Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. [PDF]
, 2013 Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an
Bowie, James U +3 more
core +3 more sources
Adaptive HIV-1 evolutionary trajectories are constrained by protein stability [PDF]
, 2017 Despite the use of combination antiretroviral drugs for the treatment of HIV-1 infection, the emergence of drug resistance remains a problem. Resistance may be conferred either by a single mutation or a concerted set of mutations.
Kandathil, Shaun M. +3 more
core +2 more sources
Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction. [PDF]
, 2020 The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization.
Myasnikov, Alexander +3 more
core +3 more sources
Highlights in BioScience, 2020 Genetic mutagenesis is a very efficient tool in studying genes function. Because of the great benefits of legumes as human food and animal feed worldwide, we used a model plant Medicago truncatula for identification gene function related to nitrogen ...
Asmaa Hamdy Hassan +2 more
doaj +1 more source
Disordered proteins and network disorder in network descriptions of protein structure, dynamics and function. Hypotheses and a comprehensive review [PDF]
, 2011 During the last decade, network approaches became a powerful tool to describe protein structure and dynamics. Here we review the links between disordered proteins and the associated networks, and describe the consequences of local, mesoscopic and global ...
Daniel V. Veres +8 more
core +4 more sources
Scientific Reports, 2022 We have recently developed a mouse monoclonal antibody (12–10H) binding to the head domain region in rat P2X4 receptor (rP2X4R, which is crucial for the pathogenesis of neuropathic pain) expressed on the cell with the highest binding affinity (K D = 20 ...
Chinatsu Shinozaki +11 more
doaj +1 more source
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. [PDF]
, 2015 The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family.
Corbett, Kevin D +5 more
core +2 more sources
Protein Structure Prediction: The Next Generation
, 2006 Over the last 10-15 years a general understanding of the chemical reaction of protein folding has emerged from statistical mechanics. The lessons learned from protein folding kinetics based on energy landscape ideas have benefited protein structure ...
Eastwood, Michael P. +4 more
core +1 more source
Protein secondary structure: Entropy, correlations and prediction [PDF]
, 2003 Is protein secondary structure primarily determined by local interactions between residues closely spaced along the amino acid backbone, or by non-local tertiary interactions?
Brenner, Steven E., Crooks, Gavin E.
core +6 more sources
Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose
Molecules, 2021 Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied.
Jing-Jing Liu +6 more
doaj +1 more source