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Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases

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Outgoing claims: the papers this work cites, builds on, or argues with.

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Relation of Diabetes to Mild Cognitive Impairment

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Angewandte Chemie International Edition

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Amyloid‐Mediated Fabrication of Organic–Inorganic Hybrid Materials and Their Biomedical Applications

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Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials

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Amyloid‐β Peptide Induces Prion Protein Amyloid Formation: Evidence for Its Widespread Amyloidogenic Effect

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An english translation of alzheimer's 1907 paper, “über eine eigenartige erkankung der hirnrinde”

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Self‐Assembly of Tyrosine into Controlled Supramolecular Nanostructures

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Amino Acid Based Self‐assembled Nanostructures: Complex Structures from Remarkably Simple Building Blocks

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Circular Dichroism of Amino Acids: Following the Structural Formation of Phenylalanine

inferredcites →https://doi.org/10.1002/ijch.201600076openalex-snapshot

Formation of Apoptosis‐Inducing Amyloid Fibrils by Tryptophan

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Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.

inferredcites →https://doi.org/10.1002/mds.28655openalex-snapshot

Linking Parkinson's Disease and Melanoma: Interplay Between α‐Synuclein and Pmel17 Amyloid Formation

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Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. Baumeister

inferredcites →https://doi.org/10.1006/jsbi.1997.3858openalex-snapshot

Polymorphic Fibrillar Assembly of Human Amylin

inferredcites →https://doi.org/10.1007/978-1-61779-551-0_9openalex-snapshot

X-Ray Fibre Diffraction Studies of Amyloid Fibrils

inferredcites →https://doi.org/10.1007/978-3-031-20565-1_19openalex-snapshot

Genetics of Prion Disease

inferredcites →https://doi.org/10.1007/s00109-003-0464-5openalex-snapshot

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

inferredcites →https://doi.org/10.1007/s001250100599openalex-snapshot

A novel mutation in islet amyloid polypeptide (IAPP) gene promoter is associated with Type II diabetes mellitus.

inferredcites →https://doi.org/10.1007/s00253-013-5216-zopenalex-snapshot

Applications of biofilms in bioremediation and biotransformation of persistent organic pollutants, pharmaceuticals/personal care products, and heavy metals

inferredcites →https://doi.org/10.1007/s12551-017-0377-0openalex-snapshot

Formation and properties of amyloid fibrils of prion protein

inferredcites →https://doi.org/10.1016/0014-5793(89)81467-xopenalex-snapshot

Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species

inferredcites →https://doi.org/10.1016/0032-3861(78)90325-7openalex-snapshot

International journal of biological macromolecules

inferredcites →https://doi.org/10.1016/0092-8674(83)90168-xopenalex-snapshot

Scrapie prions aggregate to form amyloid-like birefringent rods

inferredcites →https://doi.org/10.1016/0169-328x(90)90038-fopenalex-snapshot

An in-frame insertion in the prion protein gene in familial Creutzfeldt-Jakob disease

inferredcites →https://doi.org/10.1016/j.ajpath.2022.07.002openalex-snapshot

Neuropathologic Changes Provide Insights into Key Mechanisms of Alzheimer Disease and Related Dementia

inferredcites →https://doi.org/10.1016/j.bbagen.2022.130151openalex-snapshot

Structural and mechanistic insights into modulation of α-Synuclein fibril formation by aloin and emodin

inferredcites →https://doi.org/10.1016/j.bbamem.2018.02.020openalex-snapshot

IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies

inferredcites →https://doi.org/10.1016/j.bbamem.2018.02.031openalex-snapshot

Mechanism of aggregation and membrane interactions of mammalian prion protein

inferredcites →https://doi.org/10.1016/j.bbamem.2020.183536openalex-snapshot

Interactions of α-synuclein oligomers with lipid membranes

inferredcites →https://doi.org/10.1016/j.bcp.2017.04.004openalex-snapshot

Natural product-based amyloid inhibitors

inferredcites →https://doi.org/10.1016/j.biopsych.2017.08.010openalex-snapshot

Anti-Amyloid-β Monoclonal Antibodies for Alzheimer’s Disease: Pitfalls and Promise

