Ubiquitin is a small regulatory protein that has been found in almost all cells (''ubiquitously'') with nuclei (eukaryotes). It directs proteins to recycling and other functions.
Cryogenic electron microscopy (cryo-EM) allows scientists to investigate the assembly of DNA replication machinery where DNA is damaged.
Proteins are the building blocks of all living things and numerous studies are carried out to determine how these proteins are made and their function.
Life is organized on a 24-hour schedule. Central to this regular rhythm is the circadian clock, timekeepers that are present in virtually every organ, tissue and cell type.
A newly discovered manipulation mechanism used by parasitic bacteria to slow down plant aging, may offer new ways to protect disease-threatened food crops.
A recent study provides insight into plant chloroplasts and the proteins inside them.
Lung cancer remains the leading cause of cancer-associated death in the United States and worldwide. Patients with a subtype called lung adenocarcinoma (LUAD) have benefited from the development of new targeted medicines, but the search for effective new therapies for another subtype called lung squamous cell carcinoma (LSCC) has largely come up short.
Researchers have used sophisticated imaging technology to offer unmatched insights into the BRCA1-BARD1 protein complex.
Gross chromosomal rearrangements--where portions of the genome become moved, deleted, or inverted--can lead to cell death and diseases such as cancer in complex multicellular organisms.
S-acylation is the process of chemically linking a lipid to protein via a thioester bond. It is an important process of the cell that regulates the localization and function of numerous proteins.
Researchers from the Andalusian Centre for Molecular Biology and Regenerative Medicine (CABIMER), in collaboration with the Swiss Institute for Experimental Cancer Research (ISREC) have studied the mechanisms behind the higher tendency of people with Mulibrey syndrome to develop tumors.
An international research team has clarified the regulatory mechanism of the ubiquitin-proteasome system (*1) in recognizing and repairing DNA that has been damaged by ultraviolet (UV) light.
Research into Alzheimer's disease has long focused on understanding the role of two key proteins, beta amyloid and the tau protein. Found in tangles in patients' brain tissue, a pathological form of the tau protein contributes to propagating the disease in the brain.
Researchers reported the discovery of a new enzyme, called UCH37, that controls the waste management system of a cell.
A fresh new look at an old technique in protein biochemistry has shown that it should be reintroduced to the spectroscopy toolkit.
In a healthy brain, the multistep waste clearance process known as autophagy routinely removes and degrades damaged cell components - including malformed proteins like tau and toxic mitochondria.
According to a study, failures in a quality control system that defends protein-building fidelity in cells can result in motor neuron degeneration.
Despite immense efforts to improve pharmacology methods, over three-quarters of all human proteins still remain beyond the reach of therapeutic advancement.
The idea of the cell as a city is a common introduction to biology, conjuring depictions of the cell's organelles as power plants, factories, roads, libraries, warehouses and more.
Researchers at TMIMS have revealed that PINK1 (a serine/threonine kinase) and Parkin (a ubiquitin ligating enzyme: E3) work together to ubiquitylate the outer membrane proteins of damaged mitochondria to induce selective autophagy called mitophagy.
Chinese researchers recently discovered a protein quality control mechanism called "reubiquitination".