A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
about
Identification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286Converting the Highly Amyloidogenic Human Calcitonin into a Powerful Fibril Inhibitor by Three-dimensional Structure Homology with a Non-amyloidogenic AnalogueStructure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environmentMechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescenceSecondary Structure of Rat and Human Amylin across Force FieldsModels of membrane-bound Alzheimer's Abeta peptide assembliesHexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Cytotoxic aggregation and amyloid formation by the myostatin precursor proteinSensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsTau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeatsIdentification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregationNatural tri- to hexapeptides self-assemble in water to amyloid beta-type fiber aggregates by unexpected alpha-helical intermediate structures.Prediction and analysis of antibody amyloidogenesis from sequences.Stable and metastable states of human amylin in solution.The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfacesStructural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationRegulation and aggregation of intrinsically disordered peptidesCytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptideInvestigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityHighly neurotoxic monomeric α-helical prion protein.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Identification of minimally interacting modules in an intrinsically disordered protein.Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid BilayersPyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionAliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosisSlow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregationAdsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated AggregationIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effectsHelical conformation of the SEVI precursor peptide PAP248-286, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusion.
P2860
Q21144909-FD6CFB05-6D29-40E7-881D-5EA8A77ECAC2Q26775893-05BD6BC1-947A-4C7B-B3F8-CBA8A0F20FB0Q26830682-D14DBBBD-81FE-4160-A8AA-F18E9B33A379Q27658538-972C21E2-3A17-457D-86FB-035063E163BCQ27665898-2018C424-9767-4E4B-820B-635E72FF3256Q27670641-3FDA35A9-B477-4746-BD16-23B85CCAFE86Q28533560-3EAC888C-C1AD-48E3-BABB-4FC06FF30C60Q28546876-DE39744D-5C48-4BBD-99E6-6FB867F90410Q30155996-540D0F7F-96D4-4B90-8840-8C76E7DFF1B8Q30502077-F9A1833E-2E40-4ACD-B86D-220920F0245AQ30842640-C17AA6AE-4805-4EC8-AB45-19FECA5D32FCQ33356614-4DC11848-7B38-42F0-A55B-AC48DEB86E50Q33531807-F83790C9-3AC8-48DF-AE74-40F2943C9E98Q34114138-7F6CD8FF-CB89-4027-AA8D-7811333BC45CQ34191817-9B4AB911-A72D-40E0-A4EB-3153C53AB461Q34203739-AF8BCCD9-EE9E-4406-A486-139ED7D10AD0Q34279026-61F2E788-248C-4148-B9ED-3D8F8A495CF9Q34534029-418D74AA-7D0D-4E5C-B062-3C0EFFBA73DAQ34544805-E08857AC-0F8C-4581-9969-228A3A6E4660Q34590706-D8127222-076A-4E7E-AFCD-05C28C8AE7C3Q34978500-05ACA53F-63DA-475E-91D1-9A56E94D5422Q34979345-0A8B8D78-F7E3-458A-BF64-647ECF862FBFQ35139765-EB76088B-3167-49F4-9E76-B8845DBB30C5Q35157010-6454BD40-4F1D-477A-B5E4-9872F360D1D9Q35585206-09E3B835-99CC-4723-AD1F-7E37EDCDF58DQ35679065-B2B2F059-2288-4329-949A-73CAA99A19B2Q35691076-B35CCDD4-C5ED-4C1D-ADAE-D66CB175766CQ35779305-D0B90143-8CC6-45E1-A31F-19F6E776ADA3Q35978258-79662D4A-9BBE-484A-8BBB-F57581C8267EQ36238139-497F8F1F-0F5F-49E3-99F7-93B54901B4B0Q36329000-9F0870C3-463E-4E22-95B6-C088BE37FCA5Q36356545-16B2BBA3-7A9F-48A8-8FB9-B61930820D86Q36499539-32A9C7F3-8B53-4590-8DEA-CF5C47CDCB12Q36535089-2669EEEC-1A6A-4860-B623-AC9A66D7E06CQ36600026-8204193B-0B53-4256-B625-3C7397314437Q36657560-D5C5C9F8-BCE7-4CD9-8C69-EEAEBF2FDDB2Q36790338-0361EBF6-2E08-4F8E-BAC1-9213A1134B94Q37120813-68E52707-0D3C-4585-95B8-63B67F30619DQ37120817-AACA0B62-CF82-4D8A-933C-B6A639A015F1Q37405961-711679DC-D960-40FF-9FC1-FAF34DF44468
P2860
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@en
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@nl
type
label
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@en
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@nl
prefLabel
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@en
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@nl
P2860
P356
P1433
P1476
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
@en
P2860
P304
P356
10.1088/1478-3975/6/1/015005
P577
2009-02-10T00:00:00Z