inferredcites →https://doi.org/10.1016/j.biopsych.2017.11.020openalex-snapshot

Prion Protein as a Toxic Acceptor of Amyloid-β Oligomers

inferredcites →https://doi.org/10.1016/j.bpj.2013.04.050openalex-snapshot

In Vitro Study of α-Synuclein Protofibrils by Cryo-EM Suggests a Cu2+-Dependent Aggregation Pathway

inferredcites →https://doi.org/10.1016/j.cbpa.2021.07.005openalex-snapshot

Metabolite assemblies: A surprising extension to the amyloid hypothesis

inferredcites →https://doi.org/10.1016/j.cjche.2021.04.018openalex-snapshot

Insights into the cross-amyloid aggregation of Aβ40 and its N-terminal truncated peptide Aβ11-40 affected by epigallocatechin gallate

inferredcites →https://doi.org/10.1016/j.cocis.2012.08.001openalex-snapshot

Study of amyloid fibrils via atomic force microscopy

inferredcites →https://doi.org/10.1016/j.ijbiomac.2021.03.113openalex-snapshot

The role of amyloid oligomers in neurodegenerative pathologies

inferredcites →https://doi.org/10.1016/j.ijms.2016.09.018openalex-snapshot

1,2,3,4,6-penta-O-galloyl-β-d-glucopyranose binds to the N-terminal metal binding region to inhibit amyloid β-protein oligomer and fibril formation

inferredcites →https://doi.org/10.1016/j.jbc.2021.100510openalex-snapshot

Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners

inferredcites →https://doi.org/10.1016/j.jmb.2008.08.039openalex-snapshot

Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein

inferredcites →https://doi.org/10.1016/j.jmb.2018.08.002openalex-snapshot

Quinolinic Acid Amyloid-like Fibrillar Assemblies Seed α-Synuclein Aggregation

inferredcites →https://doi.org/10.1016/j.jsb.2005.06.006openalex-snapshot

Mechanism of thioflavin T binding to amyloid fibrils

inferredcites →https://doi.org/10.1016/j.tim.2020.09.005openalex-snapshot

Two Decades of Studying Functional Amyloids in Microorganisms

inferredcites →https://doi.org/10.1016/s0014-5793(00)01888-3openalex-snapshot

Amyloids protect the silkmoth oocyte and embryo

inferredcites →https://doi.org/10.1016/s0021-9258(20)80536-5openalex-snapshot

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

inferredcites →https://doi.org/10.1016/s0092-8674(03)01020-1openalex-snapshot

A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties

inferredcites →https://doi.org/10.1016/s0166-2236(97)01213-7openalex-snapshot

The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease

inferredcites →https://doi.org/10.1016/s0169-409x(02)00149-7openalex-snapshot

Amyloidosis and Alzheimer’s disease

inferredcites →https://doi.org/10.1016/s0925-4439(00)00029-6openalex-snapshot

Alzheimer’s amyloid fibrils: structure and assembly

inferredcites →https://doi.org/10.1016/s1074-5521(97)90255-6openalex-snapshot

Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

inferredcites →https://doi.org/10.1016/s1471-4914(01)01931-1openalex-snapshot

Prions: disease propagation and disease therapy by conformational transmission

inferredcites →https://doi.org/10.1016/s1474-4422(05)70284-2openalex-snapshot

Risk of dementia in diabetes mellitus: a systematic review

inferredcites →https://doi.org/10.1021/acs.accounts.8b00131openalex-snapshot

Organization of Amino Acids into Layered Supramolecular Secondary Structures

inferredcites →https://doi.org/10.1021/acs.analchem.0c00593openalex-snapshot

Structural Characterization of Individual α-Synuclein Oligomers Formed at Different Stages of Protein Aggregation by Atomic Force Microscopy-Infrared Spectroscopy

inferredcites →https://doi.org/10.1021/acs.analchem.8b02373openalex-snapshot

Polymer-Ligand-Based ELISA for Robust, High-Throughput, Quantitative Detection of p53 Aggregates

