Raft lipids as common components of human extracellular amyloid fibrils. - Wikidata - awgldk - TriplyDB

Raft lipids as common components of human extracellular amyloid fibrils.

Raft lipids as common components of human extracellular amyloid fibrils.

http://www.wikidata.org/entity/Q33771985

about

Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides FRET studies of lipid-protein aggregates related to amyloid-like fibers Electron tomography of early melanosomes: implications for melanogenesis and the generation of fibrillar amyloid sheets.Effects of membrane interaction and aggregation of amyloid β-peptide on lipid mobility and membrane domain structure.Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Functional amyloids as natural storage of peptide hormones in pituitary secretory granules.NBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils.Complex and multidimensional lipid raft alterations in a murine model of Alzheimer's disease A distinct subfraction of Aβ is responsible for the high-affinity Pittsburgh compound B-binding site in Alzheimer's disease brain Membrane lipid co-aggregation with α-synuclein fibrils.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL.Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits.Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2-microglobulin.Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions.Serum amyloid A and protein AA: molecular mechanisms of a transmissible amyloidosis.beta(2)-microglobulin: from physiology to amyloidosis.Review of eprodisate for the treatment of renal disease in AA amyloidosis.Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity.On the lag phase in amyloid fibril formation.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Cellular mechanism of fibril formation from serum amyloid A1 protein.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates.Sustained activation of sphingomyelin synthase by 2-hydroxyoleic acid induces sphingolipidosis in tumor cells.Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol.Retardation of Abeta fibril formation by phospholipid vesicles depends on membrane phase behavior.Influence of C-terminal truncation of murine Serum amyloid A on fibril structure.Monomer-dependent secondary nucleation in amyloid formation.Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13.The Role of Cholesterol in Driving IAPP-Membrane Interactions.Cell-to-cell transfer of SAA1 protein in a cell culture model of systemic AA amyloidosis Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's beta-amyloid peptide variants.

P2860

Q24649564-9D1B6B98-68B0-4E71-B803-4B6DAC369073 Q26774381-20F5347E-643E-4D02-B09F-D6CCB99BAB1B Q26830682-81999710-93FB-458A-A8BB-C9DFA751BF4B Q27022467-F6EA7087-EFD1-4BCD-B8B4-24AB05A39064 Q27693901-12A650FB-31FA-473E-AC0D-6203CA9A9B95 Q30485074-56B5A7D3-31F3-45AB-8375-3DE32F0302B4 Q31113633-4F9CDE5F-34E9-4FBC-9090-14D71CD0F9F4 Q33257571-1CDE9FF4-D587-4428-8A6B-759AC3546BBB Q33429003-6602DB5C-7581-4ABA-93AC-C414F20AAEE8 Q33834886-288E2ED8-D954-4081-AD6F-8363AE48156A Q34149504-0B9A0276-58B9-40D2-BFDC-C43E046CC824 Q34381556-696C8F35-0FEE-4621-8A4C-FB522B595997 Q34381799-3502BF45-3156-4EA0-B867-6AB154D6613A Q35023098-5D628090-15BC-4831-907A-D59CFA49C58E Q35139664-FCFD2C27-FB9F-4660-8D3D-F12DAA214223 Q35886290-E570449D-BCFF-4DE9-9EBB-3040F7A40848 Q36007352-B5AFFDDA-EE2C-420C-ADD6-E641FDCFFB3F Q36579443-B808CAEC-42BF-4710-9006-E2E817B6ECA3 Q36650385-D4D6CFFD-9105-461C-8EEE-3BD82EB83E7A Q37117146-78AFC42F-63E3-4505-BE9F-8EEBFC8E0B9C Q37165186-74E96667-158F-499B-AFE6-692B42FA8EEC Q37357717-BCBD2BEC-99B3-4001-AE76-18A9057E8655 Q37459593-1D25F754-021C-474E-8CB7-D9E302C3F8A6 Q37573510-907055EA-7634-450C-A04A-B389B2292685 Q37994670-D288D539-9441-45FF-B11C-AB954D1A2792 Q38033158-94A18858-F938-4AC3-BB3E-1689050874DB Q38365518-163E0EBB-6E9F-4849-8D81-4094DD3561DE Q38635739-C33313B2-65B3-4514-BA8C-C687394D338D Q38715103-3DF3A552-B193-4788-8782-2EC627400C70 Q39126169-57C29714-5132-4984-83EE-7908005AFDD2 Q39176826-EF1EDF0E-29F5-4306-A910-C1CD1B6FF834 Q39183511-BB53A455-FE11-4D7A-847A-99A047B407EA Q39864309-E3643887-6255-409F-8821-CB3F62C1B6C6 Q40626071-B766BF48-1027-4EF0-8954-E3A13B976141 Q41094376-162C2CBF-650B-4F26-A420-12842C0FA82B Q41579457-0F8A988D-C6C6-4158-8E5A-D6939BAED186 Q41816548-6578AD93-03E5-4446-804E-99E2BB5F74DA Q42182958-50FC8CAB-2A6D-4655-ABBF-13377E663806 Q42209063-17268EB9-4D92-4CA6-8C67-B4BC94F8D667 Q42273180-2A6967DA-4292-4F0B-A7DE-D3963DF13294

P2860

Raft lipids as common components of human extracellular amyloid fibrils.

http://www.wikidata.org/entity/Q33771985

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Raft lipids as common components of human extracellular amyloid fibrils.

