All Stories

  1. Databases of liquid–liquid phase separation proteins and condensates
  2. AggrescanAI: Prediction of Aggregation-Prone Regions Using Contextualized Embeddings
  3. Peptideins: Navigating the gray zone of the proteome
  4. Integrated computational identification of natural product-derived candidates targeting the bicalutamide-resistant W741L androgen receptor in castration-resistant prostate cancer
  5. Can we vaccinate the brain? The promise of precision immunology
  6. Full-Length Molecular Models of Brain-Derived α-Synuclein Fibrils Reveal a Fuzzy-Coat-Mediated Mechanism for Selective Peptide Binding
  7. Passive immunotherapy for Parkinson’s disease in 2025: Status and perspective
  8. AGGRESCAN and its evolution: A two-decade perspective on protein aggregation prediction
  9. Computational Characterization of Pathogenic LMNA Missense Variants: Structural Instability, Altered Binding, and Conformational Dynamics
  10. Recent cryo-EM structures redefine the functional amyloid landscape
  11. Mass spectrometry reveals transthyretin shape shifts to guide better amyloidosis drugs
  12. Multivalent Protein Nanorings for Broad and Potent SARS‐CoV‐2 Neutralization
  13. LRRK2-mutant microglia and neuromelanin synergize to drive dopaminergic neurodegeneration in an iPSC-based Parkinson’s disease model
  14. Comprehensive protein datasets and benchmarking for liquid–liquid phase separation studies
  15. Experimental kinetic mechanism of P53 condensation-amyloid aggregation
  16. Harnessing the immune system: vaccines to fight neurodegenerative diseases
  17. MIA40 circumvents the folding constraints imposed by TRIAP1 function
  18. Determinants of alpha-synuclein pathogenesis in Parkinson’s disease
  19. Structural commonalities determined by physicochemical principles in the complex polymorphism of the amyloid state of proteins
  20. Identification of α-Synuclein Aggregation Inhibitors via High-Throughput Screening
  21. The role of amphipathic and cationic helical peptides in Parkinson's disease
  22. The dual nature of amyloids: From pathogenic aggregates to functional biostructures
  23. Building Up Functional Coiled-Coil-Based Supramolecular Assemblies for Biomedical and Biotechnological Applications
  24. Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
  25. Aggregating amyloid resources: A comprehensive review of databases on amyloid-like aggregation
  26. The small molecule ZPD ‐2 inhibits the aggregation and seeded polymerisation of C‐terminally truncated α‐Synuclein
  27. Protein Nanoparticles for Targeted SARS‐CoV‐2 Trapping and Neutralization
  28. Exploitation of the nitro- and/or 4-Trifluoromethyl-decorated phenyl fragment to develop small inhibitors of Alpha-Syn fibril aggregation
  29. Aggrescan4D: A comprehensive tool for pH‐dependent analysis and engineering of protein aggregation propensity
  30. Beyond neurodegeneration: engineering amyloids for biocatalysis
  31. Structural information in therapeutic peptides: Emerging applications in biomedicine
  32. Design and redesign journey of a drug for transthyretin amyloidosis
  33. Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration
  34. Aggrescan4D: structure-informed analysis of pH-dependent protein aggregation
  35. An α-helical peptide-based plasmonic biosensor for highly specific detection of α-synuclein toxic oligomers
  36. A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion
  37. Mutations in human prion-like domains: pathogenic but not always amyloidogenic
  38. Effect of the aggregated protein dye YAT2150 on Leishmania parasite viability
  39. Protein-only Nanoparticles for T Cell Expansion and Activation
  40. Advances, challenges, and opportunities in structural biology
  41. Cryo-EM structures of functional and pathological amyloid ribonucleoprotein assemblies
  42. Harnessing prion-inspired amyloid self-assembly for sustainable and biocompatible proton conductivity
  43. Assembly and catalytic activity of short prion-inspired peptides
  44. Editorial: Molecular determinants of protein assemblies in health and disease, Volume II
  45. A glimpse into the structural properties of α‐synuclein oligomers
  46. PITB: A high affinity transthyretin aggregation inhibitor with optimal pharmacokinetic properties
  47. Rational optimization of a transcription factor activation domain inhibitor
  48. DisProt in 2024: improving function annotation of intrinsically disordered proteins
  49. A3D Model Organism Database (A3D-MODB): a database for proteome aggregation predictions in model organisms
  50. A3DyDB: exploring structural aggregation propensities in the yeast proteome
  51. Expanding the Landscape of Amyloid Sequences with CARs-DB: A Database of Polar Amyloidogenic Peptides from Disordered Proteins
  52. Amyloid Fibrils Formed by Short Prion-Inspired Peptides Are Metalloenzymes
  53. Editorial: Peptide assemblies in nanotechnology
  54. Chemical targeting of amyloids
