Results 111 to 120 of about 9,770,147 (265)

A protein-protein interaction dictates Borrelial infectivity

open access: yesScientific Reports, 2017
Two Borrelia burgdorferi interacting proteins, BB0238 and BB0323, play distinct roles in pathogen biology and infectivity although a significance of their interaction remained enigmatic.
Meghna Thakur   +5 more
doaj   +1 more source

Translophagy—A potential link between autophagy impairment and translational errors

open access: yesFEBS 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   +11 more
wiley   +1 more source

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

open access: yesFEBS 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   +2 more
wiley   +1 more source

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS 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   +3 more
wiley   +1 more source

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

Towards the prediction of protein interaction partners using physical docking

open access: yesMolecular Systems Biology, 2011
Deciphering the whole network of protein interactions for a given proteome (‘interactome’) is the goal of many experimental and computational efforts in Systems Biology.
Mark Nicholas Wass   +4 more
doaj   +1 more source

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

open access: yesFEBS 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-protein interaction of pathogen protein CD630_32050 (putative nitroreductase) with PDB ID: 3GFA acquired from STRING database.

open access: yes
Protein-protein interaction of pathogen protein CD630_32050 (putative nitroreductase) with PDB ID: 3GFA acquired from STRING database.
Asifullah Khan (5901902)   +8 more
core   +1 more source

Development of a Split Esterase for Protein-Protein Interaction Dependent Small Molecule Activation [PDF]

open access: yes, 2019
Split reporters based on fluorescent proteins and luciferases have emerged as valuable tools for measuring interactions in biological systems. Relatedly, biosensors that transduce measured input signals into outputs that influence the host system are key
Alexander, Lippert   +6 more
core   +1 more source

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

open access: yesFEBS 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   +6 more
wiley   +1 more source

Home - About - Disclaimer - Privacy