@ast

Raft lipids as common components of human extracellular amyloid fibrils.

@en

type

label

Raft lipids as common components of human extracellular amyloid fibrils.

@ast

Raft lipids as common components of human extracellular amyloid fibrils.

@en

prefLabel

Raft lipids as common components of human extracellular amyloid fibrils.

@ast

Raft lipids as common components of human extracellular amyloid fibrils.

@en

P1433

Q33771985-3B679B17-90C1-4DD6-A932-19B2D52929F1

P1476

Q33771985-52A6B2FA-9A2E-4728-B60E-5402FD664027

P2093

Q33771985-0923BA4C-E5B3-4087-B5DC-2BAC34A1BB86

Q33771985-17AC3B78-233E-47E2-ACA7-1FF774AA1845

Q33771985-25C89465-7304-4CBC-8E41-14A427BCA6FB

Q33771985-2ACDC27D-8F0B-421F-A67F-110A7BEA1861

Q33771985-337850A3-9845-44A7-A698-FDC6C9C97ACE

Q33771985-6CE1FEF0-8BBF-4802-A669-EEA02996CC7F

Q33771985-768FB17B-CDD5-48CD-B309-362612C1CAD9

Q33771985-87E9FFB7-F7A2-4B4A-B292-C8D7DFE65EDA

Q33771985-AB07735E-B130-464C-9771-E531009E5AA5

Q33771985-ACE333BB-F7F1-4030-ADE7-95A4E185307A

P2860

Q33771985-0749018F-B4B6-4E08-A53C-A2980F7062D5

Q33771985-1B3D66A4-2857-4B27-AC5C-DF5423FC51D0

Q33771985-2698841C-C270-4229-A082-B81789D14781

Q33771985-2CB32E94-5222-4FB0-83F1-37ED218DD8A4

Q33771985-2F5963D4-2802-478B-AA48-245E5A9C64FF

Q33771985-404B8DCD-DBDC-490E-90FD-C95DF7082A81

Q33771985-56E388E4-7668-4157-9FB6-E0CEAD77D45A

Q33771985-5947FB3B-1B6B-4CED-B0AB-8BC7702F3F7A

Q33771985-5BAFA9C6-7D95-47D5-B08C-AF6CED05E579

Q33771985-6BA95C60-F562-4CA5-95ED-B20F46C3B67B

P304

Q33771985-D8ECD721-3B8F-4A28-A159-080DDFFB1260

P31

Q33771985-8261AD37-E4E3-4E91-862B-E1096FD936C2

P356

Q33771985-A23BA291-5566-402E-92B6-246F41DF89FD

P407

Q33771985-CBE7609D-3B55-48E1-829A-59ECCE7F95E3

P433

Q33771985-36B3ADE4-DE5F-48D6-B524-5F1DFC8AA1CE

P478

Q33771985-8E5A6F00-4815-4342-80ED-32E061F184BA

P50

Q33771985-AB010FF7-11B7-48E0-A2F4-76FD4B11D775

P577

Q33771985-3C474404-265B-471B-8140-A665E6AC2950

P5875

Q33771985-88E539FF-8E0C-42A7-9AEB-5705D7630B94

P698

Q33771985-0B7F74B7-B7C8-4815-93DA-59123A96B990

P932

Q33771985-EE76A468-2891-4BFB-A5D4-845DE8E10D59

P356

PNAS.0407035102

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Raft lipids as common components of human extracellular amyloid fibrils.

@en

P2093

Anja Radestock

http://www.w3.org/2001/XMLSchema#string

Astrid Tannert

http://www.w3.org/2001/XMLSchema#string

Christian Leisner

http://www.w3.org/2001/XMLSchema#string

Gerald P Gellermann

http://www.w3.org/2001/XMLSchema#string

Marcus Fändrich

http://www.w3.org/2001/XMLSchema#string

Mordechai Pras

http://www.w3.org/2001/XMLSchema#string

Peter Hortschansky

http://www.w3.org/2001/XMLSchema#string

Reinhold P Linke

http://www.w3.org/2001/XMLSchema#string

Shmuel Shtrasburg

http://www.w3.org/2001/XMLSchema#string

Stephan Diekmann

http://www.w3.org/2001/XMLSchema#string

P2860

The structural basis of protein folding and its links with human disease

Cholesterol, lipid rafts, and disease

Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

Lipid domain structure of the plasma membrane revealed by patching of membrane components

Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry.

Amyloid fibrils from muscle myoglobin.

Review: amyloidogenesis-unquestioned answers and unanswered questions.

Transmissibility of systemic amyloidosis by a prion-like mechanism.

P304

6297-6302

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.0407035102

http://www.w3.org/2001/XMLSchema#string

P407

P433

18

http://www.w3.org/2001/XMLSchema#string

P478

102

http://www.w3.org/2001/XMLSchema#string

P50

Christoph Röcken

P577

2005-04-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7885620

http://www.w3.org/2001/XMLSchema#string

P698

15851687

http://www.w3.org/2001/XMLSchema#string

P932

1088351

http://www.w3.org/2001/XMLSchema#string