Results 51 to 60 of about 5,306,314 (299)

Dynamic insertion of membrane proteins at the endoplasmic reticulum [PDF]

open access: yes, 2005
Most eukaryotic membrane proteins are cotranslationally integrated into the endoplasmic reticulum membrane by the Sec61 translocation complex. They are targeted to the translocon by hydrophobic signal sequences which induce the translocation of either ...
Higy, Marie
core   +1 more source

Multiple novel membrane proteins involve phthalate ester degradation in Rhodococcus sp. AH-ZY2

open access: yesApplied and Environmental Microbiology
Phthalate esters (PAEs) are ubiquitous in the environment, and their microbial metabolism is associated with transport proteins. In this study, multiple novel membrane proteins were identified, revealing their pivotal role in PAEs degradation.
Zhengyu Hou   +7 more
doaj   +1 more source

Quantitative analysis of H2O2 transport through purified membrane proteins

open access: yesMethodsX, 2020
Hydrogen peroxide (H2O2) is an important signal molecule produced in animal and plant cells. The balance of H2O2 between the intra- and extracellular space is regulated by integral membrane proteins, which thereby modulate signaling. Several methods have
Hao Wang   +4 more
doaj   +1 more source

Salmonella lipopolysaccharide‐containing supported lipid bilayers as platforms to study bacteriophage interactions

open access: yesFEBS Letters, EarlyView.
We present robust protocols for the preparation of supported lipid bilayers (SLBs) incorporating either Salmonella smooth LPS or outer membrane vesicles (OMVs). We use a combination of quartz crystal microbalance with dissipation (QCM‐D) and fluorescence microscopy to both characterize the SLBs of various compositions and to probe their interactions ...
Hudson P. Pace   +6 more
wiley   +1 more source

Post-Translational Membrane Protein Targeting by the Chloroplast Signal Recognition Particle [PDF]

open access: yes, 2011
Post-translational transport of membrane proteins poses enormous challenges to the cells. The transport factors must accurately select and deliver the cargos to the appropriate target membranes.
Jaru-Ampornpan, Peera
core   +1 more source

Investigating transcription factor dynamics in health and disease using FRAP

open access: yesFEBS Letters, EarlyView.
FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...
Kannan Govindaraj   +3 more
wiley   +1 more source

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

open access: yesFEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang   +4 more
wiley   +1 more source

Microbiome‐blood–brain barrier interactions in aging — mechanisms and therapeutic potential

open access: yesFEBS Letters, EarlyView.
Aging reshapes the gut microbiome (↓SCFA‐producing commensals; ↑pro‐inflammatory outputs), shifting circulating metabolites (↓SCFAs; ↑LPS, ↑TMAO, ↑PAA) that act at the BBB to increase nonspecific transcytosis, alter transport, and promote astrocyte reactivity, heightening brain vulnerability.
Daniel Cuervo‐Zanatta   +3 more
wiley   +1 more source

Import pathways of precursor proteins into mitochondria [PDF]

open access: yes, 1988
The precursor of porin, a mitochondrial outer membrane protein, competes for the import of precursors destined for the three other mitochondrial compartments, including the Fe/S protein of the bc1- complex (intermembrane space), the ADP/ATP carrier ...
Pfaller, Rupert   +4 more
core   +1 more source

Subcellular distribution of ezrin/radixin/moesin and their roles in the cell surface localization and transport function of P-glycoprotein in human colon adenocarcinoma LS180 cells.

open access: yesPLoS ONE, 2021
The ezrin/radixin/moesin (ERM) family proteins act as linkers between the actin cytoskeleton and P-glycoprotein (P-gp) and regulate the plasma membrane localization and functionality of the latter in various cancer cells.
Takuro Kobori   +4 more
doaj   +1 more source

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