Using chemical shift perturbation to characterise ligand binding
MP Williamson - Progress in nuclear magnetic resonance spectroscopy, 2013 - Elsevier
Chemical shift perturbation (CSP, chemical shift mapping or complexation-induced changes
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …
Quantitative analysis of protein–ligand interactions by NMR
Protein–ligand interactions have been commonly studied through static structures of the
protein–ligand complex. Recently, however, there has been increasing interest in …
protein–ligand complex. Recently, however, there has been increasing interest in …
Perspectives on nuclear magnetic resonance spectroscopy in drug discovery research
J Caceres-Cortes, B Falk, L Mueller… - Journal of Medicinal …, 2024 - ACS Publications
The drug discovery landscape has undergone a significant transformation over the past
decade, owing to research endeavors in a wide range of areas leading to strategies for …
decade, owing to research endeavors in a wide range of areas leading to strategies for …
Funnel-metadynamics and solution NMR to estimate protein–ligand affinities
L Troussicot, F Guillière, V Limongelli… - Journal of the …, 2015 - ACS Publications
One of the intrinsic properties of proteins is their capacity to interact selectively with other
molecules in their environment, inducing many chemical equilibria each differentiated by the …
molecules in their environment, inducing many chemical equilibria each differentiated by the …
A unique Mdm2-binding mode of the 3-pyrrolin-2-one-and 2-furanone-based antagonists of the p53-Mdm2 interaction
E Surmiak, A Twarda-Clapa, KM Zak… - ACS chemical …, 2016 - ACS Publications
The p53 pathway is inactivated in almost all types of cancer by mutations in the p53
encoding gene or overexpression of the p53 negative regulators, Mdm2 and/or Mdmx …
encoding gene or overexpression of the p53 negative regulators, Mdm2 and/or Mdmx …
[HTML][HTML] Molecular basis for phosphorylation-dependent SUMO recognition by the DNA repair protein RAP80
A Anamika, L Spyracopoulos - Journal of Biological Chemistry, 2016 - ASBMB
Recognition and repair of double-stranded DNA breaks (DSB) involves the targeted
recruitment of BRCA tumor suppressors to damage foci through binding of both ubiquitin …
recruitment of BRCA tumor suppressors to damage foci through binding of both ubiquitin …
An allosteric hot spot in the tandem-SH2 domain of ZAP-70 regulates T-cell signaling
T-cell receptor (TCR) signaling is initiated by recruiting ZAP-70 to the cytosolic part of TCR.
ZAP-70, a non-receptor tyrosine kinase, is composed of an N-terminal tandem SH2 (tSH2) …
ZAP-70, a non-receptor tyrosine kinase, is composed of an N-terminal tandem SH2 (tSH2) …
Binding isotherms and time courses readily from magnetic resonance
J Xu, SR Van Doren - Analytical chemistry, 2016 - ACS Publications
Evidence is presented that binding isotherms, simple or biphasic, can be extracted directly
from noninterpreted, complex 2D NMR spectra using principal component analysis (PCA) to …
from noninterpreted, complex 2D NMR spectra using principal component analysis (PCA) to …
Retroviral RNase H: Structure, mechanism, and inhibition
All retroviruses encode the enzyme, reverse transcriptase (RT), which is involved in the
conversion of the single-stranded viral RNA genome into double-stranded DNA. RT is a …
conversion of the single-stranded viral RNA genome into double-stranded DNA. RT is a …
Nucleotide Binding and Active Site Gate Dynamics for the Hsp90 Chaperone ATPase Domain from Benchtop and High Field 19F NMR Spectroscopy
Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone.
In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through …
In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through …