Prion and non-prion amyloids of the HET-s prion forming domain.

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Journal of Molecular Biology

• Publication date

  2007-07-20

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JMB.2007.05.014PMID 17532341
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• "Prion-proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+].

  2007cited by this paper
• Bsoft: image processing and molecular modeling for electron microscopy.

  2007cited by this paper
• Mass Analysis by Scanning Transmission Electron Microscopy and Electron Diffraction Validate Predictions of Stacked β-Solenoid Model of HET-s Prion Fibrils*

  2007cited by this paper
• The reconstitution of mammalian prion infectivity de novo

  2007cited by this paper
• Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure

  2006cited by this paper
• Sequence and structure analysis of parallel beta helices: implication for constructing amyloid structural models.

  2006cited by this paper
• Recent atomic models of amyloid fibril structure.

  2006cited by this paper
• Prions and their partners in crime

  2006cited by this paper
• Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity.

  2006cited by this paper
• The physical basis of how prion conformations determine strain phenotypes

  2006cited by this paper
• Cell biology: Infectious Alzheimer's disease?

  2006cited by this paper
• Protein misfolding, functional amyloid, and human disease.

  2006cited by this paper
• General structural motifs of amyloid protofilaments

  2006cited by this paper
• Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils.

  2005cited by this paper
• Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.

  2005cited by this paper
• Correlation of structural elements and infectivity of the HET-s prion

  2005cited by this paper
• Prions as adaptive conduits of memory and inheritance

  2005cited by this paper
• Probing the Structure of the Infectious Amyloid Form of the Prion-forming Domain of HET-s Using High Resolution Hydrogen/Deuterium Exchange Monitored by Mass Spectrometry*

  2005cited by this paper
• Prion domains: sequences, structures and interactions

  2005cited by this paper
• Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids.

  2005cited by this paper
• Prion generation in vitro: amyloid of Ure2p is infectious

  2005cited by this paper
• Aspects on human amyloid forms and their fibril polypeptides

  2005cited by this paper
• Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.

  2005cited by this paper
• The binding of thioflavin-T to amyloid fibrils: localisation and implications.

  2005cited by this paper
• 3D structure of Alzheimer's amyloid-beta(1-42) fibrils.

  2005cited by this paper
• Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

  2005cited by this paper
• Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid.

  2005cited by this paper
• Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids*

  2005cited by this paper
• Strain-specific morphologies of yeast prion amyloid fibrils.

  2005cited by this paper
• High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.

  2005cited by this paper
• 3D structure of Alzheimer's amyloid-β(1–42) fibrils

  2005cited by this paper
• Protein-only transmission of three yeast prion strains

  2004cited by this paper
• Conformational variations in an infectious protein determine prion strain differences

  2004cited by this paper
• Dissection and Design of Yeast Prions

  2004cited by this paper
• The Yersinia adhesin YadA collagen‐binding domain structure is a novel left‐handed parallel β‐roll

  2004cited by this paper
• UCSF Chimera—A visualization system for exploratory research and analysis

  2004cited by this paper
• A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure.

  2004cited by this paper
• Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide.

  2004cited by this paper
• Progress towards a molecular-level structural understanding of amyloid fibrils.

  2004cited by this paper
• The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo

  2004cited by this paper
• FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

  2004cited by this paper
• Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide

  2004cited by this paper
• Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.

  2003cited by this paper
• Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserina

  2003cited by this paper
• An autocatalytic reaction as a model for the kinetics of the aggregation of β‐amyloid

  2003cited by this paper
• Amyloid aggregates of the HET-s prion protein are infectious

  2002cited by this paper
• A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.

  2002cited by this paper
• Bsoft: Image and Molecular Processing in Electron Microscopy

  2001cited by this paper
• Bsoft: image and molecular processing in electron microscopy.

  2001cited by this paper
• Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein.

  2000cited by this paper
• A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion.

  1998cited by this paper
• The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog.

  1997cited by this paper
• Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

  1997cited by this paper
• An analysis of side chain interactions and pair correlations within antiparallel β‐sheets: The differences between backbone hydrogen‐bonded and non‐hydrogen‐bonded residue pairs

  1995cited by this paper
• Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions

  1994cited by this paper

• Thioflavin T: induced circular dichroism and density functional theory as promising approach in amyloid fibril assays

  2025cites this paper
• YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies.

  2025cites this paper
• Uncovering supramolecular chirality codes for the design of tunable biomaterials

  2024cites this paper
• The rigid core and flexible surface of amyloid fibrils probed by Magic-Angle Spinning NMR of aromatic residues.

  2023cites this paper
• Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis

  2022cites this paper
• Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars

  2021cites this paper
• Solid state NMR reveals a parallel in register architecture for an infectious recombinant prion

  2021cites this paper
• Hybrid amyloid-based redox hydrogel for bioelectrocatalytic H2 oxidation.

  2021cites this paper
• Partial Prion Cross-Seeding between Fungal and Mammalian Amyloid Signaling Motifs

  2021influential citation
• Identification of NLR-associated amyloid signaling motifs in filamentous bacteria

  2020cites this paper
• Identification of NLR-associated amyloid signaling motifs in bacterial genomes.

  2020cites this paper
• Interplay between α-synuclein amyloid formation and membrane structure.

  2019cites this paper
• Prions and Prion-like assemblies in neurodegeneration and immunity: The emergence of universal mechanisms across health and disease.

  2019cites this paper
• Bacterial Inclusion Bodies for Anti-Amyloid Drug Discovery: Current and Future Screening Methods.

  2019cites this paper
• Auto-assemblage de protéines pour la bioélectronique : étude du tranport de charges dans les fibres amyloïdes

  2018cites this paper
• Amyloids of multiple species: are they helpful in survival?

  2018cites this paper
• 3D structure determination of amyloid fibrils using solid-state NMR spectroscopy.

  2018cites this paper
• A synthetic redox biofilm made from metalloprotein-prion domain chimera nanowires.

  2017cites this paper
• Structural Biology of PrP Prions.

  2017cites this paper
• Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry.

  2016cites this paper
• Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif*

  2016cites this paper
• The HET-S/s Prion Motif in the Control of Programmed Cell Death.

  2016cites this paper
• Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis

  2016cites this paper
• Solid-State NMR Studies of Liquid Crystals and of the HET-s(218-289) Prion

  2015cites this paper
• Characteristics and chemical properties of Escherichia coli Curli

  2015cites this paper
• Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold

  2015cites this paper
• Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution

  2015influential citation
• Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure

  2015cites this paper
• A ROLE OF CALCIUM SIGNALING GENES IN HETEROKARYON INCOMPATIBILITY IN NEUROSPORA CRASSA

  2015cites this paper
• Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability

  2014cites this paper
• Heterogeneous seeding of HET-s(218–289) and the mutability of prion structures

  2014influential citation
• Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection.

  2014cites this paper
• Fungal prion HET-s as a model for structural complexity and self-propagation in prions

  2014influential citation
• Competitive inhibition reaction mechanisms for the two-step model of protein aggregation.

  2014cites this paper
• Is Supramolecular Filament Chirality the Underlying Cause of Major Morphology Differences in Amyloid Fibrils?

  2014cites this paper
• Progress in the direct structural characterization of fibrous amphiphilic supramolecular assemblies in solution by transmission electron microscopic techniques.

  2014cites this paper
• Repliements amyloïdes à propriétés prion dans la transduction du signal chez les champignons filamenteux : Amyloid folds with prion or prion-like features as signal transducing elements in filamentous fungi

  2013cites this paper
• Heterogeneous Seeding of a Prion Structure by a Generic Amyloid Form of the Fungal Prion-forming Domain HET-s(218–289)*

  2013cites this paper
• Nearly reversible conformational change of amyloid fibrils as revealed by pH-jump experiments.

  2013cites this paper
• Thioflavin-T excimer formation upon interaction with amyloid fibers.

  2013cites this paper
• Contributions à la modélisation mathématique et numérique de problèmes issus de la biologie - Applications aux Prions et à la maladie d'Alzheimer

  2012cites this paper
• Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold.

  2012cites this paper
• Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.

  2012cites this paper
• On the possible amyloid origin of protein folds.

  2012cites this paper
• Protein aggregation: mechanisms and functional consequences.

  2012cites this paper
• Two structurally similar fungal prions efficiently cross‐seed in vivo but form distinct polymers when coexpressed

  2011cites this paper
• Bacterial Inclusion Bodies of Alzheimer's Disease β‐Amyloid Peptides Can Be Employed To Study Native‐Like Aggregation Intermediate States

  2011cites this paper
• Dynamics of polymerization shed light on the mechanisms that lead to multiple amyloid structures of the prion protein.

  2011cites this paper
• Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy

  2011cites this paper
• The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility.

  2011cites this paper
• Discovery and characterization of prions in Saccharomyces cerevisiae

  2011cites this paper
• Atomic-resolution structure determination of amyloid fibrils by solid-state NMR

  2010influential citation
• Distinct Subregions of Swi1 Manifest Striking Differences in Prion Transmission and SWI/SNF Function

  2010cites this paper
• Herencia y memoria: ¿un nuevo rol para los priones?

  2010cites this paper
• Wild‐type Shadoo proteins convert to amyloid‐like forms under native conditions

  2010cites this paper
• A yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesis.

  2010cites this paper
• Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity.

  2010cites this paper
• Structure of mammalian prions

  2009cites this paper
• Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature.

  2009cites this paper
• Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.

  2009cites this paper
• The Functional Curli Amyloid Is Not Based on In-register Parallel β-Sheet Structure*

  2009cites this paper
• Microbial Cell Factories Characterization of the Amyloid Bacterial Inclusion Bodies of the Het-s Fungal Prion

  2009cites this paper
• Driving amyloid toxicity in a yeast model by structural changes: a molecular approach

  2009cites this paper
• A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

  2009cites this paper
• Festkörper‐NMR‐Spektroskopie zeigt: Die Einschlusskörperchen von HET‐s(218–289) in E. coli sind Amyloide

  2009cites this paper
• Energy barriers for HET‐s prion forming domain amyloid formation

  2009cites this paper
• Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra.

  2008cites this paper
• Infektiöse und nichtinfektiöse Amyloide des HET‐s(218‐289)‐Prions haben unterschiedliche NMR‐Spektren

  2008cites this paper
• Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

  2008cites this paper
• On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2.

  2008cites this paper
• Structural basis of infectious and non-infectious amyloids.

  2008cites this paper
• Thioflavin T fluorescence anisotropy: an alternative technique for the study of amyloid aggregation.

  2007cites this paper
• Role of Hsp104 in the propagation and inheritance of the [Het-s] prion.

  2007cites this paper
• A Short History of Small s

  2007cites this paper