Search Results - "Hartl, F. Ulrich"

Protein Misfolding Diseases by Hartl, F. Ulrich

“…The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a…”
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The proteostasis network and its decline in ageing by Hipp, Mark S., Kasturi, Prasad, Hartl, F. Ulrich

“…Ageing is a major risk factor for the development of many diseases, prominently including neurodegenerative disorders such as Alzheimer disease and Parkinson…”
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In vivo aspects of protein folding and quality control by Balchin, David, Hayer-Hartl, Manajit, Hartl, F. Ulrich

“…Most proteins must fold into unique three-dimensional structures to perform their biological functions. In the crowded cellular environment, newly synthesized…”
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Pathways of cellular proteostasis in aging and disease by Klaips, Courtney L, Jayaraj, Gopal Gunanathan, Hartl, F Ulrich

“…Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein synthesis, folding, conformational maintenance, and degradation. A…”
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The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding by Hayer-Hartl, Manajit, Bracher, Andreas, Hartl, F. Ulrich

“…The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic molecular machine of protein folding. GroEL is a large double-ring cylinder…”
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Molecular chaperone functions in protein folding and proteostasis by Kim, Yujin E, Hipp, Mark S, Bracher, Andreas, Hayer-Hartl, Manajit, Hartl, F Ulrich

“…The biological functions of proteins are governed by their three-dimensional fold. Protein folding, maintenance of proteome integrity, and protein homeostasis…”
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Converging concepts of protein folding in vitro and in vivo by Hartl, F Ulrich, Hayer-Hartl, Manajit

“…Most proteins must fold into precise three-dimensional conformations to fulfill their biological functions. Here we review recent concepts emerging from…”
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Chaperone Machineries of Rubisco – The Most Abundant Enzyme by Hayer-Hartl, Manajit, Hartl, F. Ulrich

“…A major challenge faced by human civilization is to ensure that agricultural productivity keeps pace with population growth and a changing climate. All food…”
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Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein by Imamoglu, Rahmi, Balchin, David, Hayer-Hartl, Manajit, Hartl, F. Ulrich

“…The ATP-dependent Hsp70 chaperones (DnaK in E. coli ) mediate protein folding in cooperation with J proteins and nucleotide exchange factors ( E. coli DnaJ and…”
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Recent advances in understanding catalysis of protein folding by molecular chaperones by Balchin, David, Hayer‐Hartl, Manajit, Hartl, F. Ulrich

“…Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein…”
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Biogenesis and Metabolic Maintenance of Rubisco by Bracher, Andreas, Whitney, Spencer M, Hartl, F. Ulrich, Hayer-Hartl, Manajit

“…Ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco) mediates the fixation of atmospheric CO 2 in photosynthesis by catalyzing the carboxylation of the…”
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Functional Modules of the Proteostasis Network by Jayaraj, Gopal G, Hipp, Mark S, Hartl, F Ulrich

“…Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis) and prevent the accumulation of potentially toxic protein…”
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Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress by Leitman, Julia, Ulrich Hartl, F., Lederkremer, Gerardo Z.

“…In Huntington’s disease, as in other neurodegenerative diseases, it was initially thought that insoluble protein aggregates are the toxic species. However,…”
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Proteostasis impairment in protein-misfolding and -aggregation diseases by Hipp, Mark S, Park, Sae-Hun, Hartl, F. Ulrich

“…Highlights • Cells possess a complex proteostasis network (PN) to ensure protein homeostasis. • Aggregates permanently engage molecular chaperones and other PN…”
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Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors by Kim, Yujin E., Hosp, Fabian, Frottin, Frédéric, Ge, Hui, Mann, Matthias, Hayer-Hartl, Manajit, Hartl, F. Ulrich

“…Huntington’s disease is one of several neurodegenerative disorders characterized by the aggregation of polyglutamine (polyQ)-expanded mutant protein. How polyQ…”
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The chaperone Clusterin in neurodegeneration−friend or foe? by Yuste‐Checa, Patricia, Bracher, Andreas, Hartl, F. Ulrich

“…Fibrillar protein aggregates are the pathological hallmark of a group of age‐dependent neurodegenerative conditions, including Alzheimer's and Parkinson's…”
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Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis by Izawa, Toshiaki, Park, Sae-Hun, Zhao, Liang, Hartl, F. Ulrich, Neupert, Walter

“…Eukaryotic cells have evolved extensive protein quality-control mechanisms to remove faulty translation products. Here, we show that yeast cells continually…”
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In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment by Guo, Qiang, Lehmer, Carina, Martínez-Sánchez, Antonio, Rudack, Till, Beck, Florian, Hartmann, Hannelore, Pérez-Berlanga, Manuela, Frottin, Frédéric, Hipp, Mark S., Hartl, F. Ulrich, Edbauer, Dieter, Baumeister, Wolfgang, Fernández-Busnadiego, Rubén

“…Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link…”
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Widespread Proteome Remodeling and Aggregation in Aging C. elegans by Walther, Dirk M., Kasturi, Prasad, Zheng, Min, Pinkert, Stefan, Vecchi, Giulia, Ciryam, Prajwal, Morimoto, Richard I., Dobson, Christopher M., Vendruscolo, Michele, Mann, Matthias, Hartl, F. Ulrich

“…Aging has been associated with a progressive decline of proteostasis, but how this process affects proteome composition remains largely unexplored. Here, we…”
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Spatiotemporal Proteomic Profiling of Huntington’s Disease Inclusions Reveals Widespread Loss of Protein Function by Hosp, Fabian, Gutiérrez-Ángel, Sara, Schaefer, Martin H., Cox, Jürgen, Meissner, Felix, Hipp, Mark S., Hartl, F.-Ulrich, Klein, Rüdiger, Dudanova, Irina, Mann, Matthias

“…Aggregation of polyglutamine-expanded huntingtin exon 1 (HttEx1) in Huntington’s disease (HD) proceeds from soluble oligomers to late-stage inclusions. The…”
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