Results 61 to 70 of about 8,552,186 (306)

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

Challenges and opportunities in technologies and methods for lncRNA structure determination

open access: yesCell & Bioscience
Long non-coding RNAs (lncRNAs) play pivotal roles in diverse cellular processes ranging from gene regulation and chromatin remodeling to RNA stability and epigenetic modifications. Despite the identification of approximately 95,000 lncRNA genes in humans,
Maximilia Frazao De Souza Degenhardt   +1 more
doaj   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

open access: yesFEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy   +4 more
wiley   +1 more source

SLIDER: Mining correlated motifs in protein-protein interaction networks [PDF]

open access: yes, 2009
—Correlated motif mining (CMM) is the problem to find overrepresented pairs of patterns, called motif pairs, in interacting protein sequences. Algorithmic solutions for CMM thereby provide a computational method for predicting binding sites for protein ...
Boyen, P.   +3 more
core  

Discover protein sequence signatures from protein-protein interaction data

open access: yesBMC Bioinformatics, 2005
Background The development of high-throughput technologies such as yeast two-hybrid systems and mass spectrometry technologies has made it possible to generate large protein-protein interaction (PPI) datasets.
Haasl Ryan J   +3 more
doaj   +1 more source

Deep learning frameworks for protein–protein interaction prediction

open access: yesComputational and Structural Biotechnology Journal, 2022
Protein-protein interactions (PPIs) play key roles in a broad range of biological processes. The disorder of PPIs often causes various physical and mental diseases, which makes PPIs become the focus of the research on disease mechanism and clinical ...
Xiaotian Hu   +3 more
doaj   +1 more source

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

open access: yesFEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa   +5 more
wiley   +1 more source

The protein-protein interaction ontology: for better representing and capturing the biological context of protein interaction

open access: yesBMC Genomics, 2021
Background With the rapid increase in the amount of Protein-Protein Interaction (PPI) data, the establishment of an event-centered PPI ontology that contains temporal and spatial vocabularies is urgently needed to clarify PPI biological annotations.
Mansheng Li   +6 more
doaj   +1 more source

Gut microbiome and aging—A dynamic interplay of microbes, metabolites, and the immune system

open access: yesFEBS Letters, EarlyView.
Age‐dependent shifts in microbial communities engender shifts in microbial metabolite profiles. These in turn drive shifts in barrier surface permeability of the gut and brain and induce immune activation. When paired with preexisting age‐related chronic inflammation this increases the risk of neuroinflammation and neurodegenerative diseases.
Aaron Mehl, Eran Blacher
wiley   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura   +2 more
wiley   +1 more source

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