inferredcites →https://doi.org/10.1021/acs.biochem.8b00472openalex-snapshot

Tyrosine-Generated Nanostructures Initiate Amyloid Cross-Seeding in Proteins Leading to a Lethal Aggregation Trap

inferredcites →https://doi.org/10.1021/acs.biomac.7b00351openalex-snapshot

Sequential Release of Proteins from Structured Multishell Microcapsules

inferredcites →https://doi.org/10.1021/acs.nanolett.9b02771openalex-snapshot

Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide

inferredcites →https://doi.org/10.1021/acsami.0c01574openalex-snapshot

Nanomechanical Properties and Phase Behavior of Phenylalanine Amyloid Ribbon Assemblies and Amorphous Self-Healing Hydrogels

inferredcites →https://doi.org/10.1021/acschemneuro.0c00281openalex-snapshot

Dual Targeting of Monomeric Tau and α-Synuclein Aggregation: A New Multitarget Therapeutic Strategy for Neurodegeneration

inferredcites →https://doi.org/10.1021/acschemneuro.0c00635openalex-snapshot

Accommodation of In-Register N-Linked Glycans on Prion Protein Amyloid Cores

inferredcites →https://doi.org/10.1021/acschemneuro.1c00427openalex-snapshot

Unusual Aggregates Formed by the Self-Assembly of Proline, Hydroxyproline, and Lysine

inferredcites →https://doi.org/10.1021/acschemneuro.8b00310openalex-snapshot

Amyloid-like Structures Formed by Single Amino Acid Self-Assemblies of Cysteine and Methionine

inferredcites →https://doi.org/10.1021/acsnano.1c02957openalex-snapshot

Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation

inferredcites →https://doi.org/10.1021/acsnano.9b02284openalex-snapshot

Self-Assembly of Artificial Sweetener Aspartame Yields Amyloid-like Cytotoxic Nanostructures

inferredcites →https://doi.org/10.1021/acsomega.2c01412openalex-snapshot

Inhibition Mechanisms of (−)-Epigallocatechin-3-gallate and Genistein on Amyloid-beta 42 Peptide of Alzheimer’s Disease via Molecular Simulations

inferredcites →https://doi.org/10.1021/bi0102398openalex-snapshot

Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

inferredcites →https://doi.org/10.1021/bi200967copenalex-snapshot

Fibrillation of the Major Curli Subunit CsgA under a Wide Range of Conditions Implies a Robust Design of Aggregation

inferredcites →https://doi.org/10.1021/bi961799nopenalex-snapshot

NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

inferredcites →https://doi.org/10.1021/cn500019copenalex-snapshot

Interaction between Prion Protein and Aβ Amyloid Fibrils Revisited

inferredcites →https://doi.org/10.1021/jacs.5b05482openalex-snapshot

Phenylalanine Oligomers and Fibrils: The Mechanism of Assembly and the Importance of Tetramers and Counterions

inferredcites →https://doi.org/10.1021/jacs.6b05129openalex-snapshot

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

inferredcites →https://doi.org/10.1021/nl0505896openalex-snapshot

Self-Assembled Peptide Nanotubes Are Uniquely Rigid Bioinspired Supramolecular Structures

inferredcites →https://doi.org/10.1038/197192b0openalex-snapshot

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

inferredcites →https://doi.org/10.1038/368756a0openalex-snapshot

Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

inferredcites →https://doi.org/10.1038/41580.1471-0080openalex-snapshot

Nature Reviews Molecular Cell Biology

inferredcites →https://doi.org/10.1038/42166openalex-snapshot

α-Synuclein in Lewy bodies

inferredcites →https://doi.org/10.1038/aps.2017.28openalex-snapshot

Amyloid beta: structure, biology and structure-based therapeutic development

inferredcites →https://doi.org/10.1038/cdd.2017.105openalex-snapshot

p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis

inferredcites →https://doi.org/10.1038/nature07761openalex-snapshot

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

inferredcites →https://doi.org/10.1038/nature20416openalex-snapshot

The activities of amyloids from a structural perspective

inferredcites →https://doi.org/10.1038/nchembio.1002openalex-snapshot

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria

inferredcites →https://doi.org/10.1038/ncomms14332openalex-snapshot

Bacillus subtilis biofilm extends Caenorhabditis elegans longevity through downregulation of the insulin-like signalling pathway

