Results 71 to 80 of about 8,215,941 (358)

Transposons disrupt genomic stability and trigger cancers

open access: yesFrontiers in Cellular and Infection Microbiology
Transposons (TEs) are genetic elements that can change their positions within genome. They cause transcriptional activation or repression by inserting into regulatory elements of related genes or by modulating epigenetic modifications on regulatory ...
Weixia Dong   +7 more
doaj   +1 more source

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

Integrative Structure and Functional Anatomy of a Nuclear Pore Complex

open access: yesNature, 2018
Nuclear pore complexes play central roles as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. However, their large size and dynamic nature have impeded a full structural and functional elucidation.
Seung Joong Kim   +31 more
semanticscholar   +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

Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

open access: yesJournal of Cell Biology, 1990
We have developed an in vitro system involving digitonin-permeabilized vertebrate cells to study biochemical events in the transport of macromolecules across the nuclear envelope.
S. Adam, Rachel Sterne Marr, L. Gerace
semanticscholar   +1 more source

Real‐time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer

open access: yesFEBS Letters, EarlyView.
Ribonucleotide reductases (RNR) synthesize DNA building blocks de novo, making them crucial in DNA replication and drug targeting. FLARE introduces the first single‐tube real‐time coupled RNR assay, which enables isothermal tracking of RNR activity at nanomolar enzyme levels and allows the reconstruction of allosteric regulatory patterns and rapid ...
Jacopo De Capitani   +4 more
wiley   +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

The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins

open access: yesJournal of Cell Biology, 1993
The antigen defined by mAb Ki-67 is a human nuclear protein the expression of which is strictly associated with cell proliferation and which is widely used in routine pathology as a "proliferation marker" to measure the growth fraction of cells in human ...
Carsten Schlfiter   +6 more
semanticscholar   +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

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