about
(13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data.Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy.NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG.Structure of a AAA+ unfoldase in the process of unfolding substrate.Cytochrome-P450-cytochrome-b5 interaction in a membrane environment changes 15N chemical shift anisotropy tensors.Insights into the role of substrates on the interaction between cytochrome b5 and cytochrome P450 2B4 by NMR.Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy.Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation.An enhanced sensitivity methyl 1H triple-quantum pulse scheme for measuring diffusion constants of macromolecules.Probing slow timescale dynamics in proteins using methyl 1H CEST.Mechanism of polymer-induced hemolysis: nanosized pore formation and osmotic lysis.Reconstitution of the Cytb5-CytP450 Complex in Nanodiscs for Structural Studies using NMR Spectroscopy.Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMRCooperative subunit dynamics modulate p97 functionA Methyl-TROSY-Based 1 H Relaxation Dispersion Experiment for Studies of Conformational Exchange in High Molecular Weight Proteins
P50
Q30009121-6A427144-4F3C-49A7-8DD4-0DA9927BA579Q30369811-2F2072F5-DC6D-4887-B818-20F607282680Q30633058-4FD3727F-DA0D-46DF-B30C-46A1D04DBD2EQ30789737-1FEE4D3D-4107-48B0-A4D5-AA73D21DD9CBQ33736588-2EE74AE2-4604-47AA-86AF-21A7F160AB85Q33742617-D564FC13-1360-494F-A3BA-FCC7C069025BQ35608108-8BF2CE4B-8E21-4655-A2AA-77721032D1F3Q36118412-45947C30-CD77-45D3-B09D-635A81AB34B0Q41598312-FE5FD444-6B78-4DC9-BD90-155CF47A62EDQ42555411-35DF9EBE-4035-4C74-BD81-07F87B548B67Q43149378-03042650-FDCE-4581-AB12-A9A694AD8E93Q47583613-581C7F3C-FE19-4BE2-ABFB-58285BBBFBF2Q47820430-D3818336-2D46-4351-BB0C-1ED77AF24410Q48110827-91F4A66D-5EE0-470A-8C76-64347467CD22Q48226351-CF50A8F8-19FD-4BBB-A445-5C02A9CA2309Q50551407-09E83523-60C5-4215-8685-54CEFB818CCFQ53224877-7452E2B9-346B-4D2D-80A1-54910C9B11D4Q89865089-A7DEE93C-936A-491A-B7D7-35EAE92A2BD8Q90744846-400A2C39-1EAB-4572-AADF-2C0430EAD856Q92216221-D6B3BAA4-A6F0-45C9-820F-A49B5946733D
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Rui Huang
@ast
Rui Huang
@en
Rui Huang
@es
Rui Huang
@nl
Rui Huang
@sl
type
label
Rui Huang
@ast
Rui Huang
@en
Rui Huang
@es
Rui Huang
@nl
Rui Huang
@sl
prefLabel
Rui Huang
@ast
Rui Huang
@en
Rui Huang
@es
Rui Huang
@nl
Rui Huang
@sl
P1053
N-4022-2017
P106
P21
P31
P3829
P496
0000-0002-4064-6397