inferredcites →https://doi.org/10.1038/nm.4269openalex-snapshot

α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies

inferredcites →https://doi.org/10.1038/nmat2704openalex-snapshot

Nanoconfinement controls stiffness, strength and mechanical toughness of β-sheet crystals in silk

inferredcites →https://doi.org/10.1038/nnano.2011.102openalex-snapshot

Nanomechanics of functional and pathological amyloid materials

inferredcites →https://doi.org/10.1038/nnano.2016.186openalex-snapshot

Measuring conductivity of living Geobacter sulfurreducens biofilms

inferredcites →https://doi.org/10.1038/nrn3406openalex-snapshot

The many faces of α-synuclein: from structure and toxicity to therapeutic target

inferredcites →https://doi.org/10.1038/nrn3549openalex-snapshot

Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies

inferredcites →https://doi.org/10.1038/nsmb.1799openalex-snapshot

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

inferredcites →https://doi.org/10.1038/nsmb.2991openalex-snapshot

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

inferredcites →https://doi.org/10.1038/nsmb.3194openalex-snapshot

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

inferredcites →https://doi.org/10.1038/s41467-018-07966-5openalex-snapshot

Fibril formation and therapeutic targeting of amyloid-like structures in a yeast model of adenine accumulation

inferredcites →https://doi.org/10.1038/s41467-019-12683-8openalex-snapshot

Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue

inferredcites →https://doi.org/10.1038/s41580-018-0060-8openalex-snapshot

A new era for understanding amyloid structures and disease

inferredcites →https://doi.org/10.1038/s41594-020-0442-4openalex-snapshot

Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

inferredcites →https://doi.org/10.1038/s41598-017-02597-0openalex-snapshot

Effects of Protein Corona on IAPP Amyloid Aggregation, Fibril Remodelling, and Cytotoxicity

inferredcites →https://doi.org/10.1038/s41598-019-39261-8openalex-snapshot

Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity

inferredcites →https://doi.org/10.1038/s41598-020-61663-2openalex-snapshot

Formation of distinct prion protein amyloid fibrils under identical experimental conditions

inferredcites →https://doi.org/10.1038/s41598-020-77409-zopenalex-snapshot

α-Synuclein promotes IAPP fibril formation in vitro and β-cell amyloid formation in vivo in mice

inferredcites →https://doi.org/10.1038/s42004-018-0025-zopenalex-snapshot

Differential inhibition of metabolite amyloid formation by generic fibrillation-modifying polyphenols

inferredcites →https://doi.org/10.1038/s42004-019-0247-8openalex-snapshot

Induction of retinopathy by fibrillar oxalate assemblies

inferredcites →https://doi.org/10.1038/srep04267openalex-snapshot

Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies

inferredcites →https://doi.org/10.1038/srep08240openalex-snapshot

Inhibition of IAPP aggregation by insulin depends on the insulin oligomeric state regulated by zinc ion concentration

inferredcites →https://doi.org/10.1039/b912601eopenalex-snapshot

Metalloproteins and neuronal death

inferredcites →https://doi.org/10.1039/c8cc01423jopenalex-snapshot

Metabolite amyloid-like fibrils interact with model membranes

inferredcites →https://doi.org/10.1039/d0qm00784fopenalex-snapshot

Understanding the self-ordering of amino acids into supramolecular architectures: co-assembly-based modulation of phenylalanine nanofibrils

inferredcites →https://doi.org/10.1039/d1nj05172eopenalex-snapshot

Controlled aggregation properties of single amino acids modified with protecting groups

inferredcites →https://doi.org/10.1039/d1nr07741dopenalex-snapshot

Amyloid-mimicking toxic nanofibers generated via self-assembly of dopamine

inferredcites →https://doi.org/10.1042/etls20200002openalex-snapshot

Recent developments in antibody therapeutics against prion disease

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Amyloidosis: a convoluted story

