature Publishing Group
Published 1996Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage. Folded dihydrofolate ...Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesStaff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The evolution of complex genomes requires that new combinations of pre-existing protein domains successfully fold into modular polypeptides. During eukaryotic translation model two-domain polypeptides fold efficiently by sequential and co-translational folding of their domains. In contrast, folding ...Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesKirikae, Teruo ; Kirikae, Fumiko ; Schade, F. Ulrich ; Yoshida, Masao ; Kondo, Seiichi ; Hisatsune, Kazuhito ; Nishikawa, Shin-Ichi ; Rietschel, Ernst Th.
Oxford, UK : Blackwell Publishing Ltd
Published 1991Staff ViewISSN: 1574-6968Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Lipopolysaccharide-(LPS) binding proteins present on murine-lymphocyte and macrophage-like cell lines were identified by a ligand-blotting method and subsequent immunological detection of bound LPS. Membrane proteins of the murine-pre-B-cell line 70Z/3 were separated by SDS-PAGE, transferred electrophoretically onto nitrocellulose, and the blot was incubated with LPS of the Salmonella minnesota Re-mutant R595 (mRe-LPS). LPS bound to proteins on nitrocellulose was immunologically detected by anti-mRe-LPS antibodies; LPS was associated with one of the membrane proteins of 70Z/3 cells. This protein was 40 kDa under reducing and 45 kDa under non-reducing conditions, respectively. Treatment of 70Z/3 cells with pronase led to the disappearance of the LPS-binding protein indicating its surface location. Excess free lipid A, which represents the biologically active region of LPS, inhibited the binding of mRe-LPS to the protein. This LPS-binding protein was also identified on the pre-B-cell line CYG8, the B-cell line CYG101 and the murine-T-cell line BW5147. It was, however, not detectable on the B-cell line CYG34 and the myeloma-cell line P3-X63-Ag8.653. No other LPS-binding protein could be detected on these cell lines. In the murine-macrophage-like cell line J774.1, two LPS-binding proteins, one of 40 kDa and one of 80 kDa, were detected. These results indicate that mRe-LPS is specifically bound to a 40-kDa protein of lymphocytes, whereas in the case of macrophages it is associated with two LPS-binding proteins of 40 and 80 kDa.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesMajetschak, M. ; Obertacke, U. ; Waydhas, C. ; Nast-Kolb, D. ; Schade, F. Ulrich
Springer
Published 2000Staff ViewISSN: 1433-044XKeywords: Schlüsselwörter Sepsis ; Multiorganversagen ; Trauma ; Mediatorenmodulation ; Sepsistherapie ; inflammatorische Reaktion ; ZytokineSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Zusammenfassung In einer Übersichtsarbeit von Abraham & Marshall (1999) wurde dargelegt, dass sämtliche, an über 15.000 Patienten durchgeführten Studien mit dem Ziel der Beeinflussung der dysregulierten, inflammatorischen Reaktion bei Sepsis und Multiorganversagen enttäuschende Ergebnisse aufwiesen. Ursache hierfür liegt vorrangig in dem theoretischen Konzept einer isolierten,überschießenden Bildung endogener proinflammatorischer Mediatoren ( z.B. TNF, Interleukine, PAF), welche durch Autodestruktion zur Entwicklung eines septischen Multiorganversagens führen.Untersuchungen der letzten Jahre zeigen jedoch, dass eine inflammatorische Reaktion nicht mit einer isolierten Ausschüttung proinflammatorischer Mediatoren einhergeht, sondern gleichzeitig eine erhebliche antiinflammatorische Reaktion nachweisbar ist, die proinflammatorische Reaktion eine essentielle Komponente einer adäquaten Wirtsreaktion darstellt und aufgrund der hohen Redundanz des Zytokinnetzwerkes der therapeutische Ansatz einer Neutralisation eines einzelnen Mediators nicht mehr gerechtfertigt ist. Zukünftige mediatormodulatorische Therapieansätze setzten neben einer Charakterisierung möglicher individueller inflammatorischer Reaktionsformen und der Identifizierung klinisch relevanter immunologischer Parameter ein engmaschiges immunologisches Monitoring voraus, wodurch eine individuell adaptierte Mediatormodulation ermöglicht wird.Type of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesTrent, Jonathan D. ; Nimmesgern, Elmar ; Wall, Joseph S. ; Hartl, F.-Ulrich ; Horwich, Arthur L.
