Results 131 to 140 of about 1,514,695 (309)

YlmG1 is localized exclusively to the chloroplast envelope membrane and is involved in preprotein translocation in Arabidopsis thaliana

open access: yesFEBS Open Bio, EarlyView.
Cytosolically synthesized chloroplast preproteins are translocated across the outer and inner envelope membranes through translocons called TOC and TIC, respectively. In green algae and plants, the TIC core is composed of essential membrane proteins, Tic12, Tic20, and Tic214.
Mengyi Li, Xueyang Zhao, Masato Nakai
wiley   +1 more source

Probiotic active gel promotes diabetic wound healing through continuous local glucose consumption and antioxidant

open access: yesJournal of Nanobiotechnology
Background Diabetic foot ulcers (DFU) are severe complications of diabetes, posing significant health and societal challenges. Accumulation of reactive oxygen species (ROS) and elevated glucose levels are primary factors affecting diabetic wound healing.
Yingshuai Wang   +12 more
doaj   +1 more source

A Tachyplesin Antimicrobial Peptide from Theraphosidae Spiders with Potent Antifungal Activity Against Cryptococcus neoformans

open access: yesMicroorganisms
The venoms of Theraphosidae spiders have evolved into diverse natural pharmacopeias through selective pressures. Cryptococcus neoformans is a global health threat that frequently causes life-threatening meningitis and fungemia, particularly in ...
Brenda B. Michira   +10 more
doaj   +1 more source

Proteasomal degradation of intracellularly expressed Amblyomin‐X limits suicide gene therapy potential in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel   +4 more
wiley   +1 more source

Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function

open access: yesFEBS Open Bio, EarlyView.
We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke   +4 more
wiley   +1 more source

Intercompartmental communication in senescence

open access: yesFEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz   +3 more
wiley   +1 more source

Antifatigue Effect and Peptide Sequence of Oligopeptides Derived from Yellow Chicken

open access: yesShipin gongye ke-ji
This study focused on oligopeptides derived from yellow chicken as the research object, aiming to investigate their antifatigue activity and potential functional peptide sequences.
Miao LI   +9 more
doaj   +1 more source

Discovery and Targeted Proteomic Studies Reveal Striatal Markers Validated for Huntington's Disease

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Clinical trials for Huntington's disease (HD) enrolling persons before clinical motor diagnosis (CMD) lack validated biomarkers. This study aimed to conduct an unbiased discovery analysis and a targeted examination of proteomic biomarkers scrutinized by clinical validation. Methods Cerebrospinal fluid was obtained from PREDICT‐HD and
Daniel Chelsky   +8 more
wiley   +1 more source

An optimized energy potential can predict SH2 domain-peptide interactions [PDF]

open access: yes, 2008
Peptide recognition modules (PRMs) are used throughout biology to mediate protein-protein interactions, and many PRMs are members of large protein domain families.
Leonid Mirny, Zeba Wunderlich
core   +1 more source

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