  55. Small molecules to target tau amyloid aggregation
  56. Arabidopsismetacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence
  57. Development of Small Molecules Targeting α-Synuclein Aggregation: A Promising Strategy to Treat Parkinson’s Disease
  58. OligoBinders: Bioengineered Soluble Amyloid-like Nanoparticles to Bind and Neutralize SARS-CoV-2
  59. A targetable N-terminal motif orchestrates α-Synuclein oligomer to fibril conversion
  60. Author Correction: Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity
  61. A Review of Fifteen Years Developing Computational Tools to Study Protein Aggregation
  62. Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3
  63. Exploring cryptic amyloidogenic regions in prion-like proteins from plants
  64. aSynPEP-DB: a database of biogenic peptides for inhibiting α-synuclein aggregation
  65. LL-37 and CsgC exemplify the crosstalk between anti-amyloid, antimicrobial, and anti-biofilm protein activities
  66. Editorial: Molecular determinants of protein assemblies in health and disease
  67. Ligand-Based Discovery of a Small Molecule as Inhibitor of α-Synuclein Amyloid Formation
  68. A finely tuned interplay between calcium binding, ionic strength and pH modulates conformational and oligomerization equilibria in the Respiratory Syncytial Virus Matrix (M) protein
  69. Development of a Highly Potent Transthyretin Amyloidogenesis Inhibitor: Design, Synthesis, and Evaluation
  70. Cryo-EM Structure of a Mammalian-specific Alternative Amyloid Exon
  71. Rational optimization of a transcription factor activation domain inhibitor
  72. Is a cure for Parkinson’s disease hiding inside us?
  73. In-Silico Analysis of pH-Dependent Liquid-Liquid Phase Separation in Intrinsically Disordered Proteins
  74. CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins
  75. Correction: 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
  76. The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains
  77. A3D database: structure-based predictions of protein aggregation for the human proteome
  78. Computational methods to predict protein aggregation
  79. Discovery of Neuroprotective Agents Based on a 5-(4-Pyridinyl)-1,2,4-triazole Scaffold
  80. One ring is sufficient to inhibit α-synuclein aggregation
  81. The dynamic landscape of peptide activity prediction
  82. A3D 2.0 Update for the Prediction and Optimization of Protein Solubility
  83. Prediction of the Effect of pH on the Aggregation and Conditional Folding of Intrinsically Disordered Proteins with SolupHred and DispHred
  84. Protocols for Rational Design of Protein Solubility and Aggregation Properties Using Aggrescan3D Standalone
  85. Design, synthesis and structure-activity evaluation of novel 2-pyridone-based inhibitors of α-synuclein aggregation with potentially improved BBB permeability
  86. DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation
  87. A3D Database: Structure-based Protein Aggregation Predictions for the Human Proteome
  88. DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
  89. AlphaFold and the amyloid landscape
  90. Disease-associated mutations impacting BC-loop flexibility trigger long-range transthyretin tetramer destabilization and aggregation
  91. Multifunctional antibody-conjugated coiled-coil protein nanoparticles for selective cell targeting
  92. SGnn: A Web Server for the Prediction of Prion-Like Domains Recruitment to Stress Granules Upon Heat Stress
  93. Coiled-Coil Based Inclusion Bodies and Their Potential Applications
  94. Functionalized Prion-Inspired Amyloids for Biosensor Applications
  95. α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity
  96. Prion‐like proteins: from computational approaches to proteome‐wide analysis
  97. Prediction of the effect of pH on the aggregation and conditional folding of intrinsically disordered proteins with SolupHred and DispHred
  98. Critical assessment of protein intrinsic disorder prediction
  99. A3D 2.0 update for the prediction and optimization of protein solubility
  100. Prospects for beyond the Standard Model physics searches at the Deep Underground Neutrino Experiment
  101. MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
  102. Dual Antibody-Conjugated Amyloid Nanorods to Promote Selective Cell–Cell Interactions
  103. α-Helical peptidic scaffolds to target α-synuclein pathogenic species with high affinity and selectivity
  104. Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations
  105. Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association
  106. Decoding the role of coiled-coil motifs in human prion-like proteins
  107. Functional Amyloids Germinate in Plants
  108. pH-Responsive Self-Assembly of Amyloid Fibrils for Dual Hydrolase-Oxidase Reactions
  109. Editorial: Protein Aggregation and Solubility in Microorganisms (Archaea, Bacteria and Unicellular Eukaryotes): Implications and Applications