inferredcites →https://doi.org/10.1073/pnas.0604035103openalex-snapshot

Characterization of the nanoscale properties of individual amyloid fibrils

inferredcites →https://doi.org/10.1073/pnas.0703310104openalex-snapshot

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization

inferredcites →https://doi.org/10.1073/pnas.0712036105openalex-snapshot

Mechanisms of prion protein assembly into amyloid

inferredcites →https://doi.org/10.1073/pnas.0812227106openalex-snapshot

Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation

inferredcites →https://doi.org/10.1073/pnas.0903691106openalex-snapshot

Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein

inferredcites →https://doi.org/10.1073/pnas.1600749113openalex-snapshot

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

inferredcites →https://doi.org/10.1073/pnas.1906124116openalex-snapshot

Parkinson’s disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein

inferredcites →https://doi.org/10.1073/pnas.2011196118openalex-snapshot

Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease

inferredcites →https://doi.org/10.1073/pnas.2012171118openalex-snapshot

Structural insights into α-synuclein monomer–fibril interactions

inferredcites →https://doi.org/10.1073/pnas.2017575118openalex-snapshot

Homocysteine fibrillar assemblies display cross-talk with Alzheimer’s disease β-amyloid polypeptide

inferredcites →https://doi.org/10.1073/pnas.2019631118openalex-snapshot

Mechanism of misfolding of the human prion protein revealed by a pathological mutation

inferredcites →https://doi.org/10.1073/pnas.2217835120openalex-snapshot

Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils

inferredcites →https://doi.org/10.1073/pnas.85.12.4506openalex-snapshot

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

inferredcites →https://doi.org/10.1073/pnas.88.23.10926openalex-snapshot

Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene.

inferredcites →https://doi.org/10.1073/pnas.96.24.14088openalex-snapshot

Neuronal overexpression of mutant amyloid precursor protein results in prominent deposition of cerebrovascular amyloid

inferredcites →https://doi.org/10.1074/jbc.270.7.3063openalex-snapshot

The α-Helical to β-Strand Transition in the Amino-terminal Fragment of the Amyloid β-Peptide Modulates Amyloid Formation

inferredcites →https://doi.org/10.1074/jbc.271.4.1988openalex-snapshot

Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin

inferredcites →https://doi.org/10.1074/jbc.273.16.9443openalex-snapshot

Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes

inferredcites →https://doi.org/10.1074/jbc.m109.080390openalex-snapshot

Entacapone and Tolcapone, Two Catechol O-Methyltransferase Inhibitors, Block Fibril Formation of α-Synuclein and β-Amyloid and Protect against Amyloid-induced Toxicity

inferredcites →https://doi.org/10.1074/jbc.m112.340638openalex-snapshot

Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils

inferredcites →https://doi.org/10.1074/jbc.m117.812388openalex-snapshot

Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy

inferredcites →https://doi.org/10.1074/jbc.r116.714576openalex-snapshot

Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis

inferredcites →https://doi.org/10.1074/jbc.ra118.004267openalex-snapshot

Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils

inferredcites →https://doi.org/10.1080/19336896.2015.1053685openalex-snapshot

Amyloids or prions? That is the question

inferredcites →https://doi.org/10.1080/19336896.2015.1110293openalex-snapshot

Prion protein scrapie and the normal cellular prion protein

inferredcites →https://doi.org/10.1084/jem.20161134openalex-snapshot

Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism

inferredcites →https://doi.org/10.1093/femsre/fuv015openalex-snapshot

Giving structure to the biofilm matrix: an overview of individual strategies and emerging common themes

inferredcites →https://doi.org/10.1093/jnen/nlz037openalex-snapshot

A Novel Eight Octapeptide Repeat Insertion in PRNP Causing Prion Disease in a Danish Family

inferredcites →https://doi.org/10.1096/fj.11-199851openalex-snapshot

Identification of oligomers at early stages of tau aggregation in Alzheimer's disease

inferredcites →https://doi.org/10.1101/cshperspect.a033118openalex-snapshot

Clinical Neurology and Epidemiology of the Major Neurodegenerative Diseases

inferredcites →https://doi.org/10.1110/ps.051622005openalex-snapshot

Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils

inferredcites →https://doi.org/10.1111/bpa.12941openalex-snapshot

Accumulation of cellular prion protein within β‐amyloid oligomer plaques in aged human brains

inferredcites →https://doi.org/10.1111/febs.14587openalex-snapshot

Crucial role of protein oligomerization in the pathogenesis of Alzheimer's and Parkinson's diseases

