about
Biochemical and Structural Insights into the Mechanisms of SARS Coronavirus RNA Ribose 2′-O-Methylation by nsp16/nsp10 Protein ComplexParkinson disease drug screening based on the interaction between D(2) dopamine receptor and beta-arrestin 2 detected by capillary zone electrophoresisQuantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria.Fibrillization of human tau is accelerated by exposure to lead via interaction with His-330 and His-362.The contrasting effect of macromolecular crowding on amyloid fibril formation.Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.Fibril formation of the rabbit/human/bovine prion proteinsHow does domain replacement affect fibril formation of the rabbit/human prion proteinsSequence-dependent abnormal aggregation of human Tau fragment in an inducible cell model.Applications of isothermal titration calorimetry in protein science.The role of crowded physiological environments in prion and prion-like protein aggregationCrowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.Pathological concentration of zinc dramatically accelerates abnormal aggregation of full-length human Tau and thereby significantly increases Tau toxicity in neuronal cells.Macromolecular crowding favors the fibrillization of β2-microglobulin by accelerating the nucleation step and inhibiting fibril disassembly.DNA binding, cytotoxicity, and apoptotic-inducing activity of ruthenium(II) polypyridyl complex.Cytotoxic aggregates of alpha-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells.Zinc significantly changes the aggregation pathway and the conformation of aggregates of human prion protein.Structural changes of alpha-lactalbumin induced by low pH and oleic acid.Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry.Assembly of single-stranded polydeoxyadenylic acid and β-glucan probed by the sensing platform of graphene oxide based on the fluorescence resonance energy transfer and fluorescence anisotropy.Thermodynamics and kinetics of the cleavage of DNA catalyzed by bleomycin A5.Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase.Binding of calcium ions to Ras promotes Ras guanine nucleotide exchange under emulated physiological conditions.Thermodynamics of the interaction of aluminum ions with DNA: implications for the biological function of aluminum.Oxidative refolding of reduced, denatured lysozyme in AOT reverse micelles.Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme.Effects of macromolecular crowding on the structural stability of human α-lactalbumin.Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH.Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its CytotoxicityAuthor Correction: Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its CytotoxicityStudies on thermodynamic nature of steroselectivity for ruthenium(II) polypyridyl complex binding to DNAMixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environmentsMacromolecular crowding enhances the binding of superoxide dismutase to xanthine oxidase: implications for protein-protein interactions in intracellular environmentsMixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: implications for protein folding in intracellular environmentsBiophysical studies of a ruthenium(II) polypyridyl complex binding to DNA and RNA prove that nucleic acid structure has significant effects on binding behaviorsA maturase that specifically stabilizes and activates its cognate group I intron at high temperatures
P50
Q27675195-BC777471-B8C6-4E7C-AC05-EB8A1DF2E882Q28833697-286D3798-6C50-45AA-A99D-AFBC1E4B4B11Q33666468-FA9C8C68-E9B5-4E2E-9740-82CF57EA6F2BQ34032661-AE4918F9-98F4-4543-9007-5CA4B78279FAQ34037901-9E3E5B5A-876B-4693-A76D-A462C7E33A74Q34257414-F9052F14-F0ED-4056-B33A-7931AB8DBF7AQ34766337-B8674E6F-590C-4EA7-B1CD-26CA8DAE193DQ35009616-5A1458F2-B7E8-4DBD-9E0F-B7778448B3FCQ35224016-95B2982D-44C0-4240-B84E-B505D67DA7C4Q35424482-1DF28DE8-3140-4618-A4E9-C947986CC9AAQ35614633-03E2C33D-BAC7-4049-A960-2C926328B275Q37208354-F7845EE9-957D-492D-B0EC-687148003041Q37375301-31788E7B-30F1-4A6C-9652-BF2A3222D4E2Q37431675-7971E0D8-52AE-4AC3-9976-0815A009D553Q38956652-8E2D14F6-5195-4537-9FA0-6DF10A6094F7Q39150777-45898048-D13E-4C31-803D-E899224EA399Q39535915-8A347F81-EB74-403F-8FD0-03FE38EE1A46Q39668149-A54A5938-5498-4185-8C93-772623BBE549Q39842634-534E9D83-0731-4E73-ADE0-018FA878CB79Q41001755-DE8D03AB-8058-4C88-9366-10B0B6643CDDQ43597729-D5012222-2B9C-47CC-854A-C9796F8AD4B1Q43698058-FB088C26-4833-4B04-A0E8-89DC511A6BFCQ43829121-E2D3F690-F565-4049-B691-AD9F7830A17AQ44033092-45E13293-FD58-4FBE-B3AB-01A8986A66BBQ46253049-0B3FF619-0847-4ED6-B96B-DF900F65C3E7Q46368544-9D179802-2057-4D3B-9471-835DA2C57DE8Q46439863-44866EAA-D2FE-4574-9C41-7297A545D35AQ46673270-F1789879-D8DD-45A0-8DA2-14600909D8DFQ46770418-735953B9-734C-4861-AD4B-316660734C21Q47450172-D6901184-EBD2-4B7E-BC1E-B7278958D3DAQ47550175-122130F9-C04A-4C19-964F-4D445E8F8F6EQ50723523-B64DB4F1-22F2-4FEC-9170-76E8EC921E58Q58722021-5C6B3770-407F-4158-85E9-E93E4DF56A20Q58765802-A454564D-7F59-448F-BC39-ECDA8A0C38FFQ59462665-F75A874A-C070-4DD9-AA8D-5E6E076C2F27Q79206728-221C6CBC-92E9-4DF2-B466-7313AC9617F7Q79953869-F634664C-CDA1-4E85-8FBE-1D204289F5BEQ80884297-D3FC3201-0435-47DC-9875-37583FAAC620Q81039123-B4BD40F5-D5AE-447B-AFB5-901A6AF9E28AQ82727272-A6CE0D1F-DCD2-41E3-9E11-A901B38A69E6
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Yi Liang
@ast
Yi Liang
@en
Yi Liang
@es
Yi Liang
@nl
Yi Liang
@sl
type
label
Yi Liang
@ast
Yi Liang
@en
Yi Liang
@es
Yi Liang
@nl
Yi Liang
@sl
prefLabel
Yi Liang
@ast
Yi Liang
@en
Yi Liang
@es
Yi Liang
@nl
Yi Liang
@sl
P1053
V-1396-2017
P106
P108
P1153
26421277700
P31
P3829
P496
0000-0002-7349-8300