  110. MIRRAGGE – Minimum Information Required for Reproducible AGGregation Experiments
  111. Special Issue: “Inflammation, Oxidative Stress and Protein Aggregation; Any Links?”
  112. SolupHred: a server to predict the pH-dependent aggregation of intrinsically disordered proteins
  113. Inhibition of α-Synuclein Aggregation and Mature Fibril Disassembling With a Minimalistic Compound, ZPDm
  114. Amyloidogenicity as a driving force for the formation of functional oligomers
  115. Protocols for rational design of protein solubility and aggregation properties using Aggrescan3D standalone
  116. Multifunctional Amyloid Oligomeric Nanoparticles for Specific Cell Targeting and Drug Delivery
  117. DispHred: A Server to Predict pH-Dependent Order–Disorder Transitions in Intrinsically Disordered Proteins
  118. Reply to Comment on “N-terminal Protein Tail Acts as Aggregation Protective Entropic Bristles: The SUMO Case”
  119. Prion-like domain disease-causing mutations and misregulation of alternative splicing relevance in limb-girdle muscular dystrophy (LGMD) 1G
  120. Small molecules to prevent the neurodegeneration caused by α-synuclein aggregation
  121. Coiled-coil inspired functional inclusion bodies
  122. Detection of Protein Aggregation in Live Plasmodium Parasites
  123. Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis
  124. Chemical Chaperones as Novel Drugs for Parkinson’s Disease
  125. Soluble Assemblies in the Fibrillation Pathway of Prion-Inspired Artificial Functional Amyloids are Highly Cytotoxic
  126. The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
  127. pH-Dependent Aggregation in Intrinsically Disordered Proteins Is Determined by Charge and Lipophilicity
  128. Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications
  129. Prion domains as a driving force for the assembly of functional nanomaterials
  130. Rational design of small molecules able to inhibit α-synuclein amyloid aggregation for the treatment of Parkinson’s disease
