Search Results - "Hartl, F U"

The nucleolus functions as a phase-separated protein quality control compartment by Frottin, F, Schueder, F, Tiwary, S, Gupta, R, Körner, R, Schlichthaerle, T, Cox, J, Jungmann, R, Hartl, F U, Hipp, M S

“…The nuclear proteome is rich in stress-sensitive proteins, which suggests that effective protein quality control mechanisms are in place to ensure…”
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The formation, function and regulation of amyloids: insights from structural biology by Landreh, M., Sawaya, M. R., Hipp, M. S., Eisenberg, D. S., Wüthrich, K., Hartl, F. U.

“…Amyloid diseases are characterized by the accumulation of insoluble, β‐strand‐rich aggregates. The underlying structural conversions are closely associated…”
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Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors by Sondermann, Holger, Scheufler, Clemens, Schneider, Christine, Höhfeld, Jörg, F.-Ulrich Hartl, Moarefi, Ismail

“…Bag (Bcl2-associated athanogene) domains occur in a class of cofactors of the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family. Binding of…”
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Molecular Chaperone Functions of Heat-Shock Proteins by Hendrick, J P, Hartl, F

“…Molecular chaperones, many of them so-called heat-shock or stress proteins (hsps), have emerged over recent years as an important topic in cell biology. The…”
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Rubisco condensate formation by CcmM in β-carboxysome biogenesis by Wang, H., Yan, X., Aigner, H., Bracher, A., Nguyen, N. D., Hee, W. Y., Long, B. M., Price, G. D., Hartl, F. U., Hayer-Hartl, M.

“…Cells use compartmentalization of enzymes as a strategy to regulate metabolic pathways and increase their efficiency 1 . The α- and β-carboxysomes of…”
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Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2 by Aigner, H., Wilson, R. H., Bracher, A., Calisse, L., Bhat, J. Y., Hartl, F. U., Hayer-Hartl, M.

“…Plant RuBisCo, a complex of eight large and eight small subunits, catalyzes the fixation of CO₂ in photosynthesis. The low catalytic efficiency of RuBisCo…”
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A zinc finger‐like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates by Szabo, A., Korszun, R., Hartl, F. U., Flanagan, J.

“…The Escherichia coli heat‐shock protein DnaJ cooperates with the Hsp70 homolog DnaK in protein folding in vitro and in vivo. Little is known about the…”
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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage by Schröder, H., Langer, T., Hartl, F.U., Bukau, B.

“…Members of the conserved Hsp70 chaperone family are assumed to constitute a main cellular system for the prevention and the amelioration of stress‐induced…”
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Protein folding in the cytoplasm and the heat shock response by Vabulas, R Martin, Raychaudhuri, Swasti, Hayer-Hartl, Manajit, Hartl, F Ulrich

“…Proteins generally must fold into precise three-dimensional conformations to fulfill their biological functions. In the cell, this fundamental process is aided…”
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Polypeptide Flux through Bacterial Hsp70: DnaK Cooperates with Trigger Factor in Chaperoning Nascent Chains by Teter, Sarah A, Houry, Walid A, Ang, Debbie, Tradler, Thomas, Rockabrand, David, Fischer, Gunter, Blum, Paul, Georgopoulos, Costa, Hartl, F.Ulrich

“…A role for DnaK, the major E. coli Hsp70, in chaperoning de novo protein folding has remained elusive. Here we show that under nonstress conditions DnaK…”
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Protein folding in the cell: competing models of chaperonin function by Ellis, R J, Hartl, F U

“…The long-standing view that polypeptide chains newly synthesized inside cells fold spontaneously to their functional conformations in an energy-independent…”
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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones by Frydman, Judith, Nimmesgern, Elmar, Ohtsuka, Kenzo, Hartl, F. Ulrich

“…The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing…”
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Roles of molecular chaperones in cytoplasmic protein folding by Agashe, Vishwas R., Hartl, F.-Ulrich

“…Newly synthesized polypeptide chains must fold and assemble into unique three-dimensional structures in order to become functionally active. In many cases…”
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Recombination of protein domains facilitated by co-translational folding in eukaryotes by Hartl, F. Ulrich, Netzer, William J

“…The evolution of complex genomes requires that new combinations of pre-existing protein domains successfully fold into modular polypeptides. During eukaryotic…”
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Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle by Höfeld, Jörg, Minami, Yasufumi, Hartl, Franz-Ulrich

“…The Hsc70-interacting protein Hip, a tetratricopeptide repeat protein, participates in the regulation of the eukaryotic 70 kDa heat shock cognate Hsc70. One…”
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Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK by Harrison, Celia J., Hayer-Hartl, Manajit, Di Liberto, Maurizio, F.-Ulrich Hartl, Kuriyan, John

“…The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK…”
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Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity by Langer, T., Pfeifer, G., Martin, J., Baumeister, W., Hartl, F.U.

“…The mechanism of GroEL (chaperonin)‐mediated protein folding is only partially understood. We have analysed structural and functional properties of the…”
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Protein Sorting to Mitochondria: Evolutionary Conservations of Folding and Assembly by Hartl, Franz-Ulrich, Neupert, Walter

“…According to the endosymbiont hypothesis, mitochondria have lost the autonomy of their prokaryotic ancestors. They have to import most of their proteins from…”
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Principles of Chaperone-Assisted Protein Folding: Differences Between in Vitro and in Vivo Mechanisms by Frydman, Judith, Hartl, F. Ulrich

“…Molecular chaperones in the eukaryotic cytosol were shown to interact differently with chemically denatured proteins and their newly translated counterparts…”
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Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits by Frydman, J., Nimmesgern, E., Erdjument‐Bromage, H., Wall, J.S., Tempst, P., Hartl, F.U.

“…T‐complex polypeptide 1 (TCP‐1) was analyzed as a potential chaperonin (GroEL/Hsp60) equivalent of the eukaryotic cytosol. We found TCP‐1 to be part of a…”
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