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Heterotypic interactions in amyloid function and disease

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Expression of Concern: Antioxidant compounds have potent anti‐fibrillogenic and fibril‐destabilizing effects for α‐synuclein fibrils in vitro

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Structures for amyloid fibrils

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The Ability of Amyloid β‐Protein [AβP (1–40)] to Form Ca2+ Channels Provides a Mechanism for Neuronal Death in Alzheimer's Disease

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Prion Protein Amyloidosis

inferredcites →https://doi.org/10.1111/jnc.12202openalex-snapshot

Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils

inferredcites →https://doi.org/10.1126/sciadv.1500137openalex-snapshot

Extension of the generic amyloid hypothesis to nonproteinaceous metabolite assemblies

inferredcites →https://doi.org/10.1126/sciadv.1600998openalex-snapshot

Adhesion mechanisms of curli subunit CsgA to abiotic surfaces

inferredcites →https://doi.org/10.1126/sciadv.abg9676openalex-snapshot

Genetic prion disease–related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM

inferredcites →https://doi.org/10.1126/science.1141736openalex-snapshot

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

inferredcites →https://doi.org/10.1126/science.1173155openalex-snapshot

Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

inferredcites →https://doi.org/10.1126/science.2218531openalex-snapshot

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

inferredcites →https://doi.org/10.1126/science.276.5321.2045openalex-snapshot

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

inferredcites →https://doi.org/10.1126/science.42.1074.161openalex-snapshot

The Proceedings of the National Academy of Sciences

inferredcites →https://doi.org/10.1155/2008/429274openalex-snapshot

Transthyretin and Amyloid in the Islets of Langerhans in Type‐2 Diabetes

inferredcites →https://doi.org/10.1155/2016/2798269openalex-snapshot

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

inferredcites →https://doi.org/10.1159/000337230openalex-snapshot

Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

inferredcites →https://doi.org/10.1177/030098589303000401openalex-snapshot

Islet Amyloid Polypeptide: A Review of Its Biology and Potential Roles in the Pathogenesis of Diabetes Mellitus

inferredcites →https://doi.org/10.1186/1742-2094-8-150openalex-snapshot

The contribution of activated astrocytes to Aβ production: Implications for Alzheimer's disease pathogenesis

inferredcites →https://doi.org/10.1186/gb-2001-3-1-reviews3002openalex-snapshot

The synucleins.

inferredcites →https://doi.org/10.1186/s13041-020-00637-xopenalex-snapshot

Characterization of a pathogenic variant in GBA for Parkinson’s disease with mild cognitive impairment patients

inferredcites →https://doi.org/10.1186/s40164-022-00317-7openalex-snapshot

p53 amyloid aggregation in cancer: function, mechanism, and therapy

inferredcites →https://doi.org/10.1186/s40478-020-01012-6openalex-snapshot

P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer’s disease

inferredcites →https://doi.org/10.1186/s40478-021-01136-3openalex-snapshot

Accumulation of alpha-synuclein within the liver, potential role in the clearance of brain pathology associated with Parkinson’s disease

inferredcites →https://doi.org/10.1212/wnl.43.11.2392openalex-snapshot

A new (two‐repeat) octapeptide coding insert mutation in Creutzfeldt‐Jakob disease

inferredcites →https://doi.org/10.1212/wnl.47.3.727openalex-snapshot

Familial Creutzfeldt-Jakob disease with a five-repeat octapeptide insert mutation