  131. Atomistic fibrillar architectures of polar prion-inspired heptapeptides
  132. Computational prediction and redesign of aberrant protein oligomerization
  133. hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation
  134. C-Mannosylation supports folding and enhances stability of thrombospondin repeats
  135. ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization
  136. DisProt: intrinsic protein disorder annotation in 2020
  137. Advances in the Prediction of Protein Aggregation Propensity
  138. Dual Binding Mode of Metallacarborane Produces a Robust Shield on Proteins
  139. Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation
  140. Computational re-design of protein structures to improve solubility
  141. Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility
  142. The fitness cost and benefit of phase‐separated protein deposits
  143. Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
  144. In silico Characterization of Human Prion-Like Proteins: Beyond Neurological Diseases
  145. The fitness cost and benefit of phase separated protein deposits
  146. Aggrescan3D standalone package for structure-based prediction of protein aggregation properties
  147. AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity
  148. Prion soft amyloid core driven self-assembly of globular proteins into bioactive nanofibrils
  149. Inducing α-synuclein compaction: a new strategy for inhibiting α-synuclein aggregation?
  150. Formation of Cross-Beta Supersecondary Structure by Soft-Amyloid Cores: Strategies for Their Prediction and Characterization
  151. A pyrene-inhibitor fluorescent probe with large Stokes shift for the staining of Aβ1–42, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing Staphylococcus aureus biofilms
  152. Screening Protein Aggregation in Cells Using Fluorescent Labels Coupled to Flow Cytometry
  153. Prion-based nanomaterials and their emerging applications
  154. Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons
  155. Insight into the specificity and severity of pathogenic mechanisms associated with missense mutations through experimental and structural perturbation analyses
  156. Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
  157. Protein Environment: A Crucial Triggering Factor in Josephin Domain Aggregation: The Role of 2,2,2-Trifluoroethanol
  158. Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility
  159. Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation
  160. Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
  161. Minimalist Prion-Inspired Polar Self-Assembling Peptides
  162. The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region
  163. A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation
  164. Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases
  165. Amyloid Formation in Bacteria
  166. AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures
  167. Disulfide driven folding for a conditionally disordered protein
  168. Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
  169. Protein aggregation into insoluble deposits protects from oxidative stress
  170. Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI)
  171. Perfecting prediction of mutational impact on the aggregation propensity of the ALS‐associated hnRNPA2 prion‐like protein
  172. The Transcription Terminator Rho: A First Bacterial Prion
  173. Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation
  174. Prion-like proteins and their computational identification in proteomes
  175. High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors
  176. Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics
  177. Amyloid cores in prion domains: Key regulators for prion conformational conversion
  178. Prediction of Protein Aggregation and Amyloid Formation
  179. DisProt 7.0: a major update of the database of disordered proteins
  180. The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation
  181. DisProt 7.0: a major update of the database of disordered proteins
  182. Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure
  183. Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity
  184. A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems
  185. Characterization of Amyloid Cores in Prion Domains
  186. Understanding and predicting protein misfolding and aggregation: Insights from proteomics
  187. Editorial: Protein Solubility and Aggregation in Bacteria
  188. Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals
  189. Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation
  190. Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria
  191. Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration
  192. Mammalian prion amyloid formation in bacteria
  193. Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity
  194. Erratum
  195. 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
  196. Curing bacterial infections with protein aggregates
  197. The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core
  198. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
  199. In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time
  200. Protein Solubility and Aggregation in Bacteria
  201. Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
  202. Prion-like proteins in bacteria
  203. Protein Misfolding Diseases
  204. Aggregation Propensity of Neuronal Receptors: Potential Implications in Neurodegenerative Disorders
  205. Possible Roles of Amyloids in Malaria Pathophysiology
  206. Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor
  207. The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria
