Search Results - "Ulrich, F"

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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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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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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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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Cellular Homeostasis and Aging by Hartl, F. Ulrich

“…Aging and longevity are controlled by a multiplicity of molecular and cellular signaling events that interface with environmental factors to maintain cellular…”
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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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Mapping a Systematic Ribozyme Fitness Landscape Reveals a Frustrated Evolutionary Network for Self-Aminoacylating RNA by Pressman, Abe D, Liu, Ziwei, Janzen, Evan, Blanco, Celia, Müller, Ulrich F, Joyce, Gerald F, Pascal, Robert, Chen, Irene A

“…Molecular evolution can be conceptualized as a walk over a “fitness landscape”, or the function of fitness (e.g., catalytic activity) over the space of all…”
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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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Enhancing nanopore sensing with DNA nanotechnology by Keyser, Ulrich F.

“…Nanopores are on the brink of fundamentally changing DNA sequencing. At the same time, DNA origami provides unprecedented freedom in molecular design. Here, I…”
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Molecular chaperones in protein folding and proteostasis by Hartl, F. Ulrich, Bracher, Andreas, Hayer-Hartl, Manajit

“…Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are…”
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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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Controlling molecular transport through nanopores by Keyser, Ulrich F.

“…Nanopores are emerging as powerful tools for the detection and identification of macromolecules in aqueous solution. In this review, we discuss the recent…”
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Nanopore-Based DNA Hard Drives for Rewritable and Secure Data Storage by Chen, Kaikai, Zhu, Jinbo, Bošković, Filip, Keyser, Ulrich F

“…Nanopores are powerful single-molecule tools for label-free sensing of nanoscale molecules including DNA that can be used for building designed nanostructures…”
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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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QuipuNet: Convolutional Neural Network for Single-Molecule Nanopore Sensing by Misiunas, Karolis, Ermann, Niklas, Keyser, Ulrich F

“…Nanopore sensing is a versatile technique for the analysis of molecules on the single-molecule level. However, extracting information from data with…”
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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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