Alpha-synuclein binds large unilamellar vesicles as an extended helix
about
Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins.Dynamic structural flexibility of α-synucleinBiophysical characterization of α-synuclein and its controversial structureExploring the accessible conformations of N-terminal acetylated α-synucleinA flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceFunction and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescenceCross-Scale Integrin Regulation Organizes ECM and Tissue Topology.Structural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane SurfacesThe Synaptic Function of α-SynucleinMembrane remodeling and mechanics: Experiments and simulations of α-SynucleinInvestigation of intramolecular dynamics and conformations of α-, β- and γ-synucleinUnderstanding protein non-folding.The presence of non-native helical structure in the unfolding of a beta-sheet protein MPT63.Protein folding at single-molecule resolution.Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Biophysics of α-synuclein membrane interactions.Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.Tau mutants bind tubulin heterodimers with enhanced affinity.Tryptophan probes at the alpha-synuclein and membrane interface.The role of the lipid bilayer in tau aggregationα-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Single molecule characterization of α-synuclein in aggregation-prone states.Conformational heterogeneity of α-synuclein in membrane.Effects of curvature and composition on α-synuclein binding to lipid vesiclesAlpha-synuclein function and dysfunction on cellular membranes.Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assemblyExpression of mutant alpha-synuclein modulates microglial phenotype in vitroAcceleration of α-synuclein aggregation by exosomes.Alpha-synuclein populates both elongated and broken helix states on small unilamellar vesicles.Structural and dynamical insights into the membrane-bound α-synuclein.Copper(II) enhances membrane-bound α-synuclein helix formation.Molecular details of α-synuclein membrane association revealed by neutrons and photons.Membrane curvature sensing by amphipathic helices: a single liposome study using α-synuclein and annexin B12Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityBiophysics of α-synuclein induced membrane remodellingDepth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation.Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.α-Synuclein induces both positive mean curvature and negative Gaussian curvature in membranesNative chemical ligation of thioamide-containing peptides: development and application to the synthesis of labeled α-synuclein for misfolding studies
P2860
Q24633488-ABFAA3C6-F5CA-4CCE-BF6C-E4F27C37E046Q26770060-36407C56-56A5-45DD-AB32-C3147CE3A929Q26828504-D20B2CA9-495E-41D1-BE05-C95BF4987F37Q26852660-346C951A-C5EF-4E26-921C-073A0BDC1D56Q26997922-0A0AAD0D-F5E6-41A8-BC2B-218B4F58951CQ27026292-17967914-E819-4E1B-8D77-2C498D60BB68Q27314679-095C293F-CC47-4427-8D31-60A8C71A0A2BQ27666058-A734CFCD-4087-445B-8C67-334906D0175FQ27694711-1F92EEDE-2132-4AD7-8467-082AFE980EE0Q28066666-E74DFD1B-1EAA-4B92-8A2E-25707B1A355DQ28539243-64C1D209-41B0-418A-BA91-1DBC1CCE49C9Q30385084-567BF876-2FA8-4D9B-BA4C-9821A3F44669Q30396659-7F92A556-FB42-468E-B61B-E4B302006233Q30399457-2F2F30E7-9FCB-4918-A4CF-18D5BCA36158Q30402710-5E81CA4D-65C8-4940-BC50-C763AC423EB6Q30405705-BDDEFB4E-DCFF-4DF8-BBB3-0724C00A3298Q33647141-42C77662-1483-42FE-AA6F-D43B56CE9223Q33674452-4AAEA705-88F4-488D-B90B-0BBDB83D4F2DQ33806266-DD2074EF-9BE8-4419-B1CF-120D8B241665Q33880243-B5B3E7EA-CDF5-49C4-9111-169B3730E8BDQ33926400-61A179C0-D6D0-40E6-9250-45D00040BA5BQ34107467-AD09598B-829D-4A45-A28F-4935C6DBEF29Q34250768-86D0655C-4C45-419F-9F9D-BF44C3E8A308Q34325107-81461780-7E2F-4E31-97C3-4C21E9DD80BBQ34590790-F1FE22E2-D2D7-42F6-9C3E-3A529B61A58FQ34774324-A4D67322-AA42-41F5-ABB4-B977ED378113Q34779845-737843C2-78BC-4A30-8EEC-F5F612784489Q35014520-A895CA22-BB34-42A8-B5DC-3FF208FE1C9FQ35048929-74CA6A60-C17C-40A0-B860-A315798850AFQ35065209-D213CFD9-B6AB-4BF7-BAB7-870AECB7F774Q35078181-8ADEB916-EB4C-4A4D-8024-9B4111BE6279Q35385538-180332F9-070F-4574-8D2A-3A4BDEBAE337Q35565655-F3BE58FF-01A9-4775-AE5E-86A6F03337EDQ35604940-6F267F1D-6330-411E-8DD0-33FD7A5D38DEQ35691076-8418F78E-D466-489B-816B-B62152048D26Q35732516-2ECE7EB7-0F9D-41F9-B0CE-C582A649969DQ35743295-ED723D83-FCC0-497E-9404-6C7FB58E7D9CQ35812347-A182D45A-2A5A-4047-B7C1-74CE7E874B1AQ36020832-0C098D5D-F5DD-426F-9F19-C8E453B8E6BCQ36153110-DD80DABC-0D7C-4225-8A49-9F5D31F2FF07
P2860
Alpha-synuclein binds large unilamellar vesicles as an extended helix
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
Alpha-synuclein binds large unilamellar vesicles as an extended helix
@en
Alpha-synuclein binds large unilamellar vesicles as an extended helix.
@nl
type
label
Alpha-synuclein binds large unilamellar vesicles as an extended helix
@en
Alpha-synuclein binds large unilamellar vesicles as an extended helix.
@nl
altLabel
α-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix†
@en
prefLabel
Alpha-synuclein binds large unilamellar vesicles as an extended helix
@en
Alpha-synuclein binds large unilamellar vesicles as an extended helix.
@nl
P2860
P356
P1433
P1476
Alpha-synuclein binds large unilamellar vesicles as an extended helix
@en
P2093
Adam J Trexler
Elizabeth Rhoades
P2860
P304
P356
10.1021/BI900114Z
P407
P577
2009-03-01T00:00:00Z