Results 101 to 110 of about 3,841,423 (288)

An outer membrane vesicle‐associated two‐track model for enterotoxigenic Bacteroides fragilis oncogenesis

open access: yesMolecular Oncology, EarlyView.
Enterotoxigenic Bacteroides fragilis is a gut bacterium linked to bowel cancer. We propose that its toxin acts along two routes: at the cell surface, cutting the adhesion protein E‐cadherin and triggering inflammation; and inside the cell, delivered by bacterial vesicles, switching on NOD1 and cancer stem cell programs.
Kangchan Choi   +2 more
wiley   +1 more source

Computational modeling of intrinsically disordered and phase-separated protein states

open access: yes
Intrinsically disordered proteins possess ensembles of conformations and lack stable three-dimensional structures. Phase separation is defined as a phenomenon in which proteins and biomolecules, often including intrinsically disordered proteins, separate
Uversky, Vladimir N.   +1 more
core   +1 more source

UiO‐66 metal–organic frameworks in biomedicine: From structural tunability to bioimaging, photodiagnostics, and photodynamic cancer therapy

open access: yesFEBS Open Bio, EarlyView.
UiO‐66(Zr) metal–organic frameworks are chemically stable, biocompatible, and highly tunable nanomaterials. Their modular structure enables controlled drug delivery, multimodal bioimaging, and light‐activated photodynamic therapy, supporting integrated diagnostic and therapeutic (theranostic) applications in cancer and biomedical research.
Veronika Huntošová   +2 more
wiley   +1 more source

Hyperactive ice‐binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans

open access: yesFEBS Open Bio, EarlyView.
TisIBP8, a fungal‐derived hyperactive ice‐binding protein, helps Caenorhabditis elegans survive dehydration. It localizes near cell membranes, reduces cell damage, and helps maintain membrane structure during drying. These results suggest that ice‐binding proteins can protect cells from dehydration stress as well as freezing stress.
Daiki Shimose   +9 more
wiley   +1 more source

EPR in protein science : intrinsically disordered proteins

open access: yes, 2011
Intrinsically disordered proteins (IDPs) form a unique protein category characterized by the absence of a well-defined structure and by remarkable conformational flexibility.
Drescher, Malte, Malte Drescher
core   +1 more source

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

open access: yesFEBS Open Bio, EarlyView.
IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo   +6 more
wiley   +1 more source

Editorial: Intrinsically Disordered Proteins and Regions: The Challenge to the Structure-Function Relationship

open access: yesFrontiers in Molecular Biosciences, 2022
Angelo Toto   +3 more
doaj   +1 more source

Emergence and evolution of an interaction between intrinsically disordered proteins

open access: yeseLife, 2017
Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. However, it is not clear how such interactions emerge and evolve on a molecular level.
Greta Hultqvist   +8 more
doaj   +1 more source

Deciphering the mechanisms of binding induced folding at nearly atomic resolution : The Φ value analysis applied to IDPs

open access: yes, 2014
The Φ value analysis is a method to analyze the structure of metastable states in reaction pathways. Such a methodology is based on the quantitative analysis of the effect of point mutations on the kinetics and thermodynamics of the probed reaction.
Gianni, Stefano   +4 more
core   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability

open access: yesFEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

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