Results 111 to 120 of about 8,552,186 (306)

Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space

open access: yeseLife
Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2)-dependent formation of ...
Fabio Lolicato   +17 more
doaj   +1 more source

Decoding the dynamic extracellular matrix in cancer—3D models and bioscaffolds rewire the rules of tumor progression

open access: yesFEBS Letters, EarlyView.
Cancer progression is regulated by the dynamic matrix code of the tumor microenvironment, which influences cellular behavior and disease development. Importantly, matrix remodeling in three‐dimensional cancer models more accurately reflects in vivo conditions compared to conventional two‐dimensional systems.
Sylvia Mangani   +3 more
wiley   +1 more source

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

Identification of a Shiga toxin A‐derived peptide internalized into Gb3 receptor‐bearing cells via interaction with the Shiga toxin B subunit

open access: yesFEBS Letters, EarlyView.
The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi   +6 more
wiley   +1 more source

Protein-Protein Interactions [PDF]

open access: yesRevista Brasileira de Ciências Farmacêuticas, 2004
Pedrazzi G, Stagljar I
openaire   +5 more sources

Modulators of Protein–Protein Interactions [PDF]

open access: yesChemical Reviews, 2014
Milroy, L.   +4 more
openaire   +4 more sources

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

Exploring Protein Sequence Space Using Computationally Directed Recombination [PDF]

open access: yes, 2006
Evolution has provided us with many protein sequences. However, these sequences represent a very small fraction of the possible sequences. In the laboratory, scientists have explored areas of sequence space not represented by natural proteins both to ...
Meyer, Michelle Margaret
core   +1 more source

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