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Ion mobility-mass spectrometry for structural proteomicsActivation state-selective kinase inhibitor assay based on ion mobility-mass spectrometryBound anions differentially stabilize multiprotein complexes in the absence of bulk solvent.Integrating mass spectrometry of intact protein complexes into structural proteomicsDramatically stabilizing multiprotein complex structure in the absence of bulk water using tuned Hofmeister salts.Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes.Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexesInter-domain communication of human cystathionine β-synthase: structural basis of S-adenosyl-L-methionine activation.Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase.Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β speciesAmyloid-β-neuropeptide interactions assessed by ion mobility-mass spectrometry.Exploring the reactivity of flavonoid compounds with metal-associated amyloid-β species.Mechanism and rates of exchange of L7/L12 between ribosomes and the effects of binding EF-G.A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc.Detection of conformation types of cyclosporin retaining intramolecular hydrogen bonds by mass spectrometry.Retinol and retinol-binding protein stabilize transthyretin via formation of retinol transport complex.Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes.Ion mobility-mass spectrometry reveals conformational changes in charge reduced multiprotein complexes.Characterizing the resolution and accuracy of a second-generation traveling-wave ion mobility separator for biomolecular ionsIon mobility–mass spectrometry analysis of large protein complexesAlternate Dissociation Pathways Identified in Charge-Reduced Protein Complex IonsMethod development of a novel PK assay for antibody-conjugated drug measurement of ADCs using peptide-linker drug analyte
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Q26826931-839C6AC9-C431-4AD3-BC10-7358BB3E099BQ30352015-EBB5ADBF-31C4-4E4B-AA8D-064B0C031397Q30403879-DFD1EFF9-D4C4-40EC-8BB6-5C7951137FA4Q30417001-C6EF2D18-5B0D-4082-BE78-702CF4ADA366Q30432313-33DF3F21-7C97-4712-BB54-3F7450059F24Q33298819-0EA0C9BB-06E8-48AF-962E-94208CC0255DQ33658957-2421E15D-36CF-4992-B772-72B8C20B85E2Q34774516-91CF7C00-2DDC-40DB-9CD5-961A423D1219Q36452763-8817759D-3F62-4813-A4D6-E7B6A21FC408Q36673287-D01E6040-9D87-4570-90A4-2D08B57AB364Q36879051-CB20F059-4562-44C4-91EE-8CBE6A1AF808Q37222626-CD807C19-E7EC-4BC2-94C3-8758A5262994Q40744224-6ACBA835-73E9-4068-B27D-DA569FF509B0Q41986965-F197140A-742C-43F1-9816-6FB6033A2C01Q42203573-42729C75-4072-4824-99B8-90F8E8FCD27BQ42905854-9C0F05BA-CB97-41B2-B745-F2142F48D582Q44892400-4D53DD4F-E7C0-4587-AC38-C0348E038599Q45986284-E9F7B303-52BD-4808-98E6-A76CF74CA433Q61996148-B9664E26-2AE2-439C-A05B-5F89C0AA5B41Q61996163-8A470595-FCDC-47BF-BB8E-BF92A4B414C8Q63383769-1F4D8A89-7CEC-4DEB-AB5E-2267E2A1E9B7Q92091078-24EC3EDF-F3A6-4F0F-9604-F8CB3B4E426C
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Suk-joon Hyung
@ast
Suk-joon Hyung
@en
Suk-joon Hyung
@es
Suk-joon Hyung
@nl
Suk-joon Hyung
@sl
type
label
Suk-joon Hyung
@ast
Suk-joon Hyung
@en
Suk-joon Hyung
@es
Suk-joon Hyung
@nl
Suk-joon Hyung
@sl
prefLabel
Suk-joon Hyung
@ast
Suk-joon Hyung
@en
Suk-joon Hyung
@es
Suk-joon Hyung
@nl
Suk-joon Hyung
@sl
P1053
N-6449-2014
P106
P31
P3829
P496
0000-0001-6759-4219