Protein abundance profiling of the Escherichia coli cytosol (2008)
Ishihama, Yasushi, Schmidt, Thorsten, Rappsilber, Juri, Mann, Matthias, Hartl, F Ulrich, Kerner, Michael J, ...
Abstract Background Knowledge about the abundance of molecular components is an important prerequisite for building quantitative predictive models of cellular behavior. Proteins are central...
Rosenhagen, Marcus C., Sõti, Csaba, Schmidt, Ulrike, Wochnik, Gabriela M., Hartl, F. Ulrich, Holsboer, Florian, ...
Brinker,Achim, Scheufler,Clemens, Von Der Mülbe,Florian, Fleckenstein,Burkhard, Herrmann,Christian, Jung,Günther, ...
Protein-protein interaction modules containing so-called tetratricopeptide repeats (TPRs) mediate the assembly of Hsp70/Hsp90 multi-chaperone complexes. The TPR1 and TPR2A domains of the Hsp70/Hsp90...
Brinker, Achim, Scheufler, Clemens, Von Der Mülbe, Florian, Fleckenstein, Burkhard, Herrmann, Christian, Jung, Günther, ...
Protein-protein interaction modules containing so-called tetratricopeptide repeats (TPRs) mediate the assembly of Hsp70/Hsp90 multi-chaperone complexes. The TPR1 and TPR2A domains of the Hsp70/Hsp90...
Moroi, Yoichi, Mayhew, Mark, Trcka, Jiri, Hoe, Mee H., Takechi, Yoshizumi, Hartl, F. Ulrich, ...
Heat shock proteins 70 (hsp70) derived from tissues and cells can elicit cytotoxic T lymphocyte (CTL) responses against peptides bound to hsp70. However, peptides can markedly differ in their...
Muchowski, Paul J., Schaffar, Gregor, Sittler, Annie, Wanker, Erich E., Hayer-Hartl, Manajit K., Hartl, F. Ulrich
The deposition of protein aggregates in neurons is a hallmark of neurodegenerative diseases caused by polyglutamine (polyQ) proteins. We analyzed the effects of the heat shock protein (Hsp) 70...
Fändrich, Marcus, Tito, Mark A., Leroux, Michel R., Rostom, Adam A., Hartl, F. Ulrich, Dobson, Christopher M., ...
We have analyzed a newly described archaeal GimC/prefoldin homologue, termed MtGimC, by using nanoflow electrospray coupled with time-of-flight MS. The molecular weight of the complex from...
Mass spectrometry of ribosomes and ribosomal subunits
Benjamin, Dennis R., Robinson, Carol V., Hendrick, Joseph P., Hartl, F. Ulrich, Dobson, Christopher M.
Nanoflow electrospray ionization has been used to introduce intact Escherichia coli ribosomes into the ion source of a mass spectrometer. Mass spectra of remarkable quality result from a partial, but...
Detection and selective dissociation of intact ribosomes in a mass spectrometer
Rostom, Adam A., Fucini, Paola, Benjamin, Dennis R., Juenemann, Ralf, Nierhaus, Knud H., Hartl, F. Ulrich, ...
Intact Escherichia coli ribosomes have been projected into the gas phase of a mass spectrometer by means of nanoflow electrospray techniques. Species with mass/charge ratios in excess of 20,000 were...
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
Sakahira, Hideki, Breuer, Peter, Hayer-Hartl, Manajit K., Hartl, F. Ulrich
The formation of insoluble protein aggregates in neurons is a hallmark of neurodegenerative diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the mechanistic...
Chaperones increase association of tau protein with microtubules
Dou, Fei, Netzer, William J., Tanemura, Kentaro, Li, Feng, Hartl, F. Ulrich, Takashima, Akihiko, ...
Molecular chaperones and their functions in protein folding have been implicated in several neurodegenerative diseases, including Parkinson's disease and Huntington's disease, which are characterized...
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
Brychzy, Alexander, Rein, Theo, Winklhofer, Konstanze F., Hartl, F.Ulrich, Young, Jason C., Obermann, Wolfgang M.J.
In the eukaryotic cytosol, Hsp70 and Hsp90 cooperate with various co-chaperone proteins in the folding of a growing set of substrates, including the glucocorticoid receptor (GR). Here, we analyse the...
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P., Böttcher, Ulrike M.K., Guha, Suranjana, Hartl, F.Ulrich
The role in protein folding of the eukaryotic chaperonin TRiC/CCT is only partially understood. Here, we show that a group of WD40 β-propeller proteins in the yeast cytosol interact transiently with...
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
Young, Jason C., Hartl, F.Ulrich
The molecular chaperone Hsp90 binds and hydrolyses ATP, but how this ATPase activity regulates the interaction of Hsp90 with a polypeptide substrate is not yet understood. Using the glucocorticoid...
Bertsch, Uwe, Winklhofer, Konstanze F., Hirschberger, Thomas, Bieschke, Jan, Weber, Petra, Hartl, F. Ulrich, ...
Conformational changes and aggregation of specific proteins are hallmarks of a number of diseases, like Alzheimer's disease, Parkinson's disease, and prion diseases. In the case of prion diseases,...
In vivo analysis of the overlapping functions of DnaK and trigger factor
Genevaux, Pierre, Keppel, France, Schwager, Françoise, Langendijk-Genevaux, Petra S, Hartl, F Ulrich, Georgopoulos, Costa
Trigger factor (TF) is a ribosome-bound protein that combines catalysis of peptidyl-prolyl isomerization and chaperone-like activities in Escherichia coli. TF was shown to cooperate with the DnaK...
