Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
about
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTppIdentification of direct protein targets of small moleculesLarge extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutationsTurning a protein kinase on or off from a single allosteric site via disulfide trapping.Pharmacological chaperones for human -N-acetylgalactosaminidaseTrimming Down a Protein Structure to Its Bare Foldons: SPATIAL ORGANIZATION OF THE COOPERATIVE UNITOrdering a Dynamic Protein Via a Small-Molecule StabilizerFunctional modulation of a protein folding landscape via side-chain distortionPrediction of drug-target interactions for drug repositioning only based on genomic expression similarityDevelopment and Application of a High Throughput Protein Unfolding Kinetic AssaySynonymous variants in HTRA1 implicated in AMD susceptibility impair its capacity to regulate TGF-β signaling.Time, space, and disorder in the expanding proteome universe.A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.Conformational properties of nine purified cystathionine β-synthase mutants.Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability.Development and characterization of a novel C-terminal inhibitor of Hsp90 in androgen dependent and independent prostate cancer cells.Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions.Energetics-based discovery of protein-ligand interactions on a proteomic scale.StableIsotope Labeling with Amino Acids in Cell Culture (SILAC)-based strategy for proteome-wide thermodynamic analysis of protein-ligand binding interactions.A method for direct measurement of protein stability in vivo.The stress of protein misfolding: from single cells to multicellular organismsSimplified proteomics approach to discover protein-ligand interactions.Probing membrane protein unfolding with pulse proteolysis.Target identification for small bioactive molecules: finding the needle in the haystack.S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity.Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.Conformational stability and catalytic activity of PTEN variants linked to cancers and autism spectrum disorders.Cell-based protein stabilization assays for the detection of interactions between small-molecule inhibitors and BRD4.Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts.Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.Complete Reversible Refolding of a G-Protein Coupled Receptor on a Solid Support.Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Conformational equilibria and rates of localized motion within hepatitis B virus capsidsDevelopment of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands.Age-related macular degeneration-associated silent polymorphisms in HtrA1 impair its ability to antagonize insulin-like growth factor 1.Binding studies using Pichia pastoris expressed human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins.Energetic Coupling between Ligand Binding and Dimerization in Escherichia coli Phosphoglycerate MutaseIntegrating Native Mass Spectrometry and Top-Down MS for Defining Protein Interactions Important in Biology and Medicine
P2860
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P2860
Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Pulse proteolysis: A simple me ...... n stability and ligand binding
@ast
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en-gb
Pulse proteolysis: A simple me ...... n stability and ligand binding
@nl
type
label
Pulse proteolysis: A simple me ...... n stability and ligand binding
@ast
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en-gb
Pulse proteolysis: A simple me ...... n stability and ligand binding
@nl
altLabel
Pulse proteolysis: a simple me ...... n stability and ligand binding
@en
prefLabel
Pulse proteolysis: A simple me ...... n stability and ligand binding
@ast
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en-gb
Pulse proteolysis: A simple me ...... n stability and ligand binding
@nl
P2860
P921
P356
P1433
P1476
Pulse proteolysis: A simple me ...... n stability and ligand binding
@en
P2860
P2888
P304
P356
10.1038/NMETH740
P407
P577
2005-02-17T00:00:00Z
P5875
P6179
1021261365