The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms. - Wikidata - awgldk - TriplyDB

The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.

The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.

http://www.wikidata.org/entity/Q34107467

about

Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein Systematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activities Dynamic structural flexibility of α-synuclein Biophysical characterization of α-synuclein and its controversial structure Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation The Synaptic Function of α-Synuclein Synaptic vesicles position complexin to block spontaneous fusion Modeling Protein-Micelle Systems in Implicit Water.Biophysics of α-synuclein membrane interactions.α-Synuclein-induced tubule formation in lipid bilayers α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.Lys-63-linked ubiquitination by E3 ubiquitin ligase Nedd4-1 facilitates endosomal sequestration of internalized α-synuclein.Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Conformational heterogeneity of α-synuclein in membrane.Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity.Alpha-synuclein function and dysfunction on cellular membranes.Structural and dynamical insights into the membrane-bound α-synuclein.Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicity Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles.Characterization of a disordered protein during micellation: interactions of α-synuclein with sodium dodecyl sulfate.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.α-Synuclein induces both positive mean curvature and negative Gaussian curvature in membranes Pulsed ESR dipolar spectroscopy for distance measurements in immobilized spin labeled proteins in liquid solution.The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein.Locating a lipid at the portal to the lipoxygenase active site Conformational ensemble of the sodium-coupled aspartate transporter.Atomic-level description of protein-lipid interactions using an accelerated membrane model.N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound α-synuclein and increases its affinity for physiological membranes.Lysosomal storage disorders and Parkinson's disease: Gaucher disease and beyond.Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs)Folding and misfolding of alpha-synuclein on membranes.Hunting the chameleon: structural conformations of the intrinsically disordered protein alpha-synuclein.Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cell.ɑ-Synuclein strains and the variable pathologies of synucleinopathies.Explaining the structural plasticity of α-synuclein.

P2860

Q22061749-E844DF19-ABEA-4CFA-A832-F89620490E48 Q26269871-6D1173E0-7770-464A-94C5-3EF9B3F3CEFE Q26770060-EA030EF4-B72E-43AC-88B5-03E74F803C8D Q26828504-BC8DB5A7-9544-40C8-A96B-9D790267F435 Q27667412-305739A2-8E80-47BF-8276-21D4EC48220F Q27694711-622C92E1-4FF6-4C84-A51B-B15ABFF3D4C7 Q28284213-414E2ACA-F59A-4E88-AEAA-5826FD773CA6 Q30152916-41EB8004-CB36-4465-8833-42B7DFCF8795 Q30405705-589A8679-4B87-4ACF-A7E4-D233F5670AD7 Q30500318-F487CEA0-C186-4006-B001-577F7BD6B131 Q33926400-FAE5A1D1-0983-4D7F-AA6B-9AE5833AD763 Q33991720-B205E572-BF13-4CF5-B367-A6BA1F9F6CB6 Q34073890-D7CBD331-E986-4706-B764-942C884D0758 Q34203739-D0A3A071-6435-4AA2-915B-D09BA18B5895 Q34252869-445C3DFB-E8E4-4578-BCD2-D8660B358565 Q34325107-67A55366-6200-4629-9972-1CC24987392D Q34438315-ECD8F701-7F73-4CB3-8437-DBE4AD1C378B Q34774324-3430EE6F-A2D6-45CA-B6ED-4C821081382F Q35078181-5BDD77CE-D177-41DA-8221-9748EC584E6A Q35150090-E7561301-D4E1-4071-9358-34B2924054D9 Q35691076-831DB739-05F8-4492-A460-91B397B3F089 Q35812347-C97DD51A-07A2-4177-897E-DB2C13321F53 Q35865367-9BB3D7F7-9555-48A7-A709-030AF5220CC3 Q35902646-498C19D9-DA54-434B-8744-82B5E4AB3B26 Q35975683-187A130F-57D8-46D9-8358-174971903751 Q35978258-4CCC00C9-32C0-4F94-BC0C-AFB7BD815577 Q36020832-B90075B5-FABC-4016-8B68-9B2EDC60413E Q36130797-FADFB963-C0D8-4B2B-A481-0E53DD793EE2 Q36386314-11D24A79-3C97-4FC5-AA43-A481AD3B5246 Q36439481-4906BEC1-F311-4EA7-8F30-C990D40E4682 Q36589222-06CD7679-92FC-47A5-982E-F44D71542D80 Q36927711-5BF4566A-7357-485B-9217-5BB15C664349 Q37563546-50EC1302-C101-4CBA-B423-A18AC5B05CC6 Q37880734-E9AA9168-B02D-4F14-88FC-3782B801091D Q37891686-CCC6E86C-651C-4CC3-BA06-4FF761D389BA Q37938437-6BCECDC5-85E4-4CE5-8309-0A1244450457 Q37995991-DDF40642-7E2C-4B61-AB1B-D3637921D7CB Q38684340-33DE940B-508E-4F91-9521-5A2A4A43ECC5 Q38753941-69EDF348-4A21-43B5-9556-220EE7F8AEA1 Q39485110-81E54460-FE94-4588-AEC5-FD91D04425DD

P2860

The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.

http://www.wikidata.org/entity/Q34107467

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

The lipid-binding domain of wi ...... oken and extended helix forms.