  208. Influence of Cytoplasmatic Folding on Mitochondrial Import
  209. Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1–42 Amyloid-β Peptide
  210. PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores
  211. Amyloids or prions? That is the question
  212. AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures
  213. Structural and Computational Insights into Conformational Diseases: A Review
  214. Proteome response at the edge of protein aggregation
  215. What Makes a Protein Sequence a Prion?
  216. Protein Aggregation and Its Prediction
  217. Multifaceted Roles of Crystallography in Modern Drug Discovery
  218. Desoxipipradrol. Fármacos antiguos, problemas nuevos
  219. Characterization of Amyloid-Like Properties in Bacterial Intracellular Aggregates
  220. Amyloid Formation by Human Carboxypeptidase D Transthyretin-like Domain under Physiological Conditions
  221. The Importance of a Gatekeeper Residue on the Aggregation of Transthyretin
  222. Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates inEscherichia coli
  223. The small GTPase Rab11 co-localizes with  -synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity
  224. Human Stefin B Role in Cell's Response to Misfolded Proteins and Autophagy
  225. Association Between Foldability and Aggregation Propensity in Small Disulfide-Rich Proteins
  226. Screening for Amyloid Aggregation: In-Silico, In-Vitro and In-Vivo Detection
  227. Selection against toxic aggregation-prone protein sequences in bacteria
  228. Inclusion Bodies in the Study of Amyloid Aggregation
  229. The Mitochondrial Intermembrane Space Oxireductase Mia40 Funnels the Oxidative Folding Pathway of the Cytochrome c Oxidase Assembly Protein Cox19
  230. N-Terminal Protein Tails Act as Aggregation Protective Entropic Bristles: The SUMO Case
  231. Thioflavin-S Staining of Bacterial Inclusion Bodies for the Fast, Simple, and Inexpensive Screening of Amyloid Aggregation Inhibitors
  232. PrionScan: an online database of predicted prion domains in complete proteomes
  233. Correction: Structure-Based Analysis of A19D, a Variant of Transthyretin Involved in Familial Amyloid Cardiomyopathy
  234. Structure-Based Analysis of A19D, a Variant of Transthyretin Involved in Familial Amyloid Cardiomyopathy
  235. Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation
  236. About targets and causes in protein folding
  237. Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain
  238. Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
  239. The N-terminal Helix Controls the Transition between the Soluble and Amyloid States of an FF Domain
  240. Inhibition of Human Transthyretin Aggregation by Non-Steroidal Anti-Inflammatory Compounds: A Structural and Thermodynamic Analysis
  241. Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease
  242. Thioflavin-T excimer formation upon interaction with amyloid fibers
  243. Amyloid Formation in Bacteria
  244. Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone
  245. Discovery of Novel Inhibitors of Amyloid β-Peptide 1–42 Aggregation
  246. Evolutionary selection for protein aggregation
  247. Protein aggregation: Mechanisms and functional consequences
  248. The Effect of Amyloidogenic Peptides on Bacterial Aging Correlates with Their Intrinsic Aggregation Propensity
  249. Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide
  250. Yeast prions form infectious amyloid inclusion bodies in bacteria
  251. Native Structure Protects SUMO Proteins from Aggregation into Amyloid Fibrils
  252. Protein Oxidative Folding in the Intermembrane Mitochondrial Space: More than Protein Trafficking
  253. Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation
  254. Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy
  255. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
  256. Contribution of Disulfide Bonds to Stability, Folding, and Amyloid Fibril Formation: The PI3-SH3 Domain Case
  257. Protein aggregation profile of the human kinome
  258. Protein Aggregation Acts as Strong Constraint During Evolution
  259. Cross-β-Sheet Supersecondary Structure in Amyloid Folds: Techniques for Detection and Characterization
  260. Modeling amyloids in bacteria
  261. Multiple β‐sheet molecular dynamics of amyloid formation from two ABl‐SH3 domain peptides
  262. Temperature Dependence of the Aggregation Kinetics of Sup35 and Ure2p Yeast Prions
  263. AGGRESCAN: Method, Application, and Perspectives for Drug Design
  264. Bimolecular Fluorescence Complementation: Illuminating Cellular Protein Interactions
  265. Biological role of bacterial inclusion bodies: a model for amyloid aggregation
  266. Prediction of the aggregation propensity of proteins from the primary sequence: Aggregation properties of proteomes
  267. The aggregation properties of Escherichia coli proteins associated with their cellular abundance
  268. Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/NM23-H1 into amyloid fibrils
  269. Does Stoichiometry Drive Protein Folding?
  270. Bacterial Inclusion Bodies of Alzheimer's Disease β‐Amyloid Peptides Can Be Employed To Study Native‐Like Aggregation Intermediate States
  271. Linking amyloid protein aggregation and yeast survival
  272. Folding of Disulfide Proteins
  273. Oxidative Folding: Coupling Conformational Folding and Disulfide Formation
  274. Protease Inhibitors as Models for the Study of Oxidative Folding
  275. Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria
  276. The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils
