Biology of amyloid: structure, function, and regulation.
about
Origins of amyloid-βPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPSelf-propagation of pathogenic protein aggregates in neurodegenerative diseasesAmyloid cannot resist identificationEmerging roles of extracellular vesicles in the nervous systemTipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular InterfacesMolecular basis of -amyloid oligomer recognition with a conformational antibody fragmentAn α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation FactorAmyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicitySelf-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EASAtomic View of a Toxic Amyloid Small OligomerCarbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domainsPMEL Amyloid Fibril Formation: The Bright Steps of PigmentationMeasurement of amyloid formation by turbidity assay-seeing through the cloudRebels with a cause: molecular features and physiological consequences of yeast prionsInteraction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationInteractions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's diseaseStructure and dynamics of amyloid-β segmental polymorphismsTowards Prebiotic Catalytic Amyloids Using High Throughput ScreeningThe drive to life on wet and icy worldsLysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteinsβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic toolsSpecific chaperones and regulatory domains in control of amyloid formation.Structural gymnastics of multifunctional metamorphic proteins.Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers.Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to altered dopamine homeostasis and behavioral deficits.Insulin Resistance as a Link between Amyloid-Beta and Tau Pathologies in Alzheimer's Disease.Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionMutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenicGenomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomesThe [Het-s] prion, an amyloid fold as a cell death activation triggerInhibition study on insulin fibrillation and cytotoxicity by paclitaxel.The mechanism of toxicity in HET-S/HET-s prion incompatibility.Functional amyloidogenesis and cytotoxicity-insights into biology and pathology.An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prion.
P2860
Q21266674-C69B5AA5-3A1D-4E67-886E-B3A4F77AB4DFQ26823798-9A9A5CE5-D897-4476-AD16-EE2F29B9F1CCQ26830682-B00E4985-2E29-435C-B359-818DEEA00B2EQ26996441-01328160-25B0-4BF3-8A53-A96E3D020D6AQ27012702-A3B3D10A-1095-4D3A-A3F7-14E8FB7F9E79Q27025173-9EDD3149-64C3-4A88-A491-EE23C13FDD05Q27318564-B49A7583-D473-429D-8B29-678D14C6FE50Q27670832-EE7E11C0-8F04-4C2E-A60C-8ACBFE69F32CQ27670840-D9A51632-B696-4DF6-9F2C-FAFB28D25010Q27674676-B5A84561-055F-4B84-99E5-FC901BA81212Q27677102-6BC564D7-2638-4D3E-ABB0-24C0009DEE79Q27677948-DD4925A4-5A09-46BF-8B82-515215D3D3E3Q27684943-3758D14C-DE3E-4931-B79F-DE03A9BE12B5Q28076932-3868D533-CFBC-45FD-B27B-653A2A202A7AQ28080287-C2040793-41EE-43E9-A7D2-9ACF644E49EFQ28082218-7BD62B0C-04BF-4A97-9584-A5E063026E66Q28247808-3AA2F31C-7FB4-437B-946E-1B05EDCC27ECQ28391762-0F8CCB14-473D-4F2E-B6AE-6B09D5968828Q28481479-8672196B-695A-4967-9A00-6F38712A4EE5Q28606535-89C137CB-54E4-49E4-B042-4D1362293B20Q28658605-E66710E8-B3CF-4C63-8FA6-A38C3966FB93Q30040391-2BC28DB9-8462-464B-8B1F-2C681EDF40C4Q30155204-BAC68AE0-F042-4AD1-A306-A60DA87FB77AQ30355498-EED681B2-3A66-46F5-960B-7D8591928981Q30378979-8B3116A9-F9FA-41C1-8A45-22BB0F6C353EQ30402034-BA40F20B-8518-4C18-B772-7BF761D4E243Q30826123-5A0F5841-5F96-4CE1-8AFA-4E681AE4F6C3Q30826347-A8E1FE36-9ADA-4B1C-B843-F10C385114E7Q33628048-DD63CB63-8FD5-43C8-976E-71713538ABC0Q33749018-064E779A-E5FF-4309-8BA2-13D6AE10C32EQ33788913-F03B9928-ACE3-41F0-8171-EA4DEBA96758Q34031196-EF526324-9539-4375-8404-EC005DC929D0Q34228516-1AE451DB-A172-4758-8286-DEDEE90B1765Q34288773-0B81CA10-4628-4AA4-B88E-93A6CB6055E2Q34404870-43603F18-D961-4904-A6FC-46C6DEC71732Q34539592-620FF0DF-3772-47ED-AE5E-F72CE038D09AQ34539609-389AA117-6969-4E1E-8BFD-5536230CE793Q34575728-B4EB4D29-10D0-41D3-B30D-318EE5B2AFD2Q34650262-26E5EABA-4624-4BB9-AACC-C5CFDE7AFC9FQ34762195-5D022B03-464B-485B-B911-80745C84423C
P2860
Biology of amyloid: structure, function, and regulation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Biology of amyloid: structure, function, and regulation.
@en
Biology of amyloid: structure, function, and regulation.
@nl
type
label
Biology of amyloid: structure, function, and regulation.
@en
Biology of amyloid: structure, function, and regulation.
@nl
prefLabel
Biology of amyloid: structure, function, and regulation.
@en
Biology of amyloid: structure, function, and regulation.
@nl
P1433
P1476
Biology of amyloid: structure, function, and regulation.
@en
P2093
Jason Greenwald
Roland Riek
P304
P356
10.1016/J.STR.2010.08.009
P577
2010-10-01T00:00:00Z