Results 111 to 120 of about 543,220 (340)

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

Context-specific interactions in literature-curated protein interaction databases

open access: yesBMC Genomics, 2018
Background Databases of literature-curated protein-protein interactions (PPIs) are often used to interpret high-throughput interactome mapping studies and estimate error rates.
R. Greg Stacey   +3 more
doaj   +1 more source

Mapping RNA-Protein Interactions with Subcellular Resolution Using Colocalization CLIP [PDF]

open access: gold, 2023
Soon Yi   +3 more
openalex   +1 more source

Interplay between circadian and other transcription factors—Implications for cycling transcriptome reprogramming

open access: yesFEBS Letters, EarlyView.
This perspective highlights emerging insights into how the circadian transcription factor CLOCK:BMAL1 regulates chromatin architecture, cooperates with other transcription factors, and coordinates enhancer dynamics. We propose an updated framework for how circadian transcription factors operate within dynamic and multifactorial chromatin landscapes ...
Xinyu Y. Nie, Jerome S. Menet
wiley   +1 more source

An automated method for finding molecular complexes in large protein interaction networks

open access: yesBMC Bioinformatics, 2003
Background Recent advances in proteomics technologies such as two-hybrid, phage display and mass spectrometry have enabled us to create a detailed map of biomolecular interaction networks.
Bader Gary D, Hogue Christopher WV
doaj   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

open access: yesFEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

Bacterial two-hybrid systems evolved: innovations for protein-protein interaction research

open access: yesJournal of Bacteriology
Bacterial two-hybrid (B2H) systems offer a versatile platform for detecting protein-protein interactions (PPIs) in vivo. Originally developed to study bacterial transcriptional regulators, these systems have evolved to support a wide range of ...
Rebecca M. Richardson, Steven M. Pascal
doaj   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

The role of histone modifications in transcription regulation upon DNA damage

open access: yesFEBS Letters, EarlyView.
This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley   +1 more source

Multiplex mapping of protein-protein interaction interfaces

open access: yes
Abstract We describe peptide mapping through Split Antibiotic Resistance Complementation (SpARC-map), a method to identify the probable interface between two interacting proteins. Our method is based on in vivo affinity selection inside a bacterial host, and uses high throughput DNA sequencing to infer the probable protein-protein ...
Jingxuan He   +3 more
openaire   +2 more sources

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