The Bio3D packages for structural bioinformatics

BJ Grant, L Skjærven, XQ Yao - Protein Science, 2021 - Wiley Online Library
Bio3D is a family of R packages for the analysis of biomolecular sequence, structure, and
dynamics. Major functionality includes biomolecular database searching and retrieval …

Advances in NMR methods to map allosteric sites: from models to translation

S Boulton, G Melacini - Chemical Reviews, 2016 - ACS Publications
The last five years have witnessed major developments in the understanding of the allosteric
phenomenon, broadly defined as coupling between remote molecular sites. Such advances …

Integrating protein structural dynamics and evolutionary analysis with Bio3D

L Skjærven, XQ Yao, G Scarabelli, BJ Grant - BMC bioinformatics, 2014 - Springer
Background Popular bioinformatics approaches for studying protein functional dynamics
include comparisons of crystallographic structures, molecular dynamics simulations and …

Modeling coronavirus spike protein dynamics: implications for immunogenicity and immune escape

G Kunkel, M Madani, SJ White, PH Verardi… - Biophysical …, 2021 - cell.com
The ongoing COVID-19 pandemic is a global public health emergency requiring urgent
development of efficacious vaccines. While concentrated research efforts have focused …

Identification of high-affinity pyridoxal kinase inhibitors targeting cancer therapy: an integrated docking and molecular dynamics simulation approach

P Banerjee, A Chandra, T Mohammad… - Journal of …, 2024 - Taylor & Francis
Pyridoxal kinase (PDXK) is a vitamin B6-dependent transferase enzyme encoded by the
PDXK gene, crucial for leukemic cell proliferation. Disruption of its activity causes altered …

NMR spectroscopy on domain dynamics in biomacromolecules

YE Shapiro - Progress in Biophysics and Molecular Biology, 2013 - Elsevier
Abstract Domain dynamics in biomacromolecules is currently an area of intense research
because of its importance for understanding the huge quantity of available data relating the …

[HTML][HTML] SPECTRUS: A dimensionality reduction approach for identifying dynamical domains in protein complexes from limited structural datasets

L Ponzoni, G Polles, V Carnevale, C Micheletti - Structure, 2015 - cell.com
Identifying dynamical, quasi-rigid domains in proteins provides a powerful means for
characterizing functionally oriented structural changes via a parsimonious set of degrees of …

Comparing aminoglycoside binding sites in bacterial ribosomal RNA and aminoglycoside modifying enzymes

J Romanowska, N Reuter… - … : Structure, Function, and …, 2013 - Wiley Online Library
Aminoglycoside antibiotics are used against severe bacterial infections. They bind to the
bacterial ribosomal RNA and interfere with the translation process. However, bacteria …

[HTML][HTML] Structural plasticity of arrestin-G protein coupled receptor complexes as a molecular determinant of signaling

A Felline, L Bellucci, V Vezzi, C Ambrosio… - International Journal of …, 2024 - Elsevier
G protein coupled receptors (GPCRs) are critically regulated by arrestins. In this study, high-
resolution data was combined with molecular dynamics simulations to infer the determinants …

“Infostery” analysis of short molecular dynamics simulations identifies highly sensitive residues and predicts deleterious mutations

Y Karami, T Bitard-Feildel, E Laine, A Carbone - Scientific reports, 2018 - nature.com
Characterizing a protein mutational landscape is a very challenging problem in Biology.
Many disease-associated mutations do not seem to produce any effect on the global shape …