Results 21 to 30 of about 10,067 (226)
Molecules, 2021 Intrinsically disordered proteins (IDPs) are critical players in the dynamic control of diverse cellular processes, and provide potential new drug targets because their dysregulation is closely related to many diseases.
Yusuke Hosoya, Junko Ohkanda
doaj +1 more source
Clio y Asociados, 2017 In the capital of Catamarca, in the college Father Ramon de la Quintana, during the period 2013–2014 placed in each of their classrooms Digital Interactive screens (IDPS). Before this challenge was the role of teachers create new resources for the reform
María Luz Brizuela
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Emerging experimental and computational methods for studying redox‐regulated structural transitions
FEBS Letters, EarlyView.Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
Angewandte Chemie, EarlyView.The molecular consequences of specific lysine modifications in Alzheimer´s disease remain insufficiently resolved in the context of full‐length protein. Here we integrate protein semisynthesis, segmental isotope labelling, and high‐resolution NMR spectroscopy to achieve residue‐resolved interrogation of site‐specific acetylation and carboxymethylation.
Dominik P. Vogl +4 more
wiley +2 more sources
Neuropsychiatric Disease and Treatment, 2023 Mustafa Ali, Teresia Mutavi, John Maina Mburu, Muthoni Mathai Department of Psychiatry, University of Nairobi, Nairobi, KenyaCorrespondence: Mustafa Ali, Department of Psychiatry, School of Medicine, College of Health Sciences, University of Nairobi, P.O.
Ali M, Mutavi T, Mburu JM, Mathai M
doaj
Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
doaj +1 more source
Adenosine triphosphate as a modulator of protein interactions and stability
FEBS Open Bio, EarlyView.ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness [PDF]
MicrobiologyopenThe works examines the link between intrinsic disorder in bacterial protein structure, and bacterial function, and antimicrobial resistance. It highlights how flexible, disordered proteins support secretion, stress responses, desiccation protection, and virulence, while also suggesting that these adaptable regions may provide novel targets for ...
O' Callaghan J +3 more
europepmc +2 more sources
FEBS Open Bio, EarlyView.We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +1 more source
Advanced Materials, EarlyView.Cancer‐associated NPC remodeling creates a high‐flux, low‐stringency nuclear state that supports malignant adaptation but increases mechanical fragility. Targeting the FG‐barrier or NPC scaffold may drive mechanostat failure, envelope rupture, DNA damage, and loss of nuclear integrity.
Sílvio Terra Stefanello +5 more
wiley +1 more source