Results 101 to 110 of about 6,490,832 (265)

Emerging experimental and computational methods for studying redox‐regulated structural transitions

FEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass, Dana Reichmann, Gábor Erdős   +2 more
wiley   +1 more source

Translophagy—A potential link between autophagy impairment and translational errors

FEBS Letters, EarlyView.
Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk, Gailing Ma, Robin Antrobus, Diego Manni, Marco Trevisan‐Herraz, Mustafa Khwaja, Max Brown, Gavin D. Richardson, Masaaki Komatsu, Daniel Erskine, Viktor I. Korolchuk, Tetsushi Kataura   +11 more
wiley   +1 more source

Functional comparison of EncB and EncC cargo proteins in iron storage within the Myxococcus xanthus encapsulin

FEBS Letters, EarlyView.
Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell, Thomas Walther, Egbert Hoiczyk   +2 more
wiley   +1 more source

Evolution of Protein-Protein Interaction Network

, 2007
Protein-protein interactions (PPIs) are one of the most important components of biological networks. It is important to understand the evolutionary process of PPIs in order to elucidate how the evolution of biological networks has contributed to diversification of the existent organisms.
T, Makino, T, Gojobori
openaire   +2 more sources

Disulfide bond acquisition through eukaryotic protein evolution

, 2010
Disulfide bonds play critical roles in protein stability and function. They are generally considered to be strongly conserved among species. Although there is compelling evidence in the literature for this conservation on a case-by-case basis ...
Ho, Simon Y.W., Hogg, Philip J., Wong, Jason W.H., Jason W. H. Wong, Philip J. Hogg, Simon Y. W. Ho   +5 more
core   +1 more source

Structural and biochemical analysis of a B12 superbinder

FEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices, Jacob J. Whittaker, Dirk J. Slotboom, Albert Guskov   +3 more
wiley   +1 more source

Enhancing protein-protein docking by new approaches to protein flexibility and scoring of docking hypotheses [PDF]

, 2004
Zöllner FG. Enhancing protein-protein docking by new approaches to protein flexibility and scoring of docking hypotheses. Bielefeld (Germany): Bielefeld University; 2004.Für das Verständnis von biologischen Funktionen können Proteindockingverfahren ...
Frank G. Zöllner, Zöllner, Frank Gerrit   +1 more
core  

From junk to function — How weak selection in eukaryotes builds new parts and drives genomic complexity

FEBS Letters, EarlyView.
How do genomes gain new functional parts? In eukaryotes, which tend to evolve under weak selection, much of the genome is junk. Palazzo and Qiu borrow the logic of Markov chains to show how non‐functional DNA becomes functional through the appearance of intermediate states, which arise due to epistasis, buffering, and biochemical messiness, allowing ...
Alexander F. Palazzo, Yi Qiu
wiley   +1 more source

Protein Docking mit weichen Volumenmodellen [PDF]

, 2003
Neumann S. Soft volume models for protein-protein docking. Bielefeld (Germany): Bielefeld University; 2003.Der Begriff "Protein Docking" beschreibt die Frage, ob und wie zwei gegebene Proteine interagieren, ausgehend von der 3D Struktur.
Neumann, Steffen
core  

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

FEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 more
wiley   +1 more source