[s.l.] : Nature Publishing Group
Published 1991Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] TF55 was purified from the soluble portion of Triton X-100 cell extracts by anion exchange chromatography and glycerol gradient sedimentation. Most of the TF55 sedimented in the gradient at 20S (Fig. la). No nucleic acid was found by spectro-photometry in the 20S fraction, suggesting that ...Type of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesMartin, Jörg ; Langer, Thomas ; Boteva, Raina ; Schramel, Andrea ; Horwich, Arthur L. ; Hartl, F.-Ulrich
[s.l.] : Nature Publishing Group
Published 1991Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg–ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. ...Type of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesStaff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] THE high-resolution structure of the molecular chaperone protein GroEL from Escherichia coli, presented by Braig et al.1 on page 578 of this issue, will cause a stir in the many laboratories interested in the process of cellular protein folding. As an immediate application, the ...Type of Medium: Electronic ResourceURL: -
10Articles: DFG German National LicensesFrydman, Judith ; Nimmesgern, Elmar ; Ohtsuka, Kenzo ; Hartl, F. Ulrich
[s.l.] : Nature Publishing Group
Published 1994Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the ...Type of Medium: Electronic ResourceURL: -
11Articles: DFG German National LicensesMartin, Jörg ; Geromanos, Scott ; Tempest, Paul ; Hartl, F. Ulrich
[s.l.] : Nature Publishing Group
Published 1993Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The double-toroid GroEL protein has 14 ATP binding sites8. Binding of GroES stabilizes the interacting seven-subunit ring of GroEL in a high-affinity state for ADP and also favours ADP binding to the opposite toroid9. This results in an inhibition of the GroEL ATPase10'12. Binding of ...Type of Medium: Electronic ResourceURL: -
12Articles: DFG German National LicensesRobinson, Carol V. ; Groß, Michael ; Eyles, Stephen J. ; Ewbank, Jonathan J. ; Mayhew, Mark ; Hartl, F. Ulrich ; Dobson, Christopher M. ; Radford, Sheena E.
[s.l.] : Nature Publishing Group
Published 1994Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The conformation of a three-disulphide derivative of bovine α-lactalbumin bound to the molecular chaperone GroEL has been investigated by monitoring directly its hydrogen exchange kinetics using electrospray ionization mass spectrometry. The bound protein is weakly protected from exchange to ...Type of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesOstermann, Joachim ; Horwich, Arthur L. ; Neupert, Walter ; Hartl, F.-Ulrich
[s.l.] : Nature Publishing Group
Published 1989Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochon-dria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides. We propose that hsp60 catalyses protein ...Type of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesCheng, Ming Y. ; Hartl, F.-Ulrich ; Norwich, Arthur L.
[s.l.] : Nature Publishing Group
Published 1990Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] A high-copy (2m,) yeast plasmid, pGalhsp60, containing the Gal-1 promoter joined with the coding sequence for the wild-type hsp60 precursor, was introduced into the mif4 strain, which contains a temperature-sensitive lethal mutation in the hsp60 gene1. At 37 °C (non-permissive temperature) the ...Type of Medium: Electronic ResourceURL: -
15Articles: DFG German National LicensesLanger, Thomas ; Lu, Chi ; Echols, Harrison ; Flanagan, John ; Hayer, Manajit K. ; Hartl, F. Ulrich
[s.l.] : Nature Publishing Group
Published 1992Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. ...Type of Medium: Electronic ResourceURL: -
16Articles: DFG German National LicensesStaff View
ISSN: 1545-9985Source: Nature Archives 1869 - 2009Topics: BiologyMedicineNotes: [Auszug] Hsp90 is one of the most abundant molecular chaperones in the cytosol. In the cell, it exists as a dimer of ∼90-kDa protomers and assists the folding and conformational regulation of a specific set of client proteins, including a multitude of cell-signaling proteins such as steroid hormone ...Type of Medium: Electronic ResourceURL: -
17Articles: DFG German National LicensesStaff View
ISSN: 1545-9985Source: Nature Archives 1869 - 2009Topics: BiologyMedicineNotes: [Auszug] The ribosome is a highly conserved nucleoprotein machine whose function is to translate information encoded in an mRNA into a protein. The nascent polypeptide chain must fold into a defined three-dimensional structure to become functional. But can such a chain begin to fold while still in the ...Type of Medium: Electronic ResourceURL: -
18Articles: DFG German National LicensesKaiser, Christian M. ; Chang, Hung-Chun ; Agashe, Vishwas R. ; Lakshmipathy, Sathish K. ; Etchells, Stephanie A. ; Hayer-Hartl, Manajit ; Hartl, F. Ulrich ; Barral, José M.
[s.l.] : Nature Publishing Group
Published 2006Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The contribution of co-translational chaperone functions to protein folding is poorly understood. Ribosome-associated trigger factor (TF) is the first molecular chaperone encountered by nascent polypeptides in bacteria. Here we show, using fluorescence spectroscopy to monitor TF function and ...Type of Medium: Electronic ResourceURL: -
19Articles: DFG German National LicensesStaff View
ISSN: 1072-8368Source: Nature Archives 1869 - 2009Topics: BiologyMedicineNotes: [Auszug] Nuclear receptors, including the glucocorticoid receptor (GR) and thyroid hormone receptor (TR), selectively activate transcription of certain genes in response to the presence of their small molecule ligands. The cytoplasmic chaperone Hsp90 has long been known to be essential for the function of ...Type of Medium: Electronic ResourceURL: -
20Articles: DFG German National LicensesWeber, Frank ; Keppel, France ; Georgopoulos, Costa ; Hayer-Hartl, Manajit K. ; Hartl, F. Ulrich
[s.l.] : Nature America Inc.
Published 1998Staff ViewISSN: 1072-8368Source: Nature Archives 1869 - 2009Topics: BiologyMedicineNotes: [Auszug] Two models are being considered for the mechanism of chaperonin-assisted protein folding in E. coli: (i) GroEL/GroES act primarily by enclosing substrate polypeptide in a folding cage in which aggregation is prevented during folding. (ii) GroEL mediates the repetitive unfolding of misfolded ...Type of Medium: Electronic ResourceURL: