| Q35853137 | A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems |
| Q58559175 | A pyrene-inhibitor fluorescent probe with large Stokes shift for the staining of Aβ, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing Staphylococcus aureus biofilms |
| Q47408751 | A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation. |
| Q30373803 | AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures. |
| Q53824660 | AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures. |
| Q33275645 | AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides |
| Q46280110 | AGGRESCAN: method, application, and perspectives for drug design |
| Q61448595 | AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity |
| Q46454619 | About targets and causes in protein folding |
| Q39420309 | Advances in the prediction of protein aggregation propensity |
| Q24815513 | Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins |
| Q46869968 | Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/NM23-H1 into amyloid fibrils |
| Q37474322 | Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders. |
| Q91719617 | Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility |
| Q92066992 | Aggrescan3D standalone package for structure-based prediction of protein aggregation properties |
| Q47935433 | Amyloid cores in prion domains: Key regulators for prion conformational conversion. |
| Q30163872 | Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin. |
| Q42092379 | Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions |
| Q28118595 | Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration |
| Q42651430 | Amyloid-like properties of bacterial inclusion bodies. |
| Q33737666 | Amyloid-like protein inclusions in tobacco transgenic plants |
| Q33495551 | Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases |
| Q37568883 | Amyloids in bacterial inclusion bodies |
| Q38514465 | Amyloids or prions? That is the question |
| Q41566585 | Association between foldability and aggregation propensity in small disulfide-rich proteins |
| Q50546707 | Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states. |
| Q36056679 | Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation |
| Q64242757 | Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity |
| Q37894803 | Bimolecular fluorescence complementation: illuminating cellular protein interactions. |
| Q37875227 | Biological role of bacterial inclusion bodies: a model for amyloid aggregation |
| Q83224312 | C-mannosylation supports folding and enhances stability of thrombospondin repeats |
| Q42050715 | Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation |
| Q41237631 | Characterization of Amyloid Cores in Prion Domains |
| Q64111825 | Characterization of Human Prion-Like Proteins: Beyond Neurological Diseases |
| Q42362302 | Characterization of Soft Amyloid Cores in Human Prion-Like Proteins |
| Q38275223 | Characterization of amyloid-like properties in bacterial intracellular aggregates |
| Q42023365 | Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion |
| Q57956897 | Characterizing the Tick Carboxypeptidase Inhibitor |
| Q96122849 | Coiled-coil inspired functional inclusion bodies |
| Q90415219 | Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility |
| Q92528700 | Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation |
| Q40362652 | Computational analysis of candidate prion-like proteins in bacteria and their role |
| Q91696662 | Computational re-design of protein structures to improve solubility |
| Q27638976 | Conformational strain in the hydrophobic core and its implications for protein folding and design |
| Q30010266 | Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case |
| Q41906373 | Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics |
| Q55559685 | Correction: Structure-Based Analysis of A19D, a Variant of Transthyretin Involved in Familial Amyloid Cardiomyopathy. |
| Q84985803 | Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization |
| Q57957124 | Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation 1 1Edited by I. A. Wilson |
| Q57957151 | Crystallization and preliminary X-ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas |
| Q40853091 | Curing bacterial infections with protein aggregates. |
| Q57957089 | Cutting at the right place. The importance of selective limited proteolysis in the activation of proproteinase E |
| Q31114259 | Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria |
| Q27657754 | Deciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase Inhibitor |
| Q30155951 | Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria |
| Q41840645 | Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains. |
| Q46169343 | Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease |
| Q46063561 | Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function |
| Q35783481 | Designing proteins from the inside out. |
| Q34441836 | Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin |
| Q37370427 | Detecting and interfering protein interactions: towards the control of biochemical pathways. |
| Q30158031 | Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. |
| Q27650902 | Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid) |
| Q57204000 | DisProt 7.0: a major update of the database of disordered proteins |
| Q34546157 | DisProt 7.0: a major update of the database of disordered proteins. |
| Q56346105 | Discovering Putative Prion-Like Proteins in : A Computational and Experimental Analysis |
| Q34714516 | Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains |
| Q34420890 | Discovery of novel inhibitors of amyloid β-peptide 1-42 aggregation. |
| Q112579256 | Disease-associated mutations impacting BC-loop flexibility trigger long-range transthyretin tetramer destabilization and aggregation |
| Q98616969 | DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins |
| Q37314742 | Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure |
| Q47112353 | Disulfide driven folding for a conditionally disordered protein. |
| Q92614995 | Dual Binding Mode of Metallacarborane Produces a Robust Shield on Proteins |
| Q58434493 | Dynamics study on single and multiple β-sheets |
| Q41936040 | Editorial: Protein Solubility and Aggregation in Bacteria |
| Q53328297 | Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide. |
| Q43527952 | Energy barriers for HET-s prion forming domain amyloid formation |
| Q37369400 | Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity. |
| Q89472234 | Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast |
| Q38044424 | Evolutionary selection for protein aggregation |
| Q50462869 | Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. |
| Q33342293 | Folding of small disulfide-rich proteins: clarifying the puzzle. |
| Q30164658 | Folding specificity induced by loop stiffness |
| Q92837253 | Formation of Cross-Beta Supersecondary Structure by Soft-Amyloid Cores: Strategies for Their Prediction and Characterization |
| Q58434151 | Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation |
| Q22676705 | Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) |
| Q36296440 | High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors |
| Q58434267 | Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1–42 Amyloid-β Peptide |
| Q44979423 | Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation. |
| Q28540970 | Human stefin B role in cell's response to misfolded proteins and autophagy |
| Q45851022 | Identification of a new variant of TTR involved in familial amyloid cardiomyopathy (FAC) in Brazil: from the patient to the protein. |
| Q50239011 | In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time. |
| Q57956808 | Inclusion bodies: Specificity in their aggregation process and amyloid-like structure |
| Q91762151 | Inducing α-synuclein compaction: a new strategy for inhibiting α-synuclein aggregation? |
| Q38373484 | Influence of Cytoplasmatic Folding on Mitochondrial Import. |
| Q30165168 | Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils |
| Q35689620 | Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor |
| Q46327494 | Kinetic and thermodynamic stability of bacterial intracellular aggregates |
| Q33794914 | Linking amyloid protein aggregation and yeast survival |
| Q39972571 | Mammalian prion amyloid formation in bacteria. |
| Q40923016 | Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria. |
| Q47951186 | Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme |
| Q58434154 | Minimalist Prion-Inspired Polar Self-Assembling Peptides |
| Q39494485 | Modeling amyloids in bacteria. |
| Q43002949 | Modulation of Abeta42 fibrillogenesis by glycosaminoglycan structure |
| Q50079166 | Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases. |
| Q30159546 | Molecular dynamics study of amyloid formation of two Abl-SH3 domain peptides |
| Q52693279 | Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case. |
| Q30009967 | Multiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides |
| Q58434333 | N-Terminal Protein Tails Act as Aggregation Protective Entropic Bristles: The SUMO Case |
| Q46638076 | NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor |
| Q52624983 | Native structure protects SUMO proteins from aggregation into amyloid fibrils. |
| Q57957098 | Overexpression of Human Procarboxypeptidase A2 inPichia pastorisand Detailed Characterization of Its Activation Pathway |
| Q58434522 | Oxidative Protein Folding: From the Test Tube to In Vivo Insights |
| Q38077922 | Oxidative folding in the mitochondrial intermembrane space in human health and disease |
| Q46898912 | Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates |
| Q41482025 | Pancreatic procarboxypeptidases: oligomeric structures and activation processes revisited. |
| Q50980936 | Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein. |
| Q41020151 | Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI). |
| Q37474223 | Possible roles of amyloids in malaria pathophysiology |
| Q24815235 | Prediction of "hot spots" of aggregation in disease-linked polypeptides |
| Q37871568 | Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. |
| Q44579581 | Prion and non-prion amyloids of the HET-s prion forming domain. |
| Q96768107 | Prion domains as a driving force for the assembly of functional nanomaterials |
| Q93011646 | Prion soft amyloid core driven self-assembly of globular proteins into bioactive nanofibrils |
| Q58434147 | Prion-based nanomaterials and their emerging applications |
| Q39167900 | Prion-like proteins and their computational identification in proteomes. |
| Q41951068 | PrionScan: an online database of predicted prion domains in complete proteomes. |
| Q41488687 | PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores |
| Q28576937 | Procarboxypeptidase in rat pancreas. Overall characterization and comparison of the activation processes |
| Q37784817 | Protease inhibitors as models for the study of oxidative folding. |
| Q90452067 | Protein Environment: A Crucial Triggering Factor in Josephin Domain Aggregation: The Role of 2,2,2-Trifluoroethanol |
| Q42291713 | Protein aggregation into insoluble deposits protects from oxidative stress |
| Q33535929 | Protein aggregation profile of the bacterial cytosol |
| Q41531353 | Protein aggregation profile of the human kinome |
| Q43427116 | Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation |
| Q38020074 | Protein aggregation: mechanisms and functional consequences. |
| Q37408788 | Protein complementation assays: approaches for the in vivo analysis of protein interactions |
| Q37722588 | Protein folding and aggregation in bacteria |
| Q38970059 | Protein misfolding diseases. |
| Q38011828 | Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking. |
| Q36406887 | Protein quality in bacterial inclusion bodies. |
| Q41448210 | Proteome response at the edge of protein aggregation |
| Q97690223 | Reply to Comment on "N-terminal Protein Tail Acts as Aggregation Protective Entropic Bristles: The SUMO Case" |
| Q36615637 | Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity. |
| Q112717249 | SGnn: A Web Server for the Prediction of Prion-Like Domains Recruitment to Stress Granules Upon Heat Stress |
| Q45851842 | SOM0226, a repositioned compound for the treatment of TTR amyloidosis |
| Q46699385 | Scrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor |
| Q57785274 | Screening Protein Aggregation in Cells Using Fluorescent Labels Coupled to Flow Cytometry |
| Q38189881 | Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection |
| Q46695131 | Selection against toxic aggregation-prone protein sequences in bacteria |
| Q30365734 | Self-assembly of human latexin into amyloid-like oligomers. |
| Q24795353 | Sequence determinants of protein aggregation: tools to increase protein solubility |
| Q30164098 | Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case |
| Q57292355 | Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons |
| Q90755574 | Soluble Assemblies in the Fibrillation Pathway of Prion-Inspired Artificial Functional Amyloids are Highly Cytotoxic |
| Q100959985 | SolupHred: A Server to Predict the pH-dependent Aggregation of Intrinsically Disordered Proteins |
| Q102057869 | Special Issue: "Inflammation, Oxidative Stress and Protein Aggregation; Any Links?" |
| Q28552929 | Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis |
| Q36057962 | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| Q27640399 | Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR |
| Q33932645 | Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin |
| Q35072784 | Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy |
| Q37225671 | Studies on bacterial inclusion bodies |
| Q33314548 | Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry. |
| Q46673180 | Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond |
| Q39935358 | Sulfated polysaccharides promote the assembly of amyloid beta(1-42) peptide into stable fibrils of reduced cytotoxicity |
| Q58434410 | Temperature Dependence of the Aggregation Kinetics of Sup35 and Ure2p Yeast Prions |
| Q55351373 | The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region. |
| Q34625713 | The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain |
| Q27651262 | The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways |
| Q41773166 | The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core. |
| Q47221772 | The Transcription Terminator Rho: A First Bacterial Prion. |
| Q58434450 | The aggregation properties of Escherichia coli proteins associated with their cellular abundance |
| Q90713441 | The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers |
| Q38253736 | The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. |
| Q50505443 | The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity. |
| Q42355152 | The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation. |
| Q64067570 | The fitness cost and benefit of phase-separated protein deposits |
| Q41920394 | The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses |
| Q30157694 | The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case |
| Q38609089 | The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19. |
| Q41143473 | The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria |
| Q39649072 | The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils |
| Q38968679 | The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity |
| Q58434417 | Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation |
| Q43519224 | Thioflavin-S staining of bacterial inclusion bodies for the fast, simple, and inexpensive screening of amyloid aggregation inhibitors |
| Q50980159 | Thioflavin-T excimer formation upon interaction with amyloid fibers. |
| Q42663837 | Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain |
| Q38915018 | Understanding and predicting protein misfolding and aggregation: Insights from proteomics |
| Q41229397 | Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors |
| Q35539958 | What makes a protein sequence a prion? |
| Q42408566 | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| Q43921688 | Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone |
| Q92632808 | pH-Dependent Aggregation in Intrinsically Disordered Proteins Is Determined by Charge and Lipophilicity |