inferredcites →https://doi.org/10.1242/jcs.258316openalex-snapshot

Direct evidence of cellular transformation by prion-like p53 amyloid infection

inferredcites →https://doi.org/10.1371/journal.pbio.0040006openalex-snapshot

Functional Amyloid Formation within Mammalian Tissue

inferredcites →https://doi.org/10.1371/journal.pone.0013863openalex-snapshot

Inhibiting α-Synuclein Oligomerization by Stable Cell-Penetrating β-Synuclein Fragments Recovers Phenotype of Parkinson's Disease Model Flies

inferredcites →https://doi.org/10.1371/journal.pone.0067967openalex-snapshot

Amyloid Core Formed of Full-Length Recombinant Mouse Prion Protein Involves Sequence 127–143 but Not Sequence 107–126

inferredcites →https://doi.org/10.1371/journal.pone.0098753openalex-snapshot

Shaking Alone Induces De Novo Conversion of Recombinant Prion Proteins to β-Sheet Rich Oligomers and Fibrils

inferredcites →https://doi.org/10.1371/journal.ppat.1009628openalex-snapshot

The ultrastructure of infectious L-type bovine spongiform encephalopathy prions constrains molecular models

inferredcites →https://doi.org/10.1517/03009734000000014openalex-snapshot

Quantitative Studies of Amyloid in the Islets of Langerhans

inferredcites →https://doi.org/10.21037/atm.2018.12.12openalex-snapshot

Amino acid disorders

inferredcites →https://doi.org/10.2147/dddt.s289473openalex-snapshot

Epigallocatechin-3-Gallate Provides Protection Against Alzheimer’s Disease-Induced Learning and Memory Impairments in Rats

inferredcites →https://doi.org/10.2174/0929866529666220217124152openalex-snapshot

The Amyloid Precursor Protein Plays Differential Roles in the UVA Resistance and Proliferation of Human Retinal Pigment Epithelial Cells

inferredcites →https://doi.org/10.2174/187152709789541998openalex-snapshot

Cross Currents in Protein Misfolding Disorders: Interactions and Therapy

inferredcites →https://doi.org/10.2337/diab.27.4.357openalex-snapshot

Insular Amyloidosis and Diabetes Mellitus in Macaca Nigra

inferredcites →https://doi.org/10.26434/chemrxiv-2022-w0d5gopenalex-snapshot

Metabolite assemblies of urea cycle and uric acid pathway

inferredcites →https://doi.org/10.26434/chemrxiv-2023-9lk05-v2openalex-snapshot

Aggregation characteristics of non-aromatic polar amino acids and its association to amyloids

inferredcites →https://doi.org/10.3109/13506129.2012.762761openalex-snapshot

IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-β- d -glucose

inferredcites →https://doi.org/10.3233/jad-191346openalex-snapshot

Age-Specific Retinal and Cerebral Immunodetection of Amyloid-β Plaques and Oligomers in a Rodent Model of Alzheimer’s Disease

inferredcites →https://doi.org/10.3389/fcell.2022.852738openalex-snapshot

Aβ Assemblies Promote Amyloidogenic Processing of APP and Intracellular Accumulation of Aβ42 Through Go/Gβγ Signaling

inferredcites →https://doi.org/10.3389/fnagi.2016.00262openalex-snapshot

Tau Structures

inferredcites →https://doi.org/10.3389/fnagi.2018.00118openalex-snapshot

The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease

inferredcites →https://doi.org/10.3389/fnmol.2020.00035openalex-snapshot

Islet Amyloid Polypeptide: A Partner in Crime With Aβ in the Pathology of Alzheimer's Disease

inferredcites →https://doi.org/10.3389/fphar.2019.01084openalex-snapshot

Cajaninstilbene Acid Ameliorates Cognitive Impairment Induced by Intrahippocampal Injection of Amyloid-β1–42 Oligomers

inferredcites →https://doi.org/10.3390/biom10040548openalex-snapshot

The Status of p53 Oligomeric and Aggregation States in Cancer

inferredcites →https://doi.org/10.3390/biom12101409openalex-snapshot

Alzheimer’s Disease: Challenges and a Therapeutic Opportunity to Treat It with a Neurotrophic Compound

