Trimethylamine-N-oxide-induced folding of alpha-synuclein.
about
Dequalinium-induced protofibril formation of alpha-synucleinThe role of early life environmental risk factors in Parkinson disease: what is the evidence?The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPWhat macromolecular crowding can do to a proteinCounteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability.Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.When does trimethylamine N-oxide fold a polymer chain and urea unfold it?Effect of osmolytes on the binding of EGR1 transcription factor to DNA.Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligationForced folding of a disordered protein accesses an alternative folding landscape.Proline to the rescueAddressing mechanism of fibrillization/aggregation and its prevention in presence of osmolytes: spectroscopic and calorimetric approach.Structural characteristic of the initial unfolded state on refolding determines catalytic efficiency of the folded protein in presence of osmolytes.Solution model of the intrinsically disordered polyglutamine tract-binding protein-1.Effects of hydrophobic macromolecular crowders on amyloid β (16-22) aggregation.Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement.Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityFully reduced granulin-B is intrinsically disordered and displays concentration-dependent dynamicsGuiding protein aggregation with macromolecular crowdingAmyloidogenesis of natively unfolded proteins.Observation of molecular inhibition and binding structures of amyloid peptides.The effect of osmolytes on protein fibrillationTargeting the chameleon: a focused look at α-synuclein and its roles in neurodegeneration.Protein quality control system in neurodegeneration: a healing company hard to beat but failure is fatal.Disulfide bonds in amyloidogenesis diseases related proteins.The therapeutic potential of chemical chaperones in protein folding diseases.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Parkinson's disease: genetics and beyond.Exploring the Transition of Human α-Synuclein from Native to the Fibrillar State: Insights into the Pathogenesis of Parkinson's Disease.Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methodsHydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes.Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein.Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes.Osmolytes induce structure in an early intermediate on the folding pathway of barstar.Molecular simulations of the fluctuating conformational dynamics of intrinsically disordered proteins.Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling.
P2860
Q24298122-5F10E658-2CCF-4F4E-8393-D37CECB1B4E4Q24815642-08636888-E957-4C8F-8A0D-832C2F14F3C5Q26830682-E5E1CF1D-714D-4A2B-8A5B-1F34D30EC15EQ27012942-3C846184-D3C8-4EFB-BD38-C85FF39DB204Q30419579-C1D57A00-3501-4F66-BD84-BC8DB60B7995Q30434734-B40E0D96-FBCB-4921-B255-77195BCAF05BQ30476575-29D06278-5AE8-424D-874B-3207893509EBQ30830001-88012D1D-42A3-42D9-87D2-BAFC76B717CFQ33470625-4B5AA839-CDC0-465B-BFCE-737BC28C34B8Q34380720-D71C8436-2EBE-4675-98C9-6DA12108EB91Q34572521-D6FF09EF-D127-4C1C-97FE-4A6926FA17E0Q34675294-97890C52-AFB3-4E38-8871-EDC33355CAD0Q34856957-8A2C4AF3-4D5E-4403-8FE8-52A638B69E55Q35037186-AAFFE7C3-4264-4C3C-AB32-95ED419A85B8Q35227167-6318C7B7-6560-4F79-8D72-44ACB152DB25Q35330283-0DECE1DD-F31C-4383-A3DB-0B1B3074EF7DQ35866822-7F1D9F77-DEAB-4CEA-8DB1-AE3021F0EED6Q36062960-2D3BDAF7-DC45-480E-B898-D8EEEE793B16Q36176612-2128A288-635B-4C69-A0AB-09056314BEC6Q36331161-B4061B88-5014-44B2-8B60-6BBBF0343111Q36794765-ED0DA284-6EFD-47B7-B809-E585F8706BCAQ37178759-34CC1378-38DF-48AF-B48C-9BD9294E6348Q37184755-DFA681A5-E849-40BD-9195-D55BC7867C56Q37984010-9FBF0DFD-E9BE-4734-B1DB-130D427DE435Q38001429-EC3DB737-9169-4475-BD32-C58D38CF088CQ38039857-C1ADDBED-84FE-4FD6-B180-4E92E29A08F0Q38078868-F1771171-1A81-4FD9-BF84-E87F36A6014CQ38113990-8F642286-7F5D-4B1A-9BE8-ECB424B9D11AQ38211124-4DF920B5-8A1A-4514-B091-344864F07AB5Q39223628-D0FAAC9D-AC35-4757-A95F-EBCAE3A104ACQ39416222-21E4EAD2-75AF-4239-87FB-60BF4BD16FD9Q39640785-2F703BA2-9988-4C50-B518-8863D8F4832CQ42050087-71EB6881-2E80-45D8-ADA0-64B3CAADBB26Q42921421-650DEFE0-4D64-4203-8383-994738FA409CQ43054520-3732035B-ADE2-45A3-B1CD-EAFE075680AAQ43274561-E4233B1D-2F2B-4A32-B812-561AED413ABDQ44982138-C710FE2B-9207-47E4-A23D-80FA6F2FB911Q46308746-5815D225-D2CE-4205-818C-03E7D86D1510Q46703068-1A108BA7-125D-452B-928B-459DA561B46CQ47119009-0D8A1AC4-3B79-456C-BC43-6047050D1546
P2860
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@en
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@nl
type
label
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@en
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@nl
prefLabel
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@en
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@nl
P2093
P2860
P1433
P1476
Trimethylamine-N-oxide-induced folding of alpha-synuclein.
@en
P2093
P2860
P356
10.1016/S0014-5793(01)03121-0
P407
P577
2001-11-01T00:00:00Z