Moroi, Yoichi, Mayhew, Mark, Trcka, Jiri, Hoe, Mee H., Takechi, Yoshizumi, Hartl, F. Ulrich, ...
Heat shock proteins 70 (hsp70) derived from tissues and cells can elicit cytotoxic T lymphocyte (CTL) responses against peptides bound to hsp70. However, peptides can markedly differ in their...
Muchowski, Paul J., Schaffar, Gregor, Sittler, Annie, Wanker, Erich E., Hayer-Hartl, Manajit K., Hartl, F. Ulrich
The deposition of protein aggregates in neurons is a hallmark of neurodegenerative diseases caused by polyglutamine (polyQ) proteins. We analyzed the effects of the heat shock protein (Hsp) 70...
Fändrich, Marcus, Tito, Mark A., Leroux, Michel R., Rostom, Adam A., Hartl, F. Ulrich, Dobson, Christopher M., ...
We have analyzed a newly described archaeal GimC/prefoldin homologue, termed MtGimC, by using nanoflow electrospray coupled with time-of-flight MS. The molecular weight of the complex from...
Mass spectrometry of ribosomes and ribosomal subunits
Benjamin, Dennis R., Robinson, Carol V., Hendrick, Joseph P., Hartl, F. Ulrich, Dobson, Christopher M.
Nanoflow electrospray ionization has been used to introduce intact Escherichia coli ribosomes into the ion source of a mass spectrometer. Mass spectra of remarkable quality result from a partial, but...
Detection and selective dissociation of intact ribosomes in a mass spectrometer
Rostom, Adam A., Fucini, Paola, Benjamin, Dennis R., Juenemann, Ralf, Nierhaus, Knud H., Hartl, F. Ulrich, ...
Intact Escherichia coli ribosomes have been projected into the gas phase of a mass spectrometer by means of nanoflow electrospray techniques. Species with mass/charge ratios in excess of 20,000 were...
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
Sakahira, Hideki, Breuer, Peter, Hayer-Hartl, Manajit K., Hartl, F. Ulrich
The formation of insoluble protein aggregates in neurons is a hallmark of neurodegenerative diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the mechanistic...
Chaperones increase association of tau protein with microtubules
Dou, Fei, Netzer, William J., Tanemura, Kentaro, Li, Feng, Hartl, F. Ulrich, Takashima, Akihiko, ...
Molecular chaperones and their functions in protein folding have been implicated in several neurodegenerative diseases, including Parkinson's disease and Huntington's disease, which are characterized...
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
Brychzy, Alexander, Rein, Theo, Winklhofer, Konstanze F., Hartl, F.Ulrich, Young, Jason C., Obermann, Wolfgang M.J.
In the eukaryotic cytosol, Hsp70 and Hsp90 cooperate with various co-chaperone proteins in the folding of a growing set of substrates, including the glucocorticoid receptor (GR). Here, we analyse the...
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P., Böttcher, Ulrike M.K., Guha, Suranjana, Hartl, F.Ulrich
The role in protein folding of the eukaryotic chaperonin TRiC/CCT is only partially understood. Here, we show that a group of WD40 β-propeller proteins in the yeast cytosol interact transiently with...
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
Young, Jason C., Hartl, F.Ulrich
The molecular chaperone Hsp90 binds and hydrolyses ATP, but how this ATPase activity regulates the interaction of Hsp90 with a polypeptide substrate is not yet understood. Using the glucocorticoid...
Bertsch, Uwe, Winklhofer, Konstanze F., Hirschberger, Thomas, Bieschke, Jan, Weber, Petra, Hartl, F. Ulrich, ...
Conformational changes and aggregation of specific proteins are hallmarks of a number of diseases, like Alzheimer's disease, Parkinson's disease, and prion diseases. In the case of prion diseases,...
In vivo analysis of the overlapping functions of DnaK and trigger factor
Genevaux, Pierre, Keppel, France, Schwager, Françoise, Langendijk-Genevaux, Petra S, Hartl, F Ulrich, Georgopoulos, Costa
Trigger factor (TF) is a ribosome-bound protein that combines catalysis of peptidyl-prolyl isomerization and chaperone-like activities in Escherichia coli. TF was shown to cooperate with the DnaK...
Grallath, Silke, Schwarz, Juliane P, Böttcher, Ulrike M K, Bracher, Andreas, Hartl, F Ulrich, Siegers, Katja
The nascent chain-associated complex (NAC) is a dimeric protein complex of archaea and eukarya that interacts with ribosomes and translating polypeptide chains. We show that, in yeast, NAC and the...
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
Dragovic, Zdravko, Broadley, Sarah A, Shomura, Yasuhito, Bracher, Andreas, Hartl, F Ulrich
Hsp70 molecular chaperones function in protein folding in a manner dependent on regulation by co-chaperones. Hsp40s increase the low intrinsic ATPase activity of Hsp70, and nucleotide exchange...
Protein abundance profiling of the Escherichia coli cytosol
Ishihama, Yasushi, Schmidt, Thorsten, Rappsilber, Juri, Mann, Matthias, Hartl, F Ulrich, Kerner, Michael J, ...
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
Obermann, Wolfgang M.J., Sondermann, Holger, Russo, Alicia A., Pavletich, Nikola P., Hartl, F. Ulrich
Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol, is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress-denatured...
Hsp90: a specialized but essential protein-folding tool
Young, Jason C., Moarefi, Ismail, Hartl, F. Ulrich
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.