inferredcites →https://doi.org/10.3390/cancers13020269openalex-snapshot

p53, A Victim of the Prion Fashion

inferredcites →https://doi.org/10.3390/cancers13133344openalex-snapshot

Structural and Drug Targeting Insights on Mutant p53

inferredcites →https://doi.org/10.3390/ijmsopenalex-snapshot

International Journal of Molecular Sciences

inferredcites →https://doi.org/10.3390/ijms21176233openalex-snapshot

N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases

inferredcites →https://doi.org/10.3390/ijms22041800openalex-snapshot

The Effect of Octapeptide Repeats on Prion Folding and Misfolding

inferredcites →https://doi.org/10.3390/ijms22105075openalex-snapshot

Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils

inferredcites →https://doi.org/10.3390/ijms232112924openalex-snapshot

Amyloid Beta in Aging and Alzheimer’s Disease

showing the first 200 of 215

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.15212/bsms.7.e144070zenodo-depositor-declared

Oxidative stress and neuroregenerative processes – pathophysiological correlations and new pharmacotherapeutic approaches in the treatment of neuroregenerative diseases

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.139041openalex-snapshot

Tetrahydrofolic acid accelerates amyloid fibrillization, decreases cytotoxic oligomers and suppresses their toxicity

inferred← citeshttps://doi.org/10.1016/j.nanoso.2024.101413openalex-snapshot

Anti-amyloid activity of amino acid functionalized magnetic nanoparticles on αLactalbumin aggregation

inferred← citeshttps://doi.org/10.1021/acschemneuro.5c00403openalex-snapshot

Self-Assembled Phenylalanine-Derived Metabolites as Potential Neurotoxic Amyloids in Phenylketonuria

inferred← citeshttps://doi.org/10.1021/acschemneuro.6c00057openalex-snapshot

The Effect of Cu 2+ and Zn 2+ Ions’ Nonbonded Interactions on the Aggregation of β-Amyloid 1–16 and 25–35 Fragments─A Molecular Dynamics Simulation Study

inferred← citeshttps://doi.org/10.1039/d5na00259aopenalex-snapshot

Nucleobase self-assembly: aggregation, morphological characterization, and toxicity analysis

inferred← citeshttps://doi.org/10.1109/metroaerospace61015.2024.10591612openalex-snapshot

Thin Polymeric Film Functionalized by AuNPs for High Sensitive Protein Biosensing

inferred← citeshttps://doi.org/10.20944/preprints202312.1258.v1openalex-snapshot

Association of Parkinson’s Disease and Cancer: New Findings and Possible Mediators

inferred← citeshttps://doi.org/10.3390/biochem6030023openalex-snapshot

Mechanistic Insights into the Hypoxia-Inducible Factor-1 Paradox in Alzheimer’s Disease: A Double-Edged Sword in Neurodegeneration

inferred← citeshttps://doi.org/10.3390/ijms25073899openalex-snapshot

Association between Parkinson’s Disease and Cancer: New Findings and Possible Mediators

inferred← citeshttps://doi.org/10.3390/jpm13101511openalex-snapshot

Translating Biospectroscopy Techniques to Clinical Settings: A New Paradigm in Point-of-Care Screening and/or Diagnostics

inferredcites →https://doi.org/10.3390/life13071523openalex-snapshot

inferred← citeshttps://doi.org/10.3390/molecules28166032openalex-snapshot

Scaffold Morphing and In Silico Design of Potential BACE-1 (β-Secretase) Inhibitors: A Hope for a Newer Dawn in Anti-Alzheimer Therapeutics

inferred← citeshttps://doi.org/10.3897/bsms.7.144070openalex-snapshot

Oxidative stress and neuroregenerative processes – pathophysiological correlations and new pharmacotherapeutic approaches in the treatment of neuroregenerative diseases

inferred← citeshttps://doi.org/10.7190/shu-thesis-00568openalex-snapshot

The role of eIF2Bα in the integrity of eIF2B bodies

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