  277. Modulation of Aβ42 fibrillogenesis by glycosaminoglycan structure
  278. Amyloid-Like Protein Inclusions in Tobacco Transgenic Plants
  279. Protein folding and aggregation in bacteria
  280. Protein Aggregation Profile of the Bacterial Cytosol
  281. Deciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase Inhibitor
  282. Designing Out Disulfide Bonds of Leech Carboxypeptidase Inhibitor: Implications for Its Folding, Stability and Function
  283. Amyloids in bacterial inclusion bodies
  284. Energy barriers for HET‐s prion forming domain amyloid formation
  285. Amyloidogenic Regions and Interaction Surfaces Overlap in Globular Proteins Related to Conformational Diseases
  286. Amyloids in bacterial inclusion bodies
  287. Protein complementation assays: Approaches for the in vivo analysis of protein interactions
  288. Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease
  289. Detecting and Interfering Protein Interactions: Towards the Control of Biochemical Pathways
  290. Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
  291. Dynamics study on single and multiple β-sheets
  292. Sulfated Polysaccharides Promote the Assembly of Amyloid β1–42 Peptide into Stable Fibrils of Reduced Cytotoxicity
  293. Kinetic and thermodynamic stability of bacterial intracellular aggregates
  294. The NMR Structures of the Major Intermediates of the Two-domain Tick Carboxypeptidase Inhibitor Reveal Symmetry in Its Folding and Unfolding Pathways
  295. Inclusion bodies: Specificity in their aggregation process and amyloid-like structure
  296. Monitoring the interference of protein‐protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case
  297. Studies on bacterial inclusion bodies
  298. Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)
  299. Recent Structural and Computational Insights into Conformational Diseases
  300. The in Vivo and in Vitro Aggregation Properties of Globular Proteins Correlate With Their Conformational Stability: The SH3 Case
  301. Scrambled Isomers as Key Intermediates in the Oxidative Folding of Ligand Binding Module 5 of the Low Density Lipoprotein Receptor
  302. Oxidative Protein Folding: From the Test Tube to In Vivo Insights
  303. Oxidative Folding of Leech-Derived Tryptase Inhibitor Via Native Disulfide-Bonded Intermediates
  304. Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry
  305. Self-assembly of human latexin into amyloid-like oligomers
  306. Prion and Non-prion Amyloids of the HET-s Prion forming Domain
  307. Detection of transient protein–protein interactions by bimolecular fluorescence complementation: The Abl‐SH3 case
  308. Ile-Phe Dipeptide Self-Assembly: Clues to Amyloid Formation
  309. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
  310. Molecular dynamics study of amyloid formation of two Abl‐SH3 domain peptides
  311. Effect of temperature on protein quality in bacterial inclusion bodies
  312. Protein aggregation into bacterial inclusion bodies is a specific kinetically driven process
  313. Design and NMR conformational study of a β‐sheet peptide based on Betanova and WW domains
  314. The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells
  315. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
  316. Characterizing the Tick Carboxypeptidase Inhibitor
  317. Folding of small disulfide-rich proteins: clarifying the puzzle
  318. Protein quality in bacterial inclusion bodies
  319. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
  320. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
  321. Study of a Major Intermediate in the Oxidative Folding of Leech Carboxypeptidase Inhibitor: Contribution of the Fourth Disulfide Bond
  322. Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin
  323. NMR Structural Characterization and Computational Predictions of the Major Intermediate in Oxidative Folding of Leech Carboxypeptidase Inhibitor
  324. Sequence determinants of protein aggregation: tools to increase protein solubility
  325. Amyloid-like Properties of Bacterial Inclusion Bodies
  326. Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin
  327. Prediction of "hot spots" of aggregation in disease-linked polypeptides
  328. Amyloid fibril formation by bovine cytochromec
  329. Amyloid Fibril Formation by a Partially Structured Intermediate State of α-Chymotrypsin
  330. Role of Kinetic Intermediates in the Folding of Leech Carboxypeptidase Inhibitor
  331. Secondary Binding Site of the Potato Carboxypeptidase Inhibitor. Contribution to Its Structure, Folding, and Biological Properties†
  332. Designing proteins from the inside out
  333. Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case
  334. Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation
  335. Folding specificity induced by loop stiffness
  336. Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR
  337. Spectroscopic Analysis of Amyloid Fibril Formation in SH3‐Domains
  338. Insights into the Origin of the Tendency of the PI3-SH3 Domain to form Amyloid Fibrils
  339. Conformational strain in the hydrophobic core and its implications for protein folding and design
  340. Mapping the Pro-region of Carboxypeptidase B by Protein Engineering
  341. Overexpression of Human Procarboxypeptidase A2 in Pichia pastoris and Detailed Characterization of Its Activation Pathway
  342. Cutting at the right place
  343. 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
  344. Crystallization and preliminary X‐ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas
  345. Procarboxypeptidase in rat pancreas Overall characterization and comparison of the activation processes