@ast

The lipid-binding domain of wi ...... oken and extended helix forms.

@en

The lipid-binding domain of wi ...... oken and extended helix forms.

@nl

type

label

The lipid-binding domain of wi ...... oken and extended helix forms.

@ast

The lipid-binding domain of wi ...... oken and extended helix forms.

@en

The lipid-binding domain of wi ...... oken and extended helix forms.

@nl

prefLabel

The lipid-binding domain of wi ...... oken and extended helix forms.

@ast

The lipid-binding domain of wi ...... oken and extended helix forms.

@en

The lipid-binding domain of wi ...... oken and extended helix forms.

@nl

P1433

Q34107467-555A42BF-938C-44B6-AE64-05B78162839A

P1476

Q34107467-B4DC6EE7-9D69-49B8-8A72-8E17F172671A

P2093

Q34107467-47AD5CE3-1F77-4AEB-B0A3-A719A0672DF6

Q34107467-50D1B2B7-7B4B-4E3C-84FD-8D9563789D8F

Q34107467-54B2E6F9-8664-46A7-A8E2-6B91896592FE

Q34107467-5E5EE331-B9DA-4D0A-89CC-799473E0EBDC

Q34107467-F7442FC2-4D2B-46D3-A812-9ED8F1200796

P2860

Q34107467-00812202-5332-42D8-AA41-3FA7EF01C8CF

Q34107467-00C846D7-6471-4AAD-978F-69E825461249

Q34107467-01A49E57-F6CE-4616-AF0E-E22027AF3573

Q34107467-028FFF8F-B38F-40A0-A7A8-EAF9FE0FD661

Q34107467-09A1E212-D24D-4E37-B4BE-07130B10898C

Q34107467-119CD71B-A8EC-43BA-8AC2-E90CC88607E9

Q34107467-1470BF93-5444-47F7-90BB-2A5DE96D7880

Q34107467-26B29BE8-0DE8-4151-921A-D3E199A84290

Q34107467-2D7C9231-3BD5-4FE4-80C4-2631B6754608

Q34107467-2E1BB55A-DEE5-4A82-8319-37387CE9E9CE

P304

Q34107467-2A4801D1-F091-4B0D-B8EA-7516D6CF11B6

P31

Q34107467-9749B5CE-C772-43B7-8281-7B739CAEECD1

P356

Q34107467-B2FC6B76-EDAF-4C04-B00C-16FE9044E7C1

P407

Q34107467-8690C795-45BF-44E3-9CE9-3DCF6BD0534A

P433

Q34107467-FD4E4EA0-F834-4C41-A133-363603B88B60

P478

Q34107467-92B31322-A159-49E8-BCED-FCB33DC31F95

P577

Q34107467-205A11CC-C510-4A21-BEBA-40CD2B5E2263

P698

Q34107467-FF180710-25C7-4701-B73F-CF1E655C3C85

P921

Q34107467-A2D5521E-1CDE-413B-9083-DDBC260B74A3

P932

Q34107467-29EBF5D2-2322-4EFB-833B-F1209D4A2E72

P356

JBC.M110.157214

P1433

Journal of Biological Chemistry

P1476

The lipid-binding domain of wi ...... oken and extended helix forms.

@en

P2093

David Eliezer

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

Elka R Georgieva

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

Jack H Freed

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

Peter P Borbat

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

Trudy F Ramlall

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

P2860

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement

Residual structure, backbone dynamics, and interactions within the synuclein family

Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models

Double-knockout mice for alpha- and beta-synucleins: effect on synaptic functions

Alpha-synuclein in Lewy bodies

Mapping of a gene for Parkinson's disease to chromosome 4q21-q23

Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c

Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha -synuclein in human and transgenic mouse brain

Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl beta-D-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy

P304

28261-28274

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

P31

scholarly article

P356

10.1074/JBC.M110.157214

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

P407

P433

36

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

P478

285

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

P577

2010-06-30T00:00:00Z

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

P698

20592036

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